ID A0A1Z5TP34_HORWE Unreviewed; 1457 AA.
AC A0A1Z5TP34;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=BTJ68_02504 {ECO:0000313|EMBL:OTA37739.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA37739.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA37739.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA37739.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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:OTA37739.1}.
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DR EMBL; MUNK01000017; OTA37739.1; -; Genomic_DNA.
DR STRING; 1157616.A0A1Z5TP34; -.
DR VEuPathDB; FungiDB:BTJ68_02504; -.
DR InParanoid; A0A1Z5TP34; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000194280; 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; 3.30.70.2820; -; 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; 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; 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:UP000194280};
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 9..74
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 387..693
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 759..1205
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1244..1449
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 52..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1457 AA; 163599 MW; 2EE9ED2839856D58 CRC64;
MPVSRADRLK QLRDLRAAGK TGFDSYEVEE AESIYETVDD EGYKKVVRSR LDQDDFVVDD
NGEGYADDGR EDWQDQRVEY EDSESEQDLP KQSKAAKRKR EEDAQRQEKL NKGISKYFSA
NQGNTAPKPK PARTAEDDAF MTDLLGEVDT NIPSRAPSYG KAVRSNDRRK TRVLSPPLDD
RPKKTKAPEP ALEPENDMNS TPPAPVANDD DYYPAPQDDM MMSDPIPSSP AAKAVERREQ
ATTIKKEDVD DDDLMEVAEV QGHANIRSAN VNLKGSRPAP KLSKPTYPTP DSSSPTRPPD
DAIDMTSINN VTEKLNILSS PPSEATSFGK IAAKDAVEED GTLRFFWTDY TEVNGSLCLF
GKVKNKRDGS YVSCFVKVDN EEIDMQDVYQ EVDRLMSKFK VGMHKIKPCS RKYAFELPDV
PREADYLKLL YPYDKPSLPM DVEGETFSKV FGTNTALFEQ FVLWKNIMGP CWLKIDNANF
QAVNNASWCK LELQVDKPNN INPLGDADNL DAPPLTLMSL ALRTTMNRKE NKNEILVASL
RFYENVSLTD TTPPEKLPCR TFTVMRPHGE YPVGFKLEAE KHKGQIKMEK SENALLSVLL
AIIQRYDPDA ILGHKLDDVD YNVLLTRLRD RKTPGWHRIG RLKRGEWPKN VGKGGGSFFA
ERHLAAGRLL CDLANDMGKS IMTGCQSWTL DEMVKLSLGG NIVRRDIDND KALAMAQDRI
GLMNYVKLCE ADTYFIAAIA LKRQLLPLSK VLTNLAGNSW ARTLSGTRAE RNEYILLHEF
YRNKYICPDK VYGKGAANKK LEEAGGNDAD EDADSGKKKD KYKGGLVFEP EKGLYDKFIL
VMDFNSLYPS IIQEYNICFT TVERGEIGDD DEKVPDVPGD TANKGILPRL IRGLVARRRE
VKKLMKSKGA TEEQLQTWEV KQMALKLTAN SMYGCLGYTK SRFYARPLAA LTTSKGREIL
QSTKDLAESA HALRVIYGDT DSVMVNTNKD NLLEATKMGD EFKKAVNERY ELLEIEIDNV
FRRLLLHAKK KYAAINMVEV DGVWKEKMEV KGLDMKRREY CQLSKDTSTE LLNYLLSGED
PEQVVSKIHD HLRGLGEKMR ANEVQPFKYT IYTQLGKDPK EYPNANSMPA VQVALKLMAR
GKTVRAKDVM GFVICGNNNG SAEQAAKNAY PLDEVLKKDS GLVPDVDHYL HKQILPPVER
LCAPIGGTNV ALLAECLGLD TSKYRVSSAN NGTEQSNEIT TLESQIPDHI RFKDCEPLNL
LCLGCKRHFE YRGLNYQAPP DQEVPLTPVG VLTNNGISCP RAECKKVMST LTMSAQLEAQ
IKRHSAKYYS AWLTCDDPAC GMRTRQMSVY GTRCLGPKGL AHGCSGRVSF EYSEKAIYNQ
LLYLQSLFDV DKSLEKMGKP GLAGVKTEDS EKTKVLAGMN RERFGVCWDV VKAYLDRSGW
GWVSMESLFG YALKAMV
//
