| Basic Information | |
|---|---|
| Species | Capsella rubella |
| Cazyme ID | Carubv10025963m |
| Family | GH35 |
| Protein Properties | Length: 727 Molecular Weight: 81095.6 Isoelectric Point: 8.8466 |
| Chromosome | Chromosome/Scaffold: 8 Start: 9150098 End: 9155904 |
| Description | beta-galactosidase 4 |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH35 | 39 | 340 | 0 |
| IINGQRRILLSGSIHYPRSTPEMWPGLIQKAKEGGLDVIETYVFWNGHEPSPGQYYFGDRYDLVKFIKLAHQAGLYVNLRIGPYVCAEWNFGGFPVWLKF VPGMAFRTDNEPFKAAMKKFTEKIVWMMKAEKLFQTQGGPIILAQIENEYGPVEWSIGAPGKAYTKWVAQMALGLSTGVPWIMCKQEDAPSPIIDTCNGY YCEDFKPNSSNKPKMWTENWTGWYTEFGGAVPYRPVEDIAYSVVRFIAKGGSFVNYYMYHGGTNFDRTAGEFMASSYDYDAPLDEYGLPKEPKYSHLKAL HK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 727 Download |
| MGLNFRDKSW ILLLLGILCC SSLICIVEAS VSYDRKAVII NGQRRILLSG SIHYPRSTPE 60 MWPGLIQKAK EGGLDVIETY VFWNGHEPSP GQYYFGDRYD LVKFIKLAHQ AGLYVNLRIG 120 PYVCAEWNFG GFPVWLKFVP GMAFRTDNEP FKAAMKKFTE KIVWMMKAEK LFQTQGGPII 180 LAQIENEYGP VEWSIGAPGK AYTKWVAQMA LGLSTGVPWI MCKQEDAPSP IIDTCNGYYC 240 EDFKPNSSNK PKMWTENWTG WYTEFGGAVP YRPVEDIAYS VVRFIAKGGS FVNYYMYHGG 300 TNFDRTAGEF MASSYDYDAP LDEYGLPKEP KYSHLKALHK VIKLSEPALV SADATVTYLG 360 AKQEAHVYWS KSSCAAFLSN KDENSAARVM FRGFPYDLPP WSVSILPDCK TEFYNTAKVK 420 SPGIHRNMVS TGTRFSWGSY NEGTPSANEA GTFARNGLVE QISMTWDKSD YFWYLTDITI 480 GAGERFLKTG DFPLLTAMSA GHALHVFVNG QLAGNVYGGL EHTKVTFSQK IKLHAGVNKL 540 ALLSVAVGLP NVGTHFEQWN KGVLGPVTLK GVNSGTWDMS KWRWSYKIGV KGEALSLHTN 600 TESSSVSWSQ GSFVVKKQPL TWYKSTFATP AGNEPLALDM NTMGKGQVWI NGRNIGRHWP 660 AYKAQGSCGR CNYAGTYDAK KCLSDCGEAS QRWYHVPRSW LKSQNLIVVF EEWGGDPNGI 720 SLVKRT* |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| pfam02449 | Glyco_hydro_42 | 0.0001 | 53 | 189 | 151 | + Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. |
| COG1874 | LacA | 3.0e-22 | 31 | 341 | 354 | + Beta-galactosidase [Carbohydrate transport and metabolism] |
| pfam01301 | Glyco_hydro_35 | 1.0e-153 | 39 | 342 | 320 | + Glycosyl hydrolases family 35. |
| PLN03059 | PLN03059 | 0 | 27 | 726 | 702 | + beta-galactosidase; Provisional |
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0004565 | beta-galactosidase activity |
| GO:0005975 | carbohydrate metabolic process |
| GO:0009341 | beta-galactosidase complex |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAK96780.1 | 0 | 1 | 726 | 1 | 724 | beta-galactosidase [Arabidopsis thaliana] |
| EMBL | CAB39679.1 | 0 | 1 | 726 | 1 | 727 | putative beta-galactosidase [Arabidopsis thaliana] |
| RefSeq | NP_190852.2 | 0 | 1 | 726 | 1 | 725 | BGAL2 (beta-galactosidase 2); beta-galactosidase/ catalytic/ cation binding [Arabidopsis thaliana] |
| RefSeq | NP_200498.1 | 0 | 1 | 726 | 1 | 724 | BGAL4 (beta-galactosidase 4); beta-galactosidase [Arabidopsis thaliana] |
| RefSeq | NP_849553.1 | 0 | 1 | 726 | 1 | 726 | BGAL12 (beta-galactosidase 12); beta-galactosidase/ catalytic/ cation binding [Arabidopsis thaliana] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3thd_D | 1.99965e-42 | 31 | 346 | 11 | 339 | I Chain I, Crystal Structure The Fab Fragment Of Efalizumab In Complex With Lfa-1 I Domain, Form I |
| PDB | 3thd_C | 1.99965e-42 | 31 | 346 | 11 | 339 | I Chain I, Crystal Structure The Fab Fragment Of Efalizumab In Complex With Lfa-1 I Domain, Form I |
| PDB | 3thd_B | 1.99965e-42 | 31 | 346 | 11 | 339 | I Chain I, Crystal Structure The Fab Fragment Of Efalizumab In Complex With Lfa-1 I Domain, Form I |
