ID A0A3P6UXJ5_LITSI Unreviewed; 484 AA.
AC A0A3P6UXJ5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=ShKT domain-containing protein {ECO:0000259|PROSITE:PS51670};
GN ORFNames=NLS_LOCUS5670 {ECO:0000313|EMBL:VDK82261.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK82261.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK82261.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01005}.
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DR EMBL; UYRX01000440; VDK82261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P6UXJ5; -.
DR STRING; 42156.A0A3P6UXJ5; -.
DR Proteomes; UP000277928; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03860; M14_CP_A-B_like; 1.
DR Gene3D; 1.10.10.1940; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR11705:SF91; FI01817P-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF01549; ShK; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645};
KW Protease {ECO:0000256|ARBA:ARBA00022645};
KW Reference proteome {ECO:0000313|Proteomes:UP000277928};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 451..484
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT REGION 56..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 55121 MW; F219817347D51F25 CRC64;
MYGRRAKGSP WEWTCKQHWP STAHLLATIV VASMSCDTIA SDANLPANFT RSSSSSSLWS
SPSPSPSPSP SQSPSSIAQR TKRKITKLRE KAKKPRQYNW LRDDPLSSRG IRFNLAEYHS
YDEISSYLDH LYTAYPDRTK VRTIGLTHER RPIKLIKIGK PRTFAKPGIW IDGGIHAREW
VSPSTVLYII NQLVTKYDVD PQIRRFVDEM DWFIVPLLNP DGYEYTRSST NPEVRLWRKN
RSPMICRVLQ NGIFSQIRQE CCQGVDLNRN YDWQYGIEGS SNDPCSEIYQ GPSAFSEPET
RAVHRFIAKR RSSIKTFLTF HSYSQILMYP FGHRTRTYTA DVDDLRNTAL QAANALHAAY
GTKYTVGTGA DTLYPASGGA EDWARGRMGV KYSYLFELRP EGEVWDGFLL DESQIIPTAR
EAFEAVKVIA NRTSAVFVPK NLPNETKESA CVDNEPFCAY WAQHGYCATW EVMRTICARS
CGFC
//