| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | g5108.t1 |
| Family | GT24 |
| Protein Properties | Length: 1833 Molecular Weight: 187226 Isoelectric Point: 5.0576 |
| 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 | 1593 | 1718 | 0 |
| INVFTVASGHMYERLQKIMVLSVVRHTKSRVKFWIIKNYCSPQHRAVLPALAARYGFDYEFVTYKWPTWLHKQTDKQRLIWAYKILFLDVLFPLGVERII FVDSDQVVRTDLAELYHMDIGGAPYA | |||
| Full Sequence |
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| Protein Sequence Length: 1833 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 SRQPVNGSLR SAVASNQAAG LSAGANLLLL NGLAVDVNSL 420 DYYGFLGRLR AEMRLRDALV SPPAPAPATA AATASTATAS TATAATAGGL GLPGDVAATV 480 MALRAEEGAG AAAGGGGGVE SEPRLSLGSA STMDKHVTWL NNLDKDAKYQ RFGRSVNELL 540 SVYPGRLKPL GRNMFTAVLV AQPLCAASLQ LAAAVEQMWQ GGYPLRFGVV FELPAVQGRL 600 ATSRRYPHLT GATQAPAWED MDASERFGRA FATLREAFGG PAAWRLWGKV AELVGSGEAQ 660 DPGSAVEAAF KAAWAAAARS PPPGARAKAA ARKSAADALT MLQEGSGYAA EVGMALTDTA 720 AWLQGRGLVT APPPTPAGQA GEDAEDCSRA PLVWMNGLAG RSAGGGGGMM GGGGGPAEDL 780 LYKLMGEMQR MQEWVYFGRL ADDTAGGDVL QAVLGLAGAV ERLNPRLVGP AAARNAKVVP 840 LAPLLRGPAR QQLAALWRDT PASSSSSASS PSSSSPSASS LDDDEDAEAE EAEEQQAGGK 900 KGGGKKGAGK KADKAAKADK GPLRLHVPAV THLVAADLCG EGGEGRELVA EALRFLSDGP 960 PAAVREARLL LAPNPADPQE PPCLLEALAT AALQQAAAGR ATRAQALSFL RRLLSDGPLV 1020 SRLAGPLAGG SAEEATVAVK MAEEAGLDSS SLLGSLTSLV DAALLPGGGG LRRSSQVPAL 1080 AGRTRLAAAL TGGGGGGGAG GGAGGGGGLG LAAGEAAVVT NGRVTRVYRP GGERHELVAE 1140 DFPLLHMAVG GVASAVAAAL SKAHAAAPLP GVPPYPAAAT DAAAAAAATT DALSDLTAAT 1200 AAALAAASAA ATPEAPAGAA GGAAQLGPAA SKQLQSVMAK LRKSKIAVEI PGSSSSSSSP 1260 SSSSSPSSSS ALRLEVILNP LSRPAQRLSG LLLALREALG ADVVLALNPQ RDLTEMPLKS 1320 YYRYALPQGL SPAATAAAPP GTPAAHFARL PPRRVLTLNL ETAYAEWELD SLMLTGSCVD 1380 VTASGRLTPP RGLQLHLGTP AQPHVVDTLV MANLAYFQLK AAPGLWLLSL APGRSRELYE 1440 LTGSTGTSLH DDDNEEEEEG EGEEGEEEGR AVAVVAAGGG KGVAVGVSDP AVSTQVLISS 1500 FTGKHMILRV RKRPGMEDED VLKQGGEEDD VVEIDRPMHE LEDDEYADED DDEAPARKPS 1560 SLLGRVSDMI TGKGGKDGAA AAAAKKLPGG DVINVFTVAS GHMYERLQKI MVLSVVRHTK 1620 SRVKFWIIKN YCSPQHRAVL PALAARYGFD YEFVTYKWPT WLHKQTDKQR LIWAYKILFL 1680 DVLFPLGVER IIFVDSDQVV RTDLAELYHM DIGGAPYAKT IDLCNNPKTK EPKLTAARRI 1740 IGPLWEELDA QQEAVTREVQ ARLDAAESGL PLLAGATEAA TEAAAEAVEA AGAGTGAGVE 1800 EDWAVGDAPQ QQQQQQQQQG GGAAGGADRT EL* 1860 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd06432 | GT8_HUGT1_C_like | 9.0e-5 | 1718 | 1734 | 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 | 1610 | 1718 | 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 | 1272 | 1413 | 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 | 1593 | 1724 | 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 | 1593 | 1720 | 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 | 829 | 27 | 744 | AC016162_4 putative UDP-glucose:glycoprotein glucosyltransferase; 101200-91134 [Arabidopsis thaliana] |
| GenBank | AAG51883.1 | 0 | 927 | 1728 | 781 | 1478 | AC016162_4 putative UDP-glucose:glycoprotein glucosyltransferase; 101200-91134 [Arabidopsis thaliana] |
| GenBank | AAG51883.1 | 0.002 | 1718 | 1759 | 1593 | 1633 | AC016162_4 putative UDP-glucose:glycoprotein glucosyltransferase; 101200-91134 [Arabidopsis thaliana] |
| RefSeq | XP_002529534.1 | 0 | 7 | 828 | 30 | 720 | UDP-glucose glycoprotein:glucosyltransferase, putative [Ricinus communis] |
| RefSeq | XP_002529534.1 | 0 | 1109 | 1728 | 902 | 1436 | UDP-glucose glycoprotein:glucosyltransferase, putative [Ricinus communis] |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| HO415354 | 455 | 1305 | 1731 | 0 |
| CB629555 | 342 | 1359 | 1700 | 0 |
| HO118039 | 310 | 1409 | 1716 | 0 |
| GR153110 | 327 | 1369 | 1683 | 0 |
| HO415354 | 52 | 1718 | 1769 | 0.0003 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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