ID C5M5S2_CANTT Unreviewed; 541 AA.
AC C5M5S2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Ada DNA repair metal-binding domain-containing protein {ECO:0000259|Pfam:PF02805};
GN ORFNames=CTRG_01202 {ECO:0000313|EMBL:EER34342.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER34342.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER34342.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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DR EMBL; GG692396; EER34342.1; -; Genomic_DNA.
DR RefSeq; XP_002546897.1; XM_002546851.1.
DR AlphaFoldDB; C5M5S2; -.
DR STRING; 294747.C5M5S2; -.
DR EnsemblFungi; CTRG_01202-t43_1; CTRG_01202-t43_1-p1; CTRG_01202.
DR GeneID; 8297466; -.
DR KEGG; ctp:CTRG_01202; -.
DR VEuPathDB; FungiDB:CTRG_01202; -.
DR eggNOG; ENOG502S0C7; Eukaryota.
DR HOGENOM; CLU_027889_1_0_1; -.
DR OrthoDB; 1707513at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.40.10.10; DNA Methylphosphotriester Repair Domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR035451; Ada-like_dom_sf.
DR InterPro; IPR004026; Ada_DNA_repair_Zn-bd.
DR Pfam; PF02805; Ada_Zn_binding; 1.
DR SUPFAM; SSF57884; Ada DNA repair protein, N-terminal domain (N-Ada 10); 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 9..73
FT /note="Ada DNA repair metal-binding"
FT /evidence="ECO:0000259|Pfam:PF02805"
FT REGION 199..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 60346 MW; BB0D813CA904575C CRC64;
MVYSSETSKW KAYQFNDPFA AGSFFVCNKI NQIFCRPDCD VRPITNLKSE IKFVSNSKQA
LQLGYKPCEH CDPINTSMAI DVNLLIKCVS NVNTRIGFIP PLLDDDEESN SLKIKENILE
SKKLNQQELL NKFESSSTTN IHGHRNSVPN LISSYDNKAP KDLSLSKNDS DHYRLVDLAC
RHLALAAAIN VFQPKPIITN DESSSQDQPN SPTSNGSGKR RRRRRGGVLG FKELAAKSKL
SAWHFHRVFK SVTGLTPKTY GDKCWEFVKK VKESGEYTSF EEYSMNSPVG TTNLSDDDNS
NTTSIHKNTH ISNPNSPLNK STSGIMSNTC TSSPQDVDGT TIALYPITPT SQTTNIGGTG
TISNIDSAIS EFPEFGFPTT NIANVDSFLN FSTGLINGDD SSTRAFSYQD MSSLRGGKQD
SITNSSTGSL FNNTNNLLQY TQFQPSNQSY DPTTTTNDSY VNTYDEYSHM NDYHHQQQPQ
QQQQQQNHHS FDDLYSLTTF DENLFNNDTL FQVGNNSNNA TTATTNDENK YNYNLMTTIG
L
//
