ID A0A0C2GMT1_9BILA Unreviewed; 504 AA.
AC A0A0C2GMT1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ShTK domain protein {ECO:0000313|EMBL:KIH62610.1};
GN ORFNames=ANCDUO_07104 {ECO:0000313|EMBL:KIH62610.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH62610.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH62610.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH62610.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) 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}.
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DR EMBL; KN729192; KIH62610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2GMT1; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
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; TYROSINASE FAMILY MEMBER; 1.
DR PANTHER; PTHR11474:SF136; TYROSINASE-LIKE PROTEIN TYR-1-RELATED; 1.
DR Pfam; PF01549; ShK; 2.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SMART; SM00254; ShKT; 2.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS51670; SHKT; 2.
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:UP000054047}.
FT DOMAIN 409..443
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DOMAIN 453..487
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT REGION 368..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 409..443
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
FT DISULFID 453..487
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 504 AA; 57445 MW; D2ECBB93CB95425A CRC64;
MSRISNMWNN AILQLKRSGE YDRLSVMHRQ VGSSSGAHSG PGFLPWHREY MKRLEIAVRM
VDPGVAMPYW DSVMDSYLPD PRDSILFSAL FMGETDGAGQ VVRGPFAGFR TLEGRPHIVR
RLATEGKLFS EANINNLLSQ TEIQNVLAYT APQNGCPFRP NFGALEYTHS SVHLWVGGDM
KPPSTSANDP IFFLHHCFVD FVWEMWRQSR QNRFARETVL LLLYYIQLQP DTMLTLYEGL
EMVVMAYPPD IGTCANSQHF SYAQMRPWDK QNRDGLSNEY TDNLFRYAPR ATCSRQNPNC
GSPYLFCDTR GNPHCVSKIK PNGLCRGFEG FDACWQGTCV AAWCRPGQQF QEQPTQTTAV
QVIRQNNENQ PVQQRQQQTS ALPTRATSAR TQATTPRPLP VSPVANNNCY NDDPCCDAWA
RQGECQINVV YMNRYCRRSC RLCTNPTDNR TGCHDRHVSC AFWRAQNYCT RRRQWMAENC
QASCGWCNMS PQQLCASVAF MSRA
//
