(data stored in ACNUC7421 zone)

HOGENOM: DEHSV_1_PE10

ID   DEHSV_1_PE10                         STANDARD;      PRT;   391 AA.
AC   DEHSV_1_PE10; D2BJX9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=DNA polymerase IV; Short=Pol IV; EC=2.7.7 7;
DE   (DEHSV_1.PE10).
GN   Name=dinP; Synonyms=dinB; OrderedLocusNames=DhcVS_10;
OS   DEHALOCOCCOIDES SP. VS.
OC   Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoides.
OX   NCBI_TaxID=311424;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DEHSV_1.PE10.
CC       Dehalococcoides sp. VS chromosome, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D2BJX9_DEHSV
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, in conjunction with
CC       the beta clamp from polIII (By similarity).
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1).
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC   -!- SIMILARITY: Contains 1 umuC domain.
CC   -!- GENE_FAMILY: HOG000082707 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D2BJX9; -.
DR   EMBL; CP001827; ACZ61191.1; -; Genomic_DNA.
DR   RefSeq; YP_003329519.1; NC_013552.1.
DR   ProteinModelPortal; D2BJX9; -.
DR   GeneID; 8656969; -.
DR   GenomeReviews; CP001827_GR; DhcVS_10.
DR   KEGG; dev:DhcVS_10; -.
DR   OMA; AIGAWIR; -.
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:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:HAMAP.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:HAMAP.
DR   HAMAP; MF_01113; DNApol_IV; 1; -.
DR   InterPro; IPR017962; DNA_pol4/DinB_little_finger.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR001126; DNA_repair_prot_UmuC-like.
DR   InterPro; IPR017963; DNA_repair_prot_UmuC-like_N.
DR   InterPro; IPR022880; DNApol_IV.
DR   Gene3D; G3DSA:3.30.1490.100; DNA_pol4/DinB_little_finger; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   SUPFAM; SSF100879; DNA_pol_Y-fam_little_finger; 1.
DR   PROSITE; PS50173; UMUC; 1.
DR   HOGENOMDNA; DEHSV_1.PE10; -.
KW   DNA polymerase IV (Y-family);
KW   Complete proteome; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW   DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding;
KW   Mutator protein; Nucleotidyltransferase; Transferase.
SQ   SEQUENCE   391 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MMAIRRVMHA DLDAFFVSVE QAIRPELKGK PVIVGGKPER RGVVAAASYE ARKLGIHSGM
     PLLTAKHLCP QAIFIEGTHQ LYREYSEKFM QILADFSPFL EPMGLDEAYL EVTGFESLHG
     SIGEMACKIR RRITAELGIN ASIGIANSKV VAKIATEHAK PNGQCEVPAG EEAAFLAPLD
     ISVMPGIGKK TEQHLKSLGI DTLGKLAAPP ASFLKSSLGA YAPYLSNAAK GIDNRPVEMP
     AEAKSISRET TFETDTRNHT FLEAKLGYLS EKIAATLRKR GKQVRVVQIK IRFADFTTLT
     RQKHLNHPCS GNREIFQTAL TLMNNLLTSD RQAVRLLGVG ISDFCGPEKQ LELDPARARL
     EKLDASLDKI RQKYGFGSVQ TGRTYKLKDM F
//

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