ID A0A2G5VHR3_9PELO Unreviewed; 653 AA.
AC A0A2G5VHR3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=ShKT domain-containing protein {ECO:0000259|PROSITE:PS51670};
GN Name=Cni-tyr-3 {ECO:0000313|EMBL:PIC51126.1};
GN Synonyms=Cnig_chr_I.g1766 {ECO:0000313|EMBL:PIC51126.1};
GN ORFNames=B9Z55_001766 {ECO:0000313|EMBL:PIC51126.1};
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:PIC51126.1, 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 -!- 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:PIC51126.1}.
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DR EMBL; PDUG01000001; PIC51126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VHR3; -.
DR STRING; 1611254.A0A2G5VHR3; -.
DR Proteomes; UP000230233; Chromosome i.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 1.10.10.1940; -; 1.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR003582; ShKT_dom.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR11474:SF114; TYROSINASE-LIKE PROTEIN TYR-3-RELATED; 1.
DR Pfam; PF01549; ShK; 4.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SMART; SM00254; ShKT; 4.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS51670; SHKT; 4.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU01005};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..653
FT /note="ShKT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013593045"
FT DOMAIN 459..493
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DOMAIN 503..537
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DOMAIN 574..608
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DOMAIN 617..650
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DISULFID 459..493
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
FT DISULFID 503..537
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
FT DISULFID 574..608
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 653 AA; 72828 MW; 6D6511835B9C27DD CRC64;
MKKICIFLLL LLLIQSSNGQ LDCSKAPTDA IRIVCNQIQR WDQKARTTPT LSADVKTPGI
AGQAMAAEFS PIASNVFQCM DIACLCVFFR GTGGNNCVVQ GRPLGKVVRK EYRMLSEDER
NRLHQALRTL KQNGEYDRLA RVHAQYSESG AAHSGPAFLP WHREFVKRME FLIRQVDPSL
HLPYWDSTLD QNLPNSKDSI LWTNEFMGDA TGAVNNGPFR SWRTIEVNKA TITRAVGAQG
KGYSEDEITS MMGQTDIAQV LAFSAPQRGC PYQPNFNVPE YTHGNPHIYV GGDMLETSTA
ANDPIFWMHH SFVDLLWEQY RQTKQTRATR ETAYPADNRQ CSSEHHFRAA FMRPFTPMRN
ADGLSNMYTD NLYSFAPRPS CNAGPTCGSP YLFCDRSHGA PRCAARMKTG GNCASFTNGE
TACYQGTCQG GKCVAVSQTV TPPPTITPTK PVVTVETTCF NENECCGPWS AKGECQKNPV
YMNVWCKASC RQCTPKYDLN DECSDRHSNC AQWSRSGECN KNPLWMAENC RKSCNKCGVT
RAATCGGGAN NIAANPPASV NNRQQNEPCD SPMCYNEDQC CPIWAQRGEC QSNSKYMNCQ
CKVSCGVCRP NYAYGQCQDY HKDCAAWARR GECAKNKWMP ENCRRSCNTC MTL
//
