ID A0A1B8C365_9PEZI Unreviewed; 1446 AA.
AC A0A1B8C365;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=VE00_08976 {ECO:0000313|EMBL:OBT41272.1};
OS Pseudogymnoascus sp. WSF 3629.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622147 {ECO:0000313|EMBL:OBT41272.1, ECO:0000313|Proteomes:UP000091997};
RN [1] {ECO:0000313|EMBL:OBT41272.1, ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|EMBL:OBT41272.1,
RC ECO:0000313|Proteomes:UP000091997};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|Proteomes:UP000091997};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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}.
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DR EMBL; KV454663; OBT41272.1; -; Genomic_DNA.
DR STRING; 1622147.A0A1B8C365; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000091997; 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:UP000091997};
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 402..710
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 778..1216
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1255..1439
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 57..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..290
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1446 AA; 162794 MW; A9F64C79FA6F7D58 CRC64;
MSKSARSSKL AELRALRESG KKRLDTYEVH QEEDLYEEVD EDGYKKVIRD RLNQDDFVID
DNGEGYADDG REDWDRRQGY DSESEEEARP KGKNGKAAKR KREEDKTKRE NMDKGINNYF
TKGPVVAQPK AKPVKTQADD DFLGDLLAEV DTNVLPRASH HPPKQLTRRT RALSPPIQSA
KSLSAKRVKL GGASDAPLAH DDDDGNYMGG MDDDDVPMSD PAPSSPVQKA VQRKAQVAIK
AEEEDDYDAM EVAQADGIAA ASVNMSGSRP VPKLLKPEPY PTPASSSPTR PPPEEVDASA
WNNVTSRLNV ISSSPPTDTR TYGKMDYKDA IEGDGSLNMF WTDYTEVHGS LCLFGKVKNK
KTGEYVSCFL KVDNILRKVF FLPRDNLYKH GRETSEEVGM EDVYKEVDSI MTRMKVGMHK
IKPCSRKYAF ELEDVPKEGE YLKLLYPYNK PALPIDLTGD TFSHTFGTNT SIFEQFVLWK
NVMGPCWLKI EDADFTFLNN ASHCKLEVQV TTPNLITPLT ESDSMEPPPL TLMSLALRTT
LNAKDNKQEI LAISARIYEN ISLSDTTPAE QIPSRTITII RPVGSSFPLG FEDLIKKKSR
GLVKLCRQEP EILSFFLAQL DRVDPDVILG HQLEGVDYSI LLSRLQTRKT PGWSRIGRFK
RSDWPGSMGK IGGNFFAERS LISGRLLCDL ANDAGKSTMT KCQSWSLTEM CNLYLSSGNN
VRREVDNEVA LKTWATTRDG LVDYIGHCEA DTYFIAALAL KVQMLPLTKV LTNLAGNSWA
RTLTGTRAER NEYILLHEFH RNKYIVPDKA PFKGRPKTEQ QDQDEEGDVK KKDKYKGGLV
FEPEKGLYDK FVLVMDFNSL YPSIIQEYNI CFTTVDRTTL SDDEEKVPEV PVDQDQGILP
KLIATLVGRR RQVKSLMKDK SATSEQLATW DIKQLALKLT ANSMYGCLGY TKSRFYARPL
AVLTTYKGRE ILRSTKELAE SKSLQVIYGD TDSVMINANV DNVADAFKVG HEFKRAVNDR
YKLLEIDIDN VFRRILLQAK KKYAAINLLE IDGKFVEKME VKGLDMKRRE YCALSKEVSS
KLLNEILSGE ETEIVITRIH DYLREISGKM REDLIPLQKY TIYTKLGKNP KDYPNSDSMP
QVQVALRELA RGKTVRKDDV IAYIVTGDGK SANEPAAKRS YTPADVMKAD SELKADAEWY
LYKQIFPPVE RLCANILGTD SMRLADCLGL DVRKYSINNN VSSGGTETEI HPLESQIEDE
VRFKDAARLQ LSCRVCKGTF EFEGLLGSLD SCSPNGITCR CGATLRNLAV VAQLEHQIRQ
ETARYYEGWL VCDDQACGAR TRQMSVYGHT RCLGPRGLGQ GCLGKMGYEY SEKAMYNQLL
YFSSLFDVEK AKEKCGGTDR DQVLALGEHN RVRFDTLKGV VERYLDKCGR QWVAMDSLFG
KLGYGP
//
