ID A0A094DL81_9PEZI Unreviewed; 1102 AA.
AC A0A094DL81;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=V497_00526 {ECO:0000313|EMBL:KFY67186.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY67186.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY67186.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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|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}.
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:KFY67186.1}.
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DR EMBL; JPJZ01000065; KFY67186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DL81; -.
DR STRING; 1420910.A0A094DL81; -.
DR HOGENOM; CLU_000203_2_0_1; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000029268; 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 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:UP000029268};
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 174..471
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 535..966
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1004..1078
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 124020 MW; F564B3F3F0514FC9 CRC64;
MVGALLPQKR VFGEASSARR NIDSSPASMK KRKLEGVETP ISRLKSSQNG PKGKPGSSQP
SHFESEVLEK LTQDMTGLKN KNSEKDQQWD RPALADFNAE TDNLIFQQIE AEEGTLHGGK
ATVKLFGVTE TGHSVMLHVT DFLHYLYVAA PVSFVRTDCE NFKVFLESQV AQHQPAIHSV
QIVMRENLYG FQGNQQSPYL KITVTDPKFI NRVRTTIEGG NANWKGMWKG ADGGVLTFDS
IQYVLRFMVD TKMAGMSWVE APASSYKMIN ANERQSNCQI EAEIGYRDLI THKPEGEWSK
MAPLRILSFD IECAGRKGIF PEANHDPVIQ IANVVTRYGE KKPFVRNVFC LDTTSLIVNT
QIFEFQREEK MLMAWRDFLE KVDPDIIIGY NISNFDFPYL LDRAKHLKVG GFDYWSRLHS
IKSVAKESNF SSKQMGNRDT KATNTNGRLQ LDLLQLVQRD HQLRSYTLNS VCAQFLGEQK
EDVHHTMITE LFNGTPESRR RLAVYCLKDA YLPQRLLDKL SCLENYTEMA RVTGVPFNFL
LSRGQQVKFV SQLFRKALEQ KLVIPNQRTE ASGEQYEGAT VIEPTRGYYD VPIATLDFAS
LYPSIIQAHN LCYTTLLNKN SVEKLGLKKD EDYIVTPNGD MFCTAKQRKG LLAQILDELL
TARKQAKREL AVETDPFKKA VLNGRQLALK ISANSVYGLT GATVGKLPCL EIAGSTTSYG
RQMIEKTKAE VEAKYTIANG YAHDAQVIYG DTDSVMVKFG TKDLAESMKL GEEAADYVSS
KFVKPIKLEF EKVYFPYLLI NKKRYAGLYW TNPNKYDKMD TKGIETVRRD NCRLVQTVIE
TVLRMILIDQ DVQGAQDYVK DTISDLLQNK VDMAKLVITK ALAKADYANK QAHVELAERM
RKRDAGSAPT LGDRVAYVII KGAAGAKNFE RSEDPIYVLE HNVPIDTKYY LDNQLAKPLG
RIFEPILGET KARSLLTGAH TRSVAIAAPS VGGLMKFAKK TSTCMGCKKP LVGKEESGGA
VCKNCAPRMG ELYTKTLTKV SDLEVRFGRL WTQCQRCQES MHCEVICSSK DCPIFYMRMK
AKKDVEDAGK ELARFDKDAA AW
//