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Database: UniProt
Entry: M7TC75_EUTLA
LinkDB: M7TC75_EUTLA
Original site: M7TC75_EUTLA 
ID   M7TC75_EUTLA            Unreviewed;       405 AA.
AC   M7TC75;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   ORFNames=UCREL1_5518 {ECO:0000313|EMBL:EMR67486.1};
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:EMR67486.1, 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 M28 family.
CC       {ECO:0000256|RuleBase:RU361240}.
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DR   EMBL; KB706422; EMR67486.1; -; Genomic_DNA.
DR   RefSeq; XP_007793433.1; XM_007795242.1.
DR   AlphaFoldDB; M7TC75; -.
DR   KEGG; ela:UCREL1_5518; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_024336_0_2_1; -.
DR   OMA; YVYGLTY; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000012174; 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; 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:SF17; AMINOPEPTIDASE Y; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 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   ECO:0000313|EMBL:EMR67486.1};
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:UP000012174};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           20..405
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5005141226"
FT   DOMAIN          123..217
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          244..394
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   405 AA;  43404 MW;  FA1537013C400E1C CRC64;
     MGFYQALVAL LPLTSGVSAT YKTEVTSEKL QAEIATENLI ANLEALQEIA TANGGNRAFG
     LPGYAASVDY IWSRISNITG TKAWKQDFPG LFNEVQSIEL RVDDEAVYVF GLTYSPSTEE
     GGITAELVLG PEGEAGCDAA SYEGLDVAGK IVLVERFRCP TGGTLAGRLL PAAANGAVAV
     IIYNNIATNT TAGTLSEPNS DEYVPGGFIN QVDGQAIKAR LEAGETLEAY FQQTQIIEER
     ITQNIFVETE SGDPDNVIVL GAHLDSVQAG PGINDDGSGT SLILEVFLAL AKYQTKNKVR
     FAWWGAEENG LVGSEYYCST LPAPEINKIL AYLNFDMVSK GYFGIGDGDG SSHGSVAPSG
     SEVIEQIYVD YFTGRGLNVT SAIITNGSDY ASFWQYLNKR LLRIW
//
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