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Regulatory protein SWI6 (Cell-cycle box factor subunit SWI6) (MBF subunit P90) (Trans-acting activator of HO endonuclease gene)

 SWI6_YEAST              Reviewed;         803 AA.
P09959; D6VYI6;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
12-AUG-2020, entry version 207.
RecName: Full=Regulatory protein SWI6;
AltName: Full=Cell-cycle box factor subunit SWI6;
AltName: Full=MBF subunit P90;
AltName: Full=Trans-acting activator of HO endonuclease gene;
Name=SWI6; OrderedLocusNames=YLR182W; ORFNames=L9470.8;
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=2821408; DOI=10.1038/329651a0;
Breeden L., Nasmyth K.;
"Similarity between cell-cycle genes of budding yeast and fission yeast and
the Notch gene of Drosophila.";
Nature 329:651-654(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
Zollner A., Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
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).
[4]
CHARACTERIZATION.
PubMed=1608451; DOI=10.1038/357508a0;
Dirick L., Moll T., Auer H., Nasmyth K.;
"A central role for SWI6 in modulating cell cycle Start-specific
transcription in yeast.";
Nature 357:508-513(1992).
[5]
INTERACTION WITH STB1.
PubMed=10409718; DOI=10.1128/mcb.19.8.5267;
Ho Y., Costanzo M., Moore L., Kobayashi R., Andrews B.J.;
"Regulation of transcription at the Saccharomyces cerevisiae start
transition by Stb1, a Swi6-binding protein.";
Mol. Cell. Biol. 19:5267-5278(1999).
[6]
NUCLEOCYTOPLASMIC SHUTTLING.
PubMed=12697814; DOI=10.1128/mcb.23.9.3126-3140.2003;
Queralt E., Igual J.C.;
"Cell cycle activation of the Swi6p transcription factor is linked to
nucleocytoplasmic shuttling.";
Mol. Cell. Biol. 23:3126-3140(2003).
[7]
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).
[8]
PHOSPHORYLATION AT SER-160.
PubMed=14993267; DOI=10.1128/mcb.24.6.2277-2285.2004;
Geymonat M., Spanos A., Wells G.P., Smerdon S.J., Sedgwick S.G.;
"Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular
localization of Swi6.";
Mol. Cell. Biol. 24:2277-2285(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179 AND THR-182, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-547, 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).
[11]
INTERACTION WITH MSA1.
PubMed=18160399; DOI=10.1074/jbc.m708248200;
Ashe M., de Bruin R.A.M., Kalashnikova T., McDonald W.H., Yates J.R. III,
Wittenberg C.;
"The SBF- and MBF-associated protein Msa1 is required for proper timing of
G1-specific transcription in Saccharomyces cerevisiae.";
J. Biol. Chem. 283:6040-6049(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-176; THR-179 AND
THR-182, 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).
[14]
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).
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 188-514.
PubMed=10048928; DOI=10.1038/5845;
Foord R., Taylor I.A., Sedgwick S.G., Smerdon S.J.;
"X-ray structural analysis of the yeast cell cycle regulator Swi6 reveals
variations of the ankyrin fold and has implications for Swi6 function.";
Nat. Struct. Biol. 6:157-165(1999).
-!- FUNCTION: Part of a complex involved in cell-cycle-dependent
transcription. SWI4 and SWI6 are required for formation of the cell-
cycle box factor-DNA complex. The repeated element in the upstream
region of HO (5'-CACGAAAA-3') is called the cell cycle box (CCB).
-!- SUBUNIT: Component of the transcription complex MCB-binding factor
(MBF) composed of SWI6 and MBP1. Component of the transcription complex
SCB-binding factor (SBF) composed of SWI6 and SWI4. Interacts with MSA1
and STB1. {ECO:0000269|PubMed:10409718, ECO:0000269|PubMed:18160399}.
-!- INTERACTION:
P09959; P13365: CLN3; NbExp=2; IntAct=EBI-18641, EBI-4490;
P09959; P39678: MBP1; NbExp=4; IntAct=EBI-18641, EBI-10485;
P09959; P25302: SWI4; NbExp=8; IntAct=EBI-18641, EBI-18626;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
-!- PTM: Phosphorylated by CDC28 and dephosphorylated by CDC14.
{ECO:0000269|PubMed:14993267}.
-!- MISCELLANEOUS: Present with 3340 molecules/cell in log phase SD medium.
{ECO:0000269|PubMed:14562106}.
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EMBL; X06238; CAA29581.1; -; Genomic_DNA.
EMBL; U17246; AAB67460.1; -; Genomic_DNA.
EMBL; BK006945; DAA09502.1; -; Genomic_DNA.
PIR; S03161; RGBYW6.
RefSeq; NP_013283.1; NM_001182069.1.
PDB; 1SW6; X-ray; 2.10 A; A/B=188-512.
PDB; 2XFV; X-ray; 1.90 A; A/B=2-126.
PDB; 5XW5; X-ray; 1.85 A; C=155-164.
PDBsum; 1SW6; -.
PDBsum; 2XFV; -.
PDBsum; 5XW5; -.
SMR; P09959; -.
BioGRID; 31453; 693.
ComplexPortal; CPX-946; SBF transcription complex.
ComplexPortal; CPX-950; MBP transcription complex.
DIP; DIP-598N; -.
ELM; P09959; -.
IntAct; P09959; 57.
MINT; P09959; -.
STRING; 4932.YLR182W; -.
CarbonylDB; P09959; -.
iPTMnet; P09959; -.
MaxQB; P09959; -.
PaxDb; P09959; -.
PRIDE; P09959; -.
EnsemblFungi; YLR182W_mRNA; YLR182W; YLR182W.
GeneID; 850879; -.
KEGG; sce:YLR182W; -.
EuPathDB; FungiDB:YLR182W; -.
SGD; S000004172; SWI6.
eggNOG; ENOG502QPWC; Eukaryota.
GeneTree; ENSGT00940000173997; -.
HOGENOM; CLU_017827_0_0_1; -.
InParanoid; P09959; -.
KO; K06648; -.
OMA; YYLDILM; -.
BioCyc; YEAST:G3O-32306-MONOMER; -.
EvolutionaryTrace; P09959; -.
PRO; PR:P09959; -.
Proteomes; UP000002311; Chromosome XII.
RNAct; P09959; protein.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0030907; C:MBF transcription complex; IDA:SGD.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0033309; C:SBF transcription complex; IDA:SGD.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; IMP:SGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:SGD.
GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR040822; Swi6_N.
Pfam; PF13606; Ank_3; 1.
Pfam; PF18530; Swi6_N; 1.
SMART; SM00248; ANK; 2.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 2.
PROSITE; PS50088; ANK_REPEAT; 2.
1: Evidence at protein level;
3D-structure; Activator; ANK repeat; Cytoplasm; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation.
CHAIN 1..803
/note="Regulatory protein SWI6"
/id="PRO_0000067071"
REPEAT 318..346
/note="ANK 1"
REPEAT 347..383
/note="ANK 2"
REPEAT 384..469
/note="ANK 3"
REPEAT 470..498
/note="ANK 4"
REPEAT 499..514
/note="ANK 5"
COMPBIAS 631..640
/note="Glu-rich (acidic)"
MOD_RES 149
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19779198"
MOD_RES 160
/note="Phosphoserine; by CDC28"
/evidence="ECO:0000244|PubMed:17287358,
ECO:0000269|PubMed:14993267"
MOD_RES 176
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198"
MOD_RES 179
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198"
MOD_RES 182
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198"
MOD_RES 547
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17287358"
STRAND 3..11
/evidence="ECO:0000244|PDB:2XFV"
STRAND 16..23
/evidence="ECO:0000244|PDB:2XFV"
TURN 24..26
/evidence="ECO:0000244|PDB:2XFV"
STRAND 29..31
/evidence="ECO:0000244|PDB:2XFV"
HELIX 32..34
/evidence="ECO:0000244|PDB:2XFV"
HELIX 35..44
/evidence="ECO:0000244|PDB:2XFV"
HELIX 47..49
/evidence="ECO:0000244|PDB:2XFV"
HELIX 58..68
/evidence="ECO:0000244|PDB:2XFV"
STRAND 80..82
/evidence="ECO:0000244|PDB:2XFV"
HELIX 84..93
/evidence="ECO:0000244|PDB:2XFV"
TURN 97..100
/evidence="ECO:0000244|PDB:2XFV"
HELIX 101..103
/evidence="ECO:0000244|PDB:2XFV"
STRAND 104..106
/evidence="ECO:0000244|PDB:2XFV"
STRAND 214..216
/evidence="ECO:0000244|PDB:1SW6"
TURN 225..227
/evidence="ECO:0000244|PDB:1SW6"
HELIX 244..258
/evidence="ECO:0000244|PDB:1SW6"
HELIX 292..302
/evidence="ECO:0000244|PDB:1SW6"
HELIX 321..327
/evidence="ECO:0000244|PDB:1SW6"
HELIX 331..339
/evidence="ECO:0000244|PDB:1SW6"
HELIX 354..360
/evidence="ECO:0000244|PDB:1SW6"
HELIX 363..366
/evidence="ECO:0000244|PDB:1SW6"
HELIX 370..377
/evidence="ECO:0000244|PDB:1SW6"
HELIX 378..382
/evidence="ECO:0000244|PDB:1SW6"
HELIX 391..399
/evidence="ECO:0000244|PDB:1SW6"
HELIX 405..421
/evidence="ECO:0000244|PDB:1SW6"
HELIX 422..424
/evidence="ECO:0000244|PDB:1SW6"
STRAND 427..429
/evidence="ECO:0000244|PDB:1SW6"
HELIX 448..452
/evidence="ECO:0000244|PDB:1SW6"
HELIX 455..461
/evidence="ECO:0000244|PDB:1SW6"
TURN 462..464
/evidence="ECO:0000244|PDB:1SW6"
HELIX 473..480
/evidence="ECO:0000244|PDB:1SW6"
HELIX 483..491
/evidence="ECO:0000244|PDB:1SW6"
HELIX 506..509
/evidence="ECO:0000244|PDB:1SW6"
SEQUENCE 803 AA; 90560 MW; 9B317FCACEEC493C CRC64;
MALEEVVRYL GPHNEIPLTL TRDSETGHFL LKHFLPILQQ YHDTGNINET NPDSFPTDEE
RNKLLAHYGI AVNTDDRGEL WIELEKCLQL LNMLNLFGLF QDAFEFEEPE TDQDEEDPSH
SKLPENKTKS ENSKDNISSK RINNLQDMSL DSDAHRELGS PLKKLKIDTS VIDAESDSTP
NTARGKPNDD INKGPSGDNE NNGTDDNDRT AGPIITFTHD LTSDFLSSPL KIMKALPSPV
VNDNEQKMKL EAFLQRLLFP EIQEMPTSLN NDSSNRNSEG GSSNQQQQHV SFDSLLQEVN
DAFPNTQLNL NIPVDEHGNT PLHWLTSIAN LELVKHLVKH GSNRLYGDNM GESCLVKAVK
SVNNYDSGTF EALLDYLYPC LILEDSMNRT ILHHIIITSG MTGCSAAAKY YLDILMGWIV
KKQNRPIQSG TNEKESKPND KNGERKDSIL ENLDLKWIIA NMLNAQDSNG DTCLNIAARL
GNISIVDALL DYGADPFIAN KSGLRPVDFG AGTSKLQNTN GGDENSKMVS KGDYDGQKNG
KAKKIRSQLL KNPPETTSLI NDVQNLLNSI SKDYENETVQ YNEKLEKLHK ELNEQREELA
NSREQLANVK QLKDEYSLMQ EQLTNLKAGI EEEEESFREE SKKLGIIADE SSGIDWDSSE
YDADEPFKVE FLSDFLEDKL QKNYEGDISK LLEAESKEQI MEQIRNQLPA EKIQSMLPPT
VLLKARINAY KRNDKHLTNV LDTISTKQSE LENKFRRVLS LCLKIDENKV DNMLDGLLQA
ISSEDPQDID TDEMQDFLKK HAS


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[TAF1 BA2R CCG1 CCGS TAF2A] Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)
[GATA3] Trans-acting T-cell-specific transcription factor GATA-3 (GATA-binding factor 3)
[RPS6KA1 MAPKAPK1A RSK1] Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1)
[dcr1 SPCC188.13c SPCC584.10c] Protein Dicer (Cell cycle control protein dcr1) (RNA interference pathway protein dcr1) [Includes: Endoribonuclease dcr1 (EC 3.1.26.-); ATP-dependent helicase dcr1 (EC 3.6.4.-)]
[pyrG C4Q28_07350] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[TY1B-OR YORWTy1-2 POL YOR142W-B O3367 YOR3367W] Transposon Ty1-OR Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)]
[Taf1 Ccg1] Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)
[Gata3 Gata-3] Trans-acting T-cell-specific transcription factor GATA-3 (GATA-binding factor 3)
[rbsK C4Q28_10525] Ribokinase (RK) (EC 2.7.1.15)
[katG C4Q28_15750] Catalase-peroxidase (CP) (EC 1.11.1.21) (Peroxidase/catalase)
[GATA3] Trans-acting T-cell-specific transcription factor GATA-3 (GATA-binding factor 3)
[dapB C4Q28_23450] 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8)
[TAF1 CCG1] Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)
[kdpB C4Q28_10110] Potassium-transporting ATPase ATP-binding subunit (EC 7.2.2.6) (ATP phosphohydrolase [potassium-transporting] B chain) (Potassium-binding and translocating subunit B) (Potassium-translocating ATPase B chain)
[Rps6ka1 Mapkapk1a Rsk1] Ribosomal protein S6 kinase alpha-1 (S6K-alpha-1) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 1) (p90-RSK 1) (p90RSK1) (p90S6K) (MAP kinase-activated protein kinase 1a) (MAPK-activated protein kinase 1a) (MAPKAP kinase 1a) (MAPKAPK-1a) (Ribosomal S6 kinase 1) (RSK-1)
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p10 (MA); p20; Capsid protein p25 (CA); Nucleocapsid protein p14 (NC-pol); Protease p15 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p90 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[coaX C4Q28_03585] Type III pantothenate kinase (EC 2.7.1.33) (PanK-III) (Pantothenic acid kinase)
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[mutM fpg C4Q28_25555] Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM) (AP lyase MutM) (EC 4.2.99.18)
[mobA C4Q28_13965] Molybdenum cofactor guanylyltransferase (MoCo guanylyltransferase) (EC 2.7.7.77) (GTP:molybdopterin guanylyltransferase) (Mo-MPT guanylyltransferase) (Molybdopterin guanylyltransferase) (Molybdopterin-guanine dinucleotide synthase) (MGD synthase)
[recB C4Q28_23110] RecBCD enzyme subunit RecB (EC 3.1.11.5) (Exonuclease V subunit RecB) (ExoV subunit RecB) (Helicase/nuclease RecBCD subunit RecB)
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[leuB C4Q28_19430] 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (3-IPM-DH) (Beta-IPM dehydrogenase) (IMDH)
[TY1B-MR1 YMRCTy1-3 POL YMR045C YM9532.10C] Transposon Ty1-MR1 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[TY1B-BL YBLWTy1-1 POL YBL005W-B YBL004W-A YBL0325] Transposon Ty1-BL Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)]

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