y
Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.010G095100.1 |
Family | GH5 |
Protein Properties | Length: 513 Molecular Weight: 58032.2 Isoelectric Point: 7.1603 |
Chromosome | Chromosome/Scaffold: 10 Start: 34718200 End: 34719972 |
Description | Cellulase (glycosyl hydrolase family 5) protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH5 | 35 | 353 | 3e-35 |
EATGQRAKLVCANWAGHLKPMIPEGLDKRPLKELVGELVKHNFNCVRLTYAIYMWTRYSHENVSASFASLDAPEVVQGISKNNPSVLSMTHVQAFHAVVH ELGVQNVKVLLDNHVSEPMWCCDDDDENGFFHDRHFNPQEWVRGLTLAAKHFTGNHAVVAMSLRNELHGPRQNLQDWYRYMSQGAVAIHKTNPNVLVLIS GLNYDTELQFLKSKPLKIDLGKKMVYETHLYSWSGIGTLKLKEIWTKQPLNRICANNIKGIDYRVGFLTTGKNAAPLIFTEFGFNEEGSSVEDSRFLTCL QTYLLGKDLDWGLWAFQGS |
Full Sequence |
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Protein Sequence Length: 513 Download |
MASPLSLLIL FLVFISASHS NAYPLSTQNR WIIDEATGQR AKLVCANWAG HLKPMIPEGL 60 DKRPLKELVG ELVKHNFNCV RLTYAIYMWT RYSHENVSAS FASLDAPEVV QGISKNNPSV 120 LSMTHVQAFH AVVHELGVQN VKVLLDNHVS EPMWCCDDDD ENGFFHDRHF NPQEWVRGLT 180 LAAKHFTGNH AVVAMSLRNE LHGPRQNLQD WYRYMSQGAV AIHKTNPNVL VLISGLNYDT 240 ELQFLKSKPL KIDLGKKMVY ETHLYSWSGI GTLKLKEIWT KQPLNRICAN NIKGIDYRVG 300 FLTTGKNAAP LIFTEFGFNE EGSSVEDSRF LTCLQTYLLG KDLDWGLWAF QGSYYVKKDQ 360 VQVDESFGLM DETWHHLRYP NLTHKFQLLQ RKNIVNEKNE VELGSCETKN RWVGGENGTK 420 IILHGTKKCL TAAGEGLPVV VSDCERKSSS WKSVSLSKLH LATMNQQEEQ LCLQKDSNSS 480 SIVTSKCICI KDDSLCLDDP QSQWFQLVET NV* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam05830 | NodZ | 0.001 | 153 | 224 | 74 | + Nodulation protein Z (NodZ). The nodulation genes of Rhizobia are regulated by the nodD gene product in response to host-produced flavonoids and appear to encode enzymes involved in the production of a lipo-chitose signal molecule required for infection and nodule formation. NodZ is required for the addition of a 2-O-methylfucose residue to the terminal reducing N-acetylglucosamine of the nodulation signal. This substitution is essential for the biological activity of this molecule. Mutations in nodZ result in defective nodulation. nodZ represents a unique nodulation gene that is not under the control of NodD and yet is essential for the synthesis of an active nodulation signal. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
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 | ABD32354.1 | 0 | 6 | 511 | 5 | 534 | Glycoside hydrolase, family 5; Ricin B-related lectin [Medicago truncatula] |
RefSeq | XP_002272386.1 | 0 | 6 | 512 | 5 | 531 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002272422.1 | 0 | 6 | 512 | 88 | 614 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002509877.1 | 0 | 6 | 512 | 4 | 546 | hydrolase, hydrolyzing O-glycosyl compounds, putative [Ricinus communis] |
RefSeq | XP_002509879.1 | 0 | 30 | 512 | 32 | 535 | hydrolase, hydrolyzing O-glycosyl compounds, putative [Ricinus communis] |
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 | 1ece_B | 0.000000000001 | 27 | 350 | 8 | 321 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
PDB | 1ece_A | 0.000000000001 | 27 | 350 | 8 | 321 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
PDB | 1vrx_B | 0.000000000002 | 27 | 350 | 8 | 321 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
PDB | 1vrx_A | 0.000000000002 | 27 | 350 | 8 | 321 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
PDB | 2zun_C | 0.0003 | 23 | 266 | 41 | 300 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |