ID A0A1B7TDZ4_9ASCO Unreviewed; 1436 AA.
AC A0A1B7TDZ4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=HANVADRAFT_52754 {ECO:0000313|EMBL:OBA26979.1};
OS Hanseniaspora valbyensis NRRL Y-1626.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=766949 {ECO:0000313|EMBL:OBA26979.1, ECO:0000313|Proteomes:UP000092321};
RN [1] {ECO:0000313|Proteomes:UP000092321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-1626 {ECO:0000313|Proteomes:UP000092321};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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}.
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:OBA26979.1}.
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DR EMBL; LXPE01000012; OBA26979.1; -; Genomic_DNA.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000092321; 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; 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; 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:UP000092321};
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 344..651
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 719..1187
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1237..1435
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1436 AA; 164991 MW; E3EBEB3B2D108898 CRC64;
MSSRKEKLQQ LVNKTKKHNI IDDDEESDYD MSHNNVSNII DDVYDDDNAF VEDDEGEQAY
TKEEKYKENY YEHEDAKYAS KNNNATKKSK QETVVKVKKP SMAKLQALKA KNNNFANKTE
YSAANSTTDT KVNIDDLLQE FETKNDNTQI GDKRSLDSDI ESENLFSKKL RFMSQPQVLE
IDNNSVIEQK ADQDIEEFFA SDNNDDNTET DQIVKTEIEI EKTKPNVTSI LKTAKEEIIK
NDEQEQYDED GDAMFEKTPE ILTPTTVKVS TDNLFTDDES FNSFYYMDYL EENNKLLLFG
KMKLQNSTYK SCMIQINNLG KELYFLPKDG VTVPELAEQC YDNLLAHYGV DSLRTKNMKK
KYAFELQGIP RGKTSYLKVY VPFDCKKNGN NGRALPLETL TNGLAKIVFG NYNKIFESFT
LQKQVMGPSW LKLKNLKQSN SNKSNCALCF EIDNIDEDLF TDVNNLEVPT FKSMTLRTQQ
LLTVSQKQEL VTISYSIDND FKLINNSNEK KNIKNKTITL VRLLDEASCF TPIFKKKLNE
KYDNEFRFFN DEKTMLTAFM NIVKMNDPDF LLGHRLEQVE LDILINRLIT LNIKNFSNIG
RFQRANFPNY FSGNSKFKNS LITGGRMIVD IGNELGISLT PKCDTWDLNE MYNLYSDNKN
EVTPLEINMQ SLQHSESETL WEQALLSTRG DIDLIFKLVD NLQIIPLSLQ LTNLAGNGWR
QTLQGSRAIR NEYILLHEFT KLRYIVPDPY MRPQQQANST ANNKKSSFQG GLVFEPEKGL
HKHFTLVMDF NSLYPSIIQE FNICFTTVER NAFLTPLDGI TETKKVKEGD DENEDKEKDV
EEVLPEYPSK QDHKLGVLPK LLHTLVERRK AVKSLMATTT DPAKKSQYDI KQQALKLTAN
SMYGCLGFKQ SRFYAKPLAM MITNKGREIL QHTRQLAENN ANLQVVYGDT DSVMINSRCD
DYADAIKIGE NFKQLVNKQY GSLEIDIDNV FQRLLLTAKK KYAALNCYWD KNANELKTKL
EVKGLDMKRR EYCPLTKKTS EDVLNLLLSD KDEEESLNSI YDLLEDISTN LIENNIPLDQ
FKINTRLGKN PEEYGNGGKN MPAVQAAMRL KKDGRQVRQG TVITFVIVEN EDTENSNEKE
KSSSTSVASR AIPLREVMRK RDKYKIDSDF YLEKQLLNPI KRLLENIEGF DIKRFAESLR
ISSQKFSGSI GNGATFYSNT ISMNDGGEIM QSLDSMKSDS ERFSNCENLK INCSNCGHLF
EFHGIVRSPD YKVTNHGIKC MLCQTSISTL SLMAQLEVRT RAQITKYYET PYECDDSSCD
CKTYGLGVYG KKCLNSDCYG GTLSKRQFND KLLYNQLCYF QSLFDFERNK KQQLRILDTV
VEGGNIGVNP YLLDKSESRR LAESLKESIL LKGYDIMEGY LEINGRRYVD LSLIFF
//
