ID M5G1G9_DACPD Unreviewed; 1592 AA.
AC M5G1G9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=DACRYDRAFT_107768 {ECO:0000313|EMBL:EJU02050.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJU02050.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJU02050.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJU02050.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH795863; EJU02050.1; -; Genomic_DNA.
DR STRING; 1858805.M5G1G9; -.
DR HOGENOM; CLU_000203_3_1_1; -.
DR OMA; GRNKMGF; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000030653; 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; 2.
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:UP000030653};
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 106..185
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 759..935
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 1002..1447
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1501..1570
FT /note="C4-type zinc-finger of DNA polymerase delta"
FT /evidence="ECO:0000259|Pfam:PF14260"
FT REGION 290..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1592 AA; 181068 MW; E636C4F6D83A4631 CRC64;
MHDESILKVR ITNVDYSQQV PGPLDRTESI FATLNKVPVL NVFGHTSAGQ KACVHIHNVF
PYLYIEYKGE LDPGSVNKFI NRLGRKLNHA LTLVLRRNPY VQNTPQHIVA ILPVKGVHFY
GFHHRRSIFL KIMFSDPRLI RKVQLLLESG AICEKAWQTY ESHVDYKLQF MCDFNLYGCN
WLEVADCRFR EPLPEPPEYD IPVSSIAPHM IPWNSANTPP ELMHSVQPIP VRSTRSYNVL
ELDICAWDIL NRHALTARPI ASRLAPPFSG AGNPDELFVH SVRELWEDER RRRSAKGMDP
TPPRPKDATR TIDPERTRWV ASERFWAEVD ARIDREKDKI GRVGPDDELK VIPWEAWLMT
PFESVEALFP REHQRQRQRR REKQTEAVNA AEDDWSQRGD VENEAEDDAK WAGSQLLQRA
VEEAQGVEDE WIQDPERQVE EEEEWESGYD PPPAQPRTPL KSQRTAPVRS RSGTPTKSGK
VSPVNGDKGN GHAKRPNLFA TPSRDHTPYR SSPLKNGVRT IEQEEREGSI PVLPQNSPDP
WITSPEKEMT LKRGVHFDGE ERPPKRARIE EADNAVVDPW IVSLDSFTSS EDAAPTCSPV
ATQRDPTKPL SSSAYTYGFM PPTRVDVMET LYPHKMYTDP HYSNRFDVPE RAREYAGRMF
KLAWGGRVSE FETTTQIFDM LSDEIVLPTI TSAWEFASRA PTHREVENWL ADPANMDKEL
THAMKRRKQA QSQLDGMTPA KGYGIRATMH RPSEFSTREK QNMSVLAVEI FARSRGRLLP
DPAEDEISMV AFAFQDDAGE GGRDTYEVGL ILVANPQVDA TRLRDLASAN VDMVDAESEL
INKLIDRVLD WDPDVLTGWD VQSSSWSYLA GRAKQYGVDL SDQISRVMSP PSRNGQDRWS
LTHTSTFRVS GRHVINVWRH LRKELTLTSY TFENVAFQVL KRRMPLYLAS TLTQWFHSPV
PLHTAQLIDY LLERTVTVIE ILDETELITK TAEFARVFGV EFFSVLERGS QYMVESFMFR
IAKPENFVLI SPSKEQVGQQ NAAECVPLIM EPQSACYKGP LVVLDFQSLY PSIMIAYNYC
YSTCLGRVRN FKGKSKFGVT DLSIPPGVLE LLKDDITISA NGMMFVKDHV RRSLLSKMLS
ELLDTRVMVK QGMKTAKGDK SLLRLLNARQ LSLKYIANVT YGYTSASYSG RMPAVEIADA
IVQSGRETLE KAVHLINSTA KWGAKVVYGD TDSLFIYLPG RTKDEAFQIG HDMADTITSL
NPAPVKMKFE KVYLPCVLMA KKRYVGFKYE NPDDVQPEFD DKGIETVRRD GCALTRKMVE
ASLRILFNTQ DLSEVKEYCR RQWSKILEGR LPIQDFIIAK EVRLGTYIEG AAPPPGAAVA
AMKAVKDPQA EAQYGERVPY VIMRGEGRRL VDRAISPEVL LRNRDQRIDP IYYITRQLIP
PLERIFNLVG ADVQAWYDDM PKKLRANRAD SVVVIPRRDK DVKTSKASAS TIERHFRSNL
CLVCEEQTDS AVCPSCLRDL PTTLYSLNTR MHLGEQRLRD TQQICASCTA SPPGEPIRCE
SLDCEWLYER VKAEEEASAF AEIPKLIEQL CV
//
