Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 114109 |
Family | GT57 |
Protein Properties | Length: 450 Molecular Weight: 51538.8 Isoelectric Point: 9.6485 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT57 | 9 | 428 | 0 |
GDYEAQRHWMELTINLPVSDWYRNTTDNDLGYWGLDYPPLTAYQSYIHGVFMRKFDEQSVALHSSRGYESLHSKVLMRWTVVLSDLAIFFPAAIAFVAAY YRQRSHEERVWVLALILLQPALILIDHGHFQYNCLSLGLAIGAAAAVISRWEIVACVLFSLSLNHKQMSMYYAPAFFSHLLGISLRKKYPVLNVLKLGAA VLSTFALCWWPFLHSREAVLQVLSRLVPIHRGLFEDYVSNFWCVSNLLIKWKQLLPDRVLVQLAFVATLACILPSMLQQILRPSRRGFLLAMFNCSFAFY FFSYQVHEKSILLPVIPGTLLALDEPLVWRWLIPGALMSMFPLLVRDGLLLPYFALLLLFFLGFVPLRSFNPVAASSLLGGFVLHLAYLLLDPPARYPYL FEAFIATYTFAYFAAIFLYT |
Full Sequence |
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Protein Sequence Length: 450 Download |
GAGNPPKYGD YEAQRHWMEL TINLPVSDWY RNTTDNDLGY WGLDYPPLTA YQSYIHGVFM 60 RKFDEQSVAL HSSRGYESLH SKVLMRWTVV LSDLAIFFPA AIAFVAAYYR QRSHEERVWV 120 LALILLQPAL ILIDHGHFQY NCLSLGLAIG AAAAVISRWE IVACVLFSLS LNHKQMSMYY 180 APAFFSHLLG ISLRKKYPVL NVLKLGAAVL STFALCWWPF LHSREAVLQV LSRLVPIHRG 240 LFEDYVSNFW CVSNLLIKWK QLLPDRVLVQ LAFVATLACI LPSMLQQILR PSRRGFLLAM 300 FNCSFAFYFF SYQVHEKSIL LPVIPGTLLA LDEPLVWRWL IPGALMSMFP LLVRDGLLLP 360 YFALLLLFFL GFVPLRSFNP VAASSLLGGF VLHLAYLLLD PPARYPYLFE AFIATYTFAY 420 FAAIFLYTNY RQWSRSRVLS STQKRKKKV* |
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-95 | 1 | 409 | 432 | + 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. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_001145139.1 | 0 | 1 | 437 | 54 | 511 | hypothetical protein LOC100278369 [Zea mays] |
RefSeq | XP_001780921.1 | 0 | 1 | 444 | 2 | 464 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002280181.1 | 0 | 1 | 449 | 54 | 516 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305159.1 | 0 | 1 | 447 | 25 | 489 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002329281.1 | 0 | 1 | 447 | 21 | 484 | predicted protein [Populus trichocarpa] |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
dolichyl-diphosphooligosaccharide biosynthesis | RXN-5470 | EC-2.4.1.267 | Dol-P-Glc:Man9GlcNAc2-PP-Dol α-1,3-glucosyltransferase |