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Database: UniProt
Entry: A0A0J1B279_9TREE
LinkDB: A0A0J1B279_9TREE
Original site: A0A0J1B279_9TREE 
ID   A0A0J1B279_9TREE        Unreviewed;      1718 AA.
AC   A0A0J1B279;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   05-JUN-2019, entry version 23.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=CC85DRAFT_328733 {ECO:0000313|EMBL:KLT41724.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Trichosporonales; Trichosporonaceae;
OC   Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT41724.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT41724.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT41724.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete
RT   yeast T. oleaginosus allow insights into substrate utilization and the
RT   diverse evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ087213; KLT41724.1; -; Genomic_DNA.
DR   RefSeq; XP_018278215.1; XM_018426727.1.
DR   EnsemblFungi; KLT41724; KLT41724; CC85DRAFT_328733.
DR   GeneID; 28987330; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000053611; 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   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; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; PTHR45812; 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; 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:UP000053611};
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:UP000053611};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      975   1074       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1145   1590       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1628   1696       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      415    448       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0J1B279}.
FT   REGION      465    485       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0J1B279}.
FT   REGION      514    550       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0J1B279}.
FT   REGION      572    595       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0J1B279}.
FT   REGION      628    652       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0J1B279}.
FT   REGION      664    750       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0J1B279}.
FT   COMPBIAS    515    549       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0J1B279}.
FT   COMPBIAS    628    644       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0J1B279}.
FT   COMPBIAS    717    750       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0J1B279}.
SQ   SEQUENCE   1718 AA;  190580 MW;  43C8A4D67D83B448 CRC64;
     MSSQGGPEGE SALRLRITHI MTSQAPPLAS LRSDYVPPTL PTAVPPGVVP SSFPVLRIFG
     TTTSRQKVCV NVHLAYPYFY VPFPMDSLDP LRPERVVRLC QRFAVSLNHA ICLALRQNPT
     GPAAMTNFAG GTDPRHLHVV SVVLVKGVPF YGYHVGHAYW LKVSLTNPGR VRVAVEQLHK
     PVVLGKVWQP HEAHLSHVLQ FMCDFDLYGC GFLDLSGGQF RQPLPEPGEE EPSGWLTSES
     IPVHMAYPPN LSPPRDTRTA LELDVLPHHI LNRHRLAQRE LHHDFIELLH QPLHPEEKLV
     PAMKELWEDE RRRRLAKGLG TSEGAMLPVS GGGRGRSMAE LGYKIDGEEG ENRGGDWKIS
     EELWAILEER MAAERRRRGR LTFDQVSRAL RTGTNGERKK YDRWIMTAFE AVSAGWPKRA
     TQPRRTQKRS SPPNSQAPPS PPPEEEMEHN PFEFATQASQ EHVEVEVDAA EVQEDHEEEA
     EPGERQHLAA VREAEAFRAT QAAIGDDDIT RFLKTQAGGS PSRASTPSRA GSITAGNTRS
     GSSGTTSRRR AVEEAGFGDL SSLALSSFRL SSASSNPFAP STPTRAPNEQ QSTPRSLVRD
     FFARHSSPLS TPTKPRLSPN TVVLPASKRS FTKWTPSPQE AEPSSPLRQE EEVDMPLLTE
     IKVRRAPELP PPNAQPSPLL PSSIRKHGIS PTLVTRRPGP SPTMLNEADA TPTQRPKKRV
     RLSSPTQPFV IDPSQSSKPA SGGETSNSSA PDLAMDAWVF SDPPPSNKHV VDTMSTYGLD
     TVEYPSPFYS NPADVPPRPK AFAGRVFNVK TDTVNDLMPF EGDATPRPWL RTRKAMTGRA
     KFGWEYGAPP PCRRVVLEWC AKEDAEEARI KLAASQLAGP TQKNKYGFKL TQRSTRREQQ
     NMSVLLLEVF APSRGQLLPD PAEDEMAAVF FCFQNEDETL PDTVNHTGYH AGYVLVESEQ
     TAERRARLDG IPCHYVESEL DLINWVIDIV REWDPDVLAG WELHNASWGY VAARAAQGFG
     TDFADDISRL ISTSGPARKD AYAEHHTSAF KVAGRHVINI WRILRSEVTL NAYTFENCVF
     HVLRQRVPHY TAGALTALWR SKTPAHTARV LGIMFQRVVL YAELIDSAEV VSKNAEFGRV
     FGVDFDAVVF RGSQFKVESF LFRLAKPESF ILVTPSRAQV GLQNAPFAVP LIAEPESKYY
     SHPVIVLDFQ SLYPSVMIAY NICYSTCLGR VEKFKGTDKF GFSELKVSDG MLELLKDYLT
     VTPNGMVFVK PAVRKSLLAK MLGEILDTRV MVKHAMKGAR GDKPLMQLLN ARQLALKLMA
     NVTYGYTSAT YSGRMPCVEI ADSIVQTGRE TLEKAQELIH SRPEWAATVV YGDTDSLFVS
     LPGRSKDEAF KIGHDIADAV TALNPKPVRL KFEKVYMGCI LMAKKRYVGF KYEHPDETEP
     SFDAKGIETI RRDGCAAQAK LEEVCLKMLF RGNDLSAIKA YCRGEWAKIL ASRVSVQDFI
     IAKEVRLGTY SSKVPPPPGA AVAFRRILKD PRDEPQYAER VPYVISNAEG RRLIDRARTP
     EEMLASRALG IDAEYYIRNM LIPPLARIFN LVGGDVEQWY DSMPRARAAK RYGGAAARID
     AHFASSHCRI CAAEGGPVCR ACRDAPDEAA YSLLAKEGDV QRRVRDLHSV CASCSSIPPG
     ETMLCDSIDC PITYARVAAE RDAADAAEAH ALLAQLEW
//
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