ID A0A161X097_9PEZI Unreviewed; 855 AA.
AC A0A161X097;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:KZL87016.1};
GN ORFNames=CI238_02159 {ECO:0000313|EMBL:KZL87016.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL87016.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL87016.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL87016.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZL87016.1}.
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DR EMBL; LFIW01000342; KZL87016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161X097; -.
DR STRING; 1573173.A0A161X097; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KZL87016.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KZL87016.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..855
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007829674"
FT TRANSMEM 450..471
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..408
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 480..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 91880 MW; 48394B8351A353C1 CRC64;
MLSNTLIATM LVGIVGAQKQ SAMALTPSND WYGVDGNWST IRLQVGMPGQ SVNVLASTSL
SEFWAIGAGG CLANEPLCNS ARGNVFTIAD SKSWNPLGAW QLGLDYLGYG GNGDYGLDTL
STTLLTGDGM RMDNIITASI NSTDYYLGYL GLGVTKGSFG NQVAESPLTQ AVKNYGWIPS
YSYGYTAGAY YMGVSGTPCS VTLGGYDASR FVQHNNEFSL DPSDGLPHAL VRGIQVSTGQ
DKALPGGWNT STRILSNMST SFTAMIDSST PYLWLPDAVC DQFAEAFNLT YNSTFNLYTV
TNDQYADFKS GSSSYSFTFS FTSHDNSDDF GHPLTVPGVV NITITAAAFA QVLRYPFQGE
TIKYGEPAVP YFPLRRASNL TDTFVIGRSF LQEAYLITKY DTGVFSLHQA LFPNEPLQSL
QLKNIVQPSN SPFPPPAQVN LHGGLSTAQM GGIAAAAVAA CVIMLVCWYF YRRQKKSRAT
TRTLEDGKDA ASSIMPEPPR SPVAKMFTKI LGKKKAKRSS SHEVMGSISQ PAEVGADANH
AVYELPVPVN PAELDGDDSK SVLGHPEFGT DAIHNTDAYE LARRNVEIQL QGPVPAYTPP
ENPADFPPAE KSIQDMSPVA TFRPEEFGSL PSSSPTSTSS PSSPTACDNQ SSTRGSLPSP
MSPRGGEWTT RTSDLLSPLT EGPSHSPGFT DSNAGNTMLQ PVSPESEAFT SSPSSFPNIS
PPNPLPALPA SALPTHYRTP MEFSNVICLG PLPENISLPA PPAIPAPLAC PQGSPNVAVP
EVLAANRVST DTLGSNWTEF EEELMARELT RQVSLPEDTR SQEVESDSLR SLHRLDGSEF
IHIPQPAERR YSWEH
//