GenomeNet

Database: UniProt
Entry: U6KJV3_EIMTE
LinkDB: U6KJV3_EIMTE
Original site: U6KJV3_EIMTE 
ID   U6KJV3_EIMTE            Unreviewed;       655 AA.
AC   U6KJV3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase T3, putative {ECO:0000313|EMBL:CDJ37081.1};
GN   ORFNames=ETH_00005370 {ECO:0000313|EMBL:CDJ37081.1};
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ37081.1};
RN   [1] {ECO:0000313|EMBL:CDJ37081.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ37081.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDJ37081.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ37081.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HG673746; CDJ37081.1; -; Genomic_DNA.
DR   RefSeq; XP_013227919.1; XM_013372465.1.
DR   AlphaFoldDB; U6KJV3; -.
DR   SMR; U6KJV3; -.
DR   EnsemblProtists; CDJ37081; CDJ37081; ETH_00005370.
DR   GeneID; 25250282; -.
DR   VEuPathDB; ToxoDB:ETH2_0802300; -.
DR   VEuPathDB; ToxoDB:ETH_00005370; -.
DR   OMA; NPLFKMC; -.
DR   OrthoDB; 202750at2759; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR027791; Galactosyl_T_C.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF43; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDJ37081.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          520..637
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          70..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   655 AA;  71978 MW;  CB12E2C8FEAAEFD9 CRC64;
     MVEGALQHAD WRRPLWGCLQ LTVMALGFGS ILLNAVLLTR YMFPAAAPAA EDLTYVDAAL
     QQKAAPLPAA QQLDAARSSS SSGSSGSSSS SIGVDPERMH GPLGLKPDGT PNYVPGPPPP
     PDLNMAAELA RGGGFNLLLS DHLPLDRPVP ESRAAACAAV QYDLESLPAA SVLIVFHNEA
     LSTLLRSVHS VLNRTPPQLL QEVLLVDDGS TAADVAAEAL GGNGKLQQHL LLLPRKVQLL
     RSPQREGIVG ARLRAIRAAA AAHFVVLDSH VEVQRQWLEP LLLRLQRSSS SLVMPQVDGI
     DAETFEHVTG GIGCQLGFLW QLVEHSFEPH QLQQRQQRRR QQQQQTASAP PNHPHPHPHH
     QQQQQQQQQQ EEELELYQAS PAMAGGLFAS SKAFFFAVGG YDEGFRFWGA ENLELSFRAW
     QCGGRVECAA CSRVFHVFRR GGAGYAFPAS ALAANKLRTL AWMDRFGDLA WRVLGRPAVD
     YGAASLQQRL QFRSRSRCRS FQWFLENVFP ESDVVHLSDV PFLGKLKNED TGLCLEATGR
     PSPGSRAVLR GCQEDHQLQE FMYFKKVGHV MPVLNDEACL TPSGSLDWCR VNDLMWWDVE
     DGKLRNRAVG KCLAVKNGQL GLAECGSGDS HQKWQWDEYN PPEVFELPPV PSAKS
//
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