ID A0A0M3IG66_ASCLU Unreviewed; 952 AA.
AC A0A0M3IG66;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ShKT domain-containing protein {ECO:0000313|WBParaSite:ALUE_0001726301-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_0001726301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0001726301-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; A0A0M3IG66; -.
DR WBParaSite; ALUE_0001726301-mRNA-1; ALUE_0001726301-mRNA-1; ALUE_0001726301.
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; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SMART; SM00254; ShKT; 1.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS51670; SHKT; 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}.
FT DOMAIN 899..933
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 899..933
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 952 AA; 106800 MW; ABBAEBE94623C66C CRC64;
GHSSFQATWS SWSSSTTWSD SRSRWSQTSS SWTVWSAWST YSDSEQHGQP QSRHRLEEPL
QPSTRTGQLG APSISIVSQP ASHDRIQHSN HQANAPVEIE YTITSTVVPD GDGNIGQTEI
NTQDMQPQMS VNTVYEQKNG DEFTQTSDIV PQPPSGNAWN DGDAPIENDD NDSTWTSQHG
EVVGGQQRDA FPPRRSFSSN TWPQKSHQVQ KMQQFAAPDR STTTISRTST FSSSHTQQQQ
QHTSFKSVTH TVPAGRSRNN FVPQVQGPPR KFEKDLFSMN QDTVGPPGFQ PASDRQRNLQ
RVLPPQVADP PGLKPGEVAQ SRPGEFGSGR QLVSIGSQQA NFGAQQVFPQ TSPHLNTGVD
RRWESQRRGN MGSGGFQQST SQRRQFINDM DQQNIRIQPG QPLQSSLNQQ RFGGQQIDGA
RLPAPQFTSS RRQQTFTSNA IGARGNQTTS SKIWQNQRPL PPAPPIPPPP PRDTQFLHKP
ESFGRTQQSI NSRILHTGNF FQKNASNPYE CMDILCLCLF LRGRRIGSDC WLPSGERLGL
ALRKEYRQLT QRERSNLHAA LNVLKQSGEY DRIAEWHSSP ENSGGAHSGP AFLPWHREYI
KRLEIALRLV DHSVALPYWD STLDGRIPET AATSLFSAEL MGETDNYGNV VTGFAALWNP
PDGHTHLKRR PGFQGRPFNG ADIAAVMQRN DITNILAYTA PRQGCEHQTD WTCLEYSHGN
VLIWVGGEMF QQTTSANDPL FFLHHAFVDR IWEDWRQVKQ SAMARSLAYP PDLPQCSSED
HFARSPMRPF SPLRNIDGVA DRYLYKYAPR PSCSRGHDQQ CASDFLFCDL SHGPPQCAAK
IRRGGPCWGF VNGERPCLYG ECRENICITL GQETINVRNK RDINDVVNDE IESKEEESCF
NSHECCAVWS ENAQCDTNAA VMSEWCKASC AKCHPAYDLH NGFFVFSLFL FL
//