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CBPYA_ASPCL
ID   CBPYA_ASPCL             Reviewed;         543 AA.
AC   A1CUJ5;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; Synonyms=cpy; ORFNames=ACLA_086840;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027060; EAW06982.1; -; Genomic_DNA.
DR   RefSeq; XP_001268408.1; XM_001268407.1.
DR   AlphaFoldDB; A1CUJ5; -.
DR   SMR; A1CUJ5; -.
DR   STRING; 5057.CADACLAP00007909; -.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; EAW06982; EAW06982; ACLA_086840.
DR   GeneID; 4700272; -.
DR   KEGG; act:ACLA_086840; -.
DR   VEuPathDB; FungiDB:ACLA_086840; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 625787at2759; -.
DR   Proteomes; UP000006701; 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   Reference proteome; Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..124
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407430"
FT   CHAIN           125..543
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407431"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        458
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        520
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        179..419
FT                   /evidence="ECO:0000250"
FT   DISULFID        313..327
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        344..353
FT                   /evidence="ECO:0000250"
FT   DISULFID        382..389
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   543 AA;  60925 MW;  B3D2EB24E0FB5442 CRC64;
     MRVLPATLLV GAATAAVPPF QQILGLPKKG ADTLSKPLHD FQEQLKTLSD DARRLWDEVA
     KHFPDSMDHN PVFSLPKKHT RRPDSHWDHI VRGADVQSVW VTGANGEKER EVDGKLEAYD
     LRVKTTDPGA LGIDPGVKQY TGYLDDNEND KHLFYWFFES RNDPKNDPVV LWLNGGPGCS
     SLTGLFLELG PSSIDSKIKP VYNDFAWNSN ASVIFLDQPV NVGYSYSGSA VSDTVAAGKD
     VYALLTLFFK QFPEYAKQDF HIAGESYAGH YIPVFASEIL SHKKRNINLK SVLIGNGLTD
     PLTQYDHYRP MACGDGGYPA VLDEASCQSM DNALPRCKSM IESCYNTESS WVCVPASIYC
     NNALIGPYQR TGQNVYDVRG KCEDESNLCY KGMGYVSEYL NKREVREAVG AEVDGYDSCN
     FDINRNFLFH GDWMKPYHRL VPGLLEQIPV LIYAGDADFI CNWLGNKAWS EALEWPGQKE
     YASAELEDLV IEQNEHQGKK IGQIKSHGNF TFMRLYGGGH MVPMDQPEAS LEFFNRWIGG
     EWF
 
 
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