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Database: UniProt
Entry: S7RGH1_GLOTA
LinkDB: S7RGH1_GLOTA
Original site: S7RGH1_GLOTA 
ID   S7RGH1_GLOTA            Unreviewed;       489 AA.
AC   S7RGH1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   08-NOV-2023, entry version 46.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:EPQ51649.1};
GN   ORFNames=GLOTRDRAFT_117968 {ECO:0000313|EMBL:EPQ51649.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS   rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ51649.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ51649.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ51649.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; KB469310; EPQ51649.1; -; Genomic_DNA.
DR   RefSeq; XP_007870089.1; XM_007871898.1.
DR   AlphaFoldDB; S7RGH1; -.
DR   MEROPS; A01.078; -.
DR   GeneID; 19300419; -.
DR   KEGG; gtr:GLOTRDRAFT_117968; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_1_2_1; -.
DR   OMA; FYPAWML; -.
DR   OrthoDB; 1203010at2759; -.
DR   Proteomes; UP000030669; 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; cd05471; pepsin_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; 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:SF6; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
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:EPQ51649.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..489
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004544549"
FT   DOMAIN          89..424
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   489 AA;  50712 MW;  F4EE8327CAD8B82B CRC64;
     MRSCIPNVLL VSLLSTSAVI CSPAPSAPPS KGTTIPLTRR SVHKRSAAEW DEWAVRHREY
     VTKKYNGQVK SKRASGMNLL TDQDADSDYY GSVAIGTPAV SYNVILDTGS SDLWLASSSC
     SGCASSSGGG PTSAASNSIP LFDPASSSTF KNLTTPFAIQ YASGQATGTL GQDTVQVAGF
     QVSDQTFGVC DTANGVLSSP LSGLMGLAWQ SLASSKATPV WQTLAASGQW DSGVMGFFLT
     RFGNDSHAKE LEPGGQFSMG YVNDSLYTGS IDYQNVPSDQ VAYWTLPVTS LTVQGKSISL
     PTSGSNQYAA IDTGTTLIGG PSDLVQSLYS NIDGAQAGTG SWEGYWFYPC STSVSSSISF
     GGPSWSISPD DFEHTQVDSS GTQCVGAFFE VNTGDNTPGW IVGDAFLKNV YTAFRYSPPS
     VGFASLSSTA LGENGVDGIA PSATIGSPAA VVSSTGKASS NKNDATRSRG FSVQILALVW
     GAAGGLLLA
//
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