ID A0A2P5HYS5_9PEZI Unreviewed; 284 AA.
AC A0A2P5HYS5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DHEL01_v206195 {ECO:0000313|EMBL:POS75403.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS75403.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS75403.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS75403.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-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:POS75403.1}.
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DR EMBL; MAVT02000491; POS75403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5HYS5; -.
DR STRING; 158607.A0A2P5HYS5; -.
DR InParanoid; A0A2P5HYS5; -.
DR OrthoDB; 167601at2759; -.
DR Proteomes; UP000094444; 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.
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:UP000094444};
KW Transferase {ECO:0000256|RuleBase:RU362128, ECO:0000313|EMBL:POS75403.1}.
FT DOMAIN 82..213
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 31097 MW; 007A4485B58EFBA1 CRC64;
MPKKVMGKTL NTVKRPIRLK DLRRATDEGA KRAASPDDLQ YDADVDTSDT ELESVDPNER
ERSHRMIRLP LRSDDETMGR RLLVTGGATV PFVGLLEEAT SAEFLQTLRA QGFTHVYLQC
GSVHDQILAR LNSDGRGSGL EMETFDFCRD LKSLFKEHCR GQKCVQPAGV VMGHAGTGTI
GDALEVDCAL IIVANSTLMD DHQTAFATEM AAEHPTIVQG KLGNLTTSIS EAMEVIQENK
LDDLDPYEEL SLPSEPALTF IDEVIAGATR PESQVGILGR CIIQ
//
