ID A0A2V5J2B9_9EURO Unreviewed; 1727 AA.
AC A0A2V5J2B9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=BP00DRAFT_460071 {ECO:0000313|EMBL:PYI27596.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI27596.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI27596.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI27596.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) 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; KZ825566; PYI27596.1; -; Genomic_DNA.
DR Proteomes; UP000248817; 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 859..1044
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1111..1559
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1616..1696
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 499..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1727 AA; 197085 MW; D1303F457F171005 CRC64;
MEPFQVRLNC VDHYQAAPSD FDPPLLYRDP TSGKNDRVKV PIIRVFGATE TGQKVCVHVH
GAYPYLYVQY EGELEEEKVS AATKHLHLAI DRALAVSYNR NPNDKKFAFV AHITLVKGVP
FYGYHVGYKF YFKVYLTNPI YMTRLADLLL QGSVLKRPVQ PYESHLQYIP QWMCDYSLYG
CAYMKCSNVK FRMPVPEYLE LTNSSHRWHD RSIRPEDLSD PSVLPKQSYC PLEVDICVQD
IMNRSDVSER SIHHDFTEYL KPMASDQRLV PSMAGLWHDE ERRRKKRLGL EPGSSPFVAE
ELVSLSVDPR NTSQGGWIHE EEYREMTRHT IDEEKSHYNG GDVSFDNFLT ENPLAKNVKT
ALQSVEDFYP GKDELTRSEF RNDNGLQLPE ESDVGIGEEA FLPAKSDEEP YNSEEDDVSS
LLHGGTLGEE GINTSEDYWA DGLFDVAAHN IFDDEADPGL SDPDHDVDSQ AELLDPEYSE
IFDHTKPAHD DGLEVDQEIL DGGTQRNKRL SDYNSSRERP HKRQRFFEDA LSQQLESPTK
QVLRQHAAHF QIDSSDTEDM LDELYEFVEH LPSQEKSSQS TIRPSKAQSR RISFPVVKDP
NDPMTVLRFS QDSSLSSKDL REIDGVNVSE SNENISFRTS FNESSSQLQS SATETRSDHA
NAHSDAQASE IMGSIYGSFN IPMQTRIGLW RRACPSSSEV SSTLCHFGYP STIYQKAHYS
NENDVPDRPR DYAGREFRLE GVGIHFLPRF DPSGRSVAML GDDYGVSKDK RSREKTDQLL
RESCTLREWE FAPVPPSRSE VIEWFEKLEE EAKKDPAKVQ ALPRERVQPN VMSQIEGPTQ
KNDYGFKYSQ KGKSTSVEHQ TQYMSMMSLE VHVNTRGELA PNPEEDEISC VFWCLNSDDE
DVDANGTLPG VHVGMISQSE EDRPDAKLSK ALRIEWDHET SELDLINRVV DVVRYHDPDL
ITGYEVHNSS WGYIIERARK KYDFDICDEL SRVISQAHGR FGKDADRWGF NHTSSIRVTG
RHMINIWRAM RSELNLLQYT MENVAFHLLH RRIPHYSFRD LTAWYQSGKP RDLMKVIDYF
VSRVQMDLEI LDSNELIART SEQARLLGID FFSVFSRGSQ FKVESLMFRI AKAENFMLVS
PSRKQVGQQN ALECLPLVME PQSDFYTSPL IVLDFQSLYP SIMIAYNYCY STFLGRARQW
RGRNKMGFMD YERQPQLLEL LKDKINIAPN GMIYAKPEVR KSLLARMLAE ILETRVMVKT
GMKADKDDKT LQRLLNNRQL ALKLIANVTY GYTSASFSGR MPCSEIADSI VQSGRETLEK
AIAFIHSVER WGAEVVYGDT DSLFVYLKGR TRDQAFTIGE EIAQAVTQSN PHPVKLKFEK
VYHPCVLLAK KRYVGFKYEH RGQTEPDFDA KGIETVRRDG TPAEQKIEEK ALKLLFRTAD
LSQVKAYFQA QCTKIMQGRV SVQDFCFARE VKLGTYRDTR GLLPPPGALI SARRMAADPR
AEPQYGERVP YLVVAGAPGS RLIDRCVSPD TLLHDATLDL DADYYITKNL IPPLERIFNL
VGANVRQWYD EMPKVQRIRR LPERAGPSHA HAHATAHAHA PGLRKTLESY LRSSACLVCK
SKLDDAEAAA AAASAPPLCA ECLRRPHLPL FDLVGRQRQA ERKVAELERL CRSCMGVSFG
EEVRCDSKDC PVFYSRTRAM ASWRHTKAAL DPVIRLLQDT TESALDW
//
