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Database: UniProt
Entry: A8NYE0_COPC7
LinkDB: A8NYE0_COPC7
Original site: A8NYE0_COPC7 
ID   A8NYE0_COPC7            Unreviewed;       411 AA.
AC   A8NYE0;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 2.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=CC1G_01316 {ECO:0000313|EMBL:EAU84320.2};
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU84320.2, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU84320.2, ECO:0000313|Proteomes:UP000001861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC   {ECO:0000313|Proteomes:UP000001861};
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAU84320.2}.
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DR   EMBL; AACS02000005; EAU84320.2; -; Genomic_DNA.
DR   RefSeq; XP_001837404.2; XM_001837352.2.
DR   AlphaFoldDB; A8NYE0; -.
DR   GeneID; 6013960; -.
DR   KEGG; cci:CC1G_01316; -.
DR   VEuPathDB; FungiDB:CC1G_01316; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_025286_0_0_1; -.
DR   InParanoid; A8NYE0; -.
DR   OMA; SGSECHY; -.
DR   OrthoDB; 1384212at2759; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF59; PEPTIDASE_M28 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:EAU84320.2};
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:UP000001861};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           21..411
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5005122030"
FT   DOMAIN          263..371
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   411 AA;  45462 MW;  64ABA16C842D5F17 CRC64;
     MASTLLSLWL ILPLNSTLFS QEPCLTHSFY GNYKLQDSTV ALFQASTPDC VEYSRSYLSQ
     EPNVLLEIHR NASLVWLEKE HVDPSLLQQE SFMSDDFYRT LTRLVGEDQP LYEQEDQHTF
     NAKTDNGFPY TLFSSNDATM LALPRHAALQ VDTILPRFVK STLVPDAPFT YREVSNDDLK
     VVRDVLGTLR FNPDIASVVN NISIPQIQQD IRFLTGEDGK SGIVSRHSFS SGARTAAAWI
     KARIEETGAT CRLSTFLTGF APNVICRYSA IKKTDDTVII SGHYDSRGSF GSVRAPGADD
     DGSGTTGVLS IARTIGRKRL RFHKNVELVA FAGEEQGLYG SRAYARELRA QNASIVMMIQ
     ADMTAYRAAQ EPLQLGLPER IGTPEVTQLV ANVSAFYSPE LTVGYSGVCS I
//
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