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Pre-mRNA-splicing factor 8

 PRP8_YEAST              Reviewed;        2413 AA.
P33334; D3DLB4;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 165.
RecName: Full=Pre-mRNA-splicing factor 8;
Name=PRP8; Synonyms=DBF3, DNA39, RNA8, SLT21, USA2;
OrderedLocusNames=YHR165C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7785334; DOI=10.1002/yea.320110406;
Hodges P.E., Jackson S.P., Brown J.D., Beggs J.D.;
"Extraordinary sequence conservation of the PRP8 splicing factor.";
Yeast 11:337-342(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7838707; DOI=10.1093/nar/22.25.5555;
Shea J.E., Toyn J.H., Johnston L.H.;
"The budding yeast U5 snRNP Prp8 is a highly conserved protein which
links RNA splicing with cell cycle progression.";
Nucleic Acids Res. 22:5555-5564(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091229; DOI=10.1126/science.8091229;
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
VIII.";
Science 265:2077-2082(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=2835658; DOI=10.1128/MCB.8.3.1067;
Jackson S.P., Lossky M., Beggs J.D.;
"Cloning of the RNA8 gene of Saccharomyces cerevisiae, detection of
the RNA8 protein, and demonstration that it is essential for nuclear
pre-mRNA splicing.";
Mol. Cell. Biol. 8:1067-1075(1988).
[6]
FUNCTION, AND INTERACTION WITH PRP40.
PubMed=9150140; DOI=10.1016/S0092-8674(00)80221-4;
Abovich N., Rosbash M.;
"Cross-intron bridging interactions in the yeast commitment complex
are conserved in mammals.";
Cell 89:403-412(1997).
[7]
SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10449419; DOI=10.1093/emboj/18.16.4535;
Gottschalk A., Neubauer G., Banroques J., Mann M., Luehrmann R.,
Fabrizio P.;
"Identification by mass spectrometry and functional analysis of novel
proteins of the yeast [U4/U6.U5] tri-snRNP.";
EMBO J. 18:4535-4548(1999).
[8]
FUNCTION.
PubMed=10444596; DOI=10.1101/gad.13.15.1983;
Siatecka M., Reyes J.L., Konarska M.M.;
"Functional interactions of Prp8 with both splice sites at the
spliceosomal catalytic center.";
Genes Dev. 13:1983-1993(1999).
[9]
INTERACTION WITH SNP1.
PubMed=11425851; DOI=10.1074/jbc.M100022200;
Awasthi S., Palmer R., Castro M., Mobarak C.D., Ruby S.W.;
"New roles for the Snp1 and Exo84 proteins in yeast pre-mRNA
splicing.";
J. Biol. Chem. 276:31004-31015(2001).
[10]
IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11884590; DOI=10.1128/MCB.22.7.2011-2024.2002;
Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
"Proteomics analysis reveals stable multiprotein complexes in both
fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel
pre-mRNA splicing factors, and snRNAs.";
Mol. Cell. Biol. 22:2011-2024(2002).
[11]
FUNCTION.
PubMed=12773561; DOI=10.1128/MCB.23.12.4174-4186.2003;
McPheeters D.S., Muhlenkamp P.;
"Spatial organization of protein-RNA interactions in the branch site-
3' splice site region during pre-mRNA splicing in yeast.";
Mol. Cell. Biol. 23:4174-4186(2003).
[12]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[13]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=17934474; DOI=10.1038/nsmb1303;
Boon K.L., Grainger R.J., Ehsani P., Barrass J.D., Auchynnikava T.,
Inglehearn C.F., Beggs J.D.;
"prp8 mutations that cause human retinitis pigmentosa lead to a U5
snRNP maturation defect in yeast.";
Nat. Struct. Mol. Biol. 14:1077-1083(2007).
[14]
MUTAGENESIS OF ASP-1853 AND ASP-1854, AND LACK OF METAL-BINDING SITE.
PubMed=18836455; DOI=10.1038/nsmb.1505;
Ritchie D.B., Schellenberg M.J., Gesner E.M., Raithatha S.A.,
Stuart D.T., Macmillan A.M.;
"Structural elucidation of a PRP8 core domain from the heart of the
spliceosome.";
Nat. Struct. Mol. Biol. 15:1199-1205(2008).
[15]
SUBUNIT, IDENTIFICATION IN THE U4/U5/U6 TRI-SNRNP COMPLEX, AND
ELECTRON MICROSCOPY.
PubMed=18953335; DOI=10.1038/nsmb.1506;
Hacker I., Sander B., Golas M.M., Wolf E., Karagoz E., Kastner B.,
Stark H., Fabrizio P., Luhrmann R.;
"Localization of Prp8, Brr2, Snu114 and U4/U6 proteins in the yeast
tri-snRNP by electron microscopy.";
Nat. Struct. Mol. Biol. 15:1206-1212(2008).
[16]
FUNCTION, AND INTERACTION WITH BRR2.
PubMed=19098916; DOI=10.1038/nsmb.1535;
Maeder C., Kutach A.K., Guthrie C.;
"ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires
the C terminus of Prp8.";
Nat. Struct. Mol. Biol. 16:42-48(2009).
[17]
INTERACTION WITH CWC21 AND SNU114.
PubMed=19854871; DOI=10.1261/rna.1908309;
Grainger R.J., Barrass J.D., Jacquier A., Rain J.-C., Beggs J.D.;
"Physical and genetic interactions of yeast Cwc21p, an ortholog of
human SRm300/SRRM2, suggest a role at the catalytic center of the
spliceosome.";
RNA 15:2161-2173(2009).
[18]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2147-2413, AND LACK OF METAL
BINDING.
PubMed=17317632; DOI=10.1016/j.molcel.2007.01.023;
Pena V., Liu S., Bujnicki J.M., Luehrmann R., Wahl M.C.;
"Structure of a multipartite protein-protein interaction domain in
splicing factor Prp8 and its link to retinitis pigmentosa.";
Mol. Cell 25:615-624(2007).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1827-2092, LACK OF METAL
BINDING, DOMAIN, AND MUTAGENESIS OF ASP-1853; ASP-1854; THR-1855;
THR-1936 AND ARG-1937.
PubMed=18843295; DOI=10.1038/emboj.2008.209;
Pena V., Rozov A., Fabrizio P., Luehrmann R., Wahl M.C.;
"Structure and function of an RNase H domain at the heart of the
spliceosome.";
EMBO J. 27:2929-2940(2008).
[20]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1822-2095, LACK OF METAL
BINDING, FUNCTION, AND MUTAGENESIS OF ASP-1853.
PubMed=18779563; DOI=10.1073/pnas.0805960105;
Yang K., Zhang L., Xu T., Heroux A., Zhao R.;
"Crystal structure of the beta-finger domain of Prp8 reveals analogy
to ribosomal proteins.";
Proc. Natl. Acad. Sci. U.S.A. 105:13817-13822(2008).
[21]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1836-2092 IN COMPLEX WITH
AAR2, AND INTERACTION WITH AAR2.
PubMed=21764848; DOI=10.1101/gad.635911;
Weber G., Cristao V.F., de Lima Alves F., Santos K.F., Holton N.,
Rappsilber J., Beggs J.D., Wahl M.C.;
"Mechanism for Aar2p function as a U5 snRNP assembly factor.";
Genes Dev. 25:1601-1612(2011).
[22]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 885-2413 IN COMPLEX WITH
AAR2, FUNCTION, DOMAIN, INTERACTION WITH AAR2, AND MUTAGENESIS OF
HIS-1658; GLU-1684; HIS-1687; ASP-1700 AND ASP-1735.
PubMed=23354046; DOI=10.1038/nature11843;
Galej W.P., Oubridge C., Newman A.J., Nagai K.;
"Crystal structure of Prp8 reveals active site cavity of the
spliceosome.";
Nature 493:638-643(2013).
-!- FUNCTION: Functions as a scaffold that mediates the ordered
assembly of spliceosomal proteins and snRNAs. Required for
association of BRR2 with the spliceosomal U5 snRNP, and the
subsequent assembly of the U4/U6-U5 tri-snRNP complex. Functions
as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at
splice sites on pre-mRNA substrates, so that splicing can occur.
Interacts with both the 5' and the 3' splice site, as well as the
branch region. Has a role in branch site-3' splice site selection.
Associates with the branch site-3' splice 3'-exon region. Also has
a role in cell cycle. {ECO:0000269|PubMed:10444596,
ECO:0000269|PubMed:12773561, ECO:0000269|PubMed:17934474,
ECO:0000269|PubMed:18779563, ECO:0000269|PubMed:19098916,
ECO:0000269|PubMed:23354046, ECO:0000269|PubMed:2835658,
ECO:0000269|PubMed:9150140}.
-!- SUBUNIT: Component of the U4/U6-U5 tri-snRNP complex composed of
the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8,
PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1,
SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7,
LSM8, BRR2 and DIB1. Belongs to the CWC complex (or CEF1-
associated complex), a spliceosome sub-complex reminiscent of a
late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at
least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15,
CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3,
ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22,
PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309,
SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with PRP40 and
SNP1. Interacts (via SCwid domain) with CWC21. Interacts (via
SCwid domain) with SNU114 (via N-terminus). Interacts (via RNase H
homology domain and MPN domain) with BRR2; this modulates BRR2
ATPase and helicase activity. Interacts (via RNase H homology
domain) with AAR2. AAR2 and BRR2 compete for PRP8 binding, and
during U5 snRNP maturation BRR2 displaces the initially bound
AAR2. Is associated with snRNP U5, together with SNU114 and BRR2.
{ECO:0000269|PubMed:10449419, ECO:0000269|PubMed:11425851,
ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:17934474,
ECO:0000269|PubMed:18953335, ECO:0000269|PubMed:19098916,
ECO:0000269|PubMed:19854871, ECO:0000269|PubMed:21764848,
ECO:0000269|PubMed:23354046, ECO:0000269|PubMed:9150140}.
-!- INTERACTION:
P32357:AAR2; NbExp=11; IntAct=EBI-465, EBI-340;
P32639:BRR2; NbExp=22; IntAct=EBI-465, EBI-861;
P36006:MYO3; NbExp=4; IntAct=EBI-465, EBI-11670;
Q04439:MYO5; NbExp=4; IntAct=EBI-465, EBI-11687;
Q00916:SNP1; NbExp=3; IntAct=EBI-465, EBI-724;
P61864:UBI4 (xeno); NbExp=2; IntAct=EBI-465, EBI-19797;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17934474,
ECO:0000269|PubMed:2835658}.
-!- DOMAIN: The MPN (JAB/Mov34) domain has structural similarity with
deubiquitinating enzymes, but lacks the residues that would bind
the catalytic metal ion.
-!- DOMAIN: Contains a region with structural similarity to reverse
transcripase, presenting the classical thumb, fingers and palm
architecture, but lacks enzyme activity, since the essential
metal-binding residues are not conserved.
-!- DOMAIN: Contains a region with structural similarity to type-2
restriction endonucleases, but the residues that would bind
catalytic metal ions in endonucleases are instead involved in
hydrogen bonds that stabilize a highly conserved loop.
-!- DOMAIN: Contains a region with structural similarity to RNase H,
but lacks RNase H activity.
-!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
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EMBL; Z24732; CAA80854.1; -; Genomic_DNA.
EMBL; L29421; AAA67044.1; -; Genomic_DNA.
EMBL; U00027; AAB68011.1; -; Genomic_DNA.
EMBL; BK006934; DAA06858.1; -; Genomic_DNA.
PIR; S34670; S34670.
RefSeq; NP_012035.1; NM_001179296.1.
PDB; 2OG4; X-ray; 2.00 A; A=2147-2397.
PDB; 3E66; X-ray; 2.05 A; A/B=1822-2095.
PDB; 3E9O; X-ray; 2.00 A; A=1836-2087.
PDB; 3E9P; X-ray; 2.10 A; A/B=1833-2087.
PDB; 3JCM; EM; 3.80 A; A=1-2413.
PDB; 3SBG; X-ray; 3.28 A; A=1836-2397.
PDB; 3SBT; X-ray; 1.80 A; A=1836-2092.
PDB; 3ZEF; X-ray; 3.10 A; B/E=885-2413.
PDB; 4BGD; X-ray; 3.10 A; C=2148-2395.
PDB; 4I43; X-ray; 2.00 A; B=885-2413.
PDB; 4ILG; X-ray; 2.10 A; B=1836-2090, C=2147-2413.
PDB; 4ILH; X-ray; 1.85 A; A=1836-2090.
PDB; 4ILJ; X-ray; 2.00 A; A/B=1836-2090.
PDB; 5DCA; X-ray; 2.80 A; J=2148-2398.
PDB; 5GAM; EM; 3.70 A; A=1-735.
PDB; 5GAN; EM; 3.60 A; A=1-2413.
PDB; 5GAO; EM; 3.60 A; A=2147-2413.
PDB; 5GAP; EM; 3.60 A; A=1-2413.
PDB; 5GM6; EM; 3.50 A; A=128-2413.
PDB; 5GMK; EM; 3.40 A; A=1-2413.
PDB; 5LJ3; EM; 3.80 A; A=1-2413.
PDB; 5LJ5; EM; 3.80 A; A=1-2413.
PDB; 5LQW; EM; 5.80 A; A=1-2413.
PDB; 5M52; X-ray; 3.40 A; C/D=2147-2413.
PDB; 5M5P; X-ray; 4.20 A; B/D=2147-2413.
PDB; 5MPS; EM; 3.85 A; A=1-2413.
PDB; 5MQ0; EM; 4.17 A; A=1-2413.
PDB; 5NRL; EM; 7.20 A; A=1-2413.
PDB; 5WSG; EM; 4.00 A; A=1-2413.
PDBsum; 2OG4; -.
PDBsum; 3E66; -.
PDBsum; 3E9O; -.
PDBsum; 3E9P; -.
PDBsum; 3JCM; -.
PDBsum; 3SBG; -.
PDBsum; 3SBT; -.
PDBsum; 3ZEF; -.
PDBsum; 4BGD; -.
PDBsum; 4I43; -.
PDBsum; 4ILG; -.
PDBsum; 4ILH; -.
PDBsum; 4ILJ; -.
PDBsum; 5DCA; -.
PDBsum; 5GAM; -.
PDBsum; 5GAN; -.
PDBsum; 5GAO; -.
PDBsum; 5GAP; -.
PDBsum; 5GM6; -.
PDBsum; 5GMK; -.
PDBsum; 5LJ3; -.
PDBsum; 5LJ5; -.
PDBsum; 5LQW; -.
PDBsum; 5M52; -.
PDBsum; 5M5P; -.
PDBsum; 5MPS; -.
PDBsum; 5MQ0; -.
PDBsum; 5NRL; -.
PDBsum; 5WSG; -.
ProteinModelPortal; P33334; -.
SMR; P33334; -.
BioGrid; 36599; 162.
DIP; DIP-2427N; -.
IntAct; P33334; 65.
MINT; MINT-599605; -.
STRING; 4932.YHR165C; -.
iPTMnet; P33334; -.
MaxQB; P33334; -.
PRIDE; P33334; -.
EnsemblFungi; YHR165C; YHR165C; YHR165C.
GeneID; 856570; -.
KEGG; sce:YHR165C; -.
EuPathDB; FungiDB:YHR165C; -.
SGD; S000001208; PRP8.
GeneTree; ENSGT00390000015210; -.
HOGENOM; HOG000184103; -.
InParanoid; P33334; -.
KO; K12856; -.
OMA; QNKVNTV; -.
OrthoDB; EOG092C3X6Q; -.
BioCyc; YEAST:G3O-31199-MONOMER; -.
BRENDA; 3.1.13.2; 984.
Reactome; R-SCE-72165; mRNA Splicing - Minor Pathway.
EvolutionaryTrace; P33334; -.
PRO; PR:P33334; -.
Proteomes; UP000002311; Chromosome VIII.
GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:SGD.
GO; GO:0005682; C:U5 snRNP; IDA:SGD.
GO; GO:0097157; F:pre-mRNA intronic binding; IDA:SGD.
GO; GO:0030619; F:U1 snRNA binding; IDA:SGD.
GO; GO:0030620; F:U2 snRNA binding; IDA:SGD.
GO; GO:0030623; F:U5 snRNA binding; IDA:SGD.
GO; GO:0017070; F:U6 snRNA binding; IDA:SGD.
GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IMP:SGD.
GO; GO:0000389; P:mRNA 3'-splice site recognition; IMP:SGD.
GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:SGD.
CDD; cd13838; RNase_H_like_Prp8_IV; 1.
InterPro; IPR000555; JAMM/MPN+_dom.
InterPro; IPR012591; PRO8NT.
InterPro; IPR012592; PROCN.
InterPro; IPR012984; PROCT.
InterPro; IPR027652; PRP8.
InterPro; IPR021983; PRP8_domainIV.
InterPro; IPR019581; Prp8_U5-snRNA-bd.
InterPro; IPR019580; Prp8_U6-snRNA-bd.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR019582; RRM_spliceosomal_PrP8.
PANTHER; PTHR11140; PTHR11140; 1.
Pfam; PF08082; PRO8NT; 1.
Pfam; PF08083; PROCN; 1.
Pfam; PF08084; PROCT; 1.
Pfam; PF12134; PRP8_domainIV; 1.
Pfam; PF10598; RRM_4; 1.
Pfam; PF10597; U5_2-snRNA_bdg; 1.
Pfam; PF10596; U6-snRNA_bdg; 1.
ProDom; PD149576; Pre-mRNA-splicing_factor-8; 1.
SMART; SM00232; JAB_MPN; 1.
SUPFAM; SSF53098; SSF53098; 2.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; mRNA processing; mRNA splicing;
Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
Spliceosome.
CHAIN 1 2413 Pre-mRNA-splicing factor 8.
/FTId=PRO_0000097042.
DOMAIN 2182 2311 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
REGION 253 543 SNU114/CWC21 interacting domain (SCwid).
REGION 885 1375 Reverse transcriptase homology domain.
REGION 1376 1649 Linker.
REGION 1585 1598 Important for branch point selection.
REGION 1653 1824 Restriction endonuclease homology domain.
REGION 1839 2092 RNase H homology domain.
COMPBIAS 5 9 Poly-Pro.
COMPBIAS 20 27 Poly-Pro.
COMPBIAS 50 56 Poly-Pro.
COMPBIAS 72 78 Poly-Pro.
MUTAGEN 1658 1658 H->S: No effect on viability.
{ECO:0000269|PubMed:23354046}.
MUTAGEN 1684 1684 E->Q: No effect on viability.
{ECO:0000269|PubMed:23354046}.
MUTAGEN 1687 1687 H->S: No effect on viability.
{ECO:0000269|PubMed:23354046}.
MUTAGEN 1700 1700 D->N: No effect on viability.
{ECO:0000269|PubMed:23354046}.
MUTAGEN 1735 1735 D->N: No effect on viability.
{ECO:0000269|PubMed:23354046}.
MUTAGEN 1853 1853 D->A: Alters protein folding. Severely
impaired growth. Strongly reduced growth
at 35 degrees Celsius; when associated
with A-1854.
{ECO:0000269|PubMed:18779563,
ECO:0000269|PubMed:18836455,
ECO:0000269|PubMed:18843295}.
MUTAGEN 1853 1853 D->N: Reduced growth at 30 degrees
Celsius. Strongly reduced growth at 16
degrees Celsius.
{ECO:0000269|PubMed:18779563,
ECO:0000269|PubMed:18836455,
ECO:0000269|PubMed:18843295}.
MUTAGEN 1854 1854 D->A: Reduced growth at 30 degrees
Celsius. Strongly reduced growth at 16
degrees Celsius. Strongly reduced growth
at 35 degrees Celsius; when associated
with A-1853.
{ECO:0000269|PubMed:18836455,
ECO:0000269|PubMed:18843295}.
MUTAGEN 1854 1854 D->N: Reduced growth at 30 degrees
Celsius. Strongly reduced growth at 16
degrees Celsius.
{ECO:0000269|PubMed:18836455,
ECO:0000269|PubMed:18843295}.
MUTAGEN 1855 1855 T->A: Reduced growth at 30 degrees
Celsius. Strongly reduced growth at 16
degrees Celsius.
{ECO:0000269|PubMed:18843295}.
MUTAGEN 1936 1936 T->A: Reduced growth at 30 degrees
Celsius. Strongly reduced growth at 16
degrees Celsius.
{ECO:0000269|PubMed:18843295}.
MUTAGEN 1937 1937 R->K: Severely impaired growth. Reduced
growth at 30 degrees Celsius. Strongly
reduced growth at 16 degrees Celsius.
{ECO:0000269|PubMed:18843295}.
CONFLICT 388 420 PHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTP -> LIYI
IPGPVQCAYHGIIIQCRVLSRTMRSTTRL (in Ref. 2;
AAA67044). {ECO:0000305}.
CONFLICT 1132 1132 T -> S (in Ref. 2; AAA67044).
{ECO:0000305}.
CONFLICT 1575 1575 W -> C (in Ref. 2; AAA67044).
{ECO:0000305}.
HELIX 136 146 {ECO:0000244|PDB:5GMK}.
HELIX 152 154 {ECO:0000244|PDB:5GMK}.
HELIX 155 164 {ECO:0000244|PDB:5GMK}.
HELIX 165 167 {ECO:0000244|PDB:5GMK}.
HELIX 168 176 {ECO:0000244|PDB:5GMK}.
STRAND 188 194 {ECO:0000244|PDB:5GMK}.
STRAND 200 202 {ECO:0000244|PDB:5GMK}.
HELIX 210 230 {ECO:0000244|PDB:5GMK}.
STRAND 239 242 {ECO:0000244|PDB:5GMK}.
TURN 251 257 {ECO:0000244|PDB:5GMK}.
TURN 272 281 {ECO:0000244|PDB:5GMK}.
STRAND 282 285 {ECO:0000244|PDB:5GMK}.
STRAND 290 294 {ECO:0000244|PDB:5GMK}.
HELIX 305 314 {ECO:0000244|PDB:5GMK}.
HELIX 316 318 {ECO:0000244|PDB:5GMK}.
HELIX 325 327 {ECO:0000244|PDB:5GMK}.
HELIX 333 341 {ECO:0000244|PDB:5GMK}.
HELIX 370 372 {ECO:0000244|PDB:5GMK}.
HELIX 381 386 {ECO:0000244|PDB:5GMK}.
HELIX 388 391 {ECO:0000244|PDB:5GMK}.
STRAND 392 394 {ECO:0000244|PDB:5GMK}.
STRAND 417 419 {ECO:0000244|PDB:5GMK}.
TURN 461 464 {ECO:0000244|PDB:5GMK}.
HELIX 473 479 {ECO:0000244|PDB:5GMK}.
HELIX 484 488 {ECO:0000244|PDB:5GMK}.
HELIX 496 498 {ECO:0000244|PDB:5GMK}.
HELIX 503 507 {ECO:0000244|PDB:5GMK}.
STRAND 512 514 {ECO:0000244|PDB:5GMK}.
HELIX 516 534 {ECO:0000244|PDB:5GMK}.
TURN 541 544 {ECO:0000244|PDB:5GMK}.
HELIX 547 551 {ECO:0000244|PDB:5GMK}.
STRAND 557 563 {ECO:0000244|PDB:5GMK}.
HELIX 564 585 {ECO:0000244|PDB:5GMK}.
STRAND 590 593 {ECO:0000244|PDB:5GMK}.
STRAND 599 603 {ECO:0000244|PDB:5GMK}.
HELIX 607 612 {ECO:0000244|PDB:5GMK}.
HELIX 617 640 {ECO:0000244|PDB:5GMK}.
HELIX 647 663 {ECO:0000244|PDB:5GMK}.
HELIX 666 668 {ECO:0000244|PDB:5GMK}.
HELIX 671 673 {ECO:0000244|PDB:5GMK}.
HELIX 674 689 {ECO:0000244|PDB:5GMK}.
STRAND 697 699 {ECO:0000244|PDB:5GMK}.
HELIX 705 735 {ECO:0000244|PDB:5GMK}.
TURN 747 749 {ECO:0000244|PDB:5GMK}.
HELIX 750 769 {ECO:0000244|PDB:5GMK}.
HELIX 776 794 {ECO:0000244|PDB:5GMK}.
HELIX 806 835 {ECO:0000244|PDB:5GMK}.
HELIX 842 870 {ECO:0000244|PDB:5GMK}.
HELIX 885 892 {ECO:0000244|PDB:4I43}.
HELIX 908 924 {ECO:0000244|PDB:4I43}.
HELIX 931 945 {ECO:0000244|PDB:4I43}.
HELIX 947 960 {ECO:0000244|PDB:4I43}.
STRAND 967 969 {ECO:0000244|PDB:4I43}.
STRAND 975 979 {ECO:0000244|PDB:5GMK}.
HELIX 986 1005 {ECO:0000244|PDB:4I43}.
STRAND 1013 1015 {ECO:0000244|PDB:4I43}.
HELIX 1021 1033 {ECO:0000244|PDB:4I43}.
TURN 1036 1039 {ECO:0000244|PDB:4I43}.
STRAND 1042 1044 {ECO:0000244|PDB:5GMK}.
STRAND 1046 1053 {ECO:0000244|PDB:4I43}.
TURN 1056 1060 {ECO:0000244|PDB:4I43}.
HELIX 1063 1071 {ECO:0000244|PDB:4I43}.
HELIX 1076 1085 {ECO:0000244|PDB:4I43}.
STRAND 1087 1092 {ECO:0000244|PDB:4I43}.
STRAND 1095 1098 {ECO:0000244|PDB:4I43}.
HELIX 1110 1135 {ECO:0000244|PDB:4I43}.
STRAND 1138 1140 {ECO:0000244|PDB:3ZEF}.
HELIX 1150 1154 {ECO:0000244|PDB:4I43}.
STRAND 1156 1164 {ECO:0000244|PDB:4I43}.
STRAND 1167 1174 {ECO:0000244|PDB:4I43}.
HELIX 1176 1189 {ECO:0000244|PDB:4I43}.
TURN 1197 1200 {ECO:0000244|PDB:4I43}.
STRAND 1205 1207 {ECO:0000244|PDB:5GMK}.
HELIX 1209 1211 {ECO:0000244|PDB:4I43}.
HELIX 1217 1231 {ECO:0000244|PDB:4I43}.
TURN 1236 1238 {ECO:0000244|PDB:4I43}.
HELIX 1243 1245 {ECO:0000244|PDB:4I43}.
STRAND 1246 1252 {ECO:0000244|PDB:4I43}.
STRAND 1258 1262 {ECO:0000244|PDB:4I43}.
STRAND 1265 1271 {ECO:0000244|PDB:4I43}.
HELIX 1272 1274 {ECO:0000244|PDB:4I43}.
STRAND 1283 1289 {ECO:0000244|PDB:4I43}.
TURN 1291 1293 {ECO:0000244|PDB:4I43}.
STRAND 1295 1304 {ECO:0000244|PDB:4I43}.
HELIX 1306 1320 {ECO:0000244|PDB:4I43}.
HELIX 1328 1346 {ECO:0000244|PDB:4I43}.
HELIX 1348 1351 {ECO:0000244|PDB:4I43}.
HELIX 1354 1375 {ECO:0000244|PDB:4I43}.
TURN 1380 1382 {ECO:0000244|PDB:5GMK}.
HELIX 1385 1389 {ECO:0000244|PDB:4I43}.
HELIX 1392 1394 {ECO:0000244|PDB:4I43}.
HELIX 1409 1412 {ECO:0000244|PDB:4I43}.
STRAND 1414 1417 {ECO:0000244|PDB:4I43}.
STRAND 1422 1425 {ECO:0000244|PDB:4I43}.
HELIX 1427 1429 {ECO:0000244|PDB:4I43}.
STRAND 1434 1436 {ECO:0000244|PDB:3ZEF}.
HELIX 1440 1443 {ECO:0000244|PDB:4I43}.
HELIX 1447 1470 {ECO:0000244|PDB:4I43}.
HELIX 1477 1479 {ECO:0000244|PDB:4I43}.
TURN 1480 1482 {ECO:0000244|PDB:4I43}.
TURN 1487 1490 {ECO:0000244|PDB:4I43}.
HELIX 1491 1495 {ECO:0000244|PDB:4I43}.
HELIX 1499 1502 {ECO:0000244|PDB:4I43}.
HELIX 1508 1514 {ECO:0000244|PDB:4I43}.
HELIX 1515 1517 {ECO:0000244|PDB:4I43}.
HELIX 1530 1533 {ECO:0000244|PDB:4I43}.
HELIX 1540 1549 {ECO:0000244|PDB:4I43}.
HELIX 1552 1558 {ECO:0000244|PDB:4I43}.
STRAND 1559 1561 {ECO:0000244|PDB:5GMK}.
HELIX 1563 1565 {ECO:0000244|PDB:4I43}.
HELIX 1603 1614 {ECO:0000244|PDB:4I43}.
TURN 1617 1619 {ECO:0000244|PDB:4I43}.
STRAND 1624 1626 {ECO:0000244|PDB:5GMK}.
STRAND 1628 1630 {ECO:0000244|PDB:5GMK}.
STRAND 1633 1636 {ECO:0000244|PDB:4I43}.
HELIX 1641 1648 {ECO:0000244|PDB:4I43}.
TURN 1649 1652 {ECO:0000244|PDB:4I43}.
HELIX 1653 1670 {ECO:0000244|PDB:4I43}.
TURN 1671 1677 {ECO:0000244|PDB:4I43}.
STRAND 1678 1683 {ECO:0000244|PDB:4I43}.
HELIX 1690 1692 {ECO:0000244|PDB:4I43}.
STRAND 1700 1711 {ECO:0000244|PDB:4I43}.
STRAND 1726 1739 {ECO:0000244|PDB:4I43}.
STRAND 1743 1745 {ECO:0000244|PDB:4I43}.
HELIX 1748 1759 {ECO:0000244|PDB:4I43}.
STRAND 1763 1766 {ECO:0000244|PDB:4I43}.
STRAND 1768 1778 {ECO:0000244|PDB:4I43}.
TURN 1779 1782 {ECO:0000244|PDB:4I43}.
STRAND 1783 1788 {ECO:0000244|PDB:4I43}.
HELIX 1794 1808 {ECO:0000244|PDB:4I43}.
HELIX 1810 1822 {ECO:0000244|PDB:4I43}.
TURN 1837 1839 {ECO:0000244|PDB:4I43}.
HELIX 1840 1844 {ECO:0000244|PDB:3SBT}.
STRAND 1845 1847 {ECO:0000244|PDB:3SBT}.
STRAND 1849 1853 {ECO:0000244|PDB:3SBT}.
STRAND 1857 1864 {ECO:0000244|PDB:3SBT}.
STRAND 1866 1868 {ECO:0000244|PDB:4ILG}.
STRAND 1870 1875 {ECO:0000244|PDB:3SBT}.
STRAND 1877 1882 {ECO:0000244|PDB:3SBT}.
TURN 1884 1886 {ECO:0000244|PDB:3SBT}.
STRAND 1888 1894 {ECO:0000244|PDB:3SBT}.
HELIX 1896 1899 {ECO:0000244|PDB:3SBT}.
HELIX 1905 1923 {ECO:0000244|PDB:3SBT}.
HELIX 1926 1928 {ECO:0000244|PDB:3SBT}.
STRAND 1931 1937 {ECO:0000244|PDB:3SBT}.
HELIX 1938 1940 {ECO:0000244|PDB:3SBT}.
HELIX 1941 1947 {ECO:0000244|PDB:3SBT}.
TURN 1948 1950 {ECO:0000244|PDB:3SBT}.
STRAND 1954 1957 {ECO:0000244|PDB:3SBT}.
STRAND 1959 1961 {ECO:0000244|PDB:4I43}.
HELIX 1965 1970 {ECO:0000244|PDB:3SBT}.
HELIX 1972 1980 {ECO:0000244|PDB:3SBT}.
STRAND 1985 1990 {ECO:0000244|PDB:3SBT}.
TURN 1991 1994 {ECO:0000244|PDB:3SBT}.
HELIX 1995 1997 {ECO:0000244|PDB:3SBT}.
HELIX 2001 2017 {ECO:0000244|PDB:3SBT}.
HELIX 2019 2026 {ECO:0000244|PDB:3SBT}.
STRAND 2030 2032 {ECO:0000244|PDB:3E9P}.
STRAND 2039 2041 {ECO:0000244|PDB:4ILH}.
HELIX 2045 2067 {ECO:0000244|PDB:3SBT}.
HELIX 2071 2073 {ECO:0000244|PDB:4ILH}.
HELIX 2076 2084 {ECO:0000244|PDB:3SBT}.
HELIX 2149 2159 {ECO:0000244|PDB:2OG4}.
HELIX 2160 2167 {ECO:0000244|PDB:2OG4}.
STRAND 2168 2171 {ECO:0000244|PDB:2OG4}.
STRAND 2178 2180 {ECO:0000244|PDB:5DCA}.
STRAND 2182 2186 {ECO:0000244|PDB:2OG4}.
HELIX 2187 2195 {ECO:0000244|PDB:2OG4}.
STRAND 2199 2201 {ECO:0000244|PDB:2OG4}.
STRAND 2204 2211 {ECO:0000244|PDB:2OG4}.
STRAND 2218 2225 {ECO:0000244|PDB:2OG4}.
STRAND 2229 2231 {ECO:0000244|PDB:2OG4}.
STRAND 2236 2238 {ECO:0000244|PDB:2OG4}.
STRAND 2245 2247 {ECO:0000244|PDB:3ZEF}.
STRAND 2254 2264 {ECO:0000244|PDB:2OG4}.
HELIX 2271 2281 {ECO:0000244|PDB:2OG4}.
TURN 2282 2284 {ECO:0000244|PDB:2OG4}.
STRAND 2289 2296 {ECO:0000244|PDB:2OG4}.
STRAND 2299 2307 {ECO:0000244|PDB:2OG4}.
HELIX 2309 2316 {ECO:0000244|PDB:2OG4}.
TURN 2317 2320 {ECO:0000244|PDB:3SBG}.
TURN 2323 2325 {ECO:0000244|PDB:4BGD}.
HELIX 2331 2333 {ECO:0000244|PDB:2OG4}.
STRAND 2334 2345 {ECO:0000244|PDB:2OG4}.
STRAND 2348 2352 {ECO:0000244|PDB:2OG4}.
HELIX 2360 2362 {ECO:0000244|PDB:4I43}.
HELIX 2363 2365 {ECO:0000244|PDB:2OG4}.
STRAND 2374 2376 {ECO:0000244|PDB:2OG4}.
HELIX 2385 2387 {ECO:0000244|PDB:2OG4}.
HELIX 2389 2396 {ECO:0000244|PDB:5DCA}.
TURN 2406 2408 {ECO:0000244|PDB:5M52}.
SEQUENCE 2413 AA; 279504 MW; 8F4F6F89D34D3508 CRC64;
MSGLPPPPPG FEEDSDLALP PPPPPPPGYE IEELDNPMVP SSVNEDTFLP PPPPPPSNFE
INAEEIVDFT LPPPPPPPGL DELETKAEKK VELHGKRKLD IGKDTFVTRK SRKRAKKMTK
KAKRSNLYTP KAEMPPEHLR KIINTHSDMA SKMYNTDKKA FLGALKYLPH AILKLLENMP
HPWEQAKEVK VLYHTSGAIT FVNETPRVIE PVYTAQWSAT WIAMRREKRD RTHFKRMRFP
PFDDDEPPLS YEQHIENIEP LDPINLPLDS QDDEYVKDWL YDSRPLEEDS KKVNGTSYKK
WSFDLPEMSN LYRLSTPLRD EVTDKNYYYL FDKKSFFNGK ALNNAIPGGP KFEPLYPREE
EEDYNEFNSI DRVIFRVPIR SEYKVAFPHL YNSRPRSVRI PWYNNPVSCI IQNDEEYDTP
ALFFDPSLNP IPHFIDNNSS LNVSNTKENG DFTLPEDFAP LLAEEEELIL PNTKDAMSLY
HSPFPFNRTK GKMVRAQDVA LAKKWFLQHP DEEYPVKVKV SYQKLLKNYV LNELHPTLPT
NHNKTKLLKS LKNTKYFQQT TIDWVEAGLQ LCRQGHNMLN LLIHRKGLTY LHLDYNFNLK
PTKTLTTKER KKSRLGNSFH LMRELLKMMK LIVDTHVQFR LGNVDAFQLA DGIHYILNHI
GQLTGIYRYK YKVMHQIRAC KDLKHIIYYK FNKNLGKGPG CGFWQPAWRV WLNFLRGTIP
LLERYIGNLI TRQFEGRSNE IVKTTTKQRL DAYYDLELRN SVMDDILEMM PESIRQKKAR
TILQHLSEAW RCWKANIPWD VPGMPAPIKK IIERYIKSKA DAWVSAAHYN RERIKRGAHV
EKTMVKKNLG RLTRLWIKNE QERQRQIQKN GPEITPEEAT TIFSVMVEWL ESRSFSPIPF
PPLTYKNDTK ILVLALEDLK DVYASKVRLN ASEREELALI EEAYDNPHDT LNRIKKYLLT
QRVFKPVDIT MMENYQNISP VYSVDPLEKI TDAYLDQYLW YEADQRKLFP NWIKPSDSEI
PPLLVYKWTQ GINNLSEIWD VSRGQSAVLL ETTLGEMAEK IDFTLLNRLL RLIVDPNIAD
YITAKNNVVI NFKDMSHVNK YGLIRGLKFA SFIFQYYGLV IDLLLLGQER ATDLAGPANN
PNEFMQFKSK EVEKAHPIRL YTRYLDRIYM LFHFEEDEGE ELTDEYLAEN PDPNFENSIG
YNNRKCWPKD SRMRLIRQDV NLGRAVFWEI QSRVPTSLTS IKWENAFVSV YSKNNPNLLF
SMCGFEVRIL PRQRMEEVVS NDEGVWDLVD ERTKQRTAKA YLKVSEEEIK KFDSRIRGIL
MASGSTTFTK VAAKWNTSLI SLFTYFREAI VATEPLLDIL VKGETRIQNR VKLGLNSKMP
TRFPPAVFYT PKELGGLGMI SASHILIPAS DLSWSKQTDT GITHFRAGMT HEDEKLIPTI
FRYITTWENE FLDSQRVWAE YATKRQEAIQ QNRRLAFEEL EGSWDRGIPR ISTLFQRDRH
TLAYDRGHRI RREFKQYSLE RNSPFWWTNS HHDGKLWNLN AYRTDVIQAL GGIETILEHT
LFKGTGFNSW EGLFWEKASG FEDSMQFKKL THAQRTGLSQ IPNRRFTLWW SPTINRANVY
VGFLVQLDLT GIFLHGKIPT LKISLIQIFR AHLWQKIHES IVFDICQILD GELDVLQIES
VTKETVHPRK SYKMNSSAAD ITMESVHEWE VSKPSLLHET NDSFKGLITN KMWFDVQLRY
GDYDSHDISR YVRAKFLDYT TDNVSMYPSP TGVMIGIDLA YNMYDAYGNW FNGLKPLIQN
SMRTIMKANP ALYVLRERIR KGLQIYQSSV QEPFLNSSNY AELFNNDIKL FVDDTNVYRV
TVHKTFEGNV ATKAINGCIF TLNPKTGHLF LKIIHTSVWA GQKRLSQLAK WKTAEEVSAL
VRSLPKEEQP KQIIVTRKAM LDPLEVHMLD FPNIAIRPTE LRLPFSAAMS IDKLSDVVMK
ATEPQMVLFN IYDDWLDRIS SYTAFSRLTL LLRALKTNEE SAKMILLSDP TITIKSYHLW
PSFTDEQWIT IESQMRDLIL TEYGRKYNVN ISALTQTEIK DIILGQNIKA PSVKRQKMAE
LEAARSEKQN DEEAAGASTV MKTKTINAQG EEIVVVASAD YESQTFSSKN EWRKSAIANT
LLYLRLKNIY VSADDFVEEQ NVYVLPKNLL KKFIEISDVK IQVAAFIYGM SAKDHPKVKE
IKTVVLVPQL GHVGSVQISN IPDIGDLPDT EGLELLGWIH TQTEELKFMA ASEVATHSKL
FADKKRDCID ISIFSTPGSV SLSAYNLTDE GYQWGEENKD IMNVLSEGFE PTFSTHAQLL
LSDRITGNFI IPSGNVWNYT FMGTAFNQEG DYNFKYGIPL EFYNEMHRPV HFLQFSELAG
DEELEAEQID VFS


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