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Database: UniProt
Entry: M3D8X4_SPHMS
LinkDB: M3D8X4_SPHMS
Original site: M3D8X4_SPHMS 
ID   M3D8X4_SPHMS            Unreviewed;       194 AA.
AC   M3D8X4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=UDP-N-acetylglucosamine transferase subunit ALG13 {ECO:0000256|ARBA:ARBA00017468, ECO:0000256|RuleBase:RU362128};
DE            EC=2.4.1.141 {ECO:0000256|ARBA:ARBA00012614, ECO:0000256|RuleBase:RU362128};
DE   AltName: Full=Asparagine-linked glycosylation protein 13 {ECO:0000256|ARBA:ARBA00032061, ECO:0000256|RuleBase:RU362128};
GN   Name=ALG13 {ECO:0000256|RuleBase:RU362128};
GN   ORFNames=SEPMUDRAFT_148261 {ECO:0000313|EMBL:EMF14595.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF14595.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF14595.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF14595.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- FUNCTION: Involved in protein N-glycosylation. Essential for the second
CC       step of the dolichol-linked oligosaccharide pathway.
CC       {ECO:0000256|ARBA:ARBA00024804, ECO:0000256|RuleBase:RU362128}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-
CC         acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl
CC         diphosphodolichol + UDP; Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:9519,
CC         Rhea:RHEA-COMP:9520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58427;
CC         EC=2.4.1.141; Evidence={ECO:0000256|ARBA:ARBA00000601};
CC   -!- SUBUNIT: Heterodimer with ALG14 to form a functional enzyme.
CC       {ECO:0000256|ARBA:ARBA00011198, ECO:0000256|RuleBase:RU362128}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240, ECO:0000256|RuleBase:RU362128}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000256|ARBA:ARBA00006962, ECO:0000256|RuleBase:RU362128}.
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DR   EMBL; KB456262; EMF14595.1; -; Genomic_DNA.
DR   RefSeq; XP_016762716.1; XM_016904811.1.
DR   AlphaFoldDB; M3D8X4; -.
DR   STRING; 692275.M3D8X4; -.
DR   GeneID; 27901948; -.
DR   eggNOG; KOG3349; Eukaryota.
DR   HOGENOM; CLU_085408_2_1_1; -.
DR   OMA; QYKFRPN; -.
DR   OrthoDB; 167601at2759; -.
DR   Proteomes; UP000016931; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   InterPro; IPR007235; Glyco_trans_28_C.
DR   PANTHER; PTHR47043; UDP-N-ACETYLGLUCOSAMINE TRANSFERASE SUBUNIT ALG13; 1.
DR   PANTHER; PTHR47043:SF1; UDP-N-ACETYLGLUCOSAMINE TRANSFERASE SUBUNIT ALG13; 1.
DR   Pfam; PF04101; Glyco_tran_28_C; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU362128};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU362128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362128}.
FT   DOMAIN          5..140
FT                   /note="Glycosyl transferase family 28 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04101"
SQ   SEQUENCE   194 AA;  20934 MW;  3085F72BF9C91822 CRC64;
     MPSKTCFVTI GATASFGGLV RGVLQHDFLE ALEKQGYTDL LVQYGKDGQE LFDSCITAAK
     NSESGSFLRI AGFTIDKAGL AKYMKQAKGG NGNQEGVVIS HAGSGTILDA LRIQVPLIVV
     PNEELLDNHQ VELAEALAEQ EYVVHGSLGG LAPALNEAEQ LRVRTRSWPP PNAGYMRQPK
     TLKSIIDDEM GYLE
//
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