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Database: UniProt
Entry: M3B122_PSEFD
LinkDB: M3B122_PSEFD
Original site: M3B122_PSEFD 
ID   M3B122_PSEFD            Unreviewed;       452 AA.
AC   M3B122;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=MYCFIDRAFT_164329 {ECO:0000313|EMBL:EME83093.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME83093.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME83093.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME83093.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR   EMBL; KB446558; EME83093.1; -; Genomic_DNA.
DR   RefSeq; XP_007926416.1; XM_007928225.1.
DR   AlphaFoldDB; M3B122; -.
DR   GeneID; 19332164; -.
DR   KEGG; pfj:MYCFIDRAFT_164329; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_024336_0_0_1; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000016932; 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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016932};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   DOMAIN          69..158
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          184..397
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   452 AA;  48133 MW;  0774FEA6DBEECC65 CRC64;
     MRNRVFSSPG HDGTLDFIEG YLDSVKDYYT YERQEFIALY SQASGSLIAG ETKYPSTIYQ
     YSPSTDGTIT APIVEVQNLG CNETDYTDAV SGAIALISRG ECTFGTKSAL AGNAGAVGAI
     IYNNVLGPVS GGTLGAPPNP LGDYIPSAGV SQENGTAILE ALQAGVVEGQ LEVDSIIENR
     TTYNIVADTI GGDKNNVLAI GAHSDSVFAG PGINDDGSGT IGILETALQL ASYSTKNAIR
     FCFWSAEEFG LLGSEHYVTT LPSAEADKIK LYLNFDMIAS PNFQYALYDG DGDTFNITGP
     PGSAEVEHFF EDWFEEQGIP TKATAFDGRS DYGPFLDAGI PAGGIFTGAE QLKTAEEALL
     WGGQAGVAYD PNYHLAGDNY TNLNFEAFLT NTKAIAASIA YYGSDLSSIP PRNSTMKMVK
     TRGLHHHPHA KRNTVHTHEN TYDCGAAPKV FS
//
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