GenomeNet

Database: UniProt
Entry: B5GFC4_STRSH
LinkDB: B5GFC4_STRSH
Original site: B5GFC4_STRSH 
ID   B5GFC4_STRSH            Unreviewed;       454 AA.
AC   B5GFC4;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=dinB {ECO:0000256|HAMAP-Rule:MF_01113};
GN   ORFNames=SSBG_02857 {ECO:0000313|EMBL:EDY45020.2};
OS   Streptomyces sp. (strain SPB074).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=465543 {ECO:0000313|EMBL:EDY45020.2, ECO:0000313|Proteomes:UP000002779};
RN   [1] {ECO:0000313|Proteomes:UP000002779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA   Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA   Galagan J., Nusbaum C., Birren B.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDY45020.2, ECO:0000313|Proteomes:UP000002779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces sp. strain SPB74.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved in
CC       untargeted mutagenesis. Copies undamaged DNA at stalled replication
CC       forks, which arise in vivo from mismatched or misaligned primer ends.
CC       These misaligned primers can be extended by PolIV. Exhibits no 3'-5'
CC       exonuclease (proofreading) activity. May be involved in translesional
CC       synthesis, in conjunction with the beta clamp from PolIII.
CC       {ECO:0000256|ARBA:ARBA00025589, ECO:0000256|HAMAP-Rule:MF_01113}.
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|ARBA:ARBA00024632, ECO:0000256|HAMAP-
CC         Rule:MF_01113};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-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|ARBA:ARBA00010945, ECO:0000256|HAMAP-Rule:MF_01113}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG770539; EDY45020.2; -; Genomic_DNA.
DR   AlphaFoldDB; B5GFC4; -.
DR   Proteomes; UP000002779; Unassembled WGS sequence.
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-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProt.
DR   CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.40.1170.60; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1.
DR   HAMAP; MF_01113; DNApol_IV; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR022880; DNApol_IV.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001126; UmuC.
DR   PANTHER; PTHR11076:SF33; DNA POLYMERASE KAPPA; 1.
DR   PANTHER; PTHR11076; DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   3: Inferred from homology;
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   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   Transferase {ECO:0000256|HAMAP-Rule:MF_01113}.
FT   DOMAIN          13..195
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   BINDING         111
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   SITE            22
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ   SEQUENCE   454 AA;  48252 MW;  311D9C45412EDBE4 CRC64;
     MREHRGVRRA PTVLHLDMDA FFAAAEQAAK PSLRGKAVVV GGLGPRGVVS TASYEARAFG
     VHSAMPTAQA RRLAPNAAYL FPRFTLYRSV SEQVMELLGA LSPLVEPLSL DEAFVDLEAG
     GVAFDAASAR AVGERLRADI KARTGLTGSV GLAASKMLAK IGSERAKPDG LVLIEPGTER
     ELLAPLSVRV LPGIGPATGD HLRRAGISTI GELAEAGEDE LVRLLGKTHG AGVYAMSLAR
     DERRVVAERE GKSVSVEDTY DLDIHDRVRV RAEVAALADR CVGRLRASGR SGRTVVLKVR
     RYDFSTLTRS ETLRAPTDDP AVVREAAARL LELVDTTGGV RLLGVGVSGL ADFTQEVLFA
     RTTAGEEHAP PPLAPAPVPV AAPELAPSLP PPPRWRPGQD VLHAAYGPGW VQGSGLGRVT
     VRFETPYDER PGRVRTFAVD DADLSAAEPL PLVR
//
DBGET integrated database retrieval system