ID A0A0V0XBJ1_9BILA Unreviewed; 808 AA.
AC A0A0V0XBJ1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase {ECO:0000256|ARBA:ARBA00017659};
DE EC=2.7.8.15 {ECO:0000256|ARBA:ARBA00013225};
DE AltName: Full=GlcNAc-1-P transferase {ECO:0000256|ARBA:ARBA00029567};
DE AltName: Full=N-acetylglucosamine-1-phosphate transferase {ECO:0000256|ARBA:ARBA00033238};
GN Name=DPAGT1 {ECO:0000313|EMBL:KRX85175.1};
GN ORFNames=T06_12875 {ECO:0000313|EMBL:KRX85175.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX85175.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX85175.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX85175.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-
CC acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP;
CC Xref=Rhea:RHEA:13289, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9519,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:58427; EC=2.7.8.15;
CC Evidence={ECO:0000256|ARBA:ARBA00034004};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family.
CC {ECO:0000256|ARBA:ARBA00009317}.
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:KRX85175.1}.
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DR EMBL; JYDK01000002; KRX85175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XBJ1; -.
DR STRING; 92179.A0A0V0XBJ1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProt.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProt.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd06855; GT_GPT_euk; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 2.170.140.10; Chitin binding domain; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR033895; GPT.
DR PANTHER; PTHR10571; UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR10571:SF0; UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE; 1.
DR Pfam; PF01607; CBM_14; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
DR SMART; SM00494; ChtBD2; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 2.
DR PROSITE; PS50940; CHIT_BIND_II; 2.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..808
FT /note="UDP-N-acetylglucosamine--dolichyl-phosphate N-
FT acetylglucosaminephosphotransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006872420"
FT TRANSMEM 584..603
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 615..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 688..705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 711..732
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..409
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 454..510
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 541..595
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
SQ SEQUENCE 808 AA; 92195 MW; 0CB950B14CF4747B CRC64;
MQTTKHFFVK RMFIALQLLN AVFSVGSKSA KTCQYIRGCY FTNWAQYRTG DASYMPEHYQ
PGLCTHIFFA FAKFTDNFIV ATTEHNDIQS DNSGLYQRVN KLKQQDPNLK TLLSVGGYGF
GIQKFQQLAR NQYARSKFVN SLKEFLRRFN FDGVDLDWEY PTSADYSHFI ILVKDIADAF
HYESVTTGKP KLLLTAAVTG NEQTAADGYN VQAMARYFDF VNVMTYDFHG GWEMQTGINS
PLYRYSAAVE WAKQWNVADA AEAWFKMGMP REKIVIGFAT YGRGWNLPIG NTDHGIRVGT
RAVGPATATT LVQQTGVAAF YELCEMLENG ARRFWDDESK TPYLVHDGKW YSYDDPDSYS
EKLTWLQNQG YGGAFVWSLD FDDFQGKCTL TNNEKYPLIK MFNQLLCANA PQSNQTSTRR
PLTTFPSTGN NDMLINESDF DEDTDEKLFE NFTDKACYNK PPGFWPDPKN CAEFFLCLDN
GIYKMKCPAN LHFDPLWRHC TLPELSGCRR IPKTEPTPTT TTLADKRFTS RTTAQPSKGT
LFVCDADGFF SNPTNCTQFY RCVGGVAFKF TCPQGLQFNQ RHNLVEFLSG ILSICCMVFL
GFADDVLDLR WRHKLLLPTV ASLPLLMVYA ATYNSTSIVI PLQLQPWFGK VLNIGVLYYV
YIGMVAVFCT NAINIYAGIN GLEVGQSVII AISILIFNIV QLVRLEQECR YHMFSIYFLL
PYIATSLVLL RFNWYPASVF VGDTFCYFSG MLFAVVGILG HFSKTLMLLF LPQIFNFIFS
LPQLFRIIPC PRHRLPKYLT SFFVCKFQ
//
