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Database: UniProt
Entry: M0WW12_HORVV
LinkDB: M0WW12_HORVV
Original site: M0WW12_HORVV 
ID   M0WW12_HORVV            Unreviewed;      1001 AA.
AC   M0WW12;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   05-JUN-2019, entry version 47.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS   Hordeum vulgare subsp. vulgare (Domesticated barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=112509 {ECO:0000313|EnsemblPlants:HORVU2Hr1G020260.34, ECO:0000313|Proteomes:UP000011116};
RN   [1] {ECO:0000313|EnsemblPlants:HORVU2Hr1G020260.34, ECO:0000313|Proteomes:UP000011116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Morex {ECO:0000313|EnsemblPlants:HORVU2Hr1G020260.34}, and
RC   subsp. vulgare {ECO:0000313|Proteomes:UP000011116};
RX   PubMed=23075845; DOI=10.1038/nature11543;
RG   The International Barley Genome Sequencing Consortium;
RT   "A physical, genetic and functional sequence assembly of the barley
RT   genome.";
RL   Nature 491:711-716(2012).
RN   [2] {ECO:0000313|EnsemblPlants:HORVU2Hr1G020260.34}
RP   IDENTIFICATION.
RC   STRAIN=subsp. vulgare {ECO:0000313|EnsemblPlants:HORVU2Hr1G020260.34};
RG   EnsemblPlants;
RL   Submitted (OCT-2017) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|RuleBase:RU000442}.
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DR   EnsemblPlants; HORVU2Hr1G020260.16; HORVU2Hr1G020260.16; HORVU2Hr1G020260.
DR   EnsemblPlants; HORVU2Hr1G020260.27; HORVU2Hr1G020260.27; HORVU2Hr1G020260.
DR   EnsemblPlants; HORVU2Hr1G020260.34; HORVU2Hr1G020260.34; HORVU2Hr1G020260.
DR   EnsemblPlants; HORVU2Hr1G020260.43; HORVU2Hr1G020260.43; HORVU2Hr1G020260.
DR   Gramene; HORVU2Hr1G020260.16; HORVU2Hr1G020260.16; HORVU2Hr1G020260.
DR   Gramene; HORVU2Hr1G020260.27; HORVU2Hr1G020260.27; HORVU2Hr1G020260.
DR   Gramene; HORVU2Hr1G020260.34; HORVU2Hr1G020260.34; HORVU2Hr1G020260.
DR   Gramene; HORVU2Hr1G020260.43; HORVU2Hr1G020260.43; HORVU2Hr1G020260.
DR   Proteomes; UP000011116; Unassembled WGS sequence.
DR   ExpressionAtlas; M0WW12; baseline.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 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; IPR042087; DNA_pol_B_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; PTHR45812; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011116};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011116};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      114    323       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      390    837       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN      900    973       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      242    275       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M0WW12}.
FT   COMPBIAS    254    268       Polar. {ECO:0000256|MobiDB-lite:M0WW12}.
SQ   SEQUENCE   1001 AA;  111580 MW;  7DC79CA125F426B5 CRC64;
     MHFHRHLQQL WASGYLNTLL LIVSQEIEHH PTSRPHAEAL AFMANSPVPG SASEHTTAAF
     IDTVMMKSDQ SNKENEKLDD WHDFSQISAE DEKHKLTPLS QIGFRDPAST GGGQQLTILS
     IEVFAESRAD LRPDPRFDAI NVVSLAVEDD GDNTVEVRVL IRGNNDKLHG RRNLDGVIGC
     SVDVFPEEKD LLNHLIGALC SIDPDILVGW EIQLGSLGFL AERAAYLGIG LLKRISRTLP
     HESKHPPKNL AHESSQAPPK NLAHESSQAP EASPADDVIV DVSENDWSHT HASGVHVGGR
     IVLNLWRLMR GEVKLNNYSL EAVADEVLRR KVPLVPTKTL NRWFATGPGR GRHRCIEYVS
     SRAMLNLEII NQLDLVNRTS ELARVFGIDF FSVLSRGSQF RVESMLLRLA HTQNYLAISP
     GNQQVASQPA MECMPLVMEP ESAFYSDPVL VLDFQSLYPS MIIAYNLCYS TCLGKVFPSK
     SSVLGVSSYS ADPHTITDLK NQLLLTPNGV LYVQPEVRKG VVPRLLEEIL STRIMVKQAM
     KKLAPSQKVL QKILNARQLA LKLIANVTYG YTAAGFSGRM PCAELADSIV QCGRRTLETA
     ISFVNQHPLW NARVVYGDTD SMFVLLKGRS REEAFRIGKE IASLVTAINP DPVTLKFEKV
     YHPCFLLTKK RYVGYSYENP EQNEPIFDPK GIETVRRDTC PAVAKMLERS LRIMFEEQDL
     VKVKSYVERQ WTRILSGKIS IQDFVFAKEV RLGTYSARAS SLPPAAIVAT KAMLSDPRAE
     PRYAERVPYV VIHGEPGARL VDMVIDPYGL LQVGSPYRLN ELYYITKQII PALQRVFGLL
     GVNLNKWFNE MPRPTRSTLA KRQSAFGHGS RDSSSIRLGW NKKPSAKVAR IDTYYMSSHC
     TICGDTVQGS ETFCSYCLKN EAVVATVVAG RTSKLEREIQ HLAAICGHCG GADWIVESGV
     KCVSLACPVF YERRKIQKEL RVVSESAGEA GYYPFCCVEL F
//
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