ID R7T084_DICSQ Unreviewed; 1146 AA.
AC R7T084;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:EJF61623.1};
GN ORFNames=DICSQDRAFT_180632 {ECO:0000313|EMBL:EJF61623.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF61623.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF61623.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF61623.1,
RC ECO:0000313|Proteomes:UP000053319};
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; JH719409; EJF61623.1; -; Genomic_DNA.
DR RefSeq; XP_007365718.1; XM_007365656.1.
DR AlphaFoldDB; R7T084; -.
DR GeneID; 18840899; -.
DR KEGG; dsq:DICSQDRAFT_180632; -.
DR HOGENOM; CLU_277067_0_0_1; -.
DR OrthoDB; 1507272at2759; -.
DR Proteomes; UP000053319; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09917; F-box_SF; 1.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR032675; LRR_dom_sf.
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:SF89; SACCHAROPEPSIN; 1.
DR Pfam; PF00026; Asp; 2.
DR Pfam; PF12937; F-box-like; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EJF61623.1};
KW Protease {ECO:0000313|EMBL:EJF61623.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053319}.
FT DOMAIN 15..431
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 560..611
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 158..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1146 AA; 126148 MW; A0803FBCFCE4AC16 CRC64;
MCMRRVASIT PTSTYNVLVQ VGETFVPLLL DTGSADLWVV TDQCGDSCVQ ANVPLYPHAD
LTPAGQDVQL LYGDSRTGTH ATGPIGTATV GVAGMSIPDQ YFAAIVDTNT TVLQTGSSGI
LGLGFPPISV IWRQLLSSNT TRVIPPIYKR WVAVPEDSPA RQDHSSSSAD STGRADHTSG
SQKSRVTTQQ SFASPADSFS TLGSFFTRLV TWEILSRPLV VTSLQRDTFS LSETTGTLSL
GGLPFGLTDE DLTWVPVRSY SPSQGGLPPP PDAPNEVYPL VWEIPVDDVY LDGTKLPRSM
LSPASISLSA LIDTGNSLIR GPQDVVEQII SILGNTFDCS IPHTLSFEIG GIRFPVDPRD
FAHPRKSHHN SGYPALHARC RPALVSTDPP SSDGFSYSWS LGDPFLKSTL VAFYYGNMTR
PSVDPPRVGL RSTVPSNAGA ELEEAVSAAL FRGGIFPATS QAAPDATPLQ MQSMSPSADM
VPEETQSMPY DVNAWSFSQD NSAYKQLPPD EIQEWCLSRT AEYQTHIFFI RKHLAPAAYD
AVCEIKSKIR GLRHEYNSAA PIHRYLPPEL LMEIFAYIHP AMTHRRSLRV LRVCRYWRNL
IVKTPQFWAN LLSFPLTASS WSPLWHMDRF NVELARSAPQ SLTLSLDHCN ALTVSTLTIY
ADRISSLALA FHVLELENVT RLLQRHMPRL RHLSIRKCYQ IGNRPTLTLT FPHYPSLHSL
QLERSHFYPP LAPHTSLRHL KLKFATVHSL PTTSNFVSSM RSIHDALANF PNLETLCTAF
SLSEYGGRGF FNEPAPELTR IVRLPLLRHL EIQDMSAHIN MFLRHLDFPS TTSLVLEPAY
KFTRGPMMVP VPPGINNASH AQRAEMSLSL CVWPFDGSAR WETHGDGVRP VSVTLSMAAR
RLDIVSTFTS ELVNALAPAG GLTSLTAEGT WGHAKEYWTT LIPRLPRLRH LTCVASTTTR
DVVPLLGKPQ TNGEFLCPNL THLTVAWTLP YDVSVGSGLA TQLMPSDAAV VESREGGVDD
DRGMTASQDS LCGMLRTCLT ERAGHCGPIQ KLSVAFGGSC GIYEAVLQPR ELHSFEQRLR
DTLGMFLPEI AVMNEELALT VFWIGLEQSA TELSSSYLQN IVSITISIEF SDVTLLNQLL
TDERLS
//
