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Description:
DNA polymerase IV (EC 2.7.7.7) (Pol IV).
Molecular weight: 40438
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-JUN-2001, sequence version 1.
07-MAR-2006, entry version 29.
Phylogenetic order:
Bacteria Firmicutes Lactobacillales Streptococcaceae Lactococcus.
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_LACLA:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE006432 | AAK06127.1 | - |
| PIR | E86878 | E86878. | |
| HSSP | P96022 | 1IM4 | |
| GenomeReviews | AE005176_GR | LL2029.1 | |
| BioCyc | LLAC1360:L0305-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=IL1403;
RX MEDLINE=21235186; PubMed=11337471; DOI=10.1101/gr.169701;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K.,
RA Weissenbach J., Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
Feature:
CHAIN 1 363 DNA polymerase IV.
/FTId=PRO_0000173917.
DOMAIN 14 197 UmuC.
ACT_SITE 116 116 By similarity.
METAL 18 18 Magnesium (By similarity).
METAL 115 115 Magnesium (By similarity).
SITE 23 23 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: 363
MLTFPLINDT SRKIIHIDMD AFFASVEVRD NPSLKVKPVV IARNPLQTGG RGVVSTCSYE
ARAFGIHSAS AKEAYDLCPQ AIFISGNYEK YTKVSKQVRE IFKRYTDDIE AASIDEAYLD
VTENKIGAQS AIKIAKLIQH DIFVELGLTC SAGVSYNKFL AKIASDYEKP HGLTLIMPEE
ALEFLAKLPV EKFHGVGKAT VPKLHALGFF NGGDLQKADP VDLAERFGVY GWELYQKANG
IHNSKVKNYR ERKSVGKERT YGKLLYLPDD IKAELSKISG KVSDSLKSHQ LKGSIVILKL
RYSDFTTLTK RKSLAEKLES PEEIAEVAQE IFEELEYDES LGVRLLGVTV TEFGAQKATL
DMQ