Protein data for DPO4_CORGL:

Description:
DNA polymerase IV (EC 2.7.7.7) (Pol IV).

Molecular weight: 50688

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:
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
19-OCT-2002, sequence version 1.
07-MAR-2006, entry version 26.

Phylogenetic order:
Bacteria Actinobacteria Actinobacteridae Actinomycetales Corynebacterineae Corynebacteriaceae Corynebacterium.

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_CORGL:

DatabasePointerAdd. info#1Add. info#2
EMBLBA000036BAB99537.1-
EMBLBX927154CAF20484.1-
HSSPP960221IM4
GenomeReviewsBX927147_GRcg2355.1
GenomeReviewsBA000036_GRCgl2144.1
BioCycCGLU196627:NCGL2064-MONOMER-.1
HAMAPMF_01113-1.
InterProIPR001126UMUC_like.
PfamPF00817IMS1.
PROSITEPS50173UMUC1.

General information about the databases mentioned above

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=ATCC 13032 / DSM 20300 / NCIB 10025;
RA Nakagawa S.;
RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / NCIB 10025;
RX MEDLINE=22830012; PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT and its impact on the production of L-aspartate-derived amino acids
RT and vitamins.";
RL J. Biotechnol. 104:5-25(2003).

Feature:
CHAIN 1 467 DNA polymerase IV.
/FTId=PRO_0000173911.
DOMAIN 5 187 UmuC.
ACT_SITE 105 105 By similarity.
METAL 9 9 Magnesium (By similarity).
METAL 104 104 Magnesium (By similarity).
SITE 14 14 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: 467

     MQRWVLHIDM DAFFASCEQL TRPTLRGRPV LVGGVSGRGV VAGASYEARK FGARSAMPMH
     QAKARVGFGA VVVTPRHIVY SAASRRVFQI VEKRAGIVER LSIDEGFMEP EALVGATPEE
     VKQWAEELRA EIKEVTGLPS SVGAGSGKQI AKIGSGEAKP DGVFVVPVDK QHDLLDPLPV
     GALWGVGPVT GSKLASMGVE TIGDLAALTQ KEVEISLGAT IGISLWNLAR GIDDRPVEPR
     AEAKQISQEH TYEKDLLTRQ QVDAAIIRSA EGAHRRLLKD GRGARTVSVK LRMADFRIES
     RSYTLSYATD DYATLEATAF RLARYPGEVG PIRLVGVSFS GLEESRQDIL FPELDQQIIV
     PPAPDTDYEV GVQSSSSSES TQVEAPQDVA LSMWCATQDV YHPEYGHGWV QGAGHGVVSV
     RFETRSTTKG RTKSFSMDDP DLTPADPLDS LDWADWFAEN GETGDDE