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Database: UniProt
Entry: B9WA92_CANDC
LinkDB: B9WA92_CANDC
Original site: B9WA92_CANDC 
ID   B9WA92_CANDC            Unreviewed;       697 AA.
AC   B9WA92;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=X-Pro aminopeptidase, putative {ECO:0000313|EMBL:CAX43311.1};
GN   OrderedLocusNames=Cd36_15330 {ECO:0000313|CGD:CAL0000165861};
GN   ORFNames=CD36_15330 {ECO:0000313|EMBL:CAX43311.1};
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:CAX43311.1, ECO:0000313|Proteomes:UP000002605};
RN   [1] {ECO:0000313|EMBL:CAX43311.1, 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family.
CC       {ECO:0000256|ARBA:ARBA00008766}.
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DR   EMBL; FM992689; CAX43311.1; -; Genomic_DNA.
DR   RefSeq; XP_002418012.1; XM_002417967.1.
DR   AlphaFoldDB; B9WA92; -.
DR   MEROPS; M24.A10; -.
DR   GeneID; 8046526; -.
DR   KEGG; cdu:CD36_15330; -.
DR   CGD; CAL0000165861; Cd36_15330.
DR   VEuPathDB; FungiDB:CD36_15330; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_6_1; -.
DR   OrthoDB; 869at2759; -.
DR   Proteomes; UP000002605; Chromosome 2.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF16189; Creatinase_N_2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:CAX43311.1};
KW   Hydrolase {ECO:0000313|EMBL:CAX43311.1};
KW   Protease {ECO:0000313|EMBL:CAX43311.1}.
FT   DOMAIN          72..214
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          406..622
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   DOMAIN          632..693
FT                   /note="Peptidase M24 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16188"
SQ   SEQUENCE   697 AA;  78872 MW;  B476EE1737E5B577 CRC64;
     MSSRVARAQC ANCTCSPGLI SRANRKSIYK RLSLNRRDST PTSGCTSREG SIFTFNPSLC
     LPDAKEVNTS KRLESLRKQM KEHDLGIYIV PSEDQHQSEY VSAYDQKRSF ISGFSGSAGI
     AIITRDMNSV GDTFEGTAAL STDGRYFTQA VDELDFNWIL LKQGAKDEPN WKEWTVQQAV
     QLSLDSGIAV RIGVDPTLIT YKLYKEFQSI VEKELTKNEK VKIEFTAVKE NLINKIWEQF
     EELPPRNLGE IKSLDVNFTG RNVEDKLADV KKHLTGDIKG IVISALDEVA WLLNLRGSDI
     QYNPVFYSFV ILTDESTTLY IGENRLSEDI VGDLKTAGIN IEPYESFYPS LTTVSTKLSE
     SNKKFYIPDN ANWEVVRNLK CEFTQGLSPV EDLKAVKNNV ELEGAKIAHL KDGRALIKFF
     AWLEEQVIEK QELIDEIEAD EKLTEFKQQE DNFVGLSFDT ISATGANGAV IHYKPTKGQC
     STINPRKLYL NDSGSQFLEG TTDVTRTVHF QKPTKEEITN YTLVLKGNIA LSTLRFPQNT
     TGNLIDAIAR QYLWKYGLNY AHGTSHGVGA YLNVHEGPIG IGPRPNAAAY ALKAGNLISN
     EPGYYQEGDY GIRIENVMFI KESDLRYDGK SYLEFETVTK VPYCRRLIGI HLLNDEEISW
     INEYHADIWN SFHENFDKNS YTYKWLKRET EPLVKSK
//
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