Description:
DNA polymerase IV (EC 2.7.7.7) (Pol IV).
Molecular weight: 49267
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
07-MAR-2006, entry version 27.
Phylogenetic order:
Bacteria Proteobacteria Alphaproteobacteria Rhizobiales Brucellaceae Brucella.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein DPO4_BRUME:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE009700 | AAL53898.1 | - |
| PIR | AG3591 | AG3591. | |
| GenomeReviews | AE008918_GR | BMEII0656.1 | |
| BioCyc | BMEL29459:BMEII0656-MONOMER | -.1 | |
| HAMAP | MF_01113 | - | 1. |
| InterPro | IPR001126 | UMUC_like. | |
| Pfam | PF00817 | IMS | 1. |
| PROSITE | PS50173 | UMUC | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; DNA replication; DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding; Mutator protein; Nucleotidyltransferase; Transferase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / Biotype 1;
RX MEDLINE=20020109; PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen
RT Brucella melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
Feature:
CHAIN 1 445 DNA polymerase IV.
/FTId=PRO_0000173906.
DOMAIN 49 229 UmuC.
ACT_SITE 147 147 By similarity.
METAL 53 53 Magnesium (By similarity).
METAL 146 146 Magnesium (By similarity).
SITE 58 58 Substrate discrimination (By similarity).
Comments:
-!- FUNCTION: Poorly processive, error-prone DNA polymerase involved
in untargeted mutagenesis. Copies undamaged DNA at stalled
replication forks, which arise in vivo from mismatched or
misaligned primer ends. These misaligned primers can be extended
by polIV. Exhibits no 3'-5' exonuclease (proofreading) activity.
May be involved in translesional synthesis, in conjunction with
the beta clamp from polIII (By similarity).
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
-!- SUBUNIT: Monomer (By similarity).
-!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
-!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
-!- SIMILARITY: Contains 1 umuC domain.
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Sequence length: 445
MAESPIVNHP EQGLCRDCLS LQKTQTSRRC HACGSPRLIR HKELYRLSLA HVDCDAFYAS
VEKRDNPDLR DKPLIVGGGK RGVVSTACYL ARIHGVRSAM PMFKALEACP DAVVIKPNME
KYARVGREVR QMMRDLTPLV EPISIDEAFL DLSGTERLHK APPAVVLARF SKRVENEIGI
TASIGLSYCK YLAKVASDLE KPRGFSVIGE AEALDFLRDK PVGMIWGVGK AFAAKLESDG
IRTIGQLQTM EEGALMKAYG TMGQRLYRLS RGQDSRKVEP DHDMKSVSAE TTFNTDLSAA
GDLVPVLRAL SEKVSRRLKA GEIAGRTIVL KLKTQDFKLR TRNRQLGDPT QLADRIFRTG
LQLLEKEMDG TRFRLLGIGV SDLSPSDRAD PPDLVDIQAT KRAVAESAID RLRNKFGLNA
VETGYTFSKG NLARTQTPTD RDNEP