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Database: UniProt
Entry: S7RND1_GLOTA
LinkDB: S7RND1_GLOTA
Original site: S7RND1_GLOTA 
ID   S7RND1_GLOTA            Unreviewed;       499 AA.
AC   S7RND1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:EPQ54274.1};
GN   ORFNames=GLOTRDRAFT_62809 {ECO:0000313|EMBL:EPQ54274.1};
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:EPQ54274.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ54274.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ54274.1,
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; KB469304; EPQ54274.1; -; Genomic_DNA.
DR   RefSeq; XP_007867573.1; XM_007869382.1.
DR   AlphaFoldDB; S7RND1; -.
DR   GeneID; 19307506; -.
DR   KEGG; gtr:GLOTRDRAFT_62809; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_1_1_1; -.
DR   OMA; ITIWMEL; -.
DR   OrthoDB; 4946at2759; -.
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:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EPQ54274.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..499
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004544597"
FT   DOMAIN          179..496
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        210..218
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   499 AA;  52762 MW;  8FC999C6164A1C53 CRC64;
     MKVNMNFSGL LAAVVLAVSL GTPSDARPAP SGSGLVTVPI TRIHKTSHRD IIDTQAIHLQ
     HVNRGNQRLA LMSGRPAPTP EELQEIHRRT GELPADLSKR YWREGVVKWL EDLKTQMKGA
     GSAMSKVESF MDTDGSGSSS GGFNPMDLDA ANENTLTPAN APSYDHSLGL DISANDIGYL
     ATIQIGTPPR DFKVLVDSGS SDLWVGAENC AANGGGSCGN HTFIGSSSST SFNDTQKTWA
     ITYGSGFLSG TIAQDDIEIA GMKLPAHQFG AAQNESSQFT GSDTLFDGIM GLGGSQLSNQ
     GIPTIVEALH SAGLIQAPVT SYKLARLADG NNDGEITFGG MDPAKFDASS KVTVKNVSPK
     GYWEANVDSF KVDGKDVNLS GRTAILDTGT TLIVGPGLDV DALHEAMPVS RFDGFNWIIP
     CTTTTKVSLT FSGKEFEIDS RDLTFLPVSS TNLTGDCYSS ITRGTVGGDQ EWLVGDVFLK
     NVYFSTDVGS NEISLASLA
//
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