(data stored in ACNUC7421 zone)

SWISSPROT: C4KKS4_SULIK

ID   C4KKS4_SULIK            Unreviewed;       352 AA.
AC   C4KKS4;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
DE   RecName: Full=DNA polymerase IV {ECO:0000256|HAMAP-Rule:MF_01113};
DE            Short=Pol IV {ECO:0000256|HAMAP-Rule:MF_01113};
DE            EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_01113};
GN   Name=dbh {ECO:0000256|HAMAP-Rule:MF_01113};
GN   OrderedLocusNames=M164_0255 {ECO:0000313|EMBL:ACR40889.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40889.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40889.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved
CC       in untargeted mutagenesis. Copies undamaged DNA at stalled
CC       replication forks, which arise in vivo from mismatched or
CC       misaligned primer ends. These misaligned primers can be extended
CC       by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity.
CC       May be involved in translesional synthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_01113}.
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1). {ECO:0000256|HAMAP-Rule:MF_01113}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01113};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01113};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01113}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC       {ECO:0000256|HAMAP-Rule:MF_01113}.
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DR   EMBL; CP001402; ACR40889.1; -; Genomic_DNA.
DR   RefSeq; WP_012718352.1; NC_012726.1.
DR   EnsemblBacteria; ACR40889; ACR40889; M164_0255.
DR   GeneID; 7813363; -.
DR   KEGG; sid:M164_0255; -.
DR   HOGENOM; HOG000082707; -.
DR   KO; K04479; -.
DR   OMA; DMQSFYA; -.
DR   OrthoDB; POG093Z0779; -.
DR   BioCyc; SISL426118:GI01-257-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP.
DR   CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR   Gene3D; 3.30.1490.100; -; 1.
DR   HAMAP; MF_01113; DNApol_IV; 1.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR022880; DNApol_IV.
DR   InterPro; IPR024728; PolY_HhH_motif.
DR   InterPro; IPR001126; UmuC.
DR   PANTHER; PTHR11076:SF45; PTHR11076:SF45; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF11798; IMS_HHH; 1.
DR   SUPFAM; SSF100879; SSF100879; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KKS4.
DR   SWISS-2DPAGE; C4KKS4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01113};
KW   DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000313|EMBL:ACR40889.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Mutator protein {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000313|EMBL:ACR40889.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01113,
KW   ECO:0000313|EMBL:ACR40889.1}.
FT   DOMAIN        3    187       UmuC. {ECO:0000259|PROSITE:PS50173}.
FT   ACT_SITE    106    106       {ECO:0000256|HAMAP-Rule:MF_01113}.
FT   METAL         7      7       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01113}.
FT   METAL       105    105       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01113}.
FT   SITE         12     12       Substrate discrimination.
FT                                {ECO:0000256|HAMAP-Rule:MF_01113}.
SQ   SEQUENCE   352 AA;  40290 MW;  8F22E5C3DD4A2750 CRC64;
     MIILFVDFDY FYAQVEEVLN PSLKGKPVVV CVFSGRFEDS GAVATANYEA RKFGIKAGIP
     IVEAKKILPN AVYLPMRKEV YQQVSNRIMK LLREYSEKIE IASIDEAYLD ISDKVKNYQD
     AYNLGLEIKN KILEKEKITV TVGISKNKVF AKIAADMAKP NGIKVIDDEE VKRLIGELDI
     ADIPGIGDIT AEKLKKLGVN KLVDTLRIEF DELKRIIGEA KAKYLFSLAR DEYNEPIRAR
     VRKSIGRIVT MKRNSRDLEE IKPYLFRAIE EAYYKLDKKI PKAIHVVAVT EDLDIVSRGR
     TFTHGISKET AYREAVRLLQ KILEEDERKI RRIGVRFSKF IEAIGLDKFF DT
//

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