Description:
Putative regulatory protein ada (Regulatory protein of adaptativeresponse) [Includes: Methylated-DNA--protein-cysteinemethyltransferase (EC 2.1.1.63) (O-6-methylguanine-DNAalkyltransferase)].
Molecular weight: 53743
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 ) base-excision repair( GO:0006284 )
Important dates:
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-MAR-2006, entry version 52.
Phylogenetic order:
Bacteria Actinobacteria Actinobacteridae Actinomycetales Corynebacterineae Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex.
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 ADA_MYCTU:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | BX842576 | CAA98104.1 | - |
| EMBL | U65786 | AAB06751.1 | - |
| EMBL | AE000516 | AAK45620.1 | - |
| PIR | A70769 | A70769. | |
| HSSP | P06134 | 1ADN | |
| GenomeReviews | AE000516_GR | MT1358.1 | |
| GenomeReviews | AL123456_GR | Rv1317c.1 | |
| TIGR | MT1358 | -. | |
| TubercuList | Rv1317c | -. | |
| LinkHub | Q10630 | -.1 | |
| InterPro | IPR004026 | Ada_Zn_bd. | |
| InterPro | IPR010316 | AlkA_N. | |
| InterPro | IPR003265 | Endo_3c. | |
| InterPro | IPR012287 | Homeodomain-rel. | |
| InterPro | IPR000005 | HTHAraC. | |
| InterPro | IPR012294 | TFIID_C/glycos_N. | |
| Pfam | PF02805 | Ada_Zn_binding | 1. |
| Pfam | PF06029 | AlkA_N | 1. |
| Pfam | PF00730 | HhH-GPD | 1. |
| Pfam | PF00165 | HTH_AraC | 2. |
| SMART | SM00478 | ENDO3c | 1. |
| SMART | SM00342 | HTH_ARAC | 1. |
| PROSITE | PS00041 | HTH_ARAC_FAMILY_1 | 1. |
| PROSITE | PS01124 | HTH_ARAC_FAMILY_2 | 1. |
Keywords:
Activator; Complete proteome; DNA damage; DNA repair; DNA-binding; Hypothetical protein; Metal-binding; Methyltransferase; Transcription; Transcription regulation; Transferase; Zinc.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H37Rv;
RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the
RT complete genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX MEDLINE=22206494; PubMed=12218036;
RX DOI=10.1128/JB.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-496.
RC STRAIN=H37Rv;
RA Bourn W.R., Harington A., Wiid I., van Helden P.D.;
RT "Mycobacterium tuberculosis 3-methyladenine glycosidase and O6-
RT methylguanine methyltransferase genes.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
Feature:
CHAIN 1 496 Putative regulatory protein ada.
/FTId=PRO_0000139389.
DNA_BIND 103 122 H-T-H motif (By similarity).
COMPBIAS 181 197 Ala-rich.
ACT_SITE 65 65 Acceptor for methyl from phosphotriester
(By similarity).
ACT_SITE 403 403 Alkyl group acceptor (By similarity).
METAL 34 34 Zinc (By similarity).
METAL 38 38 Zinc (By similarity).
METAL 65 65 Zinc (By similarity).
METAL 68 68 Zinc (By similarity).
Comments:
-!- FUNCTION: Repair of alkylated guanine in DNA by stoichiometrically
transferring the alkyl group at the O-6 position to a cysteine
residue in the enzyme. This is a suicide reaction: the enzyme is
irreversibly inactivated. Can also repair O-4-methylthymine (By
similarity).
-!- FUNCTION: The methylated ADA protein acts as a positive regulator
of its own synthesis, as well as that of other proteins. The
transcription-activating function of the ADA protein resides in
its N-terminus (By similarity).
-!- CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein
L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-
cysteine.
-!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
-!- SIMILARITY: In the C-terminal section; belongs to the MGMT family.
-!- SIMILARITY: Contains 1 HTH araC/xylS-type DNA-binding domain.
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Sequence length: 496
MHDDFERCYR AIQSKDARFD GWFVVAVLTT GVYCRPSCPV RPPFARNVRF LPTAAAAQGE
GFRACKRCRP DASPGSPEWN VRSDVVARAM RLIADGTVDR DGVSGLAAQL GYTIRQLERL
LQAVVGAGPL ALARAQRMQT ARVLIETTNL PFGDVAFAAG FSSIRQFNDT VRLACDGTPT
ALRARAAARF ESATASAGTV SLRLPVRAPF AFEGVFGHLA ATAVPGCEEV RDGAYRRTLR
LPWGNGIVSL TPAPDHVRCL LVLDDFRDLM TATARCRRLL DLDADPEAIV EALGADPDLR
AVVGKAPGQR IPRTVDEAEF AVRAVLAQQV STKAASTHAG RLVAAYGRPV HDRHGALTHT
FPSIEQLAEI DPGHLAVPKA RQRTINALVA SLADKSLVLD AGCDWQRARG QLLALPGVGP
WTAEVIAMRG LGDPDAFPAS DLGLRLAAKK LGLPAQRRAL TVHSARWRPW RSYATQHLWT
TLEHPVNQWP PQEKIA