UniProt: A0A0F8UA98

Database: UniProt
Entry: A0A0F8UA98_9EURO

LinkDB:  A0A0F8UA98_9EURO 
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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (27)   

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ID   A0A0F8UA98_9EURO        Unreviewed;      1707 AA.
AC   A0A0F8UA98;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
DE   Flags: Fragment;
GN   ORFNames=ARAM_000425 {ECO:0000313|EMBL:KKK16508.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK16508.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK16508.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK16508.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKK16508.1}.
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DR   EMBL; JZBS01002999; KKK16508.1; -; Genomic_DNA.
DR   STRING; 308745.A0A0F8UA98; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000034291; 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:UP000034291};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1707
FT                   /note="DNA polymerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002528545"
FT   DOMAIN          846..1043
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1110..1556
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1602..1676
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          501..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KKK16508.1"
SQ   SEQUENCE   1707 AA;  194657 MW;  6C0B784017074026 CRC64;
     CCICSFALSL TALAVTKPTG PMESFQVRLN CVDHYQAKPS EFDPPLPYKD GIGAKDDRPK
     VPVIRIFGTT ETGQKVCVHV HGVFPYLYVR YDGDLNPEIV RSSISRLHLS IDHALAVSYR
     RNAYDKNAVY VAHITLVKGV PFYGYHVGYQ FFFKIYLLNP IYTTRLADLL LQGAVMKKSI
     QPYESHMQYV PQWMCDYSLY GCAFMKCSKV KFRSPVPEYL DLFDLSHRWH DRSIQPDWIS
     DESVLAKQSH CPLEADICTQ DILNRLEISE RSIHNDFSEY LKPVFSNERL VPSMAGLWQD
     EKRRRKKRLG LLDPDSSPFS NEDLVSFSTN PRKCSQGDWI HEKEFRQMTY QIAEEERRQD
     GDRKITFDGF LEVNSCEDNI KTALESVEDF FPGQNGFTDL NIPYKEDSKD IEEQTADYVD
     EGAVLTDSYD EGPYSSGVDS IDEAFSEDEN GDGQVDVLGN MPQDGTSGTG LQNYPVEDAF
     ELNADGFHPE LVEAEHLAGP STFLDSENGS ARTGNKRPQT EGLGDYNSHK RRKHAIGAFS
     QPFRRPLQNP LPLGIAQIQN PEAEATTSSD TLSQNAKDMA SQGKIFSSQS TVRLRGNGKN
     STLNFPIVKD PNDPMTVMRF SQDGSCSKDL WELTDSAKTD VKESINTSQL QSSRHGVEFD
     TSNIFALESA ALIYDAFNIS TNIRLGCLRR PCPTPTEVSS TLQDYDLPSI IYQNPHYSKE
     SDVPDRPRDY AGREFRLEGT SIHFLPDFDP SGRSLTTYGE RIVESGDRLD RQEVDRQLRI
     KSTPRVWEFA PVAPSRSEVL TWFENEQREC LTKAVQSKAR FEEPEVKTKA LSQIEGPTQQ
     NDYGFKYSQN GKSASVEHQA QYMSIMSLEI HVNTRGVLAP NPEEDEIASF FWCLNSEDKY
     LEANGDIPGT RVGVIFQGEG DGPEIKVSKA LKVDWEHEPT ELDLINRLVD IVRLYDPDII
     TGYEVHNSSW GYVIERARKK YDFDICDELA RVKSQAHGRF GKEADRWGFN HTSSIRITGR
     HMINIWRSMR SELNLLQYTM ENVVFHLLHR RIPHYSSQEL TTWYRSVKPR DFMKVVNYFV
     SRVQMNIEIL DSNELISRTS EQARLLGIDF FSVFSRGSQF KVESLMFRIA KPENFILVSP
     SRKQVGQQNA LECLPLVMEP QSDFYTSPLL VLDFQSLYPS IMIAYNYCYS TFLGRVQQWR
     GRNKMGFMDY NRQPRLLELL KDKINIAPNG MIYARPEVRK SLLAKMLAEI LDTRVMVKAG
     MKVDKDDKAL QRLLNNRQLA LKLIANVTYG YTSASFSGRM PCSEIADSIV QSGRETLEKA
     IAFIHSVERW GAEVVYGDTD SIFVYLKGRT REEAFDIGEE IAQAVTDINP HPVKLKFEKV
     YHPCVLLAKK RYVGFKYEHR EQKEPEFDAK GIETVRRDGT PAEQKIEEKA LKLLFRTADL
     SQVKSYFQNQ CTKILQGRVS IQDFCFAKAV KLGTYSDKAL LPAGALISTK KMLEDPRAEP
     QYGERVPYVV VTGAPGSRLV DRCVPPETLL QDAQLELDAE YYITKNIIPP LERIFNLVGA
     NVRQWYDEMP KFHRIRRVKG TTYSTGKGGK KTLESYMRSS TCVVCKTNKL HAETDTPLCS
     PCMQQSHVSL LDLISRQRQA EQKVSNLERI CRSCMDVPFG DEIKCNSLDC PVFYSRTRSL
     AHWRHTNAVF NPVVKLLQDK CESALEW
//

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