ID E3QSB7_COLGM Unreviewed; 455 AA.
AC E3QSB7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 22-FEB-2023, entry version 52.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:EFQ33744.1};
GN ORFNames=GLRG_08888 {ECO:0000313|EMBL:EFQ33744.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GG697373; EFQ33744.1; -; Genomic_DNA.
DR RefSeq; XP_008097764.1; XM_008099573.1.
DR AlphaFoldDB; E3QSB7; -.
DR STRING; 645133.E3QSB7; -.
DR MEROPS; A01.079; -.
DR EnsemblFungi; EFQ33744; EFQ33744; GLRG_08888.
DR GeneID; 24414253; -.
DR VEuPathDB; FungiDB:GLRG_08888; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_0_1; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000008782; 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 CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF23; ASPARTIC ENDOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G15950)-RELATED; 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; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EFQ33744.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..455
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003180751"
FT DOMAIN 126..434
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 142
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 328
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 455 AA; 48123 MW; AA04D28C23AB8122 CRC64;
MESVSLRSLC LYGLLATFAD ASPVEKRSNI QKRGHFVVPR VPNENFKGHD GTRQLIKAYR
KFSMPMPPGL LDAIAAQAAK NPEPVKAESV QAGGFKAFAA NDSTAAAGAP ETGTTTATPI
RNDVEYISPI KIGGQTINVD FDSGSSDLWV FTSMLDAQAQ TGHELYDPTK SQTAKMLQGQ
QFNIRYGDGS GAQGVVGTDV VDIGGAVVQN QAIEMATAVS QQFIEDTSNN GLMGLAFSKL
NTVKPNIQKT FFDNVMSSLA EPVFTADLRK KTVGAYEFGR IDNTKFTGQM NWAPINTTSG
FWQFSSEKFA VGDGKVQTGL VGGQAIADTG TTLLLANPTM VQAYYEQVQG AKNDQTVGGI
TFPCNASLPD LMMDIGGAFM ARVKGSDINF AQVDQQTCFG GLQATTSNLQ IYGDILFKSQ
FVAFNGGNNS IGMAEHVVSS QNAGVAVGTG SGAAA
//
