ID S7QIV5_GLOTA Unreviewed; 435 AA.
AC S7QIV5;
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:EPQ59571.1};
GN ORFNames=GLOTRDRAFT_136410 {ECO:0000313|EMBL:EPQ59571.1};
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:EPQ59571.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ59571.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ59571.1,
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; KB469297; EPQ59571.1; -; Genomic_DNA.
DR RefSeq; XP_007862518.1; XM_007864327.1.
DR AlphaFoldDB; S7QIV5; -.
DR GeneID; 19303527; -.
DR KEGG; gtr:GLOTRDRAFT_136410; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_1_4_1; -.
DR OMA; SINQDFW; -.
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; NAPSIN-A; 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:EPQ59571.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..435
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004556174"
FT DOMAIN 109..432
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 322
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 435 AA; 44581 MW; AE4C004616FD6CA4 CRC64;
MVPGILFGLV LLPVLASAAA IPSNNVTKIA LNRNVLFSNS GVANIPALRQ HLGNVVNKYQ
HGFSNFQKNT GHPHPLSVGS FFRHLFGGHR LKRAEGNVPL SNFQSGAVWS GAISVGTPPV
TYTVDFDTGR RAVAQQSIYS NNSVGSSDLF LPGANCDSTC AGHTLYNTAS SSTAVDQGQT
FSLAFGDGSS VTGEVFVDTV TISGLTATGQ AVGAANQYSS SFEVSQFPAD GLMGMAFQSI
SAFDQSPVFQ TLINQGQTTS PVFGFSLTST GGELTIGGVD GTQFAGTLTQ VPVTQQGYWQ
VDLAAVNVNG QATVTGVSAI IDTGTSLVLG NTANVAQFYA AIPGSADATS TVGAGFFTVP
CASIPSVSLT FGSTAFPISA DTFNLGQVSA GSADCVGGMV ASDLGSFWVA GDVFLQNVYT
SFDMGNNQVG FAALA
//