ID G3Y203_ASPNA Unreviewed; 1971 AA.
AC G3Y203;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=ASPNIDRAFT_206569 {ECO:0000313|EMBL:EHA22724.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA22724.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA22724.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(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|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EHA22724.1}.
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DR EMBL; ACJE01000010; EHA22724.1; -; Genomic_DNA.
DR STRING; 380704.G3Y203; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_206569; -.
DR HOGENOM; CLU_001718_2_0_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd01169; HMPP_kinase; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR CDD; cd19367; TenA_C_ScTHI20-like; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 6.10.10.100; -; 1.
DR Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 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; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR Pfam; PF03070; TENA_THI-4; 1.
DR Pfam; PF08996; zf-DNA_Pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 8..72
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 430..718
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 785..1230
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1269..1431
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT DOMAIN 1495..1758
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 1781..1947
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
FT REGION 56..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1971 AA; 221205 MW; 8B22D7C05ECCEBA3 CRC64;
MSASRAKLAE LRALRAAGKK RLSTYEVEEQ GDIYEEVDDE GYKKIIRNRL DQDDFVVDDN
GEGYADDGRE VWNERTADYG DSESEDDELP ARGKAAKRKR EEEKQRQEKI NNGISKYFNS
GAAPSAPKPK PVATAEDDAF MADLLGEVDT NVVPHRVPTR NIVKTEARRK VRILSPPLAD
RTRKERPIKK DENSDPVSPV KDQPELNFDD DDGALPGMDD DDVPMSDPMP SSPISKAVER
KSTTTPVKVE EFDDDDNDIM EIAQVTGQND AKATSINMAG SRPPPKLKKE STPALASSSP
TKPMPEVDAS WNDVRSKLNV LSSPASSEMR SFGKLRAQDV VEEDGSLRMF WLDFTEVNGS
LCLFGKVKNK QNGSYASAFV KVDNILRKLY FLPREYRHKN GRETDEEVDM EDVYHEVDGM
MSRLRVGMHK MKPCTRKYAF ELPGVPKETE YLKLFYPYDK SPLPMDVKGE TFSHVFGTNT
SLFEQFVLWK NIMGPCWLKI EEADFTAVNN ASWCKFECQA AKPALISPVP DSENLEAPPL
TLMSLSFRTQ LNVTENKQEI LVASARVYEN VSLTDTTPPE RLPCKTFTVM RPAGSSYPMH
FEAETRKQRG TFMLEKSEQF LLSKFLALFE KMDPDVLMGH QLQEVDLSIL LSRLKEKKTP
GWHRLGRLKR GDWPKNFNRG GGFFAERHLI AGRLMCDVAN DMGKSLMMKC QSWSLTEMCD
LYLGKENARQ ELDCEAALKT WATTKDGLMN FVNHCDADTY FIAALVLRLQ MLPLTKVLTN
IAGNSWARTL SGTRAERNEY ILLHEFHRNK YICPDKYSSK LLKAEEKMQE GDDDESADKK
KKDKYKGGLV FEPEKGLYDK FILVMDFNSL YPSIIQEYNI CFTTVERTAT ADNDKEEKVP
EVPTSDQEQG ILPKLIATLV GRRREVKKLM KDKRATPEQL ALWDTKQLAF KLTANSMYGC
LGYTQSRFYA RPLAMLTTFK GREILRSTKE LAESKQLRVI YGDTDSVMIN TNMDTISDAL
KVGDEFKKSV NERYRLLEID IDNVFRRLLL HAKKKYAAIN MTEVDGKYVD KLEVKGLDMK
RREYCSLSKE VSQKLLNEVL SGEDQEVVLN RVHDYLRELA EKMREFSVPV QKYVIYTKLS
KRPEEYPNKE SMPPVQVALR ELARGKSVRP NDVISYVVTN GDAETSSLAP AKRSYTLQDV
MKPDSGLKPD IEFYLLKQIF PPIERLCAPI PGTDAVRLAE CLGLDVRKYQ INSSSGSNQQ
NADIFPLESQ IPDSVRFENA TRLTLTCRFC KEKSVFEGLA QSTHMCTANG IICPNQACQK
PFSVLTIVAQ LEAQIRAQTS KYYEGWLVCD DTACGNRTRQ ISVYGHRCLG PRGHAEGCLG
RMTYEYSEKQ MYNQLLYFAG LWDVDKARKA AEKEPTGEKK DGVAALAEFN RIPRRFLCPP
QSPAINFTRS ILARFFFLGF WRPGLPQLIL LDITGSPLVT AVMSVARVLV IAGSDSSGGA
GLEADQRVLA AHSCYALTAT TGLTAQNTLG VQDIFIVPAE FVKKQINAGL EDVGADVVKL
GMLSSAETID VIAEALTVHQ VPAVVLDPVM VSTSGSRLLP EAAIKGLRTK LLPLTTVLTP
NIPEAVLLLK DSGVDVPEPT DLPGLIQLAK QVCSLGSKGV LLKGGHLPLT NDNRTAQNHE
DASKVIDVFY DGKDITLFET DYLISKNTHG TGCSLASAIS ANLAHGKDMR RAVQSAVRFV
EAGIKTSIDL GKGSGPINHF HSFYCLPFSP GHFVEYALDR PDVQPAWKRF TEHEFVKRLG
DGTLSEERFK SYLVQDYLYL VQFARSNALA SYKAGDMESI AASAKIVLHI QRETALHLDY
CASFGLSKEQ MESTPETIAC TAYGRYILDI GQSQDWLALQ VALAPCLLGY GAIAQRLYSD
KESVREGNRY WKWIENYVAE DYTEAVRLGS GETPTRADDN LPRNERWLTL A
//
