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Database: UniProt
Entry: A0A3P6UXJ5_LITSI
LinkDB: A0A3P6UXJ5_LITSI
Original site: A0A3P6UXJ5_LITSI 
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
//
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