ID A0A2G5VRH8_9PELO Unreviewed; 531 AA.
AC A0A2G5VRH8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=ShKT domain-containing protein {ECO:0000259|PROSITE:PS51670};
GN Name=Cni-T06A4.3 {ECO:0000313|EMBL:PIC54435.1};
GN Synonyms=Cnig_chr_I.g369 {ECO:0000313|EMBL:PIC54435.1};
GN ORFNames=B9Z55_000369 {ECO:0000313|EMBL:PIC54435.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC54435.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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}.
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:PIC54435.1}.
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DR EMBL; PDUG01000001; PIC54435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VRH8; -.
DR Proteomes; UP000230233; Chromosome i.
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; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR PANTHER; PTHR11705:SF49; SHKT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR Pfam; PF01549; ShK; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00254; ShKT; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..531
FT /note="ShKT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013869050"
FT DOMAIN 495..531
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
SQ SEQUENCE 531 AA; 61473 MW; E2B60F5FD1D94187 CRC64;
MTSLLIFLCF STVSLSTQSF SVYRLLPKSQ TDFQAIQKLY KNATDHDLNF WKTGKDKHGF
WDVMVERKNE NFLMDYLQNN GNISHIRTID DVEKLISKHE NNQTLSKMFP RLWDDSSSGH
YDFHTYGSYQ RMTDWMKQLV VKYPKMVQYI SIGKTTEGRN IDGVEIGGDS RTKKIFWIDG
GIHAREWAAP HTALFFIHQL TSRANEPGIK KLLEEITFVV VPCLNPDGYE FTRSSTNPHV
RLWRKNRSKM QCRKDIWGRN RCCRGVDLNR NFDFHFRESG TSDDPCSEIY QGPAPFSEPE
AKAVRDALLS QRYRGRTDAY ITLHTYSQIW IHPYGHKKDA YPGDIKDLYE VGKKAAQALK
RVYGTKYVVG SGADTLYPAS GGSEDWAKHE AKVKFVYLLE LRPDEKNWDG FILDEKELIP
TARETWEGVR VVAEAVLDRI VAAKATTPKE LLETDPRYPQ GYFHTPLQYP ILQYPITEAP
KARGFRFGDG TEGSCFDVRH ACKRWVQERE ELCRTVPIFM RENCAYSCNF C
//