Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10011033m |
Family | CE16 |
Protein Properties | Length: 390 Molecular Weight: 43338.8 Isoelectric Point: 8.427 |
Chromosome | Chromosome/Scaffold: 1 Start: 7019700 End: 7021490 |
Description | GDSL-like Lipase/Acylhydrolase superfamily 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 |
CE16 | 143 | 378 | 2.7e-23 |
TGVSFASGGSGYNPLTPKLSSVTPMLDQLTYFQRHIARVKKLIGKEETDQLLVKGLSVVVAGSNDLVITYYGQGAQWLKDDINYYTSKMANSAASFVMQL YEYGARQIAVLGTPPLGCVPLQRTLKGGLHRDCAEDVNYASQLFNAKLSITLDQLTKTLPNSNIIYIDIYSAFSHIIENAADYGFEEIKKGCCGTGFVEV GPLCNRFTPFVCSNVSAYMFWDSFHPTQRFYKILTK |
Full Sequence |
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Protein Sequence Length: 390 Download |
MKQYRLIHSR LVGFVFFLLS SFSIFFVTTT HSQVIHHRRL WPRPLPESGP GPPPEPSPTP 60 HNKTIPAVFF LGDSIIDTGN NNNLSTEMKC NFPPYGKDFP LGVATGRFSN GKVASDYISE 120 YLGVKPIVPA YLDPNVQLED LLTGVSFASG GSGYNPLTPK LSSVTPMLDQ LTYFQRHIAR 180 VKKLIGKEET DQLLVKGLSV VVAGSNDLVI TYYGQGAQWL KDDINYYTSK MANSAASFVM 240 QLYEYGARQI AVLGTPPLGC VPLQRTLKGG LHRDCAEDVN YASQLFNAKL SITLDQLTKT 300 LPNSNIIYID IYSAFSHIIE NAADYGFEEI KKGCCGTGFV EVGPLCNRFT PFVCSNVSAY 360 MFWDSFHPTQ RFYKILTKIL VEKYIHKLN* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01847 | Triacylglycerol_lipase_like | 1.0e-19 | 67 | 376 | 321 | + Triacylglycerol lipase-like subfamily of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Members of this subfamily might hydrolyze triacylglycerol into diacylglycerol and fatty acid anions. | ||
COG3240 | COG3240 | 3.0e-23 | 68 | 376 | 325 | + Phospholipase/lecithinase/hemolysin [Lipid metabolism / General function prediction only] | ||
cd01846 | fatty_acyltransferase_like | 3.0e-39 | 68 | 382 | 318 | + Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Might catalyze fatty acid transfer between phosphatidylcholine and sterols. | ||
PLN03156 | PLN03156 | 1.0e-102 | 65 | 389 | 328 | + GDSL esterase/lipase; Provisional | ||
cd01837 | SGNH_plant_lipase_like | 4.0e-133 | 66 | 384 | 319 | + SGNH_plant_lipase_like, a plant specific subfamily of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. |
Gene Ontology | |
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GO Term | Description |
GO:0006629 | lipid metabolic process |
GO:0016788 | hydrolase activity, acting on ester bonds |
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 | AAF79900.1 | 0.002 | 1 | 60 | 11 | 89 | AC022472_9 Contains a strong similarity to Anther-specific proline-rich protein APG precursor from Arabidopsis thaliana gi |
GenBank | AAF79900.1 | 0 | 23 | 326 | 541 | 831 | AC022472_9 Contains a strong similarity to Anther-specific proline-rich protein APG precursor from Arabidopsis thaliana gi |
GenBank | AAF79900.1 | 0 | 61 | 364 | 208 | 518 | AC022472_9 Contains a strong similarity to Anther-specific proline-rich protein APG precursor from Arabidopsis thaliana gi |
GenBank | AAF79900.1 | 0 | 64 | 376 | 835 | 1135 | AC022472_9 Contains a strong similarity to Anther-specific proline-rich protein APG precursor from Arabidopsis thaliana gi |
RefSeq | NP_001117317.1 | 0 | 7 | 389 | 1 | 383 | hydrolase, acting on ester bonds / lipase [Arabidopsis thaliana] |