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Poly(A) RNA polymerase protein 2 (EC 2.7.7.-) (DNA polymerase kappa) (DNA polymerase sigma) (Topoisomerase 1-related protein TRF4)

 PAP2_YEAST              Reviewed;         584 AA.
P53632; D6W1V2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
28-MAR-2018, entry version 155.
RecName: Full=Poly(A) RNA polymerase protein 2;
EC=2.7.7.-;
AltName: Full=DNA polymerase kappa;
AltName: Full=DNA polymerase sigma;
AltName: Full=Topoisomerase 1-related protein TRF4;
Name=PAP2; Synonyms=TRF4; OrderedLocusNames=YOL115W;
ORFNames=HRC584, O0716;
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], AND FUNCTION.
PubMed=8647385;
Sadoff B.U., Heath-Pagliuso S., Castano I.B., Zhu Y., Kieff F.S.,
Christman M.F.;
"Isolation of mutants of Saccharomyces cerevisiae requiring DNA
topoisomerase I.";
Genetics 141:465-479(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7502582; DOI=10.1002/yea.320111108;
Vandenbol M., Durand P., Portetelle D., Hilger F.;
"Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV
including the Ty1-H3 retrotransposon, the suf1(+) frameshift
suppressor gene for tRNA-Gly, the yeast transfer RNA-Thr-1a and a
delta element.";
Yeast 11:1069-1075(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
FUNCTION.
PubMed=8895658; DOI=10.1101/gad.10.20.2564;
Castano I.B., Brzoska P.M., Sadoff B.U., Chen H., Christman M.F.;
"Mitotic chromosome condensation in the rDNA requires TRF4 and DNA
topoisomerase I in Saccharomyces cerevisiae.";
Genes Dev. 10:2564-2576(1996).
[7]
FUNCTION.
PubMed=8710513; DOI=10.1093/nar/24.12.2404;
Castano I.B., Heath-Pagliuso S., Sadoff B.U., Fitzhugh D.J.,
Christman M.F.;
"A novel family of TRF (DNA topoisomerase I-related function) genes
required for proper nuclear segregation.";
Nucleic Acids Res. 24:2404-2410(1996).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10066793; DOI=10.1074/jbc.274.11.7302;
Walowsky C., Fitzhugh D.J., Castano I.B., Ju J.Y., Levin N.A.,
Christman M.F.;
"The topoisomerase-related function gene TRF4 affects cellular
sensitivity to the antitumor agent camptothecin.";
J. Biol. Chem. 274:7302-7308(1999).
[9]
FUNCTION, AND MUTAGENESIS OF 236-ASP--ASP-238.
PubMed=10926539; DOI=10.1126/science.289.5480.774;
Wang Z., Castano I.B., De Las Penas A., Adams C., Christman M.F.;
"Pol kappa: a DNA polymerase required for sister chromatid cohesion.";
Science 289:774-779(2000).
[10]
NOMENCLATURE.
PubMed=11579108; DOI=10.1074/jbc.R100056200;
Burgers P.M.J., Koonin E.V., Bruford E., Blanco L., Burtis K.C.,
Christman M.F., Copeland W.C., Friedberg E.C., Hanaoka F.,
Hinkle D.C., Lawrence C.W., Nakanishi M., Ohmori H., Prakash L.,
Prakash S., Reynaud C.-A., Sugino A., Todo T., Wang Z., Weill J.-C.,
Woodgate R.;
"Eukaryotic DNA polymerases: proposal for a revised nomenclature.";
J. Biol. Chem. 276:43487-43490(2001).
[11]
FUNCTION.
PubMed=12062100; DOI=10.1016/S0092-8674(02)00753-5;
Saitoh S., Chabes A., McDonald W.H., Thelander L., Yates J.R. III,
Russell P.;
"Cid13 is a cytoplasmic poly(A) polymerase that regulates
ribonucleotide reductase mRNA.";
Cell 109:563-573(2002).
[12]
FUNCTION, AND MUTAGENESIS OF 131-GLU--GLU-133; 140-GLU--GLU-142;
182-GLU--ASP-185; 194-ARG--GLU-198; 217-ASP--ASP-219; 224-GLU-SER-225;
236-ASP--ASP-238; 275-LYS--ARG-277; 282-LYS--GLU-285; 309-ARG-GLU-310;
332-ARG-ARG-333; 378-GLU--GLU-381; 425-ASP--GLU-429; 444-LYS-LYS-445;
467-LYS--ARG-469; 486-ARG--ASP-490; 491-GLU-ARG-492; 502-GLU--GLU-504;
508-LYS--ARG-510; 559-LYS-ARG-560 AND 572-GLU--ASP-574.
PubMed=11861546;
Wang Z., Castano I.B., Adams C., Vu C., Fitzhugh D.J., Christman M.F.;
"Structure/function analysis of the Saccharomyces cerevisiae Trf4/Pol
sigma DNA polymerase.";
Genetics 160:381-391(2002).
[13]
FUNCTION, AND INTERACTION WITH POL2.
PubMed=12665575; DOI=10.1128/MCB.23.8.2733-2748.2003;
Edwards S., Li C.M., Levy D.L., Brown J., Snow P.M., Campbell J.L.;
"Saccharomyces cerevisiae DNA polymerase epsilon and polymerase sigma
interact physically and functionally, suggesting a role for polymerase
epsilon in sister chromatid cohesion.";
Mol. Cell. Biol. 23:2733-2748(2003).
[14]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[15]
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).
[16]
FUNCTION.
PubMed=15145828; DOI=10.1101/gad.1183804;
Kadaba S., Krueger A., Trice T., Krecic A.M., Hinnebusch A.G.,
Anderson J.T.;
"Nuclear surveillance and degradation of hypomodified initiator
tRNAMet in S. cerevisiae.";
Genes Dev. 18:1227-1240(2004).
[17]
IDENTIFICATION IN TRAMP COMPLEX, AND FUNCTION OF THE TRAMP COMPLEX.
PubMed=15935758; DOI=10.1016/j.cell.2005.04.029;
LaCava J., Houseley J., Saveanu C., Petfalski E., Thompson E.,
Jacquier A., Tollervey D.;
"RNA degradation by the exosome is promoted by a nuclear
polyadenylation complex.";
Cell 121:713-724(2005).
[18]
IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND FUNCTION OF THE TRF4 COMPLEX.
PubMed=15935759; DOI=10.1016/j.cell.2005.04.030;
Wyers F., Rougemaille M., Badis G., Rousselle J.-C., Dufour M.-E.,
Boulay J., Regnault B., Devaux F., Namane A., Seraphin B., Libri D.,
Jacquier A.;
"Cryptic pol II transcripts are degraded by a nuclear quality control
pathway involving a new poly(A) polymerase.";
Cell 121:725-737(2005).
[19]
FUNCTION.
PubMed=16260630; DOI=10.1128/MCB.25.22.10183-10189.2005;
Haracska L., Johnson R.E., Prakash L., Prakash S.;
"Trf4 and Trf5 proteins of Saccharomyces cerevisiae exhibit poly(A)
RNA polymerase activity but no DNA polymerase activity.";
Mol. Cell. Biol. 25:10183-10189(2005).
[20]
IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND FUNCTION OF THE TRF4 COMPLEX.
PubMed=15828860; DOI=10.1371/journal.pbio.0030189;
Vanacova S., Wolf J., Martin G., Blank D., Dettwiler S., Friedlein A.,
Langen H., Keith G., Keller W.;
"A new yeast poly(A) polymerase complex involved in RNA quality
control.";
PLoS Biol. 3:986-997(2005).
[21]
FUNCTION.
PubMed=16373491; DOI=10.1261/rna.2207206;
Egecioglu D.E., Henras A.K., Chanfreau G.F.;
"Contributions of Trf4p- and Trf5p-dependent polyadenylation to the
processing and degradative functions of the yeast nuclear exosome.";
RNA 12:26-32(2006).
[22]
FUNCTION, AND MUTAGENESIS OF 236-ASP--ASP-238.
PubMed=16431988; DOI=10.1261/rna.2305406;
Kadaba S., Wang X., Anderson J.T.;
"Nuclear RNA surveillance in Saccharomyces cerevisiae: Trf4p-dependent
polyadenylation of nascent hypomethylated tRNA and an aberrant form of
5S rRNA.";
RNA 12:508-521(2006).
[23]
FUNCTION.
PubMed=17179095; DOI=10.1534/genetics.106.065987;
Reis C.C., Campbell J.L.;
"Contribution of Trf4/5 and the nuclear exosome to genome stability
through regulation of histone mRNA levels in Saccharomyces
cerevisiae.";
Genetics 175:993-1010(2007).
[24]
INTERACTION WITH NOP53.
PubMed=18631361; DOI=10.1111/j.1742-4658.2008.06565.x;
Granato D.C., Machado-Santelli G.M., Oliveira C.C.;
"Nop53p interacts with 5.8S rRNA co-transcriptionally, and regulates
processing of pre-rRNA by the exosome.";
FEBS J. 275:4164-4178(2008).
[25]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 161-481 IN COMPLEX WITH AIR2,
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH AIR2.
PubMed=20696927; DOI=10.1073/pnas.1003505107;
Hamill S., Wolin S.L., Reinisch K.M.;
"Structure and function of the polymerase core of TRAMP, a RNA
surveillance complex.";
Proc. Natl. Acad. Sci. U.S.A. 107:15045-15050(2010).
-!- FUNCTION: Catalytic subunit of the TRAMP complex which has a
poly(A) RNA polymerase activity and is involved in a post-
transcriptional quality control mechanism limiting inappropriate
expression of genetic information. Polyadenylation is required for
the degradative activity of the exosome on several of its nuclear
RNA substrates like cryptic transcripts generated by RNA
polymerase II and III, or hypomethylated pre-tRNAi-Met.
Polyadenylates RNA processing and degradation intermediates of
snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a
functional exosome. TRF4 is also required for proper nuclear
division in mitosis, DNA damage repair and sister chromatid
cohesion. Involved in the regulation of histone mRNA levels. May
mediate mitotic chromosome condensation.
{ECO:0000269|PubMed:10066793, ECO:0000269|PubMed:10926539,
ECO:0000269|PubMed:11861546, ECO:0000269|PubMed:12062100,
ECO:0000269|PubMed:12665575, ECO:0000269|PubMed:15145828,
ECO:0000269|PubMed:15828860, ECO:0000269|PubMed:15935758,
ECO:0000269|PubMed:15935759, ECO:0000269|PubMed:16260630,
ECO:0000269|PubMed:16373491, ECO:0000269|PubMed:16431988,
ECO:0000269|PubMed:17179095, ECO:0000269|PubMed:20696927,
ECO:0000269|PubMed:8647385, ECO:0000269|PubMed:8710513,
ECO:0000269|PubMed:8895658}.
-!- CATALYTIC ACTIVITY: ATP + RNA(n) = diphosphate + RNA(n+1).
{ECO:0000269|PubMed:20696927}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Component of the TRAMP complex (also called TRF4 complex)
composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or
AIR2. Interacts with NOP53 and POL2. Interacts directly with AIR2.
{ECO:0000269|PubMed:12665575, ECO:0000269|PubMed:15828860,
ECO:0000269|PubMed:15935758, ECO:0000269|PubMed:15935759,
ECO:0000269|PubMed:18631361, ECO:0000269|PubMed:20696927}.
-!- INTERACTION:
P40507:AIR1; NbExp=8; IntAct=EBI-19517, EBI-25083;
Q12476:AIR2; NbExp=22; IntAct=EBI-19517, EBI-31475;
P47047:MTR4; NbExp=26; IntAct=EBI-19517, EBI-11592;
P53131:PRP43; NbExp=2; IntAct=EBI-19517, EBI-505;
P0CS90:SSC1; NbExp=2; IntAct=EBI-19517, EBI-8637;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10066793,
ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 7550 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
-!- CAUTION: Was originally thought to have DNA polymerase activity.
{ECO:0000305}.
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EMBL; U31355; AAC49091.1; -; Genomic_DNA.
EMBL; Z48149; CAA88145.1; -; Genomic_DNA.
EMBL; Z74857; CAA99134.1; -; Genomic_DNA.
EMBL; AY723865; AAU09782.1; -; Genomic_DNA.
EMBL; BK006948; DAA10668.1; -; Genomic_DNA.
PIR; S51882; S51882.
RefSeq; NP_014526.1; NM_001183369.1.
PDB; 2MOW; NMR; -; B=573-584.
PDB; 3NYB; X-ray; 2.70 A; A=161-481.
PDB; 4U4C; X-ray; 2.40 A; B=111-160.
PDBsum; 2MOW; -.
PDBsum; 3NYB; -.
PDBsum; 4U4C; -.
ProteinModelPortal; P53632; -.
SMR; P53632; -.
BioGrid; 34285; 419.
DIP; DIP-4214N; -.
IntAct; P53632; 49.
MINT; P53632; -.
STRING; 4932.YOL115W; -.
iPTMnet; P53632; -.
MaxQB; P53632; -.
PaxDb; P53632; -.
PRIDE; P53632; -.
EnsemblFungi; YOL115W; YOL115W; YOL115W.
GeneID; 854034; -.
KEGG; sce:YOL115W; -.
EuPathDB; FungiDB:YOL115W; -.
SGD; S000005475; PAP2.
GeneTree; ENSGT00400000022055; -.
HOGENOM; HOG000246586; -.
InParanoid; P53632; -.
KO; K03514; -.
OMA; RKQYEMR; -.
OrthoDB; EOG092C144L; -.
BioCyc; YEAST:G3O-33512-MONOMER; -.
BRENDA; 4.2.99.B1; 984.
EvolutionaryTrace; P53632; -.
PRO; PR:P53632; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005730; C:nucleolus; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0031499; C:TRAMP complex; IDA:SGD.
GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB.
GO; GO:0006284; P:base-excision repair; IMP:SGD.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071044; P:histone mRNA catabolic process; IGI:SGD.
GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:SGD.
GO; GO:0043629; P:ncRNA polyadenylation; IDA:UniProtKB.
GO; GO:0045910; P:negative regulation of DNA recombination; IMP:SGD.
GO; GO:0071031; P:nuclear mRNA surveillance of mRNA 3'-end processing; IGI:SGD.
GO; GO:0071040; P:nuclear polyadenylation-dependent antisense transcript catabolic process; IMP:SGD.
GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IMP:SGD.
GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IGI:SGD.
GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IMP:SGD.
GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IMP:SGD.
GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
GO; GO:0071047; P:polyadenylation-dependent mRNA catabolic process; IMP:SGD.
GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IGI:SGD.
GO; GO:0071050; P:snoRNA polyadenylation; IGI:SGD.
GO; GO:0006400; P:tRNA modification; IMP:SGD.
GO; GO:0034475; P:U4 snRNA 3'-end processing; IMP:SGD.
InterPro; IPR002058; PAP_assoc.
InterPro; IPR002934; Polymerase_NTP_transf_dom.
Pfam; PF01909; NTP_transf_2; 1.
Pfam; PF03828; PAP_assoc; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Complete proteome; Magnesium;
Manganese; Metal-binding; Mitosis; Nucleotidyltransferase; Nucleus;
Reference proteome; Transferase.
CHAIN 1 584 Poly(A) RNA polymerase protein 2.
/FTId=PRO_0000120314.
DOMAIN 371 431 PAP-associated.
METAL 236 236 Magnesium or manganese; catalytic.
{ECO:0000250}.
METAL 238 238 Magnesium or manganese; catalytic.
{ECO:0000250}.
MUTAGEN 131 133 EDE->AAA: In TRF4-131; slow growth.
{ECO:0000269|PubMed:11861546}.
MUTAGEN 140 142 ERE->AAA: In TRF4-140; slow growth.
{ECO:0000269|PubMed:11861546}.
MUTAGEN 182 185 EIKD->AIAA: In TRF4-182; lethal.
{ECO:0000269|PubMed:11861546}.
MUTAGEN 194 194 R->A: In TRF4-194; lethal; when
associated with A-195; A-196 and A-198.
MUTAGEN 195 198 EEIE->AIAA: In TRF4-194; lethal.
MUTAGEN 217 219 DAD->AAA: In TRF4-217; slow growth.
{ECO:0000269|PubMed:11861546}.
MUTAGEN 224 225 GS->AA: In TRF4-224; lethal.
{ECO:0000269|PubMed:11861546}.
MUTAGEN 236 238 DID->AIA: In TRF4-236; lethal.
{ECO:0000269|PubMed:10926539,
ECO:0000269|PubMed:11861546,
ECO:0000269|PubMed:16431988}.
MUTAGEN 275 277 KAR->AAA: In TRF4-275; temperature
sensitive. {ECO:0000269|PubMed:11861546}.
MUTAGEN 282 282 K->A: In TRF4-282; lethal; when
associated with A-285.
MUTAGEN 285 285 E->A: In TRF4-282; lethal; when
associated with A-282.
MUTAGEN 309 310 RE->AA: In TRF4-309; lethal.
{ECO:0000269|PubMed:11861546}.
MUTAGEN 332 333 RR->AA: In TRF4-332; temperature
sensitive. {ECO:0000269|PubMed:11861546}.
MUTAGEN 378 378 E->A: In TRF4-378; lethal; when
associated with A-381.
MUTAGEN 381 381 E->A: In TRF4-378; lethal; when
associated with A-378.
MUTAGEN 425 425 D->A: In TRF4-425; lethal; when
associated with A-428 and A-429.
MUTAGEN 428 429 DE->AA: In TRF4-425; lethal; when
associated with A-425.
MUTAGEN 444 445 KK->AA: In TRF4-444; lethal.
{ECO:0000269|PubMed:11861546}.
MUTAGEN 467 469 KDR->AAA: In TRF4-467; temperature
sensitive. {ECO:0000269|PubMed:11861546}.
MUTAGEN 486 487 RD->AA: In TRF4-486; lethal.
MUTAGEN 490 492 DER->AAA: In TRF4-486; lethal.
MUTAGEN 502 502 E->A: In TRF4-502; lethal; when
associated with A-504.
MUTAGEN 504 504 E->A: In TRF4-502; lethal; when
associated with A-502.
MUTAGEN 508 510 KKR->AAA: In TRF4-508; lethal.
{ECO:0000269|PubMed:11861546}.
MUTAGEN 559 560 KR->AA: In TRF4-559; slow growth.
{ECO:0000269|PubMed:11861546}.
MUTAGEN 560 560 R->A: In TRF4-559; slow growth; when
associated with A-559.
MUTAGEN 572 574 EDD->AAA: In TRF4-572; slow growth.
{ECO:0000269|PubMed:11861546}.
STRAND 122 125 {ECO:0000244|PDB:4U4C}.
HELIX 162 164 {ECO:0000244|PDB:3NYB}.
HELIX 175 189 {ECO:0000244|PDB:3NYB}.
HELIX 194 212 {ECO:0000244|PDB:3NYB}.
STRAND 220 224 {ECO:0000244|PDB:3NYB}.
TURN 225 229 {ECO:0000244|PDB:3NYB}.
STRAND 237 241 {ECO:0000244|PDB:3NYB}.
HELIX 247 249 {ECO:0000244|PDB:3NYB}.
HELIX 250 263 {ECO:0000244|PDB:3NYB}.
STRAND 271 277 {ECO:0000244|PDB:3NYB}.
STRAND 279 285 {ECO:0000244|PDB:3NYB}.
TURN 286 289 {ECO:0000244|PDB:3NYB}.
STRAND 290 297 {ECO:0000244|PDB:3NYB}.
HELIX 303 313 {ECO:0000244|PDB:3NYB}.
HELIX 318 331 {ECO:0000244|PDB:3NYB}.
HELIX 337 339 {ECO:0000244|PDB:3NYB}.
HELIX 344 356 {ECO:0000244|PDB:3NYB}.
HELIX 359 362 {ECO:0000244|PDB:3NYB}.
HELIX 368 370 {ECO:0000244|PDB:3NYB}.
HELIX 372 385 {ECO:0000244|PDB:3NYB}.
TURN 389 391 {ECO:0000244|PDB:3NYB}.
STRAND 392 399 {ECO:0000244|PDB:3NYB}.
STRAND 401 405 {ECO:0000244|PDB:3NYB}.
HELIX 406 408 {ECO:0000244|PDB:3NYB}.
HELIX 410 412 {ECO:0000244|PDB:3NYB}.
STRAND 418 420 {ECO:0000244|PDB:3NYB}.
STRAND 423 425 {ECO:0000244|PDB:3NYB}.
STRAND 428 432 {ECO:0000244|PDB:3NYB}.
TURN 433 436 {ECO:0000244|PDB:3NYB}.
HELIX 440 462 {ECO:0000244|PDB:3NYB}.
HELIX 466 469 {ECO:0000244|PDB:3NYB}.
TURN 476 478 {ECO:0000244|PDB:3NYB}.
SEQUENCE 584 AA; 66031 MW; 8A58B29E4BFDC022 CRC64;
MGAKSVTASS SKKIKNRHNG KVKKSKKIKK VRKPQKSISL NDENEVEILP SRNEQETNKL
PKDHVTADGI LVLEHKSDDD EGFDVYDGHF DNPTDIPSTT EESKTPSLAV HGDEKDLANN
DDFISLSASS EDEQAEQEEE REKQELEIKK EKQKEILNTD YPWILNHDHS KQKEISDWLT
FEIKDFVAYI SPSREEIEIR NQTISTIREA VKQLWPDADL HVFGSYSTDL YLPGSDIDCV
VTSELGGKES RNNLYSLASH LKKKNLATEV EVVAKARVPI IKFVEPHSGI HIDVSFERTN
GIEAAKLIRE WLDDTPGLRE LVLIVKQFLH ARRLNNVHTG GLGGFSIICL VFSFLHMHPR
IITNEIDPKD NLGVLLIEFF ELYGKNFGYD DVALGSSDGY PVYFPKSTWS AIQPIKNPFS
LAIQDPGDES NNISRGSFNI RDIKKAFAGA FDLLTNRCFE LHSATFKDRL GKSILGNVIK
YRGKARDFKD ERGLVLNKAI IENENYHKKR SRIIHDEDFA EDTVTSTATA TTTDDDYEIT
NPPAKKAKIE EKPESEPAKR NSGETYITVS SEDDDEDGYN PYTL


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