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Database: UniProt
Entry: E3Q5J4_COLGM
LinkDB: E3Q5J4_COLGM
Original site: E3Q5J4_COLGM 
ID   E3Q5J4_COLGM            Unreviewed;       537 AA.
AC   E3Q5J4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Subtilase {ECO:0000313|EMBL:EFQ25961.1};
GN   ORFNames=GLRG_01105 {ECO:0000313|EMBL:EFQ25961.1};
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 S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; GG697333; EFQ25961.1; -; Genomic_DNA.
DR   RefSeq; XP_008089981.1; XM_008091790.1.
DR   AlphaFoldDB; E3Q5J4; -.
DR   STRING; 645133.E3Q5J4; -.
DR   EnsemblFungi; EFQ25961; EFQ25961; GLRG_01105.
DR   GeneID; 24406470; -.
DR   VEuPathDB; FungiDB:GLRG_01105; -.
DR   eggNOG; KOG1153; Eukaryota.
DR   HOGENOM; CLU_017824_0_0_1; -.
DR   OrthoDB; 2735475at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          99..327
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          36..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        108
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        146
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        309
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   537 AA;  56525 MW;  C34311AB72B091B9 CRC64;
     MDTIVNDADI PFVWRANLTS DQLETVKADS VIAGADINDP LTRDDPEPDK TQSSATRRKR
     VEIAQSPIPN NDIFDLRTLS TPPKQKATLP DYRYDDFAGH GITVYVVDTG PFDLQHEEFT
     APSTDVTRRE LNVARNKKFS LEDTQHGTCV ASKAVGVTAG VAKRANLVGV RIDFTEFGLL
     RGLQAAANEI KQKGLKGKAV VTTSILIRAP DNIYTTSMRS VIRGLINLDV PVVAAAGNKF
     LDGLTEPDKL PAVMANELPI IVVGSAGTDF NIAPTSQRGN LVTTFAIGAD IKCADPLDQT
     GLATDSGTSF AAPQVAGLVA YWMSHPEFAG NLPPGSVAET LRNITGALSY PRVAEAGFPP
     IAWNGHDLAE SCSVPNSGIG RRVRRNMRRD LSQACSFAPT SVPSATPTVP VPSAAPTVSV
     PSAAPTVSVP ASSAPTSGLV TPTATPETPT CNLCGAEFQG GTLGGQVGCA DAEVARSACA
     ADDTCNSWAF GNENRGTYTI PVCLLFDQSA TQIVSQAPPD PEGKCPFRYN DKACPAS
//
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