ID F9X632_ZYMTI Unreviewed; 509 AA.
AC F9X632;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=MYCGRDRAFT_69294 {ECO:0000313|EMBL:EGP89601.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP89601.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP89601.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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}.
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DR EMBL; CM001198; EGP89601.1; -; Genomic_DNA.
DR RefSeq; XP_003854625.1; XM_003854577.1.
DR AlphaFoldDB; F9X632; -.
DR EnsemblFungi; Mycgr3T69294; Mycgr3P69294; Mycgr3G69294.
DR GeneID; 13395812; -.
DR KEGG; ztr:MYCGRDRAFT_69294; -.
DR VEuPathDB; FungiDB:ZTRI_3.112; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_1_1_1; -.
DR InParanoid; F9X632; -.
DR OMA; YVYGLTY; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000008062; Chromosome 3.
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; cd04816; PA_SaNapH_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; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT DOMAIN 127..221
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 248..446
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 509 AA; 54671 MW; 7A843B37547CECD1 CRC64;
MKIPVSNSIY TAALAAGLAS YANASPGRGL SERLQSTIKE QGLMRNLRKL NDIAKANGGN
RAFGYPGFDA SRDYVLSRVK KGKDFKAWTQ DFPALFNNVE SISFKVGEED IYVFGLTYSP
STSPEGVTLP LVLGPNGTAA CDVASYEGLD VQGKIVLVER GTCPTGGTLA GKVKPAVAAG
AANVIVYNNV SPKVTGGTLS APDPVAYRSS GFINQDDGQR LKARLEAGEE LTAYFQQTQT
IEERITQNVI AESKGGDPHN VIMLGAHLDS VKAGAGINDD GSGSSLLLEI FDGLQKLGFR
NKIRLAWWGA EENGLVGSRY YTSQINNTRE ADNLLLYLNF DMVSRGYWGV FDGDGSTHGL
AGAPGSEVIE KLFVDYLESQ GKTVRPAVFT GGSDYASFMS TLNKPVGGLH TGTGVTEDAC
YHQECDNIDN PNPEQLTVNA RAVAHVLATL AMEGHKLIPK SGRKATRDVF SELYDRAMEM
SNSTILDDEL FPWTVMEGER HVATCGHDI
//
