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Database: UniProt
Entry: A0A0V0U908_9BILA
LinkDB: A0A0V0U908_9BILA
Original site: A0A0V0U908_9BILA 
ID   A0A0V0U908_9BILA        Unreviewed;      1004 AA.
AC   A0A0V0U908;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   SubName: Full=Serine protease 30 {ECO:0000313|EMBL:KRX47713.1};
GN   Name=Prss30 {ECO:0000313|EMBL:KRX47713.1};
GN   ORFNames=T05_855 {ECO:0000313|EMBL:KRX47713.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX47713.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX47713.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX47713.1};
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:KRX47713.1}.
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DR   EMBL; JYDJ01000039; KRX47713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0U908; -.
DR   Proteomes; UP000055048; 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:SF153; FI06405P-RELATED; 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:KRX47713.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048};
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..1004
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006869825"
FT   DOMAIN          48..288
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DOMAIN          631..862
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          429..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          912..964
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        536..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..951
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1004 AA;  113891 MW;  FCC5FF4E37D9EE6B CRC64;
     MKRFHHLEIF FYRALLIFCI IIKKTISGDC GKPYFEPYLT NPRNPNRIVG GWVAKPYSFP
     WTVHILTHVS GLLYESCGGS LISLDSTNAS DTILTASHCV RVNNRLVNAN AITVAAGVFN
     IKKLNEPHRV TSKVLAYISD NFDDVSMEND IAVLRLKVEI QHSEYISPVC LPKQNQKLPW
     GEMCFVSGWG LTRESGKPSS KLRQVGIPIL RNSNCPFIDA DDMFCAGDMT GGKDSCQGDS
     GGPLVCKLND TFVQMGIVSF GDGCARKDHP GIYTKVPHYV KWIYNQAAKL PDSSTSSEIG
     EEKPDYSNDF HHSWGSVGNY FHFPFFDSSD DIWNNENFGN ENSPFSQLPW SFLSEPMPLF
     RSRSSFINRD VEEEAGDWSP YSTNQHFQTY YGLPHIGEEG QPHYPLENWP DMNGKYPLHH
     HSEFHPPYLY SNRPSMNEGH LSTPPNFESP ENQPPYTSKN SPEMNGNQYS GKSYTKFYQP
     YLYPNGPSTN DHRPSLASNF EKPENQPQYT SKNRLEMSGN HHFGKSYRKF RSPYSYANGP
     SINGDHPSSP PNFQNHENRP TYTSERRHEM NGNYYSGNRP PYSHSNKPTM NENRSPLPPY
     FRNLDKETFS QYCGNPHFEP YLANPHYPNQ VVGEWVARPY SFPWTVHVLA HISGFWYESC
     GGSLISFDYS NASDTVLTSS HCVRVNNRLV DANAITVTAG AFDIRDLNEP HRVTSKVLAY
     IKPNDVALLR LKVKIPHSHY ISSVCLPYHS YQEMPWGETC FLSGWGFTRG RPLSELRQVG
     IPILRKSNCR FTDAYDIFCA GDMGGGNYSF QIDSGGPLVC KLNDSYVQIG IVSFGYNHAG
     KHYPGIFSNV PFYVNWIYNQ LSWLPDSFNS SDIGGEESDC PDDCYHPWRS VFNHFKHRKA
     SFHMDSLEST EGDGSDWSPY STNQHYQSNY DGSQSGEGNR PPYSHSHRPT MNENRPPPPP
     DSQNFAIAKG MVKKALSLNR LHAYITVETS EQYSQCLQIN FASI
//
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