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
//