y
Basic Information | |
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Species | Volvox carteri |
Cazyme ID | Vocar20001407m |
Family | GT57 |
Protein Properties | Length: 492 Molecular Weight: 53205.9 Isoelectric Point: 9.2143 |
Chromosome | Chromosome/Scaffold: 23 Start: 979645 End: 985087 |
Description | ALG6, ALG8 glycosyltransferase family |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT57 | 23 | 440 | 0 |
ILVRVLTGLASYSGAGDAPKYGDYEAQRHWMELTVNLPVTEWYTDSPVNNASYWPLDYPPLSGYQSWLCGKVLRAVEPASVELVRSHGYETPSSKIAMRW TVIAADLLVYIPACLAAIHVFYGAPSSPSAGSSSATAHRARTLALLALLFSPAAIIIDHGHFQYNNISLGLTLAAAAAIGSGRQLLGAALFSAALNHKQM ALFFAPGFFAHLLGWALHSERHRGVLAVAKLGLVVIATFAACWAPYLSSKGAVLQVLTRIFPVRRGLYEDYVANWWCASSLLIKWKSRFSAPVLLRAAAA ATLAAAAPSMAHQILGRPRGGGGGPSRWGFLRCLANSAFAFYMFSYQVHEKSILLPLLPVTLLAGREPSLATWLPLLAALSMFPLLDRDGVALPYVALCA LYGAVMAGPALHHARQLQ |
Full Sequence |
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Protein Sequence Length: 492 Download |
MLNLLDFVGD DRLSTAVVVL LAILVRVLTG LASYSGAGDA PKYGDYEAQR HWMELTVNLP 60 VTEWYTDSPV NNASYWPLDY PPLSGYQSWL CGKVLRAVEP ASVELVRSHG YETPSSKIAM 120 RWTVIAADLL VYIPACLAAI HVFYGAPSSP SAGSSSATAH RARTLALLAL LFSPAAIIID 180 HGHFQYNNIS LGLTLAAAAA IGSGRQLLGA ALFSAALNHK QMALFFAPGF FAHLLGWALH 240 SERHRGVLAV AKLGLVVIAT FAACWAPYLS SKGAVLQVLT RIFPVRRGLY EDYVANWWCA 300 SSLLIKWKSR FSAPVLLRAA AAATLAAAAP SMAHQILGRP RGGGGGPSRW GFLRCLANSA 360 FAFYMFSYQV HEKSILLPLL PVTLLAGREP SLATWLPLLA ALSMFPLLDR DGVALPYVAL 420 CALYGAVMAG PALHHARQLQ RLQVRRHDDT HTSQDGGAGM CICVCAQHYT LQPSTKPLFL 480 FLRYNYSSLE M* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03155 | Alg6_Alg8 | 2.0e-84 | 30 | 430 | 407 | + ALG6, ALG8 glycosyltransferase family. N-linked (asparagine-linked) glycosylation of proteins is mediated by a highly conserved pathway in eukaryotes, in which a lipid (dolichol phosphate)-linked oligosaccharide is assembled at the endoplasmic reticulum membrane prior to the transfer of the oligosaccharide moiety to the target asparagine residues. This oligosaccharide is composed of Glc(3)Man(9)GlcNAc(2). The addition of the three glucose residues is the final series of steps in the synthesis of the oligosaccharide precursor. Alg6 transfers the first glucose residue, and Alg8 transfers the second one. In the human alg6 gene, a C->T transition, which causes Ala333 to be replaced with Val, has been identified as the cause of a congenital disorder of glycosylation, designated as type Ic OMIM:603147. |
Gene Ontology | |
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GO Term | Description |
GO:0005789 | endoplasmic reticulum membrane |
GO:0016758 | transferase activity, transferring hexosyl groups |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAC79743.1 | 0 | 13 | 432 | 28 | 434 | putative alpha 3 glucosyltransferase [Oryza sativa Japonica Group] |
RefSeq | NP_001145139.1 | 0 | 15 | 438 | 32 | 442 | hypothetical protein LOC100278369 [Zea mays] |
RefSeq | XP_001699186.1 | 0 | 1 | 440 | 2 | 496 | glycosyl transferase, type ALG6, ALG8 [Chlamydomonas reinhardtii] |
RefSeq | XP_002305159.1 | 0 | 26 | 447 | 15 | 413 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002506686.1 | 0 | 22 | 428 | 1 | 398 | glycosyltransferase family 57 protein [Micromonas sp. RCC299] |