Description:
DNA polymerase IV (EC 2.7.7.7) (Pol IV).
Molecular weight: 40892
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-2002, sequence version 1.
07-MAR-2006, entry version 29.
Phylogenetic order:
Archaea Euryarchaeota Methanomicrobia Methanosarcinales Methanosarcinaceae Methanosarcina.
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_METAC:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE011115 | AAM07376.1 | - |
| HSSP | P96022 | 1K1Q | |
| GenomeReviews | AE010299_GR | MA4027.1 | |
| BioCyc | MACE188937:MA4027-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=C2A / ATCC 35395 / DSM 2834;
RX MEDLINE=21929760; PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P.,
RA FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A.,
RA Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R.,
RA Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W.,
RA Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M.,
RA Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A.,
RA Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K.,
RA Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C.,
RA Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T.,
RA Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E.,
RA Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic
RT and physiological diversity.";
RL Genome Res. 12:532-542(2002).
Feature:
CHAIN 1 366 DNA polymerase IV.
/FTId=PRO_0000173970.
DOMAIN 6 197 UmuC.
ACT_SITE 115 115 By similarity.
METAL 10 10 Magnesium (By similarity).
METAL 114 114 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 (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: 366
MMQRVIIHVD MDYFYAAIEE REKPELLGKA VVVCMLSGRS ELSGSVSTCN YIAREFGIRS
GMPCSRAKKL NPEAVFLPVR KEFYTSVSDR IMEILRSYAD PGENGDSFEQ ISVDEAFLEI
TYRAGGDFNL AFELGMQIKK EIKEKENLTC SIGIGPNKLI AKMASSAKKP DGITVVSPEN
QEAFLWPLKV SKLWGIGDVT AKKLQEMDIV TVKDLAEHDV IELISTFGKS RGTWLKQAAS
GIDDSPLKER EGSEQIGRIA TLPEDTLDQE LILSLLEKLA GDVIEKLDSR ELSFRVVTVT
VINSNFRTYT KSRTLNHPVS SKETLLEAAR EILSEFLSES KTEFRRVGVR VGGLQKKKGQ
TSLFDY