ID E3QLB6_COLGM Unreviewed; 537 AA.
AC E3QLB6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 08-NOV-2023, entry version 53.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:EFQ31654.1};
GN ORFNames=GLRG_06943 {ECO:0000313|EMBL:EFQ31654.1};
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}.
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DR EMBL; GG697356; EFQ31654.1; -; Genomic_DNA.
DR RefSeq; XP_008095674.1; XM_008097483.1.
DR AlphaFoldDB; E3QLB6; -.
DR STRING; 645133.E3QLB6; -.
DR MEROPS; A01.077; -.
DR EnsemblFungi; EFQ31654; EFQ31654; GLRG_06943.
DR GeneID; 24412308; -.
DR VEuPathDB; FungiDB:GLRG_06943; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_10_1_1; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000313|EMBL:EFQ31654.1};
KW Protease {ECO:0000313|EMBL:EFQ31654.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..537
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003179846"
FT DOMAIN 140..444
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 445..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 338
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 171..176
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 537 AA; 56968 MW; 627EDC27CE902002 CRC64;
MRSATLVYLS LLFTSTHAFF PWPSPECLEK GDCVLPTKRQ LKGQDELRSD VVDAVKAINL
PASQLGPQAT HDFSTKDAES ERVVREVERL TRKYARFQSA AVREKALRSK RESQYRIVKA
ADTKLKNAVG VAQDGTDFSY FAQVKLGNNK KPMWMLMDTG AGTSWVMGSS CKSAACEKHG
SFGPPDSATY KATGETFSVA YGSGSVKGDK VTDTLSFAGM NFNFQFGVAN ETSDDFNHFP
FDGILGLSMA GGETENFMQV VKNSTQLPAN IFCVYLSRAA DGPNTSEISF GVCNPDKYTG
DITYTAVGNA LGDWAVPLDG IAYDGLKSGA AGKLAYIDTG TSYVFGPKDD VAAFHKNIPG
STADEAGTTY KVPCDSNKDV TYTFSNISYV ISAKDWRGVP GTDGTCTSNI YGHEVVTGAW
LLGDVFLKNV YAVFDTDQKR IGFAKRVDPP PVTTTSSSDT SATPPVVGNS DNANIGTPVQ
TSKPGLGLGG HETTASATAA AQTSPVSHSG AASSASLTVV KAATVATFCL VALLGFH
//