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
//