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Database: UniProt
Entry: A0A428U8F2_9HYPO
LinkDB: A0A428U8F2_9HYPO
Original site: A0A428U8F2_9HYPO 
ID   A0A428U8F2_9HYPO        Unreviewed;       210 AA.
AC   A0A428U8F2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
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=CEP52_003576 {ECO:0000313|EMBL:RSM10484.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM10484.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSM10484.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM10484.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:RSM10484.1}.
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DR   EMBL; NKCK01000023; RSM10484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428U8F2; -.
DR   STRING; 1325735.A0A428U8F2; -.
DR   Proteomes; UP000287144; 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|RuleBase:RU362128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287144};
KW   Transferase {ECO:0000256|RuleBase:RU362128}.
FT   DOMAIN          12..152
FT                   /note="Glycosyl transferase family 28 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04101"
SQ   SEQUENCE   210 AA;  23536 MW;  BB5759C400325E3C CRC64;
     MTSDSDHTGR FCLVTVGATV GFKKLTETAL NPTFWEYLVS QGFTELHIQC GPDVVWASKE
     LVARKDDAPR GLNIDIFDMR KNLMKEEMTL CKPLNGKRQL GLVISHAGTG TILDAWKLGL
     PIIVVPNTQL LNDHQTEMAK HLSKEGYAIM STGSVDDLQE AMHKVELLWE DNKARWPPNK
     VPSAGNDRRR LWDLAPDEVA KEQNATMTHD
//
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