(data stored in ACNUC7421 zone)

HOGENOM: COLP3_1_PE1007

ID   COLP3_1_PE1007                       STANDARD;      PRT;   352 AA.
AC   COLP3_1_PE1007; Q487H6;
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   (COLP3_1.PE1007).
GN   Name=dinB; OrderedLocusNames=CPS_1040;
OS   COLWELLIA PSYCHRERYTHRAEA 34H.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS COLP3_1.PE1007.
CC       Colwellia psychrerythraea 34H chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:DPO4_COLP3
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; Q487H6; -.
DR   EMBL; CP000083; AAZ27501.1; -; Genomic_DNA.
DR   RefSeq; YP_267789.1; NC_003910.7.
DR   HSSP; Q9UNA4; 2ALZ.
DR   ProteinModelPortal; Q487H6; -.
DR   STRING; Q487H6; -.
DR   GeneID; 3521759; -.
DR   GenomeReviews; CP000083_GR; CPS_1040.
DR   KEGG; cps:CPS_1040; -.
DR   NMPDR; fig|167879.3.peg.1007; -.
DR   TIGR; CPS_1040; -.
DR   eggNOG; COG0389; -.
DR   OMA; VICAASY; -.
DR   BioCyc; CPSY167879:CPS_1040-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   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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   SMART; SM00278; HhH1; 1.
DR   SUPFAM; SSF100879; DNA_pol_Y-fam_little_finger; 1.
DR   PROSITE; PS50173; UMUC; 1.
DR   HOGENOMDNA; COLP3_1.PE1007; -.
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   352 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGNQKKIIHI DMDCFYAAIE MRDFPEYQNI PLAVGGDGPR SVLCTSNYQA RQFGVRSAMP
     AIKAKQLCPH LKIVHGRMDV YKETSKNIRE IFSRYTDLIE PLSLDEAYLD VTDATMCQGS
     ATLIAERIRA DIFNELNLTA SAGIAPNKFL AKIASDENKP NGQCVITPDK VANFVEQLSL
     KKIPGIGPKT FEKLNRHGYV TCADVRQSNI RALQNIVGKF ANSLYLKSHG VDNRDLEVSR
     QRKSLAIETT LAHDISTQDE CKLVIDSLYQ KLLTRLAPHS NREIIRQGVK LKFTDFNQTT
     VETQSNECQQ ALFISLLSKA YSRSNKRGVR LVGLTLGFAD SPGESQQLSL SL
//

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