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Database: UniProt
Entry: A0A1E4RE94_9ASCO
LinkDB: A0A1E4RE94_9ASCO
Original site: A0A1E4RE94_9ASCO 
ID   A0A1E4RE94_9ASCO        Unreviewed;      1055 AA.
AC   A0A1E4RE94;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=HYPBUDRAFT_153821 {ECO:0000313|EMBL:ODV65572.1};
OS   Hyphopichia burtonii NRRL Y-1933.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Hyphopichia.
OX   NCBI_TaxID=984485 {ECO:0000313|EMBL:ODV65572.1, ECO:0000313|Proteomes:UP000095085};
RN   [1] {ECO:0000313|Proteomes:UP000095085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-1933 {ECO:0000313|Proteomes:UP000095085};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) 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   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; KV454544; ODV65572.1; -; Genomic_DNA.
DR   RefSeq; XP_020074639.1; XM_020221748.1.
DR   AlphaFoldDB; A0A1E4RE94; -.
DR   STRING; 984485.A0A1E4RE94; -.
DR   GeneID; 30996297; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000095085; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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; 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; 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; 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   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
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:UP000095085};
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          2..292
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          358..812
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          850..1049
FT                   /note="Zinc finger DNA-directed DNA polymerase family B
FT                   alpha"
FT                   /evidence="ECO:0000259|Pfam:PF08996"
FT   REGION          387..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1055 AA;  119500 MW;  127043E0BF8988D9 CRC64;
     MKYAFELPGI PKETEYLKVL MPYNTPRNKN LIMPADLKGE TFNHIFGTNA NLFESFVLQR
     NIMGPCWLEI LSPDFDGLRN ATHCQVEVAV DSPSLIKPIT NVNIPAPHLT VTSISVQTVM
     DAKNSKQEVA AISLATYRNI PQDTPIDENT EPTESLTLAR PVGGATYFPP GLQQLGQKQG
     MNLKTLPNEK VLLNGLNAFI KSTDPDVFIG HRLENISLDV LVHRMYDLKV PTWSSLGRRN
     RKTWPDRFGR SSGGFNNSLQ IREIFQGRLL CDIANEMGQS LTPKCQSWDL PEMYDVVCHK
     KHTALEINYQ TPSFSEDASL FLMALNENDF NAKITAEISF STQILSLSKQ LTNLAGNAWS
     HTLSGTRAGR NEFILLHEFK RNNYIVPDKE DRYHKNSQQQ QNKLESSEDD ATTVTSNKKP
     KFQGGLVFEP EKGLHKNYIL VMDFNSLYPS IIQEFNICFT TVDRDDFNVS HDEDKDLPII
     PDRDSSQGVL PRLLNTLVTR RREVKKLLKD PKNSPVEKAQ FDIKQQALKL TANSMYGCLG
     YVNSRFYAKP LAMLVTNKGR EILMDTRQLA ESIGLRVVYG DTDSVMIDTG VDNLKEALKI
     GEEFKVQVNE RYRLLEIDTD NVFKRLLLHA KKKYAAMNVS IDKKTGQELT ALEVKGLDMR
     RREYCQLSKD ISTFVLQKLL SDTDPEQALG EVYDYLEETT QKIKNNEIPI DRYKVNTRLS
     KDPSNYPNGK SMPPVQVAFR LRSQGKVIKA GSVITFVITA ANDENETKES SPADRARAIT
     EVLAKNSNYK PDANYYLEKQ IFAPVERLLE RIEGIDMVRV AKCLGIDTKK YILRVKNNES
     ANGEIVPLES NITDIERFRL SSYLIMNCKC GHKFRFGGIL ASNDYKVTFN GISCGKCDYT
     FPQIRIASQL ENAIRTHLAS YYAGWLVCDD GACGITTRQI SVYGRRCIGS SGTSHGCKGV
     MKYKYTDKAL YNQLLYFNSI FDVDKAKKNE LKPIYDVFDT VENQPKKLAS GQVDALAEQN
     RELFTQCQDV IQKYLGDCGR RYVDMSGLFD WMSKA
//
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