ID A0A232FHI8_9HYME Unreviewed; 1430 AA.
AC A0A232FHI8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN ORFNames=TSAR_004391 {ECO:0000313|EMBL:OXU29928.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU29928.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU29928.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU29928.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU29928.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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:OXU29928.1}.
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DR EMBL; NNAY01000219; OXU29928.1; -; Genomic_DNA.
DR STRING; 543379.A0A232FHI8; -.
DR Proteomes; UP000215335; 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; 6.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 12.
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; PTHR24276:SF101; FI18310P1-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 6.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 6.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 6.
DR PROSITE; PS50240; TRYPSIN_DOM; 6.
DR PROSITE; PS00134; TRYPSIN_HIS; 3.
DR PROSITE; PS00135; TRYPSIN_SER; 4.
PE 3: Inferred from homology;
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:UP000215335};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1430
FT /note="Peptidase S1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012556734"
FT DOMAIN 22..251
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 252..463
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 480..714
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 739..962
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 923..1190
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 1208..1428
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 1430 AA; 156671 MW; A6F99E02B3D1B34A CRC64;
MKVLVSLLLL CCAVAIHAAP RVVGGSDAPD GKYPYQVSLQ AYGMHLCGGS ILNKRWILTA
AHCLIYIEAE SIEVHAGTNK LFGGNDHVYQ ADYITSHKEF SMKSLNHDIG LVRVNKDIVF
NEKVQPISLP THDVSKVDTP AILTGWGSTK LGGAAPNNLQ QLLLKVVSQE SCGKVWNSEY
PITESHICTL TQAGEGACHG DSGGPLVADN VQVGIVSFGR PCAQGKPDVF TRVLVSLLLL
CLAVAINASP RIVGGHDAPE GKFPYQVSLR SYGRHFCGGS IINKRWILTA AHCLQYQLPS
GIQVYVYQAE YLTYHEKFSM NRLVNDIGLI RVTEEIEFNE KVQPIALTSV DVSKVDTPVV
LSGWGRIKLG GAVPNNLQEI DLKVVSQERC NQSWSPTYPI TESHICTLTK VGEGACHGDS
GGPLVADKVQ VGIVSFGRPC AKGEPDVFTR VYTFLDWIQQ QQENLLLLCL VVAINASPRI
VGGHDAPEGK FPYQVSLKFD GSHFCGGSII NNRWILIYFN HEQIDKRVIC QLSVSLRASE
VIVYAGTNKL NDGMPQIYQA EYLTYHKDYN TSRKLNDIGL IRVAKDIEFN EKVQPIALTS
KDIPKPDTPV VLSGWGKIEY GGAVPNNLQE IDLKVVSQER CNQTWGTSYP ITESHICTLT
KTGEGPCHGD SGGPLVADKV QVGIVSFAKP CAKGQPDVFT RVYTFLDWIQ QEQEKVLSVF
VHVYLATLTF LCITASPRIV GGHDAPDGKY PYQVSLQSYG RHSCGGSIIN KRWILTAAHC
LQYQRPSNII VYAGTNKLKG GKPQVYRAEY LTYHKDHKTS RKLNDIGLIR VTKEIEFNEK
VQPIALTSED IPKPDTPVVL SGWGAVKLGG AIPNDLQEID LKVVSQERCN QTWSSEYPIT
ESHICTLTKQ GEGACHGDSG GPLVAGKVQV GIVSFAEPCA EGEPDVFTRV YTFLDWIQQE
QENCSTYRRR NDAPDGKYPY QVSMQVYGHH ICAILFSIIL FFSSNKSIII AGGVKSLKIH
AGTNKLSGGD AQVYQADYLT FHKKFSLQKL ANDIAMIHVN SDIRFNEKVQ PIALPDYDVS
KVDTSVVLTG WGTLRAGGPI PNSLQEIDLK IISQEACNHS WSSKYPITES HICTLTKVGE
GVCHGDSGGP LVAGDVQVGI VSFGNSCARG DPDVFTRVYT FLDWIKEEQE KLLMCLSFAV
VAYAAPRIVG GQDAPDGKYP HQVSLRAPFH FCGGSILNSR WILTAAHCVV GRSGNAVTVV
AGTHLLNGGS EQVFKSEYIV WHEKYNGGLF INDVGLIRVD RDIVFNKKVQ PIPLPNEDFS
KVDYPVVLTG WGRTQAGGPI PNNLQEINLK VISQTKCNEK MSVAITKSHI CTLTKIGEGA
CNGDSGGPLV ADGIQVGIVS FGMPCARGMP DVFTRVYTFI SWINEKMEKY
//
