ID A0A3S3Q6T8_9ACAR Unreviewed; 354 AA.
AC A0A3S3Q6T8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Enteropeptidase-like protein {ECO:0000313|EMBL:RWS04454.1};
GN ORFNames=B4U79_16412 {ECO:0000313|EMBL:RWS04454.1}, B4U79_17633
GN {ECO:0000313|EMBL:RWS10275.1}, B4U79_17634
GN {ECO:0000313|EMBL:RWS10262.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS04454.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS04454.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS04454.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:RWS04454.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS04454.1};
RA Dong X.;
RT "Trombidioid mite genomics.";
RL Submitted (NOV-2018) 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:RWS04454.1}.
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DR EMBL; NCKU01005534; RWS04454.1; -; Genomic_DNA.
DR EMBL; NCKU01002156; RWS10262.1; -; Genomic_DNA.
DR EMBL; NCKU01002149; RWS10275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3Q6T8; -.
DR STRING; 1965070.A0A3S3Q6T8; -.
DR Proteomes; UP000285301; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24256:SF470; IP10114P-RELATED; 1.
DR PANTHER; PTHR24256; TRYPTASE-RELATED; 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.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301}.
FT DOMAIN 1..170
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 190..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 39190 MW; 2E96E982ABA2873E CRC64;
MQNHSNDIAL IKMDKPVDFA GSESHLKPAC LDLNGLEKNL DNETRCVATG FGRLGRGNAP
LPDVLQQLDM KPYDHADCAR THRIFYEWEE SKEEVTDKQF CMVSKDNAQP DFGVSYGGGC
LGDSGGPLQC FINNNWIQIG VAWSVTDCEQ NPTVFQKIYK YADFIKNTSN YTLPPSCNVL
LLTSSFLNDD SDDEKQSTEQ TERDDQQPTK GGDKGEQNKN QSSGKKGGKD DHDEQKGTKG
DQGGKKQPRK SPQFNPRPGG KGQNEQKSTK SGQGGKRPQF KPRPAVKGQN EPKGTKGDQE
DKKQPEKSPP IKGKDGQNEK KGSKGSQEDE KQAQRRPWGK RQPGGYIKID GVKQ
//