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Protein data for DPO1_HELPJ:

Description:
DNA polymerase I (EC 2.7.7.7) (POL I).

Molecular weight: 10243

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:
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
07-MAR-2006, entry version 39.

Phylogenetic order:
Bacteria Proteobacteria Epsilonproteobacteria Campylobacterales Helicobacteraceae Helicobacter.

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 DPO1_HELPJ:

DatabasePointerAdd. info#1Add. info#2
EMBLAE001559AAD06938.1-
PIRF71816F71816.
HSSPP198211CMW
GenomeReviewsAE001439_GRJHP1363.1
BioCycHPYL85963:JHP1363-MONOMER-.1
InterProIPR0025623_5_exonuclease.
InterProIPR0024215_3_exonuclease.
InterProIPR001098DNA_pol.
InterProIPR002298DNA_polI.
InterProIPR000513Exo_N_I.
InterProIPR008918HhH2.
PfamPF013675_3_exonuc1.
PfamPF027395_3_exonuc_N1.
PfamPF00476DNA_pol_A1.
PRINTSPR00868DNAPOLI.
SMARTSM0047435EXOc1.
SMARTSM0047553EXOc1.
SMARTSM00279HhH21.
SMARTSM00482POLAc1.
TIGRFAMsTIGR00593pola1.
PROSITEPS00447DNA_POLYMERASE_A1.

General information about the databases mentioned above

Keywords:
Complete proteome; DNA damage; DNA repair; DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease; Nucleotidyltransferase; Transferase.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=99120557; PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G.,
RA Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C.,
RA Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F.,
RA Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human
RT gastric pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).

Feature:
CHAIN 1 897 DNA polymerase I.
/FTId=PRO_0000101242.

Comments:
-!- FUNCTION: In addition to polymerase activity, this DNA polymerase
exhibits 3' to 5' and 5' to 3' exonuclease activity (By
similarity).
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- SUBUNIT: Single-chain monomer with multiple functions.
-!- SIMILARITY: Belongs to the DNA polymerase type-A family.
-!- SIMILARITY: Contains 1 3'-5' exonuclease domain.
-!- SIMILARITY: Contains 1 5'-3' exonuclease domain.
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Sequence length: 897

     MEQPVIKEGT LALIDTFAYL FRSYYMSAKN KPLTNDKGFP TGLLTGLVGM VKKFYKDRKN
     MPFIVFALES QTKTKRAEKL GEYKQNRKDA PKEMLLQIPI ALEWLQKMGF TCVEVGGFEA
     DDVIASLATL SPYKTRIYSK DKDFNQLLSD KIALFDGKTE FLAKDCVEKY GILPSQFTDY
     QGIVGDSSDN YKGVKGIGSK NAKELLQRLG SLEKIYENLD LAKNLLSPKM YQALIQDKGS
     AFLSKELATL ERGCIKEFDF LSCAFPSENP LLKIKDELKE YGFISTLRDL ENSPFIVENV
     PILNSTPILD NTPALDNAPK KSRMIVLESA EPLSMFLEKL ENPNARVFMR LVLDKDKKIL
     ALAFLLQDQG YFLPLEEALF SPFSLEFLQN AFSQMLQHAC IIGHDLKPLL SFLKAKYQVP
     LENIRIQDTQ ILAFLKNPEK VGFDEVLKEY LKEDLIPHEK IKDFKTKSKA EKSELLSMEL
     NALKRLCEYF EKGGLEEDLL TLARDIETPF VKVLMGMEFQ GFKIDAPYFK RLEQEFKNEL
     NVLERQILDL IGVDFNLNSP KQLGEVLYDK LGLPKNKSHS TDEKNLLKIL DKHPSIPLIL
     EYRELNKLFN TYTTPLLRLK DKDDKIHTTF IQTGTATGRL SSHSPNLQNI PVRSPKGLLI
     RKGFIASSKE YCLLGVDYSQ IELRLLAHFS QDKDLMEAFL KGRDIHLETS KALFGEDLAK
     EKRSIAKSIN FGLVYGMGSK KLSETLSIPL SEAKSYIEAY FKRFPSIKDY LNGMREEILK
     TSKAFTLLGR YRVFDFTGVN DYVKGNYLRE GVNAIFQGSA SDLLKLGMLK VSERFKNNPS
     VRLLLQVHDE LIFEIEEKNA PELQQEIQRI LNDEVYPLRV PLETSAFIAK RWNELKG

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