ID A0A0F0I5M6_ASPPU Unreviewed; 1460 AA.
AC A0A0F0I5M6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=P875_00042531 {ECO:0000313|EMBL:KJK61288.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK61288.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK61288.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
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 -!- 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:KJK61288.1}.
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DR EMBL; JZEE01000687; KJK61288.1; -; Genomic_DNA.
DR STRING; 1403190.A0A0F0I5M6; -.
DR Proteomes; UP000033540; 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:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 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; 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; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
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; PF08996; zf-DNA_Pol; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000033540};
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 416..714
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 781..1226
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1265..1455
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 56..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 165465 MW; 537CC6CAB9264BBF CRC64;
MASARAKLAE LRALRASGKK RISTYEVEEQ DDIYEEVDDE GYKKIIRNRL DEDDFVVDDN
GEGYADDGRE DWTVDYHDSE SDDGDLPANG KAAKRKREED KQRKEKINNG ISKYFNKGSG
ASAPKPKPVA TAEDEAFMAD LLGEVDTNVV SNHVPTQNVI KSETRRKVRV LSPPLSHRPR
PQKKQTKDEN SDPMSPIGQK PDLDIDNDDG PLPVADDDDV PMSDPMPSSP VSKAVERKTA
IAVKTEDPDE EDNDLMEIAE VSGQHEAKTT SVNMAGSRPP PKIKKEAYST PANSSPVKAM
PDVANASWND VRNKLNVLSS PASESRTFGK LRAQDVVEDD GSLRMFWIDF TEVNGSLCLF
GKVKNKQTGN YASAFVKVDN ILRKLYFLPR EYRHKHGRDT DEEVDMEDVY NEVDGMMSRL
KVGMHKIKPC TRKYAFEMPG VPKETEYLKL LYPYDKPALP METKGETFSH VFGTNTSLFE
QFVLWKNIMG PCWLRFEGAD FSAVNNASWC KFECQVSKPA LISPVPDSEN LEAPPLTLMS
LAFRTQLNVK ENKQEILIAS ARVYENVSLT DTTPPEKVPC KTFTVMRPVG SSYPMHFEAE
TKRQRGTYIL ERSEQFLLSK FLALFEKMDP DVLMGHQLQE VDLSILLNRL KEKKTPGWHR
LGRLKRGDWP KNFNRGGGFF AERHLIAGRL MCDVANDMGK SLMMKCQSWS LTEMCNLYLG
PGNVRQELDS EAALKTWATT KDGLMNFVNH CDTDTYFVAA LVLRLQMLPL TKVLTNIAGN
SWARTLSGTR AERNEYILLH EFHRNKYICP DKYSAKLQKA EVKLQDGDDD DATDKKKKDK
YKGGLVFEPE KGLYDRFVLV MDFNSLYPSI IQEYNICFTT VERTATAENE NEEKVPEVPS
SDQEQGILPR LIATLVGRRR EVKKLMKDKR ATPEQLALWD TKQLAFKLTA NSMYGCLGYT
QSRFYARPLA MLTTFKGREI LRSTKELAES KQLRVIYGDT DSVMINTNMD TLSDALKVGE
EFKKSVNERY RLLEIDIDNI FRRLLLHAKK KYAAINMTEM DGKYVDKLEV KGLDMKRREY
CALSKEVSQR LLNEVLSGED QEIVLNRVHD YLRDLAGKMR EFAVPVQKYV IYTKLSKRPE
EYPNKETMPP VQVALRELAR GKSVRPNDVI SYIVTSGDSE TSSLAPAKRS YTLQDVMKPD
SGLNPDIEFY LLKQIFPPIE RLCAPIPGTD AVRLAECLGL DVRKYQINTS SGGNQQNTDI
FPLESQIPDS VRFESAARLT LTCRSCKEKS VFEGLAASSH MCNANGLFCP NTACQKQFTV
LTIIAQLESQ IRAQTSKYYE GWLVCDDSAC GNRTRQMSVY GHRCLGPRGH AEGCLGRMSY
EYSEKQLYNQ LLYFAGLWDV DKARVAAEKE ASGEKKDSVV ALASFNRARF ETVKGVVDAY
LKKCGRQWVE MDSLFRFMLP
//
