(data stored in SCRATCH3701 zone)

SWISSPROT: D5E9N7_METMS

ID   D5E9N7_METMS            Unreviewed;       363 AA.
AC   D5E9N7;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 55.
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=Mmah_0356 {ECO:0000313|EMBL:ADE35888.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35888.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35888.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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. {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:11130,
CC         Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:83828; EC=2.7.7.7; Evidence={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|HAMAP-Rule:MF_01113}.
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DR   EMBL; CP001994; ADE35888.1; -; Genomic_DNA.
DR   RefSeq; WP_013036831.1; NC_014002.1.
DR   EnsemblBacteria; ADE35888; ADE35888; Mmah_0356.
DR   GeneID; 8982490; -.
DR   KEGG; mmh:Mmah_0356; -.
DR   eggNOG; arCOG04582; Archaea.
DR   eggNOG; COG0389; LUCA.
DR   HOGENOM; HOG000082707; -.
DR   KO; K04479; -.
DR   OMA; DMQSFYA; -.
DR   OrthoDB; 55139at2157; -.
DR   BioCyc; MMAH547558:G1GHT-352-MONOMER; -.
DR   Proteomes; UP000001059; 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-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-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR   Gene3D; 3.30.1490.100; -; 1.
DR   HAMAP; MF_01113; DNApol_IV; 1.
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; IPR001126; UmuC.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   SUPFAM; SSF100879; SSF100879; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9N7.
DR   SWISS-2DPAGE; D5E9N7.
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:ADE35888.1}; 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:ADE35888.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01113, ECO:0000313|EMBL:ADE35888.1}.
FT   DOMAIN          5..193
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   COILED          311..331
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   METAL           9
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   METAL           110
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   SITE            14
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ   SEQUENCE   363 AA;  40439 MW;  DDBA115BB862B6C1 CRC64;
     MSRIVVHVDM DYFYAAVEER EDPSLRGRSV VVCMYSGRGE HRGSVSTSNY TARKYGIKSG
     MPCSRAIKLN QDAVFLPVRK EFYTEVSDSI MEVLRSHADS DESFEQISID EAFIEVTANC
     NDDFECALKL GEDIKQKILE KEQLTCSVGI GPNKLIAKMA SSENKPNGIT VISQHDVKPF
     LEDRTPSQLW GVGDVTAGRL EQMGIKKVGQ LASSDIVSLT DAFGKKKGSW LKKAAQGMDE
     SPVRQREGSE QIGRIATLPE NSSEYDLIMP VLDNLADDVI RKTIERGVSF RQVTLIVITS
     DFKTQTRNHT LQRAVAEKEI LRSNLDKLLT TFLEENKSAI RRIGVRVAGL QEVSSQTTLA
     SYF
//

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