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CBPYA_PARBP
ID   CBPYA_PARBP             Reviewed;         550 AA.
AC   C0SGX7;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=PABG_06849;
OS   Paracoccidioides brasiliensis (strain Pb03).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=482561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb03;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- FUNCTION: Vacuolar carboxypeptidase involved in degradation of small
CC       peptides. Digests preferentially peptides containing an aliphatic or
CC       hydrophobic residue in P1' position, as well as methionine, leucine or
CC       phenylalanine in P1 position of ester substrate (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity.;
CC         EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074};
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; KN305544; EEH16762.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0SGX7; -.
DR   SMR; C0SGX7; -.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; EEH16762; EEH16762; PABG_06849.
DR   VEuPathDB; FungiDB:PABG_06849; -.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; C0SGX7; -.
DR   Proteomes; UP000002740; Unassembled WGS sequence.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR008442; Propeptide_carboxypepY.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF05388; Carbpep_Y_N; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Signal; Vacuole; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..131
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407465"
FT   CHAIN           132..550
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407466"
FT   REGION          20..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        463
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        525
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        185..424
FT                   /evidence="ECO:0000250"
FT   DISULFID        319..333
FT                   /evidence="ECO:0000250"
FT   DISULFID        343..366
FT                   /evidence="ECO:0000250"
FT   DISULFID        350..359
FT                   /evidence="ECO:0000250"
FT   DISULFID        388..394
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  61894 MW;  E186344B3C6D2D0E CRC64;
     MKSLVLGLLV GSAIASGPLQ HVLHAPPDPE PKPEPEPQVV KDPFEELRDT FDRLRNKAGD
     IWDDVMDNIP NIMSNMRPLT IPAKKFTRRP DSEWTHIVRG ADLEALWVDD ESGYKHRKID
     GKLAQYDLRI KAVDPSDLGI DKVKQYSGYL DDNANDKHLF FWFFESRNDP FGDPVVLWLN
     GGPGCSSLTG MFFELGPASI DENITANYNP YSWNSNSSII FLDQPVNVGY SYSSQAVSDT
     VTAAKDVYAL LTLFFTQFRQ YSAQDFHIAG ESYAGHYIPV FASEILHHNN TNINLQSVLI
     GNGLTDPLSQ YPFYRPMACG DGGYPSVLDS QSCQSMDNAL PRCLSMIKSC YDIESTFTCL
     PASIYCNNAL IGPYQKTGRN PYDVRTNCTG NDLCYPQLNY ITEYLNKPHV MRSLGVEVDS
     YESCNMDINR NFLFHGDWMK PYHRLVPSLL ARIPVLIYAG DADFICNWLG NKAWTEALEY
     PGHAKFAEAP MENLTMINSQ GKNEVFGEVK SHSNLTFMRI FKAGHMTPFD SPQASLEFAN
     SWLSGEWSEV
 
 
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