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Description:
DNA polymerase IV (EC 2.7.7.7) (Pol IV).
Molecular weight: 41025
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 Firmicutes Clostridia Clostridiales Clostridiaceae Clostridium.
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_CLOPE:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | BA000016 | BAB81272.1 | - |
| HSSP | P96022 | 1K1S | |
| GenomeReviews | BA000016_GR | CPE1566.1 | |
| BioCyc | CPER1502:CPE1566-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=13 / Type A;
RX MEDLINE=21664373; PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A.,
RA Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic
RT flesh-eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
Feature:
CHAIN 1 359 DNA polymerase IV.
/FTId=PRO_0000173910.
DOMAIN 7 188 UmuC.
ACT_SITE 107 107 By similarity.
METAL 11 11 Magnesium (By similarity).
METAL 106 106 Magnesium (By similarity).
SITE 16 16 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: 359
MKENRKIIHI DMDAFYASIE QRDNPKYKGK PLIVGGDPNR RGVVATCSYE ARKYGIHSAM
PSLTAYKLCP KAIFIRPRME VYKKVSRQVM NILNEYSNIV EPLSLDEAFV DVSKSKRCKG
SATLIALEIK ERIFKEVGLT ASAGVSFNKF LAKMASDFRK PDGITVITEE NSKDFIRKLP
IGKFFGVGRV TKNKLNNIGV FKGEDLLGFS EKELIGILGD RGKILYEFAR GIDNRQVNPY
RIRKSIGKEI TLREDIEDIE EMIEILEKIS ERVSESLCLL NKKGKTVTLK VKFNDFKHIT
RSITLEHFLK EQKEIMECVK DLISIVDFKN KKVRLLGITI SSLEENIITE EREQLSFDV