Description:
DNA polymerase IV (EC 2.7.7.7) (Pol IV).
Molecular weight: 39931
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 Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Xanthomonas.
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_XANAC:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE012012 | AAM38465.1 | - |
| HSSP | P96022 | 1IM4 | |
| GenomeReviews | AE008923_GR | XAC3622.1 | |
| 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=306 / ATCC 13902 / XV 101;
RX MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing
RT host specificities.";
RL Nature 417:459-463(2002).
Feature:
CHAIN 1 359 DNA polymerase IV.
/FTId=PRO_0000173966.
DOMAIN 4 184 UmuC.
ACT_SITE 103 103 By similarity.
METAL 8 8 Magnesium (By similarity).
METAL 102 102 Magnesium (By similarity).
SITE 13 13 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
MRKIVHVDMD AFYASVEQRD DPSLRGKPVV VAWRGARSVV CAASYEARIF GIRSAMPAVR
AERLCPDAIF VPPDFTRYKA VSRQVREIFH RHTDLVEPLS LDEAYLDVTH AKTGMQLATE
VAQLIRTQIR EETQLTASAG IAPNKFLAKI ASDWRKPDGQ FVIAPSRVDA FLLPLKVNRI
PGVGKVMDGK LAALGIVTVA DLRQRPLEEL QAHFGSFGQS LYRRARGIDE RPVEPDQEVQ
SVSSEDTFSE DLALDALAPH ILRLAEKTWL ATRRTERIGR TVVLKLKTSN FRILTRSYTP
EQPPTSQEAL AQIALALTRR VELPAQTRYR LVGVGLGGFS DVENGAVQGQ LFGQMPPLE