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Database: UniProt
Entry: A0A077YY47_TRITR
LinkDB: A0A077YY47_TRITR
Original site: A0A077YY47_TRITR 
ID   A0A077YY47_TRITR        Unreviewed;       501 AA.
AC   A0A077YY47;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Alpha (1,6) fucosyltransferase {ECO:0000313|EMBL:CDW52701.1};
GN   ORFNames=TTRE_0000096301 {ECO:0000313|EMBL:CDW52701.1};
OS   Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW52701.1};
RN   [1] {ECO:0000313|EMBL:CDW52701.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Aslett M.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDW52701.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate host-
RT   pathogen interaction.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 23 family.
CC       {ECO:0000256|PROSITE-ProRule:PRU00992}.
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DR   EMBL; HG805829; CDW52701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077YY47; -.
DR   STRING; 36087.A0A077YY47; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd11300; Fut8_like; 1.
DR   CDD; cd11792; SH3_Fut8; 1.
DR   Gene3D; 3.40.50.11350; -; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR045573; Fut8_N_cat.
DR   InterPro; IPR035653; Fut8_SH3.
DR   InterPro; IPR027350; GT23_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR13132; ALPHA- 1,6 -FUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR13132:SF29; ALPHA-(1,6)-FUCOSYLTRANSFERASE; 1.
DR   Pfam; PF19745; FUT8_N_cat; 2.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51659; GT23; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|PROSITE-
KW   ProRule:PRU00992}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00992}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          148..416
FT                   /note="GT23"
FT                   /evidence="ECO:0000259|PROSITE:PS51659"
FT   DOMAIN          425..486
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          296..297
FT                   /note="Important for donor substrate binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00992"
SQ   SEQUENCE   501 AA;  58221 MW;  86BF8CA1132E0606 CRC64;
     MLRLTKLTIF VVSLCVLCFF VAVVLVSKLS FPADPARLRE RNNSWMILAR LLETQKQLEY
     FSQKTHQLQD QVKQIEIRIY GKWCVWKTFL GSINGYLGIS VTLYSKLFDS QVCYLRSLVA
     LSLRKLHQLS KVVQNQLYDL QHPLSCEKAR RLICSLDKPC GFACQVHHVT YCLQVAYYTN
     RTMVLNDNSW SYSSHGWTSV FQPVSNSCRY NYDEETPRVG KCNCRILTLR GKLVCFSLLL
     SSKRFRLLRL HSYPPAWWTG ELVSYLMRYN SEMSDKLEQM ATLYNFSYPI VGIHVRRTDK
     VGTEARFHGL EEYMVEVEKC PGQKRKVYIA TDDPSVFSEA RRTYPNYTFI GSSDVARTAD
     LKWRYSDTSL QGIVTDIHFL SLSNFLVCTF SSQVCRLAYE KMQHLYGDAG YNFRSLDDIY
     YYGGQREHTW LAVMDHVPRK SDEIELRRGD RIAVAGNHWD GYSKGTNMRT SVSGLFPTYK
     TVETWRFAKT PFSWLNATTL I
//
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