ID   A0A0N5BC49_STREA        Unreviewed;       396 AA.
AC   A0A0N5BC49;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Beta-1,4-N-acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU368121};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU368121};
DE   AltName: Full=Beta-4-GalNAcT {ECO:0000256|RuleBase:RU368121};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000359800.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0000359800.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the transfer of galactose onto proteins or lipids.
CC       {ECO:0000256|RuleBase:RU368121}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU368121};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368121}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606,
CC       ECO:0000256|RuleBase:RU368121}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU368121}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
CC       {ECO:0000256|ARBA:ARBA00005735, ECO:0000256|RuleBase:RU368121}.
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DR   AlphaFoldDB; A0A0N5BC49; -.
DR   STRING; 174720.A0A0N5BC49; -.
DR   WBParaSite; SPAL_0000359800.1; SPAL_0000359800.1; SPAL_0000359800.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000046392; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniRule.
DR   InterPro; IPR003859; Galactosyl_T.
DR   InterPro; IPR027791; Galactosyl_T_C.
DR   InterPro; IPR027995; Galactosyl_T_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR19300; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19300:SF46; BETA-1,4-N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU368121};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU368121}; Manganese {ECO:0000256|RuleBase:RU368121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368121};
KW   Metal-binding {ECO:0000256|RuleBase:RU368121};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW   ECO:0000256|RuleBase:RU368121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368121};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU368121};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU368121}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368121"
FT   DOMAIN          139..254
FT                   /note="Galactosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13733"
FT   DOMAIN          258..335
FT                   /note="Galactosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02709"
SQ   SEQUENCE   396 AA;  46248 MW;  34FC6FF2D40496B5 CRC64;
     MCITRMRFAS IQIGILKKIL ILFGIFVFFY LFLVNLYIPK YFSNSADHIA LVNKITSRQN
     ENIEDIVDEK DHIKYNYNLN YWIFSPSYQQ TDETIIKKTT KHTPKTENSK HKKVHLRNCL
     PLDALNITGK IGQGLLLLDE LTIEEVQLAH QDINIGGSWK PNDCISLHKI AIIIPYRDRE
     SHLTRLIDFL IPILQKQKLD FRFIVSEQTG DDLFNKGRIM NAAFVYAETL KVDCVIFHDV
     DMFPQDYGTP YNCPKTPRHL GAYVNNLGYQ LWYPEIAGGV LVINTNDYRK INGYSNMYWA
     WGGEDDDMGK RIMSNNYTIE RPNPNIATFS MLKHTKRKRT APKLIYDLLK NAGERWPIDG
     LNETNKWQIE KVIIEPLYHH IYVNVFEPPK EWKPTV
//