ID B9W7Y9_CANDC Unreviewed; 544 AA.
AC B9W7Y9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Carboxypeptidase {ECO:0000256|RuleBase:RU361156};
DE EC=3.4.16.- {ECO:0000256|RuleBase:RU361156};
GN Name=CPY2 {ECO:0000313|EMBL:CAX44802.1};
GN OrderedLocusNames=Cd36_05440 {ECO:0000313|CGD:CAL0000164808};
GN ORFNames=CD36_05440 {ECO:0000313|EMBL:CAX44802.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX44802.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX44802.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431, ECO:0000256|RuleBase:RU361156}.
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DR EMBL; FM992688; CAX44802.1; -; Genomic_DNA.
DR RefSeq; XP_002417210.1; XM_002417165.1.
DR AlphaFoldDB; B9W7Y9; -.
DR MEROPS; S10.A49; -.
DR GeneID; 8044747; -.
DR KEGG; cdu:CD36_05440; -.
DR CGD; CAL0000164808; Cd36_05440.
DR VEuPathDB; FungiDB:CD36_05440; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000002605; Chromosome 1.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.410; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000256|RuleBase:RU361156};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361156};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361156};
KW Signal {ECO:0000256|RuleBase:RU361156}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT CHAIN 20..544
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361156"
FT /id="PRO_5005124639"
FT REGION 84..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 61372 MW; D82AD8E38EB5EE22 CRC64;
MQLSTLVNWL AALTVGAQAV SFGNNLKDQI ILDSEESSPD LYLESMFKDL GSLPIDLITA
WAEMQSELSP EQIAKLINQY DSKNEKPKKN KFNPMTSSSS PTAKFEKLSN EKFTGYSMRV
KESFPEILGL DTVKQYTGYL DIDSLDKHLF YWFFESRNDP KNDPIILWLN GGPGCSSSTG
LFFELGPSSI NKTLHPVYNP YSWNSNASVI FLDQPVGVGY SYTGGDEVKN TLTAAKDVYV
FLELFFQKFP QFLNNKFHIA GESYAGHYIP AFASEIINNA DRSFELASVL IGNGITDPLI
QDGSYKPMGC GEGGYKPVLT TEQCDQMERD YPKCAKLTKL CYSFQTALTC IPAQFYCDTR
LFKPYEETGL NPYDIRKHCA DQGGNCYVEL DYLDEYLNLD YVKEAVGASN IDIFTSCDDT
VFRNFILDGD EMKPFQQYVA ELLDNNVPVL IYAGDKDFIC NWVGNLAWVN ELEYSDSEQF
APKPLQLWKP NGKNPAGEVK NHKHFTFLRI YDAGHMVPFD QPENALAMVN TWIQGDYAFG
LESN
//
