ID A0A0J1B279_9TREE Unreviewed; 1718 AA.
AC A0A0J1B279;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; 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 yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT 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-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; KQ087213; KLT41724.1; -; Genomic_DNA.
DR RefSeq; XP_018278215.1; XM_018426727.1.
DR STRING; 879819.A0A0J1B279; -.
DR GeneID; 28987330; -.
DR OrthoDB; 211439at2759; -.
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 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:UP000053611};
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 975..1074
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1144..1590
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1628..1696
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 415..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//
