ID A0A158Q2H0_DRAME Unreviewed; 593 AA.
AC A0A158Q2H0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Kunitz/Bovine pancreatic trypsin inhibitor domain protein {ECO:0000313|WBParaSite:DME_0000001901-mRNA-1};
GN ORFNames=DME_LOCUS4379 {ECO:0000313|EMBL:VDN54406.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000001901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000001901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN54406.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; UYYG01001150; VDN54406.1; -; Genomic_DNA.
DR STRING; 318479.A0A158Q2H0; -.
DR WBParaSite; DME_0000001901-mRNA-1; DME_0000001901-mRNA-1; DME_0000001901.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00109; Kunitz-type; 2.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 5.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR24039; FIBRILLIN-RELATED; 1.
DR PANTHER; PTHR24039:SF38; PROTEIN CBR-MEC-9; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00014; Kunitz_BPTI; 5.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00131; KU; 5.
DR SUPFAM; SSF57362; BPTI-like; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 5.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000274756};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 58..93
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 108..161
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 207..247
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 279..319
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 325..381
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 393..449
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 460..516
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 553..591
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 562..579
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 581..590
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 593 AA; 68612 MW; 005C40A18E754B3B CRC64;
MESMDPGPCQ YYQCLVQFFS AVTSVGYYLM KGINSFFRQK FAAAEGIEKN FIFFHQIKWY
WEKNSSECKT FYYGGCLGNR NRFDTKQLCT KQCIYKTHNP FAIPGNLCLL NFDQGHCDDD
RRGQWWYYFD AANGRCEKFF YYGCGGNANR FYSLYQCRKI CGERLAPQLA CERCDLRTSY
CKSHSKFNYS CECRDGFKKD LYGECNDIDE CRMHTASCDR NAWCVNTIGS FTCECMGGYR
GDGHKCTYVG LGKLPHATCT NGVCICKEGY VGDGFECADV NECLTIPRRC DKNAKCRNIN
GSFICECVPG FAGNGYSCTN RTTACLNSFD RNYKEQCGMQ NWREYYFFNH ETRRCELFWY
DGCEGNSENI FASLDTCENM CEITSVLDIS DICWDKFDNN YRNQCKNGDW KYRFYFDHAS
MTCKSFWYDG CTSKSRNIFE DFSACQWLCK EQALYNSKAC LEDFDEHYRD ECSGGRWKQY
FYFDKSKNKC FPFWFDGCTG TSQNIFPNHG TCKELCMTPK NKAGFKVESK FDQCSQNPCM
NGGTCILKDV NLVLEPCDVN PCLNNGICRT TNSNSKFFCE CRQKFGGKLC DIG
//
