CBPYA_NEUCR
ID CBPYA_NEUCR Reviewed; 554 AA.
AC Q7RXW8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=cpyA; ORFNames=NCU00477;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002238; EAA27560.1; -; Genomic_DNA.
DR RefSeq; XP_956796.1; XM_951703.3.
DR AlphaFoldDB; Q7RXW8; -.
DR SMR; Q7RXW8; -.
DR STRING; 5141.EFNCRP00000000022; -.
DR ESTHER; neucr-CBPYA; Carboxypeptidase_S10.
DR MEROPS; S10.001; -.
DR EnsemblFungi; EAA27560; EAA27560; NCU00477.
DR GeneID; 3872943; -.
DR KEGG; ncr:NCU00477; -.
DR VEuPathDB; FungiDB:NCU00477; -.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; Q7RXW8; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
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..137
FT /evidence="ECO:0000250"
FT /id="PRO_0000407459"
FT CHAIN 138..554
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407460"
FT ACT_SITE 278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 191..431
FT /evidence="ECO:0000250"
FT DISULFID 325..339
FT /evidence="ECO:0000250"
FT DISULFID 349..372
FT /evidence="ECO:0000250"
FT DISULFID 356..365
FT /evidence="ECO:0000250"
FT DISULFID 394..401
FT /evidence="ECO:0000250"
SQ SEQUENCE 554 AA; 62153 MW; 77DFFCEBCCF91249 CRC64;
MRISASTVLL GAASAASAAS FQNQAQHVLA DNFHKAHDAV KPVADSFAHT TLESFEEAFN
GMNSQAKALW DEIKLLVPEN AFDKPTWFSK PKAAKRRKDW DHVVKGADVQ KLWVKGADGE
KHREVGGQLD NFNLRVKSVD PSKLGVDKVK QYSGYLDDEE NDKHLFYWFF ESRNDPKNDP
VVLWLNGGPG CSSLTGLFLE LGPSSIDKKL RVVSNEYAWN NNASVIFLDQ PVNVGYSYSG
NAVSNTVAAG KDVYALLTLF FHQFPEYAKQ DFHIAGESYA GHYIPVFASE ILSHKDRNIN
LKSVLIGNGL TDPLTQYEHY RPMACGEGGY PAVLSESECR SMDNALPRCQ SLIRNCYESG
SVWSCVPAAI YCNNQFIGPY QRTGQNVYDI RGKCEDDSNL CYSALGWISD YLNQKDVMDA
LGVEVEGYES CNFDINRNFL FQGDWMQPFH RLVPGILKEI PVLIYAGDAD FICNWLGNKA
WSEALEWPGK NGFNKAELED LSLPKADKEY GKVKSSGNFT FMQIYQAGHM VPMDQPENSL
DFLNRWLGGE WFEQ
