UniProt: A0A1W0W7Q9

Database: UniProt
Entry: A0A1W0W7Q9_SORBI

LinkDB:  A0A1W0W7Q9_SORBI 
Original site:  A0A1W0W7Q9_SORBI

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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (2)   
   PubMed (2)   
All databases (30)   

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ID   A0A1W0W7Q9_SORBI        Unreviewed;      1796 AA.
AC   A0A1W0W7Q9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=SORBI_3002G409700 {ECO:0000313|EMBL:OQU90438.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:OQU90438.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:OQU90438.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         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|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; CM000761; OQU90438.1; -; Genomic_DNA.
DR   STRING; 4558.A0A1W0W7Q9; -.
DR   EnsemblPlants; OQU90438; OQU90438; SORBI_3002G409700.
DR   Gramene; OQU90438; OQU90438; SORBI_3002G409700.
DR   InParanoid; A0A1W0W7Q9; -.
DR   OMA; CYSELRG; -.
DR   Proteomes; UP000000768; Chromosome 2.
DR   ExpressionAtlas; A0A1W0W7Q9; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IBA:GO_Central.
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; IBA:GO_Central.
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:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR   CDD; cd05778; DNA_polB_zeta_exo; 1.
DR   CDD; cd05534; POLBc_zeta; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 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; IPR042087; DNA_pol_B_thumb.
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; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 2.
DR   Pfam; PF14260; zf-C4pol; 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|RuleBase:RU000442};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
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   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          121..197
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          920..1117
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1184..1631
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1696..1769
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          543..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1796 AA;  199425 MW;  B732EDD5F492D317 CRC64;
     MSSSQSPEPC TPGTPSPVLS VRIVSLDYYM APPLPGFGFS RSPFHGDGVE EVPVVRIYGS
     TPAGQKTCLH IHRVLPYFYI PCPEELLDNL EKGDSYITGL LSALEKALQA RGPSKRKHVH
     GCNLVRAKKL YGYHSSEELF MKIYLYYPHE VSRAASLVLS GAVSNRAFQP YESHIPYLLH
     FLVDYNLYGM GHIHVKDFKF RPPLPDDFHP KSSLHRKAQS DNLEIKSPTV WISSTVSHSS
     TLGSSAPSLH LGGTNLSFTI RQSSSMLEAD SRIEGILNEK YKMYTSLSQT TEDTKMVQSL
     EAIWEELERL RLLDETKYAD LGRPLREEVL KDFLHGIKYE SALSVLFSQE GPHHKVSTIE
     ESERLERCLK SLTDIIGTVT FSQDDYCGHI DVGNSADVQN GKPNASLCSG SLEQNMQIIS
     PERNSEYPVS SSVPQRTLSQ LSDEGEKHVD AEALGLLSWL ASSQAAEEPT TDDELINEVI
     LSPLFAKKSI EVALESAHLD FDSASQQECQ DILDSVDPVR EAEEPNLHTS YLDSVKSSSA
     ASLGKTIPQV DGSSDENPKV SQECDRSKVT RKAVVSPCYT STKNPSKSAS KRAGTEHLWG
     SLPLSRKKRQ HGDADDSCSA MPSQKALSAS NKSTIDKDYH DTIGSTDKES SRFLGVHDSV
     CHSVRDLMRR RRSFRCEQLE FGCSGAATCT MDNESETVNS GGLEFHDFTS DIPNLALTRM
     AFVQKPPSKN DACSGLESRS GCEQRGSEKL GVADLLPFFN QNMEENKQNE SFQHMESNDF
     TGDVLGVPTH FQNDGSALYL LTHALSPPSA GAVSHWLTQE SSSSIFSGYT NYDEGVPADK
     EEAHSSTLSR NSPTRFTKEN SAKNIFVHGD VMESALSNKE SKHLDEWHDF SQISAGNEKD
     KLTPLSQIGF RDPASIGGGQ QLTILSMEVL TESRGELRPD PRFDAINAVS LAIEDDADNT
     VDVHVFICDN NSKSHRRNLD GIAGYNVDVF PEEKDLLNNF ISAVCSIDPD ILVGWEIQLG
     SLGFLAERAA YLGIGLLKRI SRTPPHELNH PPKIPVDNSS QVLSETSSAD DIIDDVSEND
     WSHTHASGIH VGGRIVLNLW RLMRAEVKLN NYSLEAVADE VLRRKIPLIP SRILNRWFAT
     GPGRGRHRCI EYISNRTRIN LEIMNQLDLV NRTSELARVF GIDFFSVLSR GSQYRVESML
     LRLAHTQNYL AISPGNQQVA SQPAMECLPL VMEPESAFYP DPVVVLDFQS LYPSMIIAYN
     LCYSTCLGKV FPSKSNVLGV SSYSADPHTL VDLKNQLLLT PNGVLYVQPK IRKGVLPRLL
     EEILSTRIMV KQAMKKLSPS QQVLHRIFNA RQLALKLIAN VTYGYTAAGF SGRMPCAELA
     DSIVQCGRRT LETAISFVNQ HPLWKARVVY GDTDSMFVLL KGRSREEAFR IGKEIASSIT
     AMNPDPVTLK FEKVYQPCFL LTKKRYVGYS YESPEQNEPI FDAKGIETVR RDTCPAVAKI
     LERSIRTMFE EQDLTKVRTY LERQWTRILS GKVSIQDFIF AKEVRLGTYS ARASTLPPAA
     IVATKAMLSD PRAEPRYAER VPYVVIHGEP GARLADMVID PYGLLENGSP YRLNEQYYIT
     KQIIPALQRV FGLLGADLNK WFNEMPRPIR PTLAKRQSAA GHGSFSRDGS FIRLGLNNKA
     LGKAGRIDTY YMSSHCSICG DIIQGTETFC NNCLKNEAVV ATIVAGRTSK LEREIQHLAA
     ICGHCGGADW IIESGIKCVS LACPVFYERR KVQRELGVVS ESAEAGYYPF CCAELF
//

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