Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 874761 |
Family | GT37 |
Protein Properties | Length: 535 Molecular Weight: 61502.6 Isoelectric Point: 8.0123 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT37 | 47 | 504 | 0 |
DTTKDIEESERPVDKLIGGLLTADFDESSCLSRYHKHFLYRKPSPYKPSEYLVSKLRSYEMLHKRCGPDTKAYKEATEKLSRDEYYASEANGECRYIVWV AGYGLGNRLLTLASVFLYALLTERIILVDNRKDVSDLLCEPFPGTSWLLPLDFPMLNYTYAWGYNKEYPRCYGTMEENHSINSTSIPPHLYMHNLHDSRD SDKLFICQKDQSLIDKVPWLIVQANVYFVPSLWFNPNFQTELVKLFPQKDTVFHHLARYLFHPTNQVWDMVTKYYDAHLSKADERLGIQIRVFGKPSGFF QHVMDQVVACTQREKLLPEFATQEELKVNISKTPKLKAVLVASLYPEYSGNLTNMFSKRPSSTGEIVEVYQPSGERVQQTDKKIHDQKALAEMYLLSLTD NIVTSARSTFGYVSYSLGGLKPWLLYQPTNFTTPNPPCVRSKSMEPCYLTPPSHGCEA |
Full Sequence |
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Protein Sequence Length: 535 Download |
MYHIFQIYRK SFKALGLKKK ILIAVVFGCL VIILSFSNNF NNQILNDTTK DIEESERPVD 60 KLIGGLLTAD FDESSCLSRY HKHFLYRKPS PYKPSEYLVS KLRSYEMLHK RCGPDTKAYK 120 EATEKLSRDE YYASEANGEC RYIVWVAGYG LGNRLLTLAS VFLYALLTER IILVDNRKDV 180 SDLLCEPFPG TSWLLPLDFP MLNYTYAWGY NKEYPRCYGT MEENHSINST SIPPHLYMHN 240 LHDSRDSDKL FICQKDQSLI DKVPWLIVQA NVYFVPSLWF NPNFQTELVK LFPQKDTVFH 300 HLARYLFHPT NQVWDMVTKY YDAHLSKADE RLGIQIRVFG KPSGFFQHVM DQVVACTQRE 360 KLLPEFATQE ELKVNISKTP KLKAVLVASL YPEYSGNLTN MFSKRPSSTG EIVEVYQPSG 420 ERVQQTDKKI HDQKALAEMY LLSLTDNIVT SARSTFGYVS YSLGGLKPWL LYQPTNFTTP 480 NPPCVRSKSM EPCYLTPPSH GCEADSGKNS GKILPFVRHC EDIMYGGLKL YDEF* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11548 | NodZ_like | 7.0e-6 | 150 | 465 | 335 | + Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ. Bradyrhizobium NodZ is an alpha 1,6-fucosyltransferase involved in the biosynthesis of the nodulation factor, a lipo-chitooligosaccharide formed by three-to-six beta-1,4-linked N-acetyl-d-glucosamine (GlcNAc) residues and a fatty acid acyl group attached to the nitrogen atom at the non-reducing end. NodZ transfers L-fucose from the GDP-beta-L-fucose donor to the reducing residue of the chitin oligosaccharide backbone, before the attachment of a fatty acid group. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes. | ||
pfam03254 | XG_FTase | 0 | 32 | 504 | 480 | + Xyloglucan fucosyltransferase. Plant cell walls are crucial for development, signal transduction, and disease resistance in plants. Cell walls are made of cellulose, hemicelluloses, and pectins. Xyloglucan (XG), the principal load-bearing hemicellulose of dicotyledonous plants, has a terminal fucosyl residue. This fucosyltransferase adds this residue. |
Gene Ontology | |
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GO Term | Description |
GO:0008107 | galactoside 2-alpha-L-fucosyltransferase activity |
GO:0016020 | membrane |
GO:0042546 | cell wall biogenesis |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAL50624.1 | 0 | 20 | 534 | 2 | 515 | AF417475_1 fucosyltransferase-like protein FUT5 [Arabidopsis thaliana] |
RefSeq | NP_179137.1 | 0 | 94 | 534 | 2 | 440 | FUT10 (FUCOSYLTRANSFERASE 10); fucosyltransferase/ transferase, transferring glycosyl groups [Arabidopsis thaliana] |
RefSeq | NP_179139.1 | 0 | 1 | 534 | 1 | 533 | FUT5; fucosyltransferase/ transferase, transferring glycosyl groups [Arabidopsis thaliana] |
RefSeq | NP_973468.2 | 0 | 1 | 534 | 1 | 535 | FUT4; fucosyltransferase/ transferase, transferring glycosyl groups [Arabidopsis thaliana] |
Swiss-Prot | Q9SJP6 | 0 | 20 | 534 | 2 | 514 | FUT10_ARATH RecName: Full=Putative fucosyltransferase 10; Short=AtFUT10 |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2wft_B | 0.0009 | 151 | 243 | 140 | 218 | A Chain A, Crystal Structure Of The Human Hip Ectodomain |
PDB | 2wft_A | 0.0009 | 151 | 243 | 140 | 218 | A Chain A, Crystal Structure Of The Human Hip Ectodomain |
PDB | 3ho5_B | 0.0009 | 151 | 243 | 161 | 239 | H Chain H, Crystal Structure Of Hedgehog-interacting Protein (hhip) And Sonic Hedgehog (shh) Complex |
PDB | 3ho5_A | 0.0009 | 151 | 243 | 161 | 239 | H Chain H, Crystal Structure Of Hedgehog-interacting Protein (hhip) And Sonic Hedgehog (shh) Complex |
PDB | 3ho4_B | 0.0009 | 151 | 243 | 161 | 239 | A Chain A, Crystal Structure Of Hedgehog-Interacting Protein (Hhip) |