ID   K1XDH2_MARBU            Unreviewed;       765 AA.
AC   K1XDH2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=MBM_03165 {ECO:0000313|EMBL:EKD18923.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD18923.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD18923.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD18923.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(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; JH921432; EKD18923.1; -; Genomic_DNA.
DR   RefSeq; XP_007291054.1; XM_007290992.1.
DR   AlphaFoldDB; K1XDH2; -.
DR   GeneID; 18759100; -.
DR   KEGG; mbe:MBM_03165; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_364879_0_0_1; -.
DR   InParanoid; K1XDH2; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000006753; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   DOMAIN          413..498
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          513..717
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   REGION          89..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  82667 MW;  9E553C4A6C5D9815 CRC64;
     MRAGPGHLSS LFARGPAINN GALIQKRPNQ KECHAHEKRI AINAIAVLGF IRSTCHNRLD
     HPPAEFLIPH IADSLAVHDN PPNYAHRIRK KQVSRKSTPA MGKQVRTTQR NPNPNPSPNP
     KFAYSDPDFC QNTSNSALLI DIPSDDAPDL TFSVRDGQFQ RPGLLRCMLR RSGVRAINDF
     MREKMLLSPW HLPRPSRGVI LATGREGLKC LVDLLNEESR IGVSRTGGLS WTCIWAMQDA
     DRRSQVPHSS GHRGCITCKQ SGDKVQKRQR RRLFCIPVVQ KDRSSVMKLS SYASIVATIA
     SLTEALPTES SLASRALPLV ESNKLRRVLL RSELLKKGQL LQDFAYAWEG RNRYSGTPGH
     QSTIDYIQES LNATGYYDTY TQEFIVPSTS GALSVAGAPL PAAPMSFSPA GNITAQVVAV
     ANLGCDAADY PAAVSGAIAL ISRGNCTFGA KSSLAKAAGA VGAIIYNNIP DTLLQGTLGE
     AGDYAPTLGA TQEDGLALAA SLPIASLEVQ VINTVTQTKG GDPENVLMVG AHTDSVQAGP
     GINDNGSGTI GILEVALRLA KFSTNNGVRF GWWSGEEDGL LGAEHYVAEL PQEERDKIRI
     YLNFDMIASP NFVYEIYDGD GSAFNISGAP GSAEAEKLWE DYFKNEVAIP TNPSAFDGRS
     DYGPFLDVGI AAGGLTSGAD GVKTQEDYDK YGGVIGAIYD PNYHTAQDTV ENTNVGVWIG
     LTKGIAHAVA TYGRSWDSFP AKTKRSAPVK KRDRGFQRKG NKFLW
//