ID G7XFS8_ASPKW Unreviewed; 1675 AA.
AC G7XFS8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=AKAW_03901 {ECO:0000313|EMBL:GAA85787.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA85787.1};
RN [1] {ECO:0000313|EMBL:GAA85787.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA85787.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(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; DF126454; GAA85787.1; -; Genomic_DNA.
DR STRING; 1033177.G7XFS8; -.
DR VEuPathDB; FungiDB:AKAW_03901; -.
DR eggNOG; KOG0968; Eukaryota.
DR InParanoid; G7XFS8; -.
DR Proteomes; UP000006812; 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 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 823..1003
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1074..1520
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1572..1644
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 464..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1675 AA; 191098 MW; 9EC3E5F7CDC357FD CRC64;
MEPFQVRLNC VDHYQATPSE LDPPLPYRDG AAGKNDRSKV PVIRIFGATE TGQKVCVHVH
GAFPYLYVEY DGDLETEKVS SAIRSLRLSI DHALAVSYNR NENAKKIAFV AHITLVKGVP
FYGYHVGYKF YFKIYLMNPI YMTRLADLLL QGAVLKRPLQ PYESHLQFVP QWMCDYSLYG
CAYLKCSKVK FRSPVPEYFE LTDLSHRWHD RSVQPDDLLD DSLFPKQSHC PLEVDICVQD
ILNRSEISER PIHQDFTELF KQMTSDERLV PSMAGLWQDE TRRRKKRLGL EPGSSPFDPN
ELVSLSVNPR DTFRGGWIHE EEYREMAAQT VNEEKQQNGG GDVTFDDLLS QKPFAQDVKT
AMQSVEDFYP DKNNFDKYQQ QPVEPDTAAN AEVNVDESAA WPVVSDDDLY LSDDDIFDVL
PGEDNDREAA SALDENQAGD ILDLTQDEPE YSVDDLNAYE MSATRKAGSD EMVGRTESRE
PSHNNMRKRK RFFDDTPSQM LDRPRKSRIA EVQVNSTTPK IEDTANTLDA DAVVRGKSSQ
KKPSQSTVRS KRPEQSGRLN FPVVKDPNDP MTILRFSQDG APSSKELREL EKDLASSGPE
VISKDTRAEN SSSQPQSSVT VTSPDAGIDP QIFEIASGFY AAFNVPMNAR ICFLRNFSPS
TSEVASTPHS YDYPSVIYQK AHYSDESDVP DRARDYAGRE FRLEGNGIHY LPDFDPSGRS
MAMLGEYTPP RDKNEQEVVD QQLREFSTSR FWEFGPVPPS RSEVIEWFEK CQAEEKADAA
QPQAPKQVQM KANVLSQIEG PTQKNGYGFK YSQKGRSTSV EHQTQYMSIM SLEVHVNTRG
VLLPNPEEDE ITCVFWCLQS EDEDLDANGT VPGVHVGMIS QSEHDRPDTK ASKALRIDWE
HETSELDLIN RVVDIVRWHD PDIITGYEVH NSSWGYLIER ARKKYDFDIC DELSRVKSQA
HGRFGKDADR WGFNHTSSIR VTGRHMINIW RAMRGELNLL QYTQENVAFH LLHRRVPHYS
FQDLTDWYRS GKPRNILKVV EYFVSRVQMD LEILESNELI PRTSEQARLL GIDFFSVFSR
GSQFKVESLM FRIAKPENFI LVSPSRKQVG QQNALECLPL VMEPQSDFYT SPLVVLDFQS
LYPSIMIAYN YCYSTFLGRA HQWRGRNKMG FTDYKRQPRI LELLQDKINI APNGMIYAKP
EVRKSLLARM LAEILETRVM VKNGMKLDKD DKALQRLLNN RQLALKLIAN VTYGYTSASF
SGRMPCSEIA DSIVQSGRET LEKAIAFIHS VERWGAEVVY GDTDSLFVYL KGRTRDEAFT
IGEEIAKAVT SINPHPVKLK FEKVYHPCVL LAKKRYVGFK YEHRDQKEPE FDAKGIETVR
RDGTPAEQKI EEKALKLLFR TADLSQVKRY FQSQCTKIMQ GRVSVQDFCF AREVRLGTYS
DRGLPPPGAL ISTKKMIADP RSEPQYGERV PYVVVTGAPG ARLIDRCVPP ETLLHDPHLD
LDADYYITKN LIPPLERIFN LVGANVRQWY DEMPKVQRVR RVEGAMIRGP GGGGGGGGGR
RTLESYMRAS TCIVCKTKLR DTDTPLCGNC SRQPHLAMFE LVSRQRAAEK RVVDLQRICR
SCMGVTFGDE VKCDSKDCPV FYSRTRDEAN WRYTKAVLDP VVGLLRDRCE KELEW
//