ID A0A0V1BDK5_TRISP Unreviewed; 886 AA.
AC A0A0V1BDK5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Serine protease 30 {ECO:0000313|EMBL:KRY34989.1};
GN Name=Prss30 {ECO:0000313|EMBL:KRY34989.1};
GN ORFNames=T01_15237 {ECO:0000313|EMBL:KRY34989.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY34989.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY34989.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY34989.1};
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:KRY34989.1}.
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DR EMBL; JYDH01000059; KRY34989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1BDK5; -.
DR Proteomes; UP000054776; 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; 2.
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:SF165; PEPTIDASE S1 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 1.
DR Pfam; PF00089; Trypsin; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
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:KRY34989.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
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..886
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006875085"
FT DOMAIN 48..288
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 507..745
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 400..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 100078 MW; 4129CDB620BADBA9 CRC64;
MKRCHYLEIF FYHALLIFCI IIKKTFSEEC GKPYFEPYLT NPRNPNRIVG GWVAKPYSFP
WTVHILTHVS GLLYESCGGS LISLDSTNAS DTILTASHCV RVNNRLVNAN AITVAAGVFN
IKKLNEPHRV TSKVLAYVSD NFDDVSMEND IAVLRLKVEI QHSEYISPVC LPKQNQKLPW
GKMCFVSGWG LTRESGKPSS KLRQVGIPIL RNSNCPFIDA DDMFCAGDMS GGKDSCQGDS
GGPLVCKLNG TYVQMGIVSF GDGCARKDHP GIYTKVPHYV KWIYNQAAKL PDSSTSSEIG
EEKPDYSNDF HHSWGSVGNY FHFPFFDSSD DIWNNENFGN ENSPFLQLPW SFLSEPMPLF
RKEAGDWPPY STNQHFQTYG RPHIGEEGQP QYPLENWPDM NGKYPLHHHS ENQPPYTSEN
SPEMNGNQYS GRSYTKFHQP YLYPNGPSSN DHRPPLASNF EKPEFRSPYS YANGPSINGD
HPSKSTNYCG NPYFEPYLTN PHYPDQTVGE WVARPYSFPW TVHVLAHISG FWYESCGGSL
ISFDYSNASD TVLTSSHCVR VNNRLVDANA ITVTAGAFNI RELNEPHRVT SKVLAYMSDN
FGDVGKPNDV AMLRLKVKIP HSHYISSVCL PYPFQEIPYG ETCFLSGWGF TRGRPLSELR
QVGIPILRSS NCRFTDAYDI FCAGDMGEGN YSFQIDSGGP LVCKLNDSYV QIGIVSFGYN
HAGKHHPGIY SKVPYYLNWI YNQLSWLPDS FNSSDIGGEE SDCPDDCYHP WRSVFKHFKH
RKASFRNRPP YSHSLRLTMN ENRPPPPPDS QNFDMESLES TEGDPSDWSP YSTNQHYQSN
YDGSQTGKGN RPPYSHSHRP TMNENRPPPP PDSQNFAMQL CGIVIL
//