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Database: UniProt
Entry: A8NAD2_COPC7
LinkDB: A8NAD2_COPC7
Original site: A8NAD2_COPC7 
ID   A8NAD2_COPC7            Unreviewed;       509 AA.
AC   A8NAD2;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=CC1G_05883 {ECO:0000313|EMBL:EAU89967.1};
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:EAU89967.1, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU89967.1, 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. M28A subfamily.
CC       {ECO:0000256|ARBA:ARBA00005957}.
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:EAU89967.1}.
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DR   EMBL; AACS02000007; EAU89967.1; -; Genomic_DNA.
DR   RefSeq; XP_001831784.1; XM_001831732.1.
DR   AlphaFoldDB; A8NAD2; -.
DR   GeneID; 6008260; -.
DR   KEGG; cci:CC1G_05883; -.
DR   VEuPathDB; FungiDB:CC1G_05883; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   InParanoid; A8NAD2; -.
DR   OMA; FDMMASP; -.
DR   OrthoDB; 51543at2759; -.
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   CDD; cd03876; M28_SGAP_like; 1.
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; IPR041756; M28_SGAP-like.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 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:UP000001861};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           22..509
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5005122006"
FT   DOMAIN          133..224
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          251..463
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   509 AA;  54115 MW;  05EEDD319E6B75F3 CRC64;
     MKLPLPFIAL LVSLRPYLIS ATPEEIQAGP HRPLVDSDEL QASISAHNLL AHARQLDAFA
     DLTSTGIGRN RAFGSLGHNA TVDYIKQLLD ETGYYDTYLE TFPWQYSESR VQFFVGEEQY
     ATAPFTYGPA GDVEAPIVPV NALGCTAADF PDEVAGSIAL IQRGECEYGL KVALAGAAGA
     SGAILYNNID AGFGSGGSLA QPSRPVIGPY VPVGGISGVQ GKALIAAIEA GEEVVGKIQA
     TGFTEVRYSS NVIATSKSGD KDNIVFAGAH SDSVPAGPGI NDDGSGTIAV LEIALHLTKY
     RVNNAVRFGF WTTEEFGLVG SEHHVSNLSD EERQKIALYL NFDMLASPNA AYFVHDGDGS
     TFGLVGPPGS DKIEKLYQGW YEARGLKTAA AAFSGSSDYD PFLQVGIPVG GVLTGASGLK
     TAEGVEQWGG EVGVAYDKCY HLLCDTVDNL NVPFWVNNAK AAAHSIAIYA RSLDGIPREQ
     RASVASLPIT RMSWEERRHF ACNHPVSYV
//
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