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Database: UniProt
Entry: A0A0V1DBD9_TRIBR
LinkDB: A0A0V1DBD9_TRIBR
Original site: A0A0V1DBD9_TRIBR 
ID   A0A0V1DBD9_TRIBR        Unreviewed;       967 AA.
AC   A0A0V1DBD9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Serine protease 30 {ECO:0000313|EMBL:KRY58839.1};
GN   Name=Prss30 {ECO:0000313|EMBL:KRY58839.1};
GN   ORFNames=T03_12428 {ECO:0000313|EMBL:KRY58839.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY58839.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY58839.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY58839.1};
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:KRY58839.1}.
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DR   EMBL; JYDI01000018; KRY58839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1DBD9; -.
DR   Proteomes; UP000054653; 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:KRY58839.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
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..967
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006876612"
FT   DOMAIN          48..288
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DOMAIN          585..825
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          536..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          875..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..914
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   967 AA;  109095 MW;  BE6D57316E2EC21B 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 ENSPFSQFPW SFLSEPMPLF
     RSRSSFINRD VEEEAGDWSP YSTNQHFQTY YGLPHIGEEG QPHYPLENWP DMNGKYPLHH
     HSEFHPPYLY SNRPSMNEGH LSTPPNFESP ENQPPYTSKN SPEMNGNQYS GKSYTKFYQP
     YLYPNGPSTN DHRPSLASNF EKPENQPQYT SKNRLEMSGN HHFGKSYRKF RSPYSYANGP
     SINGDHPSSP PNFQNHENRP TKSSTYCGNP HFEPYLANPH YPNQVVGEWV ARPYSFPWTV
     HVLAHISGFW YESCGGSLIS FDYSNASDTV LTSSHCVRVN NRLVDANAIT VTAGAFDIRD
     LNEPHRVTSK VLAYMSDNFG DVGKPNDVAM LRLKVKIPHS EYISPVCLPY TYQDMPWGET
     CFLSGWDLSK ESGKPSSKLY QVGIPILQKN NCRFVDAYDI FCVGDAIGGI DPSQIDSGGP
     LVCKLNDSYV QIGIVSFGYN HAGKHHPGIF SNVPFYVNWI YNQLSWLPDS FNSSDIGGEE
     SDCPDDCYHP WRSVFNHFKH RKASFHMDSL ESTEGDGSDW SPYSTNQHYQ SNYDGSQSGE
     GNRPPYSHSH RPTMNENRPP PPPDSQNFAI AKGMVKKALS LNRLHAYITV ETSEQYSQCL
     QINFASI
//
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