| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | g5108.t2 |
| Family | GT24 |
| Protein Properties | Length: 1853 Molecular Weight: 189078 Isoelectric Point: 5.1446 |
| Chromosome | Chromosome/Scaffold: 5 Start: 328465 End: 349208 |
| Description | UDP-glucose:glycoprotein glucosyltransferases;transferases, transferring hexosyl groups;transferases, transferring glycosyl groups |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT24 | 1613 | 1738 | 0 |
| INVFTVASGHMYERLQKIMVLSVVRHTKSRVKFWIIKNYCSPQHRAVLPALAARYGFDYEFVTYKWPTWLHKQTDKQRLIWAYKILFLDVLFPLGVERII FVDSDQVVRTDLAELYHMDIGGAPYA | |||
| Full Sequence |
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| Protein Sequence Length: 1853 Download |
| MCTPVLSSKP KGASLTVRAR FNATSYLLEA LEFLAEEEPA LVWKYLDAMG SAAPPRAAGE 60 GDGCWQRLTT EATRLVSPSV GKLLPLVLGS RQYSAKLAMV AQLAAQFHPG QTSCCFVAVG 120 GATLTDPAQL PAALKAAAAT AATATAAATA GGEHAEAEQL FPFDHVYPTT AAAAAAAATA 180 TADGDSSSTG SSTAPAAVLY GSPGLGCFGP LHAALRAAAE AGRATYVFRP LLQPHCESAA 240 GCAASGAGGP LLLPGWGVEA ALKNTEYSAL DDKGNKDKEA AADSGAGGSD ALGSGEAAVV 300 RGFRLDVLAA RKPTLRQELL TLRDQLLTAA EDDADGSGSL KVWDLADVGL AAAQRVLGSS 360 DPLALLAEVA GNFPGLVSSL SRQLLGAGGG GKGRGLVSSL SRQPVNGSLR SAVASNQAAG 420 LSAGANLLLL NGLAVDVNSL DYYGFLGRLR AEMRLRDALV SPPAPAPATA AATASTATAS 480 TATAATAGGL GLPGDVAATV MALRAEEGAG AAAGGGGGVE SEPRLSLGSA STMDKHVTWL 540 NNLDKDAKYQ RFGRSVNELL SVYPGRLKPL GRNMFTAVLV AQPLCAASLQ LAAAVEQMWQ 600 GGYPLRFGVV FELPAVQGRL ATSRRYPHLT GATQAPAWED MDASERFGRA FATLREAFGG 660 PAAWRLWGKV AELVGSGEAQ DPGSAVEAAF KAAWAAAARS PPPGARAKAA ARKSAADALT 720 MLQEGSGYAA EVGMALTDTA AWLQGRGLVT APPPTPAGQA GEDAEDCSRA PLVWMNGLAG 780 RSAGGGGGMM GGGGGPAEDL LYKLMGEMQR MQEWVYFGRL ADDTAGGDVL QAVLGLAGAV 840 ERLNPRLVGP AAARNAKVVP LAPLLRGPAR QQLAALWRDT PASSSSSASS PSSSSPSASS 900 LDDDEDAEAE EAEEQQAGGK KGGGKKGAGK KADKAAKADK GPLRLHVPAV THLVAADLCG 960 EGGEGRELVA EALRFLSDGP PAAVREARLL LAPNPADPQE PPCLLEALAT AALQQAAAGR 1020 ATRAQALSFL RRLLSDGPLV SRLAGPLAGG SAEEATVAVK MAEEAGLDSS SLLGSLTSLV 1080 DAALLPGGGG LRRSSQVPAL AGRTRLAAAL TGGGGGGGAG GGAGGGGGLG LAAGEAAVVT 1140 NGRVTRVYRP GGERHELVAE DFPLLHMAVG GVASAVAAAL SKAHAAAPLP GVPPYPAAAT 1200 DAAAAAAATT DALSDLTAAT AAALAAASAA ATPEAPAGAA GGAAQLGPAA SKQLQSVMAK 1260 LRKSKIAVEI PGSSSSSSSP SSSSSPSSSS ALRLEVILNP LSRPAQRLSG LLLALREALG 1320 ADVVLALNPQ RDLTEMPLKS YYRYALPQGL SPAATAAAPP GTPAAHFARL PPRRVLTLNL 1380 ETAYAEWELD SLMLTGSCVD VTASGRLTPP RGLQLHLGTP AQPHVVDTLV MANLAYFQLK 1440 AAPGLWLLSL APGRSRELYE LTGSTGTSLH DDDNEEEEEG EGEEGEEEGR AVAVVAAGGG 1500 KGVAVGVSDP AVSTQVLISS FTGKHMILRV RKRPGMEDED VLKQGGEEDD VVEIDRPMHE 1560 LEDDEYADED DDEAPARKPS SLLGRVSDMI TGKGGKDGAA AAAAKKLPGG DVINVFTVAS 1620 GHMYERLQKI MVLSVVRHTK SRVKFWIIKN YCSPQHRAVL PALAARYGFD YEFVTYKWPT 1680 WLHKQTDKQR LIWAYKILFL DVLFPLGVER IIFVDSDQVV RTDLAELYHM DIGGAPYAKT 1740 IDLCNNPKTK EPKLTAARRI IGPLWEELDA QQEAVTREVQ ARLDAAESGL PLLAGATEAA 1800 TEAAAEAVEA AGAGTGAGVE EDWAVGDAPQ QQQQQQQQQG GGAAGGADRT EL* 1860 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd06432 | GT8_HUGT1_C_like | 9.0e-5 | 1738 | 1754 | 17 | + The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family. C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity. | ||
| cd04194 | GT8_A4GalT_like | 5.0e-11 | 1630 | 1738 | 113 | + A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS. | ||
| pfam06427 | UDP-g_GGTase | 2.0e-22 | 1292 | 1433 | 169 | + UDP-glucose:Glycoprotein Glucosyltransferase. The N-terminal region of this group of proteins is required for correct folding of the ER UDP-Glc: glucosyltransferase. | ||
| cd00505 | Glyco_transf_8 | 6.0e-33 | 1613 | 1744 | 133 | + Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+. | ||
| cd06432 | GT8_HUGT1_C_like | 2.0e-74 | 1613 | 1740 | 128 | + The C-terminal domain of HUGT1-like is highly homologous to the GT 8 family. C-terminal domain of glycoprotein glucosyltransferase (UGT). UGT is a large glycoprotein whose C-terminus contains the catalytic activity. This catalytic C-terminal domain is highly homologous to Glycosyltransferase Family 8 (GT 8) and contains the DXD motif that coordinates donor sugar binding, characteristic for Family 8 glycosyltransferases. GT 8 proteins are retaining enzymes based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. The non-catalytic N-terminal portion of the human UTG1 (HUGT1) has been shown to monitor the protein folding status and activate its glucosyltransferase activity. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAG51883.1 | 0 | 7 | 849 | 27 | 744 | AC016162_4 putative UDP-glucose:glycoprotein glucosyltransferase; 101200-91134 [Arabidopsis thaliana] |
| GenBank | AAG51883.1 | 0 | 947 | 1748 | 781 | 1478 | AC016162_4 putative UDP-glucose:glycoprotein glucosyltransferase; 101200-91134 [Arabidopsis thaliana] |
| GenBank | AAG51883.1 | 0.002 | 1738 | 1779 | 1593 | 1633 | AC016162_4 putative UDP-glucose:glycoprotein glucosyltransferase; 101200-91134 [Arabidopsis thaliana] |
| RefSeq | XP_002529534.1 | 0 | 7 | 848 | 30 | 720 | UDP-glucose glycoprotein:glucosyltransferase, putative [Ricinus communis] |
| RefSeq | XP_002529534.1 | 0 | 1129 | 1748 | 902 | 1436 | UDP-glucose glycoprotein:glucosyltransferase, putative [Ricinus communis] |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO415354 | 455 | 1325 | 1751 | 0 |
| CB629555 | 342 | 1379 | 1720 | 0 |
| HO118039 | 310 | 1429 | 1736 | 0 |
| GR153110 | 327 | 1389 | 1703 | 0 |
| HO415354 | 52 | 1738 | 1789 | 0.0003 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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