(data stored in ACNUC7421 zone)

HOGENOM: DEHSB_1_PE10

ID   DEHSB_1_PE10                         STANDARD;      PRT;   390 AA.
AC   DEHSB_1_PE10; A5FSS1;
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   (DEHSB_1.PE10).
GN   Name=dinB; OrderedLocusNames=DehaBAV1_0010;
OS   DEHALOCOCCOIDES SP. BAV1.
OC   Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoides.
OX   NCBI_TaxID=216389;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DEHSB_1.PE10.
CC       Dehalococcoides sp. BAV1, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:DPO4_DEHSB
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; A5FSS1; -.
DR   EMBL; CP000688; ABQ16602.1; -; Genomic_DNA.
DR   RefSeq; YP_001213480.1; NC_009455.1.
DR   ProteinModelPortal; A5FSS1; -.
DR   STRING; A5FSS1; -.
DR   GeneID; 5131175; -.
DR   GenomeReviews; CP000688_GR; DehaBAV1_0010.
DR   KEGG; deb:DehaBAV1_0010; -.
DR   eggNOG; COG0389; -.
DR   OMA; AIGAWIR; -.
DR   ProtClustDB; CLSK836830; -.
DR   BioCyc; DSP216389:DEHABAV1_0010-MON; -.
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-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; DEHSB_1.PE10; -.
KW   DNA-directed DNA polymerase;
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   390 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSIRRVMHVD LDAFFVSVEQ AVRPEFKDKP VIVGGKPERR GVVAAASYEA RKFGIHSGMP
     LITAKHLCPQ AIFIEGNHQL YREYSEKFML ILSDFSPFLE PMGLDEAYLE VTGFESLHGS
     IAQMASKIRR RITAELGINA SIGIANSKVA AKIATEQAKP NGQCEVPAGE EASFLAPLDI
     AVMPGIGKKT EQHLKSLGID TLGKLAALPA SFLKSCLGTY APYLSNAAMG IDNRPVEMPS
     EAKSISRETT FETDTRNQTF LEAKLSYLSE KITATLRKRG KQTRVVQIKI RFADFTTLTR
     QKHLGQPASG NREIFQTALS LMNGILDSDR QAVRLLGVGI SDFCGPEKQL EIDPAKARLE
     KLDASLDKIR QKYGFSSVQT GRTYRLKDMF
//

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