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Protein URA2 [Includes: Glutamine-dependent carbamoyl-phosphate synthase (EC 6.3.5.5); Aspartate carbamoyltransferase (EC 2.1.3.2)]

 PYR1_YEAST              Reviewed;        2214 AA.
P07259; A2TBN0; D6VW55; Q06HN1;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
21-SEP-2011, sequence version 5.
25-APR-2018, entry version 211.
RecName: Full=Protein URA2;
Includes:
RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
EC=6.3.5.5;
Includes:
RecName: Full=Aspartate carbamoyltransferase;
EC=2.1.3.2;
Name=URA2; OrderedLocusNames=YJL130C; ORFNames=J0686;
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].
STRAIN=ATCC 28383 / FL100 / VTT C-80102;
PubMed=2570735; DOI=10.1016/0378-1119(89)90092-9;
Souciet J.-L., Nagy M., le Gouar M., Lacroute F., Potier S.;
"Organization of the yeast URA2 gene: identification of a defective
dihydroorotase-like domain in the multifunctional carbamoylphosphate
synthetase-aspartate transcarbamylase complex.";
Gene 79:59-70(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269;
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
X.";
EMBO J. 15:2031-2049(1996).
[3]
GENOME REANNOTATION, AND SEQUENCE REVISION TO 123.
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-510.
STRAIN=ATCC 28383 / FL100 / VTT C-80102;
PubMed=3039294; DOI=10.1007/BF00331595;
Souciet J.-L., Potier S., Hubert J.-C., Lacroute F.;
"Nucleotide sequence of the pyrimidine specific carbamoyl phosphate
synthetase, a part of the yeast multifunctional protein encoded by the
URA2 gene.";
Mol. Gen. Genet. 207:314-319(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-276.
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8948101;
DOI=10.1002/(SICI)1097-0061(199611)12:14<1471::AID-YEA30>3.0.CO;2-4;
Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
"Sequencing analysis of a 40.2 kb fragment of yeast chromosome X
reveals 19 open reading frames including URA2 (5' end), TRK1, PBS2,
SPT10, GCD14, RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes,
three remnant delta elements and a Ty4 transposon.";
Yeast 12:1471-1474(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-119.
STRAIN=ATCC 201390 / BY4743;
PubMed=17351133; DOI=10.1101/gr.6049107;
Zhang Z., Hesselberth J.R., Fields S.;
"Genome-wide identification of spliced introns using a tiling
microarray.";
Genome Res. 17:503-509(2007).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-117.
STRAIN=ATCC 201390 / BY4743;
PubMed=17244705; DOI=10.1073/pnas.0610354104;
Juneau K., Palm C., Miranda M., Davis R.W.;
"High-density yeast-tiling array reveals previously undiscovered
introns and extensive regulation of meiotic splicing.";
Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-2214.
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8813765;
DOI=10.1002/(SICI)1097-0061(19960630)12:8<787::AID-YEA954>3.3.CO;2-W;
Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
"Sequence analysis of a 40.7 kb segment from the left arm of yeast
chromosome X reveals 14 known genes and 13 new open reading frames
including homologues of genes clustered on the right arm of chromosome
XI.";
Yeast 12:787-797(1996).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 838-877.
PubMed=9150260; DOI=10.1007/s004380050415;
Akada R., Yamamoto J., Yamashita I.;
"Screening and identification of yeast sequences that cause growth
inhibition when overexpressed.";
Mol. Gen. Genet. 254:267-274(1997).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1268-2214.
PubMed=2498313;
Nagy M., le Gouar M., Potier S., Souciet J.-L., Herve G.;
"The primary structure of the aspartate transcarbamylase region of the
URA2 gene product in Saccharomyces cerevisiae. Features involved in
activity and nuclear localization.";
J. Biol. Chem. 264:8366-8374(1989).
[11]
PROTEIN SEQUENCE OF 1855-1874, AND PHOSPHORYLATION AT SER-1857.
PubMed=1977585; DOI=10.1111/j.1432-1033.1990.tb19376.x;
Denis-Duphil M., Lecaer J.-P., Hardie D.G., Carrey E.A.;
"Yeast carbamoyl-phosphate-synthetase--aspartate-transcarbamylase
multidomain protein is phosphorylated in vitro by cAMP-dependent
protein kinase.";
Eur. J. Biochem. 193:581-587(1990).
[12]
SUBCELLULAR LOCATION.
PubMed=11015727;
DOI=10.1002/1097-0061(200010)16:14<1299::AID-YEA593>3.0.CO;2-6;
Benoist P., Feau P., Pliss A., Vorisek J., Antonelli R., Raska I.,
Denis-Duphil M.;
"The yeast Ura2 protein that catalyses the first two steps of
pyrimidines biosynthesis accumulates not in the nucleus but in the
cytoplasm, as shown by immunocytochemistry and Ura2-green fluorescent
protein mapping.";
Yeast 16:1299-1312(2000).
[13]
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).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1853, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: This protein is a "fusion" protein encoding three
enzymatic activities of the pyrimidine pathway (GATase, CPSase,
and ATCase).
-!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
ADP + phosphate + L-glutamate + carbamoyl phosphate.
-!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate
+ N-carbamoyl-L-aspartate.
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
-!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
-!- INTERACTION:
P03965:CPA2; NbExp=2; IntAct=EBI-14372, EBI-4034;
P53691:CPR6; NbExp=12; IntAct=EBI-14372, EBI-5429;
P32902:MRP4; NbExp=4; IntAct=EBI-14372, EBI-16248;
P10591:SSA1; NbExp=3; IntAct=EBI-14372, EBI-8591;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11015727,
ECO:0000269|PubMed:14562095}.
-!- DOMAIN: The DHOase domain is defective.
-!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
(carbamoyl phosphate synthase) form together the glutamine-
dependent CPSase (GD-CPSase) (EC 6.3.5.5).
-!- MISCELLANEOUS: In eukaryotes EC 6.3.5.5 is synthesized by two
pathway-specific (arginine and pyrimidine) genes under separate
control.
-!- MISCELLANEOUS: Present with 11000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: In the central section; belongs to the metallo-
dependent hydrolases superfamily. DHOase family. CAD subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABI95879.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; M27174; AAA68280.1; -; Genomic_DNA.
EMBL; Z49405; CAA89425.1; -; Genomic_DNA.
EMBL; X05553; CAA29068.1; -; Genomic_DNA.
EMBL; DQ881452; ABI95879.1; ALT_INIT; mRNA.
EMBL; EF123133; ABM97477.1; -; mRNA.
EMBL; X87371; CAA60825.1; -; Genomic_DNA.
EMBL; D28139; BAA05680.1; -; Genomic_DNA.
EMBL; J04711; AAA35198.1; -; Genomic_DNA.
EMBL; BK006943; DAA08671.2; -; Genomic_DNA.
PIR; S56911; QZBYU2.
RefSeq; NP_012405.2; NM_001181563.2.
SMR; P07259; -.
BioGrid; 33626; 169.
DIP; DIP-7215N; -.
IntAct; P07259; 483.
MINT; P07259; -.
STRING; 4932.YJL130C; -.
MEROPS; C26.956; -.
CarbonylDB; P07259; -.
iPTMnet; P07259; -.
MaxQB; P07259; -.
PaxDb; P07259; -.
PRIDE; P07259; -.
EnsemblFungi; YJL130C; YJL130C; YJL130C.
GeneID; 853311; -.
KEGG; sce:YJL130C; -.
EuPathDB; FungiDB:YJL130C; -.
SGD; S000003666; URA2.
GeneTree; ENSGT00910000145257; -.
HOGENOM; HOG000234584; -.
InParanoid; P07259; -.
KO; K11541; -.
OMA; NIPCTSM; -.
OrthoDB; EOG092C0957; -.
BioCyc; MetaCyc:YJL130C-MONOMER; -.
BioCyc; YEAST:YJL130C-MONOMER; -.
BRENDA; 6.3.5.5; 984.
Reactome; R-SCE-70635; Urea cycle.
UniPathway; UPA00070; UER00115.
UniPathway; UPA00070; UER00116.
PRO; PR:P07259; -.
Proteomes; UP000002311; Chromosome X.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IDA:SGD.
GO; GO:0016597; F:amino acid binding; IEA:InterPro.
GO; GO:0004070; F:aspartate carbamoyltransferase activity; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IBA:GO_Central.
GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:InterPro.
GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IDA:SGD.
GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
GO; GO:0006541; P:glutamine metabolic process; IDA:SGD.
GO; GO:0045984; P:negative regulation of pyrimidine nucleobase metabolic process; IDA:SGD.
GO; GO:0000050; P:urea cycle; IBA:GO_Central.
CDD; cd01744; GATase1_CPSase; 1.
Gene3D; 1.10.1030.10; -; 1.
Gene3D; 3.30.1490.20; -; 1.
Gene3D; 3.40.50.1370; -; 3.
Gene3D; 3.40.50.1380; -; 1.
Gene3D; 3.40.50.880; -; 1.
Gene3D; 3.50.30.20; -; 1.
HAMAP; MF_00001; Asp_carb_tr; 1.
HAMAP; MF_01209; CPSase_S_chain; 1.
InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
InterPro; IPR002082; Asp_carbamoyltransf.
InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR006275; CarbamoylP_synth_lsu.
InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
InterPro; IPR006274; CarbamoylP_synth_ssu.
InterPro; IPR002474; CarbamoylP_synth_ssu_N.
InterPro; IPR036480; CarbP_synth_ssu_N_sf.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR035686; CPSase_GATase1.
InterPro; IPR017926; GATASE.
InterPro; IPR032466; Metal_Hydrolase.
InterPro; IPR011607; MGS-like_dom.
InterPro; IPR036914; MGS-like_dom_sf.
InterPro; IPR016185; PreATP-grasp_dom_sf.
Pfam; PF02786; CPSase_L_D2; 2.
Pfam; PF02787; CPSase_L_D3; 1.
Pfam; PF00988; CPSase_sm_chain; 1.
Pfam; PF00117; GATase; 1.
Pfam; PF02142; MGS; 1.
Pfam; PF00185; OTCace; 1.
Pfam; PF02729; OTCace_N; 1.
PRINTS; PR00100; AOTCASE.
PRINTS; PR00101; ATCASE.
PRINTS; PR00098; CPSASE.
SMART; SM01096; CPSase_L_D3; 1.
SMART; SM01097; CPSase_sm_chain; 1.
SMART; SM00851; MGS; 1.
SUPFAM; SSF48108; SSF48108; 1.
SUPFAM; SSF51556; SSF51556; 1.
SUPFAM; SSF52021; SSF52021; 1.
SUPFAM; SSF52317; SSF52317; 1.
SUPFAM; SSF52335; SSF52335; 1.
SUPFAM; SSF52440; SSF52440; 2.
SUPFAM; SSF53671; SSF53671; 1.
TIGRFAMs; TIGR00670; asp_carb_tr; 1.
TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
PROSITE; PS50975; ATP_GRASP; 2.
PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PROSITE; PS00866; CPSASE_1; 2.
PROSITE; PS00867; CPSASE_2; 2.
PROSITE; PS51273; GATASE_TYPE_1; 1.
PROSITE; PS51855; MGS; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Ligase;
Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
Pyrimidine biosynthesis; Reference proteome; Repeat; Transferase;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 2214 Protein URA2.
/FTId=PRO_0000199511.
DOMAIN 228 413 Glutamine amidotransferase type-1.
DOMAIN 562 754 ATP-grasp 1.
DOMAIN 1099 1290 ATP-grasp 2.
DOMAIN 1356 1508 MGS-like. {ECO:0000255|PROSITE-
ProRule:PRU01202}.
REGION 2 400 GATase (Glutamine amidotransferase).
REGION 401 440 Linker.
REGION 441 1482 CPSase (Carbamoyl-phosphate synthase).
REGION 1483 1492 Linker.
REGION 1493 1821 Defective DHOase domain.
REGION 1822 1909 Linker.
REGION 1910 2214 ATCase (Aspartate transcarbamylase).
ACT_SITE 302 302 For GATase activity. {ECO:0000250}.
ACT_SITE 386 386 For GATase activity. {ECO:0000250}.
ACT_SITE 388 388 For GATase activity. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 1857 1857 Phosphoserine; by PKA.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:1977585}.
CROSSLNK 1853 1853 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CONFLICT 86 86 H -> D (in Ref. 4; CAA29068).
{ECO:0000305}.
CONFLICT 123 123 A -> R (in Ref. 2; CAA89425).
{ECO:0000305}.
CONFLICT 250 257 ELKVVPWN -> RIESCSMD (in Ref. 4;
CAA29068). {ECO:0000305}.
CONFLICT 270 270 I -> Y (in Ref. 4; CAA29068).
{ECO:0000305}.
CONFLICT 313 314 GA -> VQ (in Ref. 4; CAA29068).
{ECO:0000305}.
CONFLICT 372 373 GI -> RF (in Ref. 4; CAA29068).
{ECO:0000305}.
CONFLICT 394 402 RDTEFLFDV -> EIQNSCLT (in Ref. 4;
CAA29068). {ECO:0000305}.
CONFLICT 431 433 KAH -> QGT (in Ref. 4; CAA29068).
{ECO:0000305}.
CONFLICT 482 482 I -> T (in Ref. 4; CAA29068).
{ECO:0000305}.
CONFLICT 485 485 I -> N (in Ref. 4; CAA29068).
{ECO:0000305}.
CONFLICT 492 492 A -> G (in Ref. 4; CAA29068).
{ECO:0000305}.
CONFLICT 501 510 TAEFVRKVIL -> NAAKQRDVDR (in Ref. 4;
CAA29068). {ECO:0000305}.
CONFLICT 1411 1412 EV -> S (in Ref. 10; AAA35198).
{ECO:0000305}.
CONFLICT 1582 1582 I -> M (in Ref. 10; AAA35198).
{ECO:0000305}.
CONFLICT 1588 1588 N -> K (in Ref. 10; AAA35198).
{ECO:0000305}.
CONFLICT 1592 1592 V -> G (in Ref. 10; AAA35198).
{ECO:0000305}.
CONFLICT 1595 1595 S -> A (in Ref. 10; AAA35198).
{ECO:0000305}.
CONFLICT 1872 1872 Missing (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 1937 1937 A -> R (in Ref. 1; AAA68280 and 10;
AAA35198). {ECO:0000305}.
CONFLICT 1997 1997 T -> I (in Ref. 10; AAA35198).
{ECO:0000305}.
CONFLICT 2039 2039 H -> L (in Ref. 10; AAA35198).
{ECO:0000305}.
CONFLICT 2158 2165 KILAHAKE -> VRSWHTQQK (in Ref. 10;
AAA35198). {ECO:0000305}.
SEQUENCE 2214 AA; 245041 MW; D5A47F4E42A9B1A7 CRC64;
MATIAPTAPI TPPMESTGDR LVTLELKDGT VLQGYSFGAE KSVAGELVFQ TGMVGYPESV
TDPSYEGQIL VITYPLVGNY GVPDMHLRDE LVEELPRYFE SNRIHIAGLV ISHYTDEYSH
YLAKSSLGKW LQNEGIPAVY GVDTRSLTKH LRDAGSMLGR LSLEKSGSDR TISRSSSWRS
AFDVPEWVDP NVQNLVSKVS INEPKLYVPP ADNKHIELQT GPDGKVLRIL AIDVGMKYNQ
IRCFIKRGVE LKVVPWNYDF TKEDYDGLFI SNGPGDPSVL DDLSQRLSNV LEAKKTPVFG
ICLGHQLIAR AAGASTLKLK FGNRGHNIPC TSTISGRCYI TSQNHGFAVD VDTLTSGWKP
LFVNANDDSN EGIYHSELPY FSVQFHPEST PGPRDTEFLF DVFIQAVKEF KYTQVLKPIA
FPGGLLEDNV KAHPRIEAKK VLVLGSGGLS IGQAGEFDYS GSQAIKALKE EGIYTILINP
NIATIQTSKG LADKVYFVPV TAEFVRKVIL HERPDAIYVT FGGQTALSVG IAMKDEFEAL
GVKVLGTPID TIITTEDREL FSNAIDEINE KCAKSQAANS VDEALAAVKE IGFPVIVRAA
YALGGLGSGF ANNEKELVDL CNVAFSSSPQ VLVEKSMKGW KEVEYEVVRD AFDNCITVCN
MENFDPLGIH TGDSIVVAPS QTLSDEDYNM LRTTAVNVIR HLGVVGECNI QYALNPVSKD
YCIIEVNARL SRSSALASKA TGYPLAYTAA KLGLNIPLNE VKNSVTKSTC ACFEPSLDYC
VVKMPRWDLK KFTRVSTELS SSMKSVGEVM SIGRTFEEAI QKAIRSTEYA NLGFNETDLD
IDIDYELNNP TDMRVFAIAN AFAKKGYSVD KVWEMTRIDK WFLNKLHDLV QFAEKISSFG
TKEELPSLVL RQAKQLGFDD RQIARFLDSN EVAIRRLRKE YGITPFVKQI DTVAAEFPAY
TNYLYMTYNA DSHDLSFDDH GVMVLGSGVY RIGSSVEFDW CAVTAVRTLR ANNIKTIMVN
YNPETVSTDY DEADRLYFET INLERVLDIY EIENSSGVVV SMGGQTSNNI AMTLHRENVK
ILGTSPDMID SAENRYKFSR MLDQIGVDQP AWKELTSMDE AESFAEKVGY PVLVRPSYVL
SGAAMNTVYS KNDLESYLNQ AVEVSRDYPV VITKYIENAK EIEMDAVARN GELVMHVVSE
HVENAGVHSG DATLIVPPQD LAPETVDRIV VATAKIGKAL KITGPYNIQF IAKDNEIKVI
ECNVRASRSF PFISKVVGVN LIELATKAIM GLPLTPYPVE KLPDDYVAVK VPQFSFPRLA
GADPVLGVEM ASTGEVATFG HSKYEAYLKS LLATGFKLPK KNILLSIGSY KEKQELLSSV
QKLYNMGYKL FATSGTADFL SEHGIAVQYL EVLNKDDDDQ KSEYSLTQHL ANNEIDLYIN
LPSANRFRRP ASYVSKGYKT RRLAVDYSVP LVTNVKCAKL LIEAISRNIT LDVSERDAQT
SHRTITLPGL INIATYVPNA SHVIKGPAEL KETTRLFLES GFTYCQLMPR SISGPVITDV
ASLKAANSVS QDSSYTDFSF TIAGTAHNAH SVTQSASKVT ALFLPLRELK NKITAVAELL
NQWPTEKQVI AEAKTADLAS VLLLTSLQNR SIHITGVSNK EDLALIMTVK AKDPRVTCDV
NIYSLFIAQD DYPEAVFLPT KEDQEFFWNN LDSIDAFSVG ALPVALANVT GNKVDVGMGI
KDSLPLLLAA VEEGKLTIDD IVLRLHDNPA KIFNIPTQDS VVEIDLDYSF RRNKRWSPFN
KDMNGGIERV VYNGETLVLS GELVSPGAKG KCIVNPSPAS ITASAELQST SAKRRFSITE
EAIADNLDAA EDAIPEQPLE QKLMSSRPPR ELVAPGAIQN LIRSNNPFRG RHILSIKQFK
RSDFHVLFAV AQELRAAVAR EGVLDLMKGH VITTIFFEPS TRTCSSFIAA MERLGGRIVN
VNPLVSSVKK GETLQDTIRT LACYSDAIVM RHSEEMSVHI AAKYSPVPII NGGNGSREHP
TQAFLDLFTI REEIGTVNGI TVTFMGDLKH GRTVHSLCRL LMHYQVRINL VSPPELRLPE
GLREELRKAG LLGVESIELT PHIISKTDVL YCTRVQEERF NSPEEYARLK DTYIVDNKIL
AHAKENMAIM HPLPRVNEIK EEVDYDHRAA YFRQMKYGLF VRMALLAMVM GVDM


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