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Description:
DNA polymerase IV (EC 2.7.7.7) (Pol IV).
Molecular weight: 41391
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:
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
07-MAR-2006, entry version 17.
Phylogenetic order:
Bacteria Spirochaetes Spirochaetales Leptospiraceae Leptospira.
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_LEPIN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE011236 | AAN47702.1 | - |
| HSSP | P96022 | 1K1S | |
| GenomeReviews | AE010300_GR | LA0503.1 | |
| BioCyc | LINT189518:LA0503-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=56601 / Serogroup Icterohaemorrhagiae / Serovar lai;
RX MEDLINE=22598143; PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H.,
RA Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F.,
RA Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F.,
RA Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W.,
RA Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A.,
RA Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z.,
RA Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira
RT interrogans revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
Feature:
CHAIN 1 364 DNA polymerase IV.
/FTId=PRO_0000173920.
DOMAIN 8 189 UmuC.
ACT_SITE 108 108 By similarity.
METAL 12 12 Magnesium (By similarity).
METAL 107 107 Magnesium (By similarity).
SITE 17 17 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: 364
MIMETRKIIH VDMDAFYASV EQRDFPEYKG KPLIVGGPPN SRSVVSAASY EARKFGVRSA
MPCSKAAQLA PQAIFVFPRF EVYKEVSKQI REIFLEYTDL VEMLSLDEGY LDVTFNKKNI
PYAVTIAKEI RTEIFKRTEL TASAGVGNSK FISKLASEKN KPNGLTVVLP DDVISFIDPL
PVSSFHGVGK VTARKMKELG IYTGKDLRTK SIDELVQHFG KMGIYYYKIS RGEDERMVQS
SRERKSLGAE STFDRDKLDY DDLLKQLKDV AVVVERRLEK KDFAGKTLTL KIKFYDFSLK
TRSKTLSEPI FKADELYSTA IELFEEFFEI KYGKKSAIKA IRLLGISLSH PNSENEDPNL
FLNL