ID A0A423XFH2_9PEZI Unreviewed; 1476 AA.
AC A0A423XFH2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=VPNG_03385 {ECO:0000313|EMBL:ROW14955.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW14955.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROW14955.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROW14955.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROW14955.1}.
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DR EMBL; LKEB01000011; ROW14955.1; -; Genomic_DNA.
DR STRING; 1230097.A0A423XFH2; -.
DR InParanoid; A0A423XFH2; -.
DR Proteomes; UP000285146; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000285146};
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 10..75
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 419..727
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 794..1232
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1273..1468
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 58..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..218
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1476 AA; 165953 MW; 2E4BBAA23DE8BFFD CRC64;
MPKLDKRAKL EQLKALRKAG KKTFDNYKVD EVDDLYEEVD EDRYKTIVRD RLNQDDFVVD
DNGEGYADDG REEWDRVHAY QSDSEDDLPV RGKEGKKSKK QRDEEQAKRD ATDRDISQFF
TKGGNTAQPK AKVVKTEEDD EFLAGLLGGI DANISAPTPR QAKKRDRSPE KRPARVPSPA
PDLRRRAPKR VRLSPEPTLP PQEDDTLMDD DDALLPMGDD DDALPAHLPA NDVPTSDPAP
SSPIVKAVER RTKPKAEAED DEDEDMLEVS HAGTVNAGSV NLTASRLPKR ILKADPYLTP
VNSSPPKGQV EPAVDSSAWT SINQRLNVVS SPAADSRGIN KIDYNDAIEE DGSLNMFWTD
YTEVNGSLCL FGKVLNKKTR SYVSCFVKVD NILRKLYFLP RQTRVVGGED TAEEVGMMDV
YQEIDSLMTK MNVGMFKIKG CTRKYAFELP DVPKEAQYMK LLYPYTKPQI DAEATGETYS
RVFGTSTALF EQFVMWKNIM GPCWLKIQDA DFGALKNASH CKLEVLVEHP NMISPLSDSD
NLDAPPLTLM SFAMRTTFNV KENKQEILAM SARIYENVSL SDKTTADKLP CRTFTLIRPV
GAVFPMGFEQ EARNRKKGLI KTMKQESEML AFFLAQVDVV DPDVILGHQL EGVDYSVLLN
RLHEKKTHQW SRLGRLRRSQ WPSSIGKMGG NVFAERQVMA GRLLCDLAND MGKSTMYKCS
TWGLTEMCSL YLSGDNKRRD FDNEAALKTW ATTKNGLLDY VSHVETDTYF ITALALSVQI
LPLTKILTNL AGNSWARTLT GTRAERNEYI LLHEFHRNKY ICPDKQTFKG RQRMEQENAD
EENGDSKKKD KYKGGLVFEP EKGLYDKFVL VMDFNSLYPS IIQEFNICFT TVDRFSTSED
EDAVPEVPTD QEQGILPKLI ATLVSRRREV KKLMKDKTAT AEQINTWDIK QLALKLTANS
MYGCLGYTKS RFYARPLAVL TTYKGREILR STKELAESNS LQVIYGDTDS VMINANVDNV
ADAFKVGNEF KKAVNERYRL LEIDIDNVFR RILLQAKKKY AAINLIEQGD KWIEKMEVKG
LDMKRREYCS LSKEISSRLL NEILSGDDTE VAIQRIHEYL RETAGKMREQ AIPVNKYIIF
TQLGKAPKEY PNADSMPQVQ VALRELARGK TVRKGDVISY VITGDSQSSD PVAKRAYTPQ
DVLKGDSGLT PDVEWYIGKQ IFPPVERLCA NIVGTSSSQL AECLGLDIRR YANNANNSAN
GNSNDLEIHP LESQIPDEVR FCDCTRLQLR CRSCKTTSTF EGLLASPDRV TPAGVACGSC
GATISTLSVV AQVERAIRTA TAKYYEGWLV CDDSSCGNRT RQMSVYGGRC LGPKGLARDC
LGRMRYEVSE KDIYNQLVYF ASLWDVDKAK AKAAAGASEV ANALDRDTKD KVLALAEHNR
TRFGTVKGVV DRYLDKCGRQ WVAMDTLFTK LGFTVA
//
