ID A0A287D4N9_ICTTR Unreviewed; 1098 AA.
AC A0A287D4N9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ALG13 UDP-N-acetylglucosaminyltransferase subunit {ECO:0000313|Ensembl:ENSSTOP00000028556.1};
GN Name=ALG13 {ECO:0000313|Ensembl:ENSSTOP00000028556.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000028556.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000028556.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000256|ARBA:ARBA00006962}.
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DR EMBL; AGTP01029603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01029604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01029605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01029606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_013213212.1; XM_013357758.1.
DR AlphaFoldDB; A0A287D4N9; -.
DR Ensembl; ENSSTOT00000040827.1; ENSSTOP00000028556.1; ENSSTOG00000006799.3.
DR GeneID; 101978575; -.
DR CTD; 79868; -.
DR GeneTree; ENSGT00940000159922; -.
DR OrthoDB; 5406292at2759; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd20447; Tudor_TDRD13; 1.
DR Gene3D; 3.90.70.80; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR039042; Alg13-like.
DR InterPro; IPR007235; Glyco_trans_28_C.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR12867:SF7; BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE TRANSFERASE AND DEUBIQUITINASE ALG13-RELATED; 1.
DR PANTHER; PTHR12867; GLYCOSYL TRANSFERASE-RELATED; 1.
DR Pfam; PF04101; Glyco_tran_28_C; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 232..336
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 476..536
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 412..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 122324 MW; D8FA2AFC5B99CB04 CRC64;
MKCLFVTVGT TSFDDLIACV SAHDSLQIIK SLGYNRLILQ IGRGTVVPKP FSTESFTLDV
YRYKESLKED LQKADLVISH AGAGSCLETL EKGKPLVVVI NEKLMNNHQL ELARKLHKEG
HLFYCTCRAP SYPEEARRFA FPALEKSQDS VVLIPTAALC LDFELFSEYL QKQALVIATN
FYRYPALSFS PRFCSFYPLT TLGTMHKGWK KHASQKSLNE VSMDEYLGTL GLFRKLTAKD
ASCLFRAISE QLFCSQVHHL QVRKACVSYM KENQQNFESE SAGQLEIRAL SLIYNRDFIL
YRHPGKPPTC ITENGYEDKI LLCSSSNGHY DSVYSKQFQS SAAICQAILY EILYKDVFVV
DEEALKTAVE VFRSGSKRNR NIAVTGSENA YIDYKNSTED RTDEWGASCK DENTLESHNQ
ETEESKSPEN PSKMLFPYKV LKALDPEIYR NVEFDVWLDS RKELQKSEYM EYAGRQYYLG
DKCQVRLESS GKYYNAHIQE VGNENNSVTV FIEELAEKHV VPLADLKPVT QVTPVSSWNA
IRKGRGYQKI SGGFVPEMAM SEMDMKQRKK LFKKVRGKEV YMTMAYSKGG SLIAPRLQHE
MRYGHEPPLH YSPTGGDGLS DEHFHSPNSS HRQGRGYGMP RDSPRFLNRH NMPGPKVSFY
PGPGKRCCQS YDNFSYRSRS FRRSHRQMRC MNKECQYAFV PVNGQIPSGL EETITFYEVE
EGGETAYPTV PNQGGPATMV PAASGYCVAR RGHSSGKQTF NSEEGNVQTD SGEYHEEYLY
PSEPDYETSG VYSTTVSTAN LSLQDRRSCS LSPQDTVTSY SYPQKMMGNS AAVAASCANN
VPAAVLSNCT AANQASNTSP VSSQNVIQPL FVSPPTGGRS VIATPSYPYH SVPAAGSSLP
PPPLPLSASA LEMGEASNLP PPPPPYSCDP SGSDLPQDTK VLQYYFNLGL QCYHHNYWHS
MVCAPQMQQQ QLYVENYPMY CEPPSLVDQT APHFYSEVGR ASGTHIEAST HGTFLNIDPG
SIPRGAVYYP VMSDPYGQPP LPGFDSCLPV VPDHSYVASW HPVGIAYGGS QIHGAINPGP
VGYIASPSSA SHYVPQNM
//
