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Database: UniProt
Entry: E3QLB6_COLGM
LinkDB: E3QLB6_COLGM
Original site: E3QLB6_COLGM 
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
//
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