y
Basic Information | |
---|---|
Species | Capsella rubella |
Cazyme ID | Carubv10008758m |
Family | GH5 |
Protein Properties | Length: 553 Molecular Weight: 61555.2 Isoelectric Point: 7.9953 |
Chromosome | Chromosome/Scaffold: 1 Start: 4580975 End: 4584785 |
Description | Cellulase (glycosyl hydrolase family 5) protein |
View CDS |
External Links |
---|
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH5 | 42 | 355 | 2.4e-41 |
IVDEKGQRVKLVCVNWPSHLQPIVAEGLSKQPVDALAKKIVDMGFNCVRLTWPLDLMTNETLANNVTVRQSFQSLGLNDDIVGFQTNNPSIIDLSLIEAY KMVVTTLGNNDVMVILDNHLTKPGWCCDNNDGNGFFGDQFFDPTVWVAALKKMAGTFDGVSNVVGMSLRNELRGPKQNVNDWFKYMQQGAEAVHSANKNV LVILSGLSFDCDLSFVRSRPVKVSFTGKLVFELHWYSFSDGNSWATNNPNDICGRVLNRIGNGGGFLLNQGFPLFLSEFGIDERGGNANDDRYFGCLTGW AAEHDLDWSLWALT |
Full Sequence |
---|
Protein Sequence Length: 553 Download |
MTRKEPKRMF CIFTFFCFFF SFTAQHTVPN MAHPLSTSSR WIVDEKGQRV KLVCVNWPSH 60 LQPIVAEGLS KQPVDALAKK IVDMGFNCVR LTWPLDLMTN ETLANNVTVR QSFQSLGLND 120 DIVGFQTNNP SIIDLSLIEA YKMVVTTLGN NDVMVILDNH LTKPGWCCDN NDGNGFFGDQ 180 FFDPTVWVAA LKKMAGTFDG VSNVVGMSLR NELRGPKQNV NDWFKYMQQG AEAVHSANKN 240 VLVILSGLSF DCDLSFVRSR PVKVSFTGKL VFELHWYSFS DGNSWATNNP NDICGRVLNR 300 IGNGGGFLLN QGFPLFLSEF GIDERGGNAN DDRYFGCLTG WAAEHDLDWS LWALTGSYYL 360 RQGVVGLNEY YGVLDKDWIS VRNSSFLQKL SLLQSPLQGP HPQTDAYNLV FHPLTGLCIV 420 RSLKDTTMLT LGPCNSSEPW SYTKKAIRIK DQPLCLQSNG PKNPVTLTRT SCSTSSSIWQ 480 TVSASRMHLS STTSNKTSLC LDVDATNNVV ANACKCLSKD STCEPMSQWF KIIKATRPLK 540 HSSLHKEISS MS* 600 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00458 | RICIN | 0.006 | 411 | 463 | 57 | + Ricin-type beta-trefoil. Carbohydrate-binding domain formed from presumed gene triplication. | ||
cd00161 | RICIN | 6.0e-5 | 407 | 532 | 133 | + Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. The domain is found in a variety of molecules serving diverse functions such as enzymatic activity, inhibitory toxicity and signal transduction. Highly specific ligand binding occurs on exposed surfaces of the compact domain sturcture. | ||
pfam00150 | Cellulase | 2.0e-6 | 71 | 356 | 298 | + Cellulase (glycosyl hydrolase family 5). |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAD31066.1 | 0 | 31 | 551 | 1 | 521 | AC007357_15 F3F19.15 [Arabidopsis thaliana] |
RefSeq | NP_172772.2 | 0 | 1 | 551 | 1 | 551 | glycosyl hydrolase family 5 protein / cellulase family protein [Arabidopsis thaliana] |
RefSeq | NP_189245.1 | 0 | 31 | 537 | 1 | 508 | glycosyl hydrolase family 5 protein / cellulase family protein [Arabidopsis thaliana] |
RefSeq | XP_002315653.1 | 0 | 31 | 537 | 1 | 506 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002515055.1 | 0 | 32 | 537 | 31 | 535 | hydrolase, hydrolyzing O-glycosyl compounds, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1vrx_B | 0.00000000000003 | 37 | 321 | 8 | 284 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
PDB | 1vrx_A | 0.00000000000003 | 37 | 321 | 8 | 284 | A Chain A, Endocellulase E1 From Acidothermus Cellulolyticus Mutant Y245g |
PDB | 1ece_B | 0.0000000000002 | 37 | 321 | 8 | 284 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
PDB | 1ece_A | 0.0000000000002 | 37 | 321 | 8 | 284 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |
PDB | 2zun_C | 0.003 | 50 | 386 | 61 | 402 | A Chain A, Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose |