Protein data for DPO4_NEIMB:

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

Molecular weight: 35966

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-OCT-2000, sequence version 1.
07-MAR-2006, entry version 33.

Phylogenetic order:
Bacteria Proteobacteria Betaproteobacteria Neisseriales Neisseriaceae Neisseria.

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_NEIMB:

DatabasePointerAdd. info#1Add. info#2
EMBLAE002098AAF41808.1-
PIRA81083A81083.
HSSPP960221IM4
GenomeReviewsAE002098_GRNMB1448.1
TIGRNMB1448-.
BioCycNMEN491:NMB1448-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=MC58 / Serogroup B;
RX MEDLINE=20175755; PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C.,
RA Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F.,
RA Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D.,
RA Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D.,
RA Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E.,
RA Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M.,
RA Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M.,
RA Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R.,
RA Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).

Feature:
CHAIN 1 318 DNA polymerase IV.
/FTId=PRO_0000173929.
DOMAIN 6 186 UmuC.
ACT_SITE 105 105 By similarity.
METAL 10 10 Magnesium (By similarity).
METAL 104 104 Magnesium (By similarity).
SITE 15 15 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: 318

     MSSRKIIHID MDAFYASVEL REQPHLKGRP VVVAWEGARS VICAASYEAR QFGLHSAMSV
     ATAKRLCPQA VYVPPHFDLY RQVSAQIHAV FRRYTDLIEP LSLDEAYLDV TRNFKNIPYA
     GDVAKEIRAA IFAETGLTAS AGIAPNKFLA KIASDWRKPN GQFVLPPHKV MAFLETLPLG
     KIPGVGKVTL KKMQSLGMRT AGDLRRFERG ELLNHFGRYG YRLYDLVRGT DERPVKAERE
     RLQISTEITL PEDLPLEQAA GHLPHLAEDL WRQITRKNVE AQSVTLKLKT YDFRIITRTL
     TYSSVLPDCA LCCRLRKC