ID A0A074YD91_AURSE Unreviewed; 1098 AA.
AC A0A074YD91;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=AUEXF2481DRAFT_4720 {ECO:0000313|EMBL:KEQ95763.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ95763.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ95763.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ95763.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584758; KEQ95763.1; -; Genomic_DNA.
DR RefSeq; XP_013344078.1; XM_013488624.1.
DR AlphaFoldDB; A0A074YD91; -.
DR STRING; 1043005.A0A074YD91; -.
DR GeneID; 25368266; -.
DR HOGENOM; CLU_000203_2_0_1; -.
DR InParanoid; A0A074YD91; -.
DR OMA; CNNCRPR; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000030641; Unassembled WGS sequence.
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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000030641};
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 167..467
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 531..962
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1000..1074
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 57..84
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 17..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 124445 MW; 41FD8540D490501F CRC64;
MPAAKVKDVQ PSKRVLVDAP SSRQNIQTDN ASKRRKLNGG PKNFKTPGGP NSSQVKSQFE
EEVLEKLTQD LDDLKQHNAE KDQQWARPSL DDFDETRDNL CFQQIEVEEG TLHGGKTCVK
LFGVTETGHS VLLHVTDFMH YLYVAAPPSF QQSDCEAFKA YLETHLAQHQ PVIYSVQMVL
RENLYGFQGN QKSPYLKITV TDPKHINKLR TSIESGSANF KGFWKGADGG VLTFDSIQYV
LRFMIDTKVS GMSWVETPAS KYTMIPARDR HSNCQIEAYC HYRDLIAHPA EGEWAKMAPL
RTLSFDIECA GRKGIFPEAN VDPVIQIANV VTRYGEEKPF VRNVFCLDTC SLIVNTQIFE
FADEDKMLMA WRDFLEKVDP DVIIGYNISN FDFPYLLDRA KHLKVGKFPF WSRLRNVQSV
AKDTNFSSKQ MGNRDTKATN TNGRLQLDLL QLIQRDHQLR SYTLNSVCAH FLNEQKEDVH
HTMITELFNG TPESRRRLAV YCLKDAYLPQ RLMDRLLCLV NYTEMARVTG VPFNYLLSRG
QQVKFISQLF RKALEQQLVI PNLRSEGTDE QYEGATVIEP TRGYYDVPIA TLDFASLYPS
IMQAHNLCYT TLLNKNAVDK LGFVKDEDYI VTPNGDLFCT AKIRKGLLTQ ILEELLGARK
RARKELAVET DPFKKAVLNG RQLALKISAN SVYGITGATV GKLPCLAIAS STTSYGRQMI
EKTRDEVQKR YTIANGYTHD AEVIYGDTDS VMVKFGPNDL AKAMELGEEA ANYVSSKFIK
PIKLEFEKVY FPYLLINKKR YAGLYWTNPN KWDKMDSKGI ETVRRDNCRL VQTVIETSLR
MLLIDRDVQG AQDFVKETIA ELLQNKVDMS NLVITKALTK NDYAAKQAHV ELAERMKKRD
AGSAPALGDR VAYVMVKGAA GAKNYEKSED PIFVLENNLP IDTRYYLDNQ LAKPLGRIFE
PILGEKKAGQ LLTGEHTRSI SVAAPTMGGL MKFAKKTETC MGCKKPLTGK DEKGGAVCEN
DRDRLGELYQ KTLSKVAELE VRFARLWTQC QRCQGSMHNE VICSSRDCPI FYMRMKAKKD
VEDSGKELVR FDNDGALW
//
