ID A0A0M3IJ33_ASCLU Unreviewed; 697 AA.
AC A0A0M3IJ33;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=ShTK domain protein {ECO:0000313|WBParaSite:ALUE_0001861501-mRNA-1};
OS Ascaris lumbricoides (Giant roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0001861501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0001861501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01005}.
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DR AlphaFoldDB; A0A0M3IJ33; -.
DR WBParaSite; ALUE_0001861501-mRNA-1; ALUE_0001861501-mRNA-1; ALUE_0001861501.
DR Proteomes; UP000036681; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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:SF21; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..697
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005657234"
FT DOMAIN 470..504
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DOMAIN 514..548
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DOMAIN 581..615
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DOMAIN 625..658
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DISULFID 470..504
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
FT DISULFID 514..548
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
FT DISULFID 581..615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 697 AA; 78032 MW; A7EE845FAE9805E3 CRC64;
MGMSLVWVAV FCMIAELNAV SRCINAPTQA KRIFCEQLHR WDAGARALPP VAAAPPLPPA
IEESEMRLIA GGFAPIAATP YQCKDLACLC SYLRGKWQPG WNTCTLPNGQ QLMKAVRREY
RTLSNEERQR LHTAFRAIKE SGEYDKLATV YSQHGKSGGA HSGPAFLPWH REFLKRLEIA
LRLADAEVSL PYWDSTLDSL LADPKDSILW TDELMGSTDE NGTVQGDFSN WKVPQGRRML
RREVGTHGSP LTKHDIDYIM SMTSADDILA FTAPRQGCYY RTDYNALEYA QGGVQVFVGG
DMLDIATAAN DPVFYLHHAF VDFLWEQWRQ QRQAALTKHE RQNSYPPDMQ LCSSGSHFGS
AFMRPFEPLR NIDGLSSSYT DFLYDYAPRP SCEDGPSCGS KYLFCDHSRL PARCVSKVKP
GGNCTGFHRG EAVCYRGRCV DGTCVADSIT FPSTRSPVVT NRIIPVLNNC YNEHECCSTW
AARGECTRNK SYMNLWCKAS CHICRPTFNI ALECADFHRK CIQWSRSGEC SKNPLWMAEN
CRKSCARCAA TRAQICNGGK QPPTTTSPAP AYLEKCASPG CYNENICCPL WGLQGQCTTN
ATYMSCYCRV SCGLCIPRDY FYGTCKNYHR RCEEWASRGE CEKSAWMLEN CRESCGSCFT
QTQLKPKCRI GSGKLVVTRK AKQLFLPTVD EIPIGAA
//
