UniProt: A0A194SC37

Database: UniProt
Entry: A0A194SC37_RHOGW

LinkDB:  A0A194SC37_RHOGW 
Original site:  A0A194SC37_RHOGW

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (30)   

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ID   A0A194SC37_RHOGW        Unreviewed;      1991 AA.
AC   A0A194SC37;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=RHOBADRAFT_50779 {ECO:0000313|EMBL:KPV78298.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV78298.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV78298.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV78298.1,
RC   ECO:0000313|Proteomes:UP000053890};
RX   PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA   Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA   Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT   graminis WP1.";
RL   Front. Microbiol. 6:978-978(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; KQ474073; KPV78298.1; -; Genomic_DNA.
DR   RefSeq; XP_018274347.1; XM_018415494.1.
DR   STRING; 578459.A0A194SC37; -.
DR   GeneID; 28975942; -.
DR   OMA; GRNKMGF; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000053890; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
DR   CDD; cd05778; DNA_polB_zeta_exo; 1.
DR   CDD; cd05534; POLBc_zeta; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          156..227
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1412..1859
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1901..1971
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          338..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1114..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..41
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..518
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..591
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..689
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..716
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..848
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..888
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..938
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        950..993
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1114..1134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1137..1154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1991 AA;  221728 MW;  199652E840F67231 CRC64;
     MGNQGDPPAA PSSHPATAPP PAPPPPPPPP PLDPSAPSTP PPDSFIRFRL SAIDTVLAYD
     HSQYDIRRSP FTSEPLRQVP LIRIWGATDR GQRVTALVHG VFPYVYVEYK GRLDPDSVHD
     YIRRFGAALN RAMDLSLPNK YGKKQAPQYV AFVVLCKGTN FYGYHVGHSP FLKVYLVNPR
     HKNRLSEVLR SGAVLRTQFD VFEGHVPYLL QFMLDANLYG CGWVEVGECR FREELPDHVV
     KSSDDFAPDS CDGPYSERLY TVDTVPPHRL HPSVDAGGPA KISYEALELD LPYTAILNRR
     VLTPRDLHHD FVELLHPDSV ERGKLVRSLK EIWADEARRR AERGETGPAD TADTAQREWD
     ERDAAQAIWR REPEFRDKVA AKLGEDLRRW RDQVGPRGKA QPEFASFVDD TARHARGGNR
     HWLTKVRTTF EQVDAVSIDR FAQDERDKYE FGAWAVQGIG IPVPKVDEAD VDLARLRAST
     AAASAARRTA RRRPQDAAEG EGDDDEMDGD DFDSGEDEYG DGPGQGGGGG RGRGGQAPPA
     TQAEALARQR RSGAADRIER RGRMASTQEG EWDREPDERD DDDDEEEDNF WGVDAGTDRP
     ASRAPSEASF FCGGDEDEDA EDGRSSMRPD SLSPVKRSSP SKRLTPSKRP LASPAQLGHV
     DHDHGHTDEP SAKRVKADEE ERVRKMAEQG GEFGKQAASF TTPTHPRSTP SSARAARTAH
     HISPAVTPSR RSARNPFASP SKALSFRIAA PSSSGSTLRP GPEDDGEAAL FSSPPPDLKL
     DPDTAVEPQG AQQVQPSVAA PRQLAHHVSN LSTALSLEEY LQSSAESADV RSPSPPGRSR
     SNVTPSQALA DLKDLPDDAL DEYMPTPTLK EEVPSQLPPH PRSSPPPPLF DFDDMHVEER
     PSRPSSPPHA SPMLEIEPAS PVLTDLDRDV KPPLEPTLRP TKKHVMFQLA RTDLSSSAAS
     AGTTPTPVAS VNGSQRSTTP LQTSQNTTDS ADSVVAPAPP RRVSTYPLSA RSFTFAEPPP
     TTSTVVAALE RDNRSYVVYK DPYYSKPADV PRRKREYAGR SFRLKGSRIV DLTPFVHHDA
     LGPLPSETPS APLSRMLDVR AWEYAVRPPT RENLDEWLSK NGGRKDEKKP RFNPIKSQVE
     GPTQKTGSEK FQSIKGASQR EKQHMAVLAM ELHVNTRGKL LPNPQHDAIE FLVFCLKSDN
     EREDEYWNGR NEKTHVGYIV VGEGKKYERL DNRCHVHVVE TERDLIELFL DKLRMEWDPE
     CVAGFEVHHG SWGYLLERAE TAFEWNLVPE LGRVKSFDTG KFGDKHSDRW GFSQSSVLNF
     TGRHVLPVWR ILKADNKFQQ NSFEHIALHV LGIRTPHFSY ETLTAWYASG EAVDMARVVE
     YWRNRVEMDV EMLDAAEVVE QSCEEARVFG VDFNSVRTRG SQFKVESVMF KLAKPESFLL
     LSPNRVQVGR QNAAECMPLI MEPQSAFYKG PLLVMDFQSL YPSCMIAYNY CYSTFLGRVS
     DFKGSNKFGV SEVDLPDGLL NLLKDDITIS PNGMMFAKER VRKSLLAKMV GELLETRVMV
     KGSMKAVADD KALTKLLNAR QLALKFLANV TYGYTSATFS GRMPAVEVAD AIVQTGRESL
     EKAMETIKAT RRWGAQVVYG DTDSLFIYLP GKTKDEAFRI GNEMADVITQ QNPRPIKLKF
     EKVYLPCVLV AKKRYVGFKY EYQQQKDPDF DAKGIETIRR DGIPATQKMQ ETCLKILFRT
     SDLSLVKEYC QRQWKKIQAG DVSPQDFTIA KKVKLGSYAE GRLPPPGAVV AGRAMAEDPR
     AEPEYGERVP YVMFQAAPGQ KQVHRALAPQ EFLADSRLRL DDVHYIERMM IPPLERIFNL
     VGADVKSWYR EMAKAKRVHR VGEGKSGRAV MLEQHFISDR CVACDGPEGH GGLCPDCAAH
     PTAVAHTLSA RQQALLSRQF ALRAVCVSCS GTPSFATIAC DSIDCPNMYA RARNDNELEK
     LPNLANLHLA F
//

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