ID Q6FSV1_CANGA Unreviewed; 563 AA.
AC Q6FSV1;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN OrderedLocusNames=CAGL0G07623g {ECO:0000313|CGD:CAL0130677,
GN ECO:0000313|EMBL:CAG59620.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG59620.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG59620.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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DR EMBL; CR380953; CAG59620.1; -; Genomic_DNA.
DR RefSeq; XP_446693.1; XM_446693.1.
DR AlphaFoldDB; Q6FSV1; -.
DR STRING; 284593.Q6FSV1; -.
DR MEROPS; M28.001; -.
DR EnsemblFungi; CAGL0G07623g-T; CAGL0G07623g-T-p1; CAGL0G07623g.
DR GeneID; 2888341; -.
DR KEGG; cgr:CAGL0G07623g; -.
DR CGD; CAL0130677; CAGL0G07623g.
DR VEuPathDB; FungiDB:CAGL0G07623g; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_0_1_1; -.
DR InParanoid; Q6FSV1; -.
DR Proteomes; UP000002428; Chromosome G.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IEA:EnsemblFungi.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02130; PA_ScAPY_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF17; AMINOPEPTIDASE Y; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 19..563
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005144033"
FT DOMAIN 206..297
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 324..524
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 563 AA; 62203 MW; 4D466F950B7CE02C CRC64;
MKFSTIAVTA ALVAYSNASV LPFYGEQQAF DLSALKETKE TDWDSIISGV KDALSQGHSE
QDAAEVYEDD DEDVSPCKKS FWSFLWKPHV PYLLKPIVES DKLQDKIELD DLNKTAHDLL
KIAKKSKKKF GHPTRVIGSP GHGKTIDYIL DAFDDMKDYY DVSVQEFDAL AGKIRSYNLT
DAKTGKTFKN TTAFALSPPV KPFVGRVIEI PNLGCHEKDF AAVHRKGSKH KHDIALIERG
ECPFGVKSDL AGKYGFHAVV IYDNEPLSLD GLKGTLGAPT NHTVSTIGVT YVTGKEIIAK
LAFDPDYSLY FAMDSYVGKI KTKNIIADTK HGDENNIVGL GAHSDSVEEG PGLNDDGSGT
ISLLTVAKQL THFKINNKVR FAWWAAEEEG LLGSNYYANS LSKEENLKLR VFMDYDMMAS
PNYEYEVYDA NNTVNPPGSQ ELRDLYINYY KDQGLNYTLI PFDGRSDYVG FIENGIPAGG
IATGAEKKNV FNGGVLDKCY HQLCDDISNL AWDAFLVNTK LIAHSVATYA NSFEGFPERI
GSNKTISALQ APSFPYRGSN LII
//
