ID   M7T5I4_EUTLA            Unreviewed;       496 AA.
AC   M7T5I4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Putative vacuolar aminopeptidase 1 protein {ECO:0000313|EMBL:EMR72128.1};
GN   ORFNames=UCREL1_825 {ECO:0000313|EMBL:EMR72128.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR72128.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KB705518; EMR72128.1; -; Genomic_DNA.
DR   RefSeq; XP_007788781.1; XM_007790590.1.
DR   AlphaFoldDB; M7T5I4; -.
DR   STRING; 1287681.M7T5I4; -.
DR   KEGG; ela:UCREL1_825; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   HOGENOM; CLU_019532_3_0_1; -.
DR   OMA; LLDTHYY; -.
DR   OrthoDB; 1156at2759; -.
DR   Proteomes; UP000012174; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05658; M18_DAP; 1.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF4; VACUOLAR AMINOPEPTIDASE 1; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   496 AA;  53279 MW;  AA97BDFD2F3DF525 CRC64;
     MSQGNAIILR EARPAGSNWG PCQTCALSNL TPETFTGPFC NFLRDNPTIF HSVEYFKKKA
     AAVGYKELPA RADWSGKLEA GGKYFVTRNG SSIIAFTVGK AYKPGNGVAM IAGHIDALTA
     KLKPVSNKPT KAGYVQLGVA QYAGALNETW WDRDLTIGGR VIVKDENGKT STKLVKFDWP
     IARIPTLAPH FGVGMLGQNN AETQAVPIIG LDNSDLDSNA KPAEPLGPVG SFVSTQPPKL
     VKLISQELGL KDHSEIVNWE LELFDLQPAT VGGLDKEFIF AGRIDDKLCS WGALQGLLLA
     EDNEDDGTIK LVTLFDDEEI GSLLRQGAKG NFLSSVIERA VESLSTKEKP FGPGVIGQTY
     ARSFLVSADV THATNPNFLS RYLDDHAPRL NVGIVICTDS NGHMTTDSVA AAVLTRVCEL
     SGVTPQRFQI RNDSRSGGTV GPTLSSALGV KAADAGMPQL SMHSIRATTG ALDPGLGVQF
     FKGFLDKWEK VDAEWE
//