ID A0A0V0VMY7_9BILA Unreviewed; 1162 AA.
AC A0A0V0VMY7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Transmembrane protease serine 9 {ECO:0000313|EMBL:KRX64878.1};
GN ORFNames=T09_742 {ECO:0000313|EMBL:KRX64878.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX64878.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX64878.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX64878.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX64878.1}.
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DR EMBL; JYDN01000021; KRX64878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VMY7; -.
DR STRING; 181606.A0A0V0VMY7; -.
DR Proteomes; UP000054681; 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; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4.
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 PANTHER; PTHR24250:SF50; CHYMOTRYPSIN-LIKE PROTEASE CTRL-1; 1.
DR PANTHER; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 4.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 4.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 4.
DR PROSITE; PS50240; TRYPSIN_DOM; 4.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KRX64878.1};
KW Membrane {ECO:0000313|EMBL:KRX64878.1};
KW Protease {ECO:0000313|EMBL:KRX64878.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000313|EMBL:KRX64878.1}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1162
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006871076"
FT DOMAIN 51..306
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 355..625
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 645..921
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 928..1159
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 1162 AA; 129453 MW; 7C813B7E799C9671 CRC64;
MMMCRTNLQR MFAISLLIIL INGNLSDELY DDGICGRPKF QPKFVSEDNR ITGGIEALPH
SHPWIVLLTS SSDTEYKCGG TIIPSRELNR SSYILTAAHC VEYIAISEII VTAGMHDSSV
SSEMGRQVAR VSSASISPEF KSNRRYDYAI LTLEQPFIFN NYVRSACLSA RHEYLKPRTK
CFAAGWGATT GGYYKPVMEG QILRAELPSF PAKLRQTTLT VHSHSFCEDK SVFSTSYDSK
INLCAGDVFG ENGINNCDSG GPLICLKEGL WTLYGISKGR SLNHVTQPSL FVKVSGITSF
LEEITGFTKY LKHKYLFFTI LIIQMDRSRS FKVNDDGICG RPKYQPKFNV SDNRITGGEE
AIPHSHPWIV FLSLTHGRKF VCGGVVLQSH EKNVTSYVLT AAHCVKNINL ANLIVQAGFH
DLTYNTEKGK QVVTVSRIII SDLYMTNYDH DYAVLVLSSP LKFTDYVIPA CLSQELENFP
LGSKCLIAGW GGIDGGIYKP VIRKSGRNVK SISSRYLVLP KTLMQAVITI IDDNNCSNAF
FASYDSAINL CAADAMGVIG INNYDSGGPL VCLKDGLWSL HGMGVSRAFF DSTQPSINGR
FCHIFHYLRL YNINFYPVYY TTSYDDGSCG RPVFQVKYNM SEHRITGGVE ANPHSHPWIV
LLRSFHSNKY CGGIILPTYS VNFSSFILTS AHCVYRSNIS HLLVLAGVHD IQSLSDEGIV
AATVKNVFIH PFYLYNSDYD VAILKLKNPL LYNSYILPAC LPRKNEYLKP RTRCLASGWG
AIDGVQNSII SRTPIFTTKL MQTEIIIHSH SFCQHESVFY DSYDDEIYIC GGDIFGIKGT
NTRDSGGPLV CMKSGVWTLY GVVKARGHHH ETQPSLEQIK DGNLECGLPK YQPIYEFSEN
RVTAGVEAIP HSHPWLVFIT SKIKDDKCGG AILPSRERNS SSFILTAAHC IFYLRKEEIM
VTAGMHDQSL NNEIGRQSAD VKRRVINITY KKNKGYDYGI LILLQPLKFN DYVKPICICK
EREHLMPGTK CLIAGWGAID GGAYKPIIKN NTITRRQTVF PTVLMQTVLA VYSNAYCANA
SFFSTGYDSV INLCAGDDLG EKGVNNADSG MPLVCLSEGL WTMYGIARGR SAFSPKQLSL
FIQIASITRF INFYTGYLMQ GK
//