ID G8BQU6_TETPH Unreviewed; 1096 AA.
AC G8BQU6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=TPHA0C04580 {ECO:0000313|EMBL:CCE62608.1};
GN OrderedLocusNames=TPHA_0C04580 {ECO:0000313|EMBL:CCE62608.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE62608.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE62608.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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|ARBA:ARBA00024632,
CC 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; HE612858; CCE62608.1; -; Genomic_DNA.
DR RefSeq; XP_003685042.1; XM_003684994.1.
DR AlphaFoldDB; G8BQU6; -.
DR STRING; 1071381.G8BQU6; -.
DR GeneID; 11535287; -.
DR KEGG; tpf:TPHA_0C04580; -.
DR eggNOG; KOG0969; Eukaryota.
DR HOGENOM; CLU_000203_2_0_1; -.
DR OMA; CNNCRPR; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000005666; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004527; F:exonuclease 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 CDD; cd05777; DNA_polB_delta_exo; 1.
DR CDD; cd05533; POLBc_delta; 1.
DR Gene3D; 2.40.50.730; -; 2.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA 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|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU000442};
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666};
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 183..481
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 545..972
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1008..1079
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
SQ SEQUENCE 1096 AA; 124744 MW; DFD694D32C1DA542 CRC64;
MSSLKRPGEE EESELQVAVH DKKIKLQSHD HGVGSEPVST IEIIPSDRFR KVKEQGFKAK
DADLHGTQME SAFEKELLEM EHEAAIVDEQ ASIDTYGREP VASDFSPDTH DISFQQLDCD
QTMLSGSTDE NTPFIVRFFG VTQEGHSILC NVTGFKHYLY VPSPIAQEQT DKQDLDGFVK
YINEQLDNCV DSIEITQRQS IWGYSGDTKL PFWKVYLKNP HMINKLRTSF EKGYFTYKSW
FSNGTTTYDN IAYTLRLMID CGIVGMSWIT LPKSKYKLIT EQNKISNCQL EVSINYRDLI
SHPAEGDWSH SAPLRILSFD IECAGRIGVF PEPEHDSVIQ IANVVSIAGA KRPFIRNVFT
VDTCSPITGS HIFSHEKEED MLRQWREFVV KADPDVIIGY NTSNFDLPYL IDRAKALKVN
EFPYFGRLVN VNQEVKESTF SSKAYGTRSS KNVNIDGRLQ LDLLQFVQRE YKLRSYTLNA
VSAHFLGEQK EDVHYSIITD LQNGDSETRR RLAVYCLKDA YLPLRLLENL MALVNYTEMS
RVTGVPFSYL LSRGQQIKVV SQLFRKCLEI DTLIPNMGSQ GSDEQYEGAT VIEPIRGYYD
LPIATLDFNS LYPSIMMAHN LCYTTLCNRE TVQRLDLKLN EDYIITPNND YFVTTKKRHG
ILPIILNELI SARKRAKNDL KNEKDPFKRD VLNGRQLALK ISANSVYGFT GATVGKLPCL
AISSSVTAFG RDMIMTTKNA VQEKYSIKNG YKNDAVVVYG DTDSVMVKFG TSDLGEAMEL
GTEAAAYVSS LFKDPINLEF EKAYFPYLLI NKKRYAGLYW TKTEKYDKLD QKGLASVRRD
SCPLVSIVMN KVLKMILIER NVDGALAYIK SVIDELLHNK ADISKLIISK TLAPNYTNPQ
PHQVLTERMK RRDGVGPNVG DRVDYIIIGG NDKLYNRAED PLYALEHNIQ VDSRYYLTNQ
LQNPIISIIA PIIGEKQANS MFVVKSIKIN TGTMKGGLMG FMKKVEVCRY CKGPLTKGES
PLCSNCKERS GELYMKTLYE VRDLQEKFAR VWTQCQRCAG TLHNEVLCSN KNCDIFYMRV
KVKKELQEKV EQLNKW
//
