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Database: UniProt
Entry: S7RKM8_GLOTA
LinkDB: S7RKM8_GLOTA
Original site: S7RKM8_GLOTA 
ID   S7RKM8_GLOTA            Unreviewed;       728 AA.
AC   S7RKM8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Acid protease {ECO:0000313|EMBL:EPQ54930.1};
GN   ORFNames=GLOTRDRAFT_62321 {ECO:0000313|EMBL:EPQ54930.1};
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:EPQ54930.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ54930.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ54930.1,
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}.
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DR   EMBL; KB469303; EPQ54930.1; -; Genomic_DNA.
DR   RefSeq; XP_007867146.1; XM_007868955.1.
DR   AlphaFoldDB; S7RKM8; -.
DR   GeneID; 19307470; -.
DR   KEGG; gtr:GLOTRDRAFT_62321; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_014988_0_0_1; -.
DR   OMA; SSPMYDI; -.
DR   OrthoDB; 1449676at2759; -.
DR   Proteomes; UP000030669; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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; 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:SF92; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00026; Asp; 2.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:EPQ54930.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EPQ54930.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        465..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          54..399
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          600..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..625
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..728
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   728 AA;  76924 MW;  61EA0B8E639ADA17 CRC64;
     MSARAGIPLR RWKGKGREVL LESRSASTTE GNGGNDGVVM PMQMTGDGTY NVEYTVPITV
     GNGQTLSVQV DTGSSDLWLA STSCSSSACS STNGRLYNPG QALPTGQTFN INYLIGNVSG
     PIVWDEVQLG GYSITNQALA AASKVDGEPL SQNFDGVLGL ALPGNSIIQA AIMPTLGDSP
     DGAAFSSNLF GITPVSQAPP VRFLSLSLER PGSDRTPSLL GIGRHPSQVA PDPSKIAYST
     LLASSSAGVR FWETSIRAIT VYVDGGAKAV SLGHSHTGAV YPIAVVDSGV PYIITTSAIA
     NGIYGAIGIN PAANGQYYVP CSTPLNMTIS LDGQPELPLH PLDLTAVPLQ DASSPNCIGL
     IQAADGALAN IPGDMILGVP FLRNVYTVLA YDVPDSNGAF PQVSASTTAN SINPRLGLLS
     LTNATTALDE FHTVRVLNQP LSKTPKTSDT NGVAGKKGLS VGLDVLIGLL SFFGLCAVLF
     GLRWVLAKRQ WRRSHPRGEE GQLDAKDSGY ALAALHPNGD GPSEETLRTL RYEAYKRNKR
     MHSEYSTDSA LTKVDVDERE DSGYLPDHEL GFRPSFYDKG RHDPHASIAT DWRDTLVGEA
     DSAGTPRAKD ESPSPEMHRR HLSDPEAPVT APLLAHARTH SQTSQGSDVG QAGDRVSMAG
     IGSASRGSRH LEHGLRDSVG SFGSFHDVDG SGNRVYAPSP LRPHPTHAPD RPRSPLEDRG
     GARPEYEP
//
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