ID A0A0V1PJL3_9BILA Unreviewed; 1318 AA.
AC A0A0V1PJL3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Serine protease 30 {ECO:0000313|EMBL:KRZ96357.1};
GN Name=Tmprss9 {ECO:0000313|EMBL:KRZ96357.1};
GN ORFNames=T08_10189 {ECO:0000313|EMBL:KRZ96357.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ96357.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ96357.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ96357.1};
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:KRZ96357.1}.
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DR EMBL; JYDM01000008; KRZ96357.1; -; Genomic_DNA.
DR Proteomes; UP000054924; 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; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
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; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 1.
DR PANTHER; PTHR24253:SF153; TRANSMEMBRANE PROTEASE SERINE 13; 1.
DR Pfam; PF00089; Trypsin; 3.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 3.
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, ECO:0000313|EMBL:KRZ96357.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1318
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006884260"
FT DOMAIN 48..288
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 646..886
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 989..1205
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 429..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1318 AA; 150551 MW; 5A4D363D743BFC77 CRC64;
MKRFHHLEIF FYRALLIFCI IIKKTFSGDC GKPYFEPYLT NPRNPNRIVG GWVAKPYSFP
WTVHILTHVS GLLYESCGGS LISLDSTNAS DTILTASHCV RVNNRLVNAN AITVAAGVFN
IKKLNEPHRV TSKVLAYISD NFDDVSMEND IAVLRLKVEI QHSEYISPVC LPKQNQKLPW
GEMCFVSGWG LTRESGKPSS KLRQVGIPIL RNSNCPFIDA DDMFCAGDMS GGKDSCQGDS
GGPLVCKLND TFVQMGIVSF GDGCARKDHP GIYTKVPHYV KWIYNQAAKL PDSSTSSEIG
EEKPDYSNDF HHSWGSVGNY FHFPFFDSSD DIWNNENFGN ENSPFSQLPW SFLSEPMPLF
RSRSSFINRD VEEEAGDWSP YSTNQHFQTY YGRPHIGEEG QPHYPLENWP DMNGKYPLHH
HSEFHPPYLY SNRPSMNEGH LSRPPNFESP ENQPPYTSEN SPEMNGNQYS GKSYTKFYHP
YLYPNGPSTN DHRPSLASNF EKPENQPQYT SKNRLEMSGN HHFGKSYRKF RSPYSYANGP
SINGDHPSSP PNFQNHENRP TYTSERRHEM NGNYYSGNRL PYSHSNRPTM NENPYALNMK
RWHPFGIPFH NAFLLFCIII KETFSQYCGN PYFEPYLTNP HYPNQIVGEW VARPYSFPWT
VHVLAHISGF WYESCGGSLI SFDYSNASDT VLTSSHCVRV NNRLVDANAI TVTAGAFDIR
DLNEPHRVTS KVLAYMSDNF GDVGKPNDVA MLRLKVKIPH SEYISPVCLP YTYQDMPWGE
TCFLSGWDLS KESGKPSSKL YQVGIPILQK NNCRFVDAYD IFCVGDVIGG IDPSQVDSGG
PLVCKLNDSY VQIGIVSFRY GHAGKDHVGI YSKVPYYLNW IYNQLWWLPD SFNSSYAGMT
IKMRLQISTD NEAGDWYPYS TNRHTQTYYG RPYICETYAL SMKRWHPFGI PFHNAFLLFC
IIIKETFSQY CGNPYFEPYF TNPHYPNQIV GEWVAKPYSF PWTVHVLAHI SGFWYESCVG
SLISFDYTNA SDTVLTSSHC VRVNNRLVDA NAITVTAGAF NIRELNEPHR VTSKVLAYMS
DNFGDVSKPN DVALLRLKVK IPHSHYISSV CLPYHSYQEM PWGETCFLSG WGFTRDHCLS
CARLESQFYE KATADLLMRM TFFAQVIWVE EIIPSNFGYN HAGKHHPGIF SNVPFYVNWI
YNQLSWLPDS FNSSDIGGEE SDCPDDCYHP WRSVFNHFKH RKASFHMDSL ESTEGDGSDW
SPYSTNQHYQ SNYDGSQSGE RNRPPYLHSH RPTMNENRPP PPPDSQNFAI QPCGIVIL
//
