ID M7TLT3_EUTLA Unreviewed; 819 AA.
AC M7TLT3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 22-FEB-2023, entry version 44.
DE SubName: Full=Putative secreted aspartic proteinase protein {ECO:0000313|EMBL:EMR70896.1};
GN ORFNames=UCREL1_2065 {ECO:0000313|EMBL:EMR70896.1};
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:EMR70896.1, 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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KB705747; EMR70896.1; -; Genomic_DNA.
DR RefSeq; XP_007790019.1; XM_007791828.1.
DR AlphaFoldDB; M7TLT3; -.
DR KEGG; ela:UCREL1_2065; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_345130_0_0_1; -.
DR OrthoDB; 4946at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..819
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004085722"
FT DOMAIN 83..401
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 103
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 331..364
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 819 AA; 84794 MW; 9172DAE613797A18 CRC64;
MTLSRLLAHW LTASALLCAS SYAQGPRDGA LGEVVDETSS FSEDPIKLLS LPLWRVDHFG
VGTPSVAKRF FKTDVLGVFG AAYLTQLTIG TGSGRQNVSV LLDTGSFELW VNPDCASSNV
PSLCQDFGHY DPALSSTSVN LNKPYSISYG SGSTSGTYYT DDIHINSVQI SDQQFGVANQ
SDIVWFGIMG LAHGMGNGFI KYPTIIDSLA AQNYTESKLF SLDLGGQVPP GIATTGQMVF
GGVDRNKYAG RLRKVPTDPS DPHYTITLTG LSHRAPSSSS TQPIVDASLP LRVVVDSGTT
LSLLPENLVR AIAALFPGAA PDGNGGYTVS CDYQQRDGSV EFLFGQVNIS VTYRDFVWNS
GGNCFLGVWY TPNVNVWILG DTFLRGAYVA FDQDNNALYM ANYLSCGSGP SLVPVPGGLD
AAANIPGACQ VAVPGTTPIP STRTLPVPNY YIAYPHPNNV TTVTIAITIS VTIAISVTIS
ITVTVITIVT RTTATVQATY TYTSTVTEQV ISTIGPQPCP DQAGDTPCSS GGPAQLVTSF
RTYITTICST ADASAAEQQP TGQPIMTIAA ATTAPASNPP VAAAGNGGGS GEDDDDVVVP
TTAEAKAKIQ TIEVVTEHCS TKTYTVTACD GTLDDDDDDD EDCTVGMMKT RVVTLQALQT
IVVTAVPDAV AQEGGGAVPV SLPVPMPTLS PMTTELTQAM ATAPAVEVVA VETVRGGTAE
VEAETEALTT IWSTVVVSPS PAVGVGAVSA AAGGYSWSVS NGSSTAGVVN GVACGATCGG
VSVVPTGGVA VVAGAEGRRR GLLGLDGRMA LLGGWFERV
//