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
//