ID T1KUT8_TETUR Unreviewed; 737 AA.
AC T1KUT8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur22g01230.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur22g01230.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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DR EMBL; CAEY01000581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1KUT8; -.
DR STRING; 32264.T1KUT8; -.
DR EnsemblMetazoa; tetur22g01230.1; tetur22g01230.1; tetur22g01230.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_006842_17_0_1; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF10; SERINE PROTEASE 56; 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; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Serine protease {ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 496..736
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 132..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 78188 MW; 500D60BEE282C5A6 CRC64;
MSTIESSPAA IIFYLYSVII TVTQAVPVYQ DYLRYYVKDY SDSRSIRPLT CKSLDGTVGV
CMFSLACRHA NGHPIGLCKD TIYSGSCCRL PVNNNNTHDG SHVDEVENFL EYPVGTNRTS
PKVPIVNVSQ SLSPSSTASL PSSPSTSTTA FSPSISTTIT TAASISTTTQ ADNTTPIASS
YPATLLSSSS TSQSTSQSTS QSTSQSTSSS TSPPTLSTSS STSASSAASS TASPSTSPAT
SPATSSATAS STSSSPSSST SSPTSSILST LSSEPSSLKT TQQSSSTVSN LVTTVTSLDT
SEFPTTQGDG EEETKKESMY MIDDGKVRSS STTAFLTSTS STQVPTKLTE STISSQSMIT
SDAPSSQLTN KPDSLTNPST ASTSSTSSES TSLHSTLTSS TATRTATVST SPPTTPLKTA
PPTPAIVSTL STSTTTTTTT KSPPPSSTTS TTTIKIPTLN RITSPSTVAP KNHTNHQGIK
AICGRKMNGP GPTARIVGGS QSSFSEWPWM VSTRQWKKNA FLHKCGAALL NEYWAITAAH
CVENVAPTDL LLRLGEYDIS HEDEPFGHIE RRVQIIAPHP KFDPRTFEYD LALLRFYEPI
TFRKNILPIC IPEGNKSFVG RKATVTGWGR LYEEGPLPNT LQHVEVPVIT NQECEMMYRR
AGYLEEIPNI FICAGMSSGG KDSCEGDSGG PLVIEENGQW NLIGIISWGI GCALPNQPGV
YTRITEFARW IHQIIAY
//
