ID A0A5N6UBC8_ASPTM Unreviewed; 1948 AA.
AC A0A5N6UBC8;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=BDV40DRAFT_293961 {ECO:0000313|EMBL:KAE8155887.1};
OS Aspergillus tamarii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=41984 {ECO:0000313|EMBL:KAE8155887.1, ECO:0000313|Proteomes:UP000326950};
RN [1] {ECO:0000313|EMBL:KAE8155887.1, ECO:0000313|Proteomes:UP000326950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117626 {ECO:0000313|EMBL:KAE8155887.1,
RC ECO:0000313|Proteomes:UP000326950};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) +
CC diphosphate; Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-
CC COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112;
CC EC=2.7.7.7; 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ML738793; KAE8155887.1; -; Genomic_DNA.
DR OrthoDB; 6755010at2759; -.
DR Proteomes; UP000326950; Unassembled WGS sequence.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IEA:TreeGrafter.
DR GO; GO:0003682; F:chromatin binding; IEA:TreeGrafter.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:TreeGrafter.
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:0003697; F:single-stranded DNA binding; IEA:TreeGrafter.
DR GO; GO:0050334; F:thiaminase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-ARBA.
DR GO; GO:0006273; P:lagging strand elongation; IEA:TreeGrafter.
DR GO; GO:0006272; P:leading strand elongation; IEA:TreeGrafter.
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 FunFam; 1.10.132.60:FF:000004; DNA polymerase; 1.
DR FunFam; 1.10.3200.20:FF:000002; DNA polymerase; 1.
DR FunFam; 3.30.420.10:FF:000036; DNA polymerase; 1.
DR FunFam; 3.30.70.2820:FF:000001; DNA polymerase; 1.
DR FunFam; 1.20.910.10:FF:000003; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20; 1.
DR FunFam; 3.40.1190.20:FF:000034; Putative hydroxymethylpyrimidine/ phosphomethylpyrimidine kinase 2; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 3.40.1190.20; -; 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; 1.20.910.10; Heme oxygenase-like; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
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; IPR027574; Thiaminase_II.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR NCBIfam; TIGR00592; pol2; 1.
DR NCBIfam; TIGR04306; salvage_TenA; 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|ARBA:ARBA00022705,
KW 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000326950};
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 473..717
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 784..1229
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1268..1432
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT DOMAIN 1459..1716
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 1739..1946
FT /note="Thiaminase-2/PQQC"
FT /evidence="ECO:0000259|Pfam:PF03070"
FT REGION 75..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..235
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1948 AA; 219086 MW; AE3FB6B26354DD92 CRC64;
MASARAKLAE LRALRASGKK RISTYEVEEQ DDIYEEVDDE GYKKIIRNRL DEDDFVVDDN
GEGYADDGRE VWNERTADYY ESESDDGELP ANSKAAKRKR EEDKQRKEKI NNGISKYFNK
GSNASAPKPK PVATAEDEAF MADLLGEVDT NVVSNHVPTQ NVIKSETRRK VRVLSPPLSH
RPRPQKKETK DENSDPMSPI GQKPDLDLNN DDGPLPVADD DDVPMSDPMP SSPVSKAVER
KSAVAVKMED LEEEDNDLME IAEATGQHEA KTTSVNMTGS RPPPKIKKEA YSTPANSSPV
KAMPEVANAS WNDVRNKLNV LSSPASETRT FGKLRAQDVV EEDGSLRMFW IDFTEVNGSL
CLFGKVKNKQ TGNYASAFVK VDNILRKLYF LPREYRHKHG RDTDEEVDME DVYNEVDGMM
SRLKVGMHKI KPCTRKYAFE MPGIPKETEY LKLLYPYDKP ALPMETKGET FSHVFGTNTS
LFEQFVLWKN IMGPCWLRFE GADFSAVNNA SWCKFECQVS KPALISPVPD SENLEAPPLT
LMSLAFRTQL NVKENKQEIL IASARVYENV SLTDTTPPEK LPCKTFTVMR PVGSSYPMHF
EAETKKQRGT YILERSEQFL LSKFLALFEK MDPDVLMGHQ LQEVDLSILL SRLKEKKTPG
WHRLGRLKRG DWPKNFNRGG GFFAERHLIA GRLMCDVAND MGKSLMMKCQ SWSLTEMCNL
YLGSGNVRQE LDSEAALKTW ATTKDGLMNF VNHCDADTYF VAALVLRLQM LPLTKVLTNI
AGNSWARTLS GTRAERNEYI LLHEFHRNNY ICPDKYSAKL QKAEEKLHDG DDDDATDKKK
KDKYKGGLVF EPEKGLYDRF ILVMDFNSLY PSIIQEYNIC FTTVERTATA ENENEEKVPE
VPSSDQEQGI LPRLIATLVG RRREVKKLMK DKRATPEQLA LWDTKQLAFK LTANSMYGCL
GYTQSRFYAR PLAMLTTFKG REILRSTKEL AESKQLRVIY GDTDSVMINT NMDTLSDALK
VGEEFKKSVN ERYRLLEIDI DNIFRRLLLH AKKKYAAINM TEMDGKYVDK LEVKGLDMKR
REYCALSKEV SQRLLNEVLS GEDQEVVLNR VHDYLRDLAG KMREFAVPVQ KYVIYTKLSK
RPEEYPNKET MPPVQVALRE LARGKSVRPN DVISYIVTSG DSETSSLAPA KRSYTLQDVM
KPDSGLNPDI EFYLLKQIFP PIERLCAPIP GTDAVRLAEC LGLDVRKYQI NTSSGGNQQN
TDIFPLESQI PDSVRFESAA RLTLTCRFCK EKSVFEGLAA STHMCNANGL FCPNAACQKQ
FTVLTIIAQL ESQIRAQTSK YYEGWLVCDD SACGNRTRQM SVYGHRCLGP RGHAEGCLGR
MSYEYSEKQL YNQLLYFAGL WDVDKARVAA EKETSGEKKD SVVALASFNR ARHISPSISN
GVYSCDITVQ SSCLPSCRGL EADQRVLAAH GCYALTATTG LTAQNTLGVQ DIFIVPAEFV
KKQINAGLED IGADAVKLGM LSSAETIDII AETLVTHQVP SVVLDPVMVS TSGSKLLPEA
AVEKLRTKLL PLTTVLTPNI PEAKLLLKDA GLDVPEPEGL SDVLQLVKQV KALGPKAVLL
KGGHLPLTKD HKTARNQDEA TAVIDVLYDG EDTTLFETDF LLSKNTHGTG CSLASSIAAN
LALGKDLKRA VHSAVRFVEA GIKTSFDIGK GSGPINHFHS VYTLPFAPGR FLEYALDRPD
IRPVWQKFTE HEFVLGMGSG TLPVERFKEY LVQDYLYLVQ FARSNALAAY KAKDMESIAA
SAQIVLHIQR ETALHLDYCA SFGLSKPEME RTPETIACTA YSRYILDVGQ SEDWLALQMA
LAPCLIGYGA IAQRLYTDKD TLRQGNRYWK WIENYVAEDY SEAVRLGSEL LERHMREVSP
SRMEELIKIF IRATELEIRF WDMALGAR
//
