Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 426997 |
Family | CE16 |
Protein Properties | Length: 356 Molecular Weight: 38253.6 Isoelectric Point: 8.9705 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE16 | 104 | 344 | 3.4e-24 |
GQNIVTGVNFATGGSGYLSETGATLNVPGLDGQLQWFKSYTQNLVKIVGKANATNIISQGVYTLSTGSNDYVANYYVNPLVQEKYSRNAFRSLLLSSFTQ FTKALYSLGARRIAVVSMAPLGCLPSQVTLYGKGSLSCVDFANRDARLFNRALNSTVTSIRASLKDIKLAYIDIYPLVEDVIKNPSKNGFEQTTTGCCGI GRLAVSILCNEHSIGTCSNASKYVFWDSFHPTSTMNQLIAN |
Full Sequence |
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Protein Sequence Length: 356 Download |
MISLAISLLF CSLSVSRAQL IPAAFTFGDS TVDAGNNDYL KTIFRANFPP YGRDFDTKQP 60 TGRFSNGRTP SDYLAIDSGK CALFAAALLG LPLALPYLDP SAKGQNIVTG VNFATGGSGY 120 LSETGATLNV PGLDGQLQWF KSYTQNLVKI VGKANATNII SQGVYTLSTG SNDYVANYYV 180 NPLVQEKYSR NAFRSLLLSS FTQFTKALYS LGARRIAVVS MAPLGCLPSQ VTLYGKGSLS 240 CVDFANRDAR LFNRALNSTV TSIRASLKDI KLAYIDIYPL VEDVIKNPSK NGFEQTTTGC 300 CGIGRLAVSI LCNEHSIGTC SNASKYVFWD SFHPTSTMNQ LIANTAFNQG IGQLL* 360 |
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-13 | 25 | 349 | 327 | + 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 | 4.0e-21 | 1 | 343 | 364 | + Phospholipase/lecithinase/hemolysin [Lipid metabolism / General function prediction only] | ||
cd01846 | fatty_acyltransferase_like | 1.0e-34 | 25 | 349 | 328 | + 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-89 | 4 | 348 | 345 | + GDSL esterase/lipase; Provisional | ||
cd01837 | SGNH_plant_lipase_like | 9.0e-121 | 22 | 348 | 327 | + 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. |
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 | ACU20309.1 | 0 | 1 | 351 | 8 | 349 | unknown [Glycine max] |
GenBank | ACU24285.1 | 0 | 20 | 351 | 28 | 350 | unknown [Glycine max] |
RefSeq | XP_002271400.1 | 0 | 20 | 351 | 26 | 347 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002283363.1 | 0 | 18 | 352 | 28 | 353 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002527431.1 | 0 | 6 | 351 | 22 | 355 | zinc finger protein, 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 | 3kvn_A | 0.003 | 27 | 348 | 21 | 314 | X Chain X, Crystal Structure Of The Full-Length Autotransporter Esta From Pseudomonas Aeruginosa |
PDB | 3kvn_X | 0.003 | 27 | 348 | 21 | 314 | X Chain X, Crystal Structure Of The Full-Length Autotransporter Esta From Pseudomonas Aeruginosa |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
triacylglycerol degradation | TRIACYLGLYCEROL-LIPASE-RXN | EC-3.1.1.3 | triacylglycerol lipase |