PTASE_MBVLF
ID PTASE_MBVLF Reviewed; 657 AA.
AC Q9YPD6;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Putative serine protease;
DE EC=3.4.21.-;
GN ORFNames=ORF2;
OS Mushroom bacilliform virus (isolate Australia/AUS LF-1) (MBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Barnaviridae; Barnavirus.
OX NCBI_TaxID=650482;
OH NCBI_TaxID=5341; Agaricus bisporus (White button mushroom).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8030251; DOI=10.1006/viro.1994.1412;
RA Revill P.A., Davidson A.D., Wright P.J.;
RT "The nucleotide sequence and genome organization of mushroom bacilliform
RT virus: a single-stranded RNA virus of Agaricus bisporus (Lange) Imbach.";
RL Virology 202:904-911(1994).
CC -!- FUNCTION: Putative serine protease. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S39B family. {ECO:0000305}.
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DR EMBL; U07551; AAA53089.1; -; Genomic_RNA.
DR RefSeq; NP_042509.1; NC_001633.1.
DR SMR; Q9YPD6; -.
DR GeneID; 1497108; -.
DR KEGG; vg:1497108; -.
DR Proteomes; UP000006824; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000382; Peptidase_S39B_luteovirus.
DR Pfam; PF02122; Peptidase_S39; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51868; PEPTIDASE_S39; 1.
PE 3: Inferred from homology;
KW Host membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..657
FT /note="Putative serine protease"
FT /id="PRO_0000402445"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 239..434
FT /note="Peptidase S39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT REGION 513..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 284
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 318
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 386
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
SQ SEQUENCE 657 AA; 73415 MW; A55C331F24675888 CRC64;
MSKYLATSVR LCLMVCIVGW LLMPSYKELD GWCSSLSSLE RDKSNWLLTG LSTWFCIVPS
GTDQSSLVSY FSPLEKLSKF VQDLDLDFVK LWWLETITLI NTLNTTEKLL SGVTFSVVLW
YPRILVTVLM LVWKLWFPVR FLVVASSLLC LRILVWPFEV IADVILETCA WFTRKYHKLM
DVIEDLMMIP QRVMEWCSGN TAKMVVPTVA SCVSESIESK LDRILMALGR KGTVLEAAQP
GSDFVECEQW PNGLVAIRRH DGRIVGMGFL VVLNGKWRLV TAAHVARECK RGIMLSAGID
SKTVTFQDLD VVLQTQVDAC IMNVPAGTAA SLGVRKVVIN RTPSESKVVR TYGYNSGKFC
MSEGLVGTTS ANMGFRHGCS TLRGWSGTPI YRDNKVVGIH SRCNGIYENF GLSLDLLVGR
LESEETDRYA RTMEEFNTED RPVTPPMEFS WEFEEKFERV RSTRKSFARI ESEVATFTAT
KLSGFDWTDD APMDFDELPV FESTMVSVFQ ERPLGGLPIS NGNKAEEKKI TSEALEPSKS
STPEAAKHTR RRRRNKKKSK NSETGHGPEE QSQQQSRPSS PIPDDSAPVS SPPVSPPSTG
SVPKSWTQAY TQKLVLLLGS MDGQSKEKVD LAILEAKSFA SALFPPSKPK SSEESEK