ID A0A0G4EMQ1_VITBC Unreviewed; 617 AA.
AC A0A0G4EMQ1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=polypeptide N-acetylgalactosaminyltransferase {ECO:0000256|ARBA:ARBA00012644};
DE EC=2.4.1.41 {ECO:0000256|ARBA:ARBA00012644};
GN ORFNames=Vbra_12501 {ECO:0000313|EMBL:CEL98450.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEL98450.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEL98450.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00001386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00000440};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
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DR EMBL; CDMY01000270; CEL98450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4EMQ1; -.
DR STRING; 1169540.A0A0G4EMQ1; -.
DR VEuPathDB; CryptoDB:Vbra_12501; -.
DR InParanoid; A0A0G4EMQ1; -.
DR OMA; VEMITCH; -.
DR OrthoDB; 276098at2759; -.
DR PhylomeDB; A0A0G4EMQ1; -.
DR Proteomes; UP000041254; Unassembled WGS sequence.
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 CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
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:SF119; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 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 Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 159..317
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 507..595
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF00652"
FT REGION 106..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 70742 MW; A75CB365069430F1 CRC64;
MKKALRFALL LVIPVASVLL GASLSYSYIA VGVSVIAILI DPLRVESKAL PFFVYLLLVS
AIQLGFLLLY MNPITGGTST SDGSPTPAPF SQRLMKLRAR REKLPPVKVV DQQQKQKQQN
KQGGDVSAAK GGQMAKLRMV SPERFENSTD MVHDLRMVSV ILAAHNEQQY CERTLASIYD
ATPPDILKEI IIVDDGSDPP MSTAYNHTRF PNVKIIRNEE REGLIRSKLI GGDAAEGDLI
VFLDAHVKPD PGWTAPLIRH TNTNYKRVVV PLIPILNGET WEINRAAVGV KMMFDWTLQF
QWFEDHNDLV PCMSGGLLAM TKRWWEESGK LDDGMYEWGG ENIEQSIRIW LCGGEIYVAR
DSIVGHVFRE KFPYKIDNEK IMVNKARAVE VWWDEYKEKF YQHYPSGRKF KDRMGNTTER
ETIKERLNCK PFSWYVEKFH DVFVDRGMLP MNTFLIQKAG TDQCLIPSQH VLNQRNPPLS
RDRLAYTTCD KESKAQRFQW RNQGRTLQNV ESKKCFDAAN PPSEGHETIL FLCEGTNHNQ
VWEHTNGRLT HSSFCAGTKN DQLTLHLWHC SDKPAEEGQL FKFVDYKAEF QNVPKKKKKD
KDKDKDKDKD KEKDKRQ
//
