ID A0A016VXF1_9BILA Unreviewed; 632 AA.
AC A0A016VXF1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=N-acetylgalactosaminide beta-1,3-galactosyltransferase {ECO:0000256|ARBA:ARBA00012557};
DE EC=2.4.1.122 {ECO:0000256|ARBA:ARBA00012557};
GN Name=Acey_s0003.g1495 {ECO:0000313|EMBL:EYC32284.1};
GN ORFNames=Y032_0003g1495 {ECO:0000313|EMBL:EYC32284.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC32284.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-D-galactosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:15621,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28257, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:133470; EC=2.4.1.122;
CC Evidence={ECO:0000256|ARBA:ARBA00000862};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC32284.1}.
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DR EMBL; JARK01001339; EYC32284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016VXF1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01650; RT_nLTR_like; 1.
DR Gene3D; 3.90.550.50; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR003378; Fringe-like.
DR InterPro; IPR000477; RT_dom.
DR PANTHER; PTHR23033; BETA1,3-GALACTOSYLTRANSFERASE; 1.
DR PANTHER; PTHR23033:SF14; GLYCOPROTEIN-N-ACETYLGALACTOSAMINE 3-BETA-GALACTOSYLTRANSFERASE 1-RELATED; 1.
DR Pfam; PF02434; Fringe; 1.
DR Pfam; PF00078; RVT_1; 1.
DR PRINTS; PR01345; CERVTRCPTASE.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..264
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
SQ SEQUENCE 632 AA; 72969 MW; 270875A7A41B6D9F CRC64;
MSSRIGDAGP RCARSICEKR SYFRLIYFTI GISIGIILFQ IQEQHTSHIK AFQSDEAYRI
DEQEQDINET STETAMLSAL NHWTSTLDDK KPLDVVYFDF AKAFDKVSHE LLLLKLAKIG
IHEQIISWLK CFLTERTFQV CINDTLSSIR RISSGVPQGG VLSPILFNIY TCELPDIIAE
EGVGCIAYAD DLKIYNPIVT PSDNMCLQKA IDAVATWASE WKLPLSKQKT KVLHIGRNNP
KLKYNLCSEF VSETSEIVDL GYIIDENLSF DKYCKEITAK ATRQIYCLFK ALRTKNVAIM
IKAYKTYVRP IMEYGTTIFN PHKKSLINMI EKVQNNFTRK LMVRTVDLVK VAKVIESKVR
IFCWVLTGKQ NHERRAQHIK ETWVRRCNKY LFMSSEENST LPAHNLNVSE GRKFLWMKTR
EAFKYIHDKY LNDFDWFLKA DDDTYVIVEN LRYLLLPYSS KDALHFGFKF RPYTKRGYHS
GGAGYILSRE ALRRFVNKAY SNDKICQVKG ISVEDVAIGR CLERIGVRAG DTRDQEGLHR
FSPLSPDSMI SGPYPKWMLK MTYYNIPTSS WCCSRYAVSF HYVSPTLLYM MEYLIYRVKV
FGLARNLRLD EDEAIFKAAH ESALAAKGPD RI
//