|
|
|
|
|
|
Description:
DNA polymerase I (EC 2.7.7.7) (POL I).
Molecular weight: 11221
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:
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
07-MAR-2006, entry version 50.
Phylogenetic order:
Bacteria Spirochaetes Spirochaetales Spirochaetaceae Treponema.
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_TREPA:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U57757 | AAB17467.1 | - |
| EMBL | AE000520 | AAC26553.1 | - |
| PIR | F71365 | F71365. | |
| HSSP | P19821 | 1CMW | |
| GenomeReviews | AE000520_GR | TP0105.1 | |
| TIGR | TP0105 | -. | |
| InterPro | IPR002562 | 3_5_exonuclease. | |
| InterPro | IPR002421 | 5_3_exonuclease. | |
| InterPro | IPR001098 | DNA_pol. | |
| InterPro | IPR002298 | DNA_polI. | |
| InterPro | IPR000513 | Exo_N_I. | |
| InterPro | IPR006055 | Exonuclease. | |
| InterPro | IPR008918 | HhH2. | |
| InterPro | IPR012337 | RNaseH_fold. | |
| Pfam | PF01612 | 3_5_exonuc | 1. |
| Pfam | PF01367 | 5_3_exonuc | 1. |
| Pfam | PF02739 | 5_3_exonuc_N | 1. |
| Pfam | PF00476 | DNA_pol_A | 1. |
| PRINTS | PR00868 | DNAPOLI. | |
| SMART | SM00474 | 35EXOc | 1. |
| SMART | SM00475 | 53EXOc | 1. |
| SMART | SM00279 | HhH2 | 1. |
| SMART | SM00482 | POLAc | 1. |
| TIGRFAMs | TIGR00593 | pola | 1. |
| PROSITE | PS00447 | DNA_POLYMERASE_A | 1. |
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 [GENOMIC DNA].
RC STRAIN=Nichols;
RX MEDLINE=20337940; PubMed=10882092;
RA Rodes B., Liu H., Johnson S., George R., Steiner B.M.;
RT "Molecular cloning of a gene (polA) coding for an unusual DNA
RT polymerase I from Treponema pallidum.";
RL J. Med. Microbiol. 49:657-667(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
RA Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA Weidman J.F., Smith H.O., Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis
RT spirochete.";
RL Science 281:375-388(1998).
Feature:
CHAIN 1 997 DNA polymerase I.
/FTId=PRO_0000101261.
CONFLICT 782 782 V -> A (in Ref. 1).
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).
-!- SIMILARITY: Belongs to the DNA polymerase type-A family.
-!- SIMILARITY: Contains 1 3'-5' exonuclease domain.
-!- SIMILARITY: Contains 1 5'-3' exonuclease domain.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
Sequence length: 997
MQEKKTLYLL DAYGLIYRSY HAFARAPLIN DSGANVSAVY GFFRSLHTLL CHYRPRYFVA
VFDSLTPTFR HVQYPAYKAK RDKTSAELYA QIPLIEEILC ALGITVLRHD GFEADDLIAT
LAKRVAAEHC HVVIISSDKD VLQLVCDTVQ VLRLDIDHKW TCCDAAYVQQ RWTVMPTQLL
DLFSLMGDSS DNVPGVRGIG PKTAAHLLHC FGTLDGIYRH TYSLKEALRT KIVCGKKDAF
FSRSLIELRD DVPCVFSLED SCCIPLDVTS AARIFVREGL HALAQQYRAC VQEIDTEATN
DTLQMTESSV LTSGRCANEC FLSQVEGRAS TPEVNSVLKS ELKTSAVSGA IPIENRDLRQ
DVMLARSAGH YRGVTDPVEL KRIIDCACAN GVVAFDCETD GLHPHDTRLV GFSICFQEAE
AFYVPLIVPD VSLHTESTQC TCARSTNVET EKECTEQHGV SASAVQDPAY VQAVMHQLRR
LWNDETLTLV MHNGKFDYHV MHRAGVFEHC ACNIFDTMVA AWLLDPDRGT YGMDVLAASF
FQIRTITFEE VVAKGQTFAH VPYECAVRYA AEDADITFRL YHYLKLRLET AGLLSVFETI
EMPLLPILAR MEEVGIFLRK DVVQQLTRSF SDLIQQYEHD IFSLAGHEFN IGSPKQLQTV
LFQELHLPPG KKNTQGYSTD HSVLKKLARK HPIAEKILLF RDLSKLRSTY TESLAKLADQ
TGRVHTSFVQ IGTATGRLSS RNPNLQNIPI KSTEGRKIRQ AFQATVGHEL ISADYTQIEL
VVLAHLSQDR NLLNAFRQHI DIHALTAAYI FNVSIDDVQP AMRRIAKTIN FGIVYGMSAF
RLSDELKISQ KEAQSFIYRY FETYPGVYAF STQVAEQTRK TGYVTSLAGR RRYIRTIDSR
NTLERARAER MALNTQIQSS AADIVKIAMI AIQRAFARRP LRAQLLLQVH DELIFEAPAA
ETAIVKEILF AEMEHAVELS IPLRIHVESG NSWGDFH