ID A0A2A4JZ21_HELVI Unreviewed; 546 AA.
AC A0A2A4JZ21;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN ORFNames=B5V51_9048 {ECO:0000313|EMBL:PCG76632.1};
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG76632.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG76632.1, ECO:0000313|Proteomes:UP000218220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG76632.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG76632.1};
RA Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA Gould F.;
RT "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT response to modern agricultural practices.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCG76632.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NWSH01000406; PCG76632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4JZ21; -.
DR STRING; 7102.A0A2A4JZ21; -.
DR Proteomes; UP000218220; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR041515; PPAF-2-like_Clip.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24258:SF150; FI16631P1-RELATED; 1.
DR PANTHER; PTHR24258; SERINE PROTEASE-RELATED; 1.
DR Pfam; PF18322; CLIP_1; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..546
FT /note="Peptidase S1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012020097"
FT DOMAIN 291..544
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 51..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 56424 MW; B9A225EC99FE915E CRC64;
MCLWILTACL GLLPANPSPV VVVNGVPAPI IVPTAAPTVA TTAATTAATT AATTAATTRP
PTPAPTTAAT TAATTASPVT PPPTTAAPTT AAPTTSTPVT PPPTTAATTV TPAPPTTVTT
AAATTLGGMD LSLIICIDPD VVCIFNPDET IAGPLPIDPR LGTTPAPSAA VNMPPISGYS
AQLPTYDSAV KFPRQRRSLD DEHAVNMKDF LCSVGTGRKH SIVKRQSNCA CVPTGTCVRT
TTNNGAGMID IRIVTPVATQ CPSGQEYCCT DSTTSTLINC GTLQSVPATA ITPAAGQANF
GEFPWQALIL TKQNDYIAGG VLVDQLNVLT VTHRLLPYVV SGTAPNVKVR LGEWDAAGTY
EPVPFQEYTV TKVFSHPSYN ANTLQYDIMV LRLSASVPIT PNVGAAVTIN RACLPPSSTT
TYTGQRCWVS GWGKNMFGLQ GQYQQILKKV DVPIVAPATC QTQLQTARLG ATYVLDTTSF
VCAGGEANKD SCTGDGGSGL VCQVNGQWVV VGLVSWGLGC ANANVPAAYV NIAGLLPWIQ
QQIATT
//
