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Database: UniProt
Entry: A0A194SD55_RHOGW
LinkDB: A0A194SD55_RHOGW
Original site: A0A194SD55_RHOGW 
ID   A0A194SD55_RHOGW        Unreviewed;      1145 AA.
AC   A0A194SD55;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   05-JUN-2019, entry version 17.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=RHOBADRAFT_50999 {ECO:0000313|EMBL:KPV78544.1};
OS   Rhodotorula graminis (strain WP1).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV78544.1, ECO:0000313|Proteomes:UP000053890};
RN   [1] {ECO:0000313|EMBL:KPV78544.1, ECO:0000313|Proteomes:UP000053890}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:KPV78544.1,
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.,
RA   Redman R.S., Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT   "Genome sequence of the plant growth promoting endophytic yeast
RT   Rhodotorula 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-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; 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|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; KQ474073; KPV78544.1; -; Genomic_DNA.
DR   RefSeq; XP_018274593.1; XM_018415598.1.
DR   EnsemblFungi; KPV78544; KPV78544; RHOBADRAFT_50999.
DR   GeneID; 28976046; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000053890; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005657; C:replication fork; IEA:EnsemblFungi.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:EnsemblFungi.
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:0043137; P:DNA replication, removal of RNA primer; IEA:EnsemblFungi.
DR   GO; GO:0045005; P:DNA-dependent DNA replication maintenance of fidelity; IEA:EnsemblFungi.
DR   GO; GO:0006278; P:RNA-dependent DNA biosynthetic process; IEA:EnsemblFungi.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 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; IPR042087; DNA_pol_B_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
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; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053890};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      170    519       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      583   1014       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1051   1124       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1    108       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A194SD55}.
FT   COMPBIAS     36     50       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A194SD55}.
FT   COMPBIAS     81    108       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A194SD55}.
SQ   SEQUENCE   1145 AA;  128302 MW;  28C08B6D923F0196 CRC64;
     MDAEPAAKRP RLSQGEPALL AGEPTADAVL PADDAPPATT TTTTTTDTLP DEEHAAPPSS
     AAGAHAKPLS AIWAAKSPSP RKKKQPVDLK GKGKARAPGH GPEDDDKENF TSLLERLEAE
     TSTGEQEKWG RPAAPKLNPQ RDGFVFQQID LEEYSAPGAG PTIRAFGVSK AGHSVLLHVK
     GFLPYFWVAA PKGFTNSDCV PFLEHLNLTF FFTVSGEQTS YFNGTRPIRS ITLANKRNLW
     GYKGEAVVPF IKITTVDTKN YPKVRNGFER GEVTYRDFFD GSSLLTFESN IAYTLRFMID
     HHIVGMNWLE IKAGGWQHKR DKISSCQYEI ECDHSALISH EAVGDWSGVA PLRILSFDIE
     CAGRKGIFPE ADKDPVIQIA NMVTRQGESK PFIRNVFTLN TCAHIVGSEV LEFEREKDLL
     SQWRKFVEEV DPDLIIGYNT SQFDLPYLMD RAKALKVTEF PYFSRLKGVK TEVKDTHFSS
     KAYGTRDSKE TNMDGRLQLD ILQVMQRDYK LRSYTLNSVC AHFLGEQKED VHHSVITDLQ
     NGNAESRRRL AVYCLKDAYL PQRLMDKLMC FINYTEMARV TGIPFNYLLS RGQQIKVISQ
     LYRQALKVGY VVPALKQEGS DEQYEGATVL EPEQGYYDVP IATLDFASLY PSIMQAHNLC
     YTTLLDARIA QSLNLVEDED YVRTPNGDLF VKASRRKGLL PTILEDLLAA RKRARAELKN
     ETDPFKRAVL DGRQLALKVS ANSVYGFTGA TVGKLPCLPI SMSVTAYGRE MIDRTKQEVQ
     DRYNTANGYD YDATVIYGDT DSVMVRFGCP DLETAMKLGA EAADFVTSKF VKPIKLEFEK
     VYFPYLLISK KRYAGLYWTR PEKYDKMDTK GIETVRRDNC RLVVTVIDTC LRKMLIERDV
     KGAEAYAKQV ISDLLQNKVD LSQLVITKAL AKADYAAKQA HVELAERMKK RDAGSAPAMG
     DRVAYVIIKG TKDARAYEKS EDPLYVLENN IPIDTKYYLE NQLSKPLMRI FEPIMGERAS
     SLLAGDHTRT VSIVAPTVGG LMKFAVKTVT CLGCKTPLKP GTPNQAVCHN CRPRTAELHR
     RQVTLAASAE TAFARLWTQC QRCQGSLHQD VLCTSKDCPI FYMRKKAQKE AVEAVGTLQR
     FDGEW
//
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