y
Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa001667m |
Family | CE16 |
Protein Properties | Length: 784 Molecular Weight: 86404.5 Isoelectric Point: 7.9388 |
Chromosome | Chromosome/Scaffold: 6 Start: 26975274 End: 26984245 |
Description | GDSL-like Lipase/Acylhydrolase superfamily protein |
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 | 436 | 760 | 4.6e-23 |
NFGDSNSDTGNLVSSGIETLLSPNGQIYFKNPSGRYSDGRLIVDFLMNAMELPFLNAYLDSVGLPSFKKGCNFAAAGSTILPATATSICPFSFGIQVNQF LRFKARVLELLAKGKNFSKYLPTEDFFSKGLYMFDIGQNDLAGAFYSKTLDQILASIPTILAEFETGIKKLYDQGGRNFWIHNTAPLGCLTQNVAKFGTN PSRLDERGCVSSHNEAAKLFNLQLHALTKKLQGQYTDANVVYVDIFSIKYELISNYSRYGFEQAIMACCGYGGPPLNYDSQITCGQTKTLNGTSVTAKGC SDSTDYVSWDGIHYTEAANQFVSSK |
Full Sequence |
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Protein Sequence Length: 784 Download |
MSSMTICARF RPLSSKERRD HGDTVCIRCI DAETFLFKDE KDEEFTFSFD KVFYEKSEQA 60 QVYEFLAWPI VKGKNIVDYA VDAINGTIIT YGQTGAGKTY SMEQCNRLDY HLHWFISTNM 120 HISVSDPAEA LQSLSSGIAN RAVGETQMNM ASSRSHCIYI FTVHQEVKRD DRLKTGKLIL 180 VDLAGSEKVE KTGAEGKVLE EAKTINKSLS VLGNVINALT CGSPGKVNHI PFRDSKLTRI 240 LQDSLGGNSR TALLCCCSPS PSNALESLST LRFGMSFIAD FMLLQLKREN KGLKERLAAA 300 ERCHAAGKEA GDNNTSSLVH KLPGILSSFV SWVRSLSSIK LLNCESKFYY PAVFNFGDSN 360 SDTGELAGGL GFQLPPPYGQ TYFKTPSGRF SDGRLMTDFL SKLLTFATRI LQILTLISIS 420 LPLAKSIHFD HPAVFNFGDS NSDTGNLVSS GIETLLSPNG QIYFKNPSGR YSDGRLIVDF 480 LMNAMELPFL NAYLDSVGLP SFKKGCNFAA AGSTILPATA TSICPFSFGI QVNQFLRFKA 540 RVLELLAKGK NFSKYLPTED FFSKGLYMFD IGQNDLAGAF YSKTLDQILA SIPTILAEFE 600 TGIKKLYDQG GRNFWIHNTA PLGCLTQNVA KFGTNPSRLD ERGCVSSHNE AAKLFNLQLH 660 ALTKKLQGQY TDANVVYVDI FSIKYELISN YSRYGFEQAI MACCGYGGPP LNYDSQITCG 720 QTKTLNGTSV TAKGCSDSTD YVSWDGIHYT EAANQFVSSK ILTGKYSDPP FSDKMPFLLK 780 LKF* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01837 | SGNH_plant_lipase_like | 3.0e-17 | 351 | 404 | 56 | + 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. | ||
cd01369 | KISc_KHC_KIF5 | 6.0e-25 | 1 | 103 | 103 | + Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward. | ||
cd01369 | KISc_KHC_KIF5 | 5.0e-83 | 122 | 275 | 154 | + Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward. | ||
cd00106 | KISc | 8.0e-86 | 3 | 274 | 334 | + Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward. | ||
cd01837 | SGNH_plant_lipase_like | 3.0e-107 | 432 | 764 | 340 | + 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:0003777 | microtubule motor activity |
GO:0005524 | ATP binding |
GO:0006629 | lipid metabolic process |
GO:0007018 | microtubule-based movement |
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 | ABD32376.1 | 0 | 421 | 783 | 17 | 380 | Lipolytic enzyme, G-D-S-L [Medicago truncatula] |
RefSeq | XP_002319029.1 | 4e-17 | 348 | 400 | 26 | 78 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002319029.1 | 0 | 408 | 783 | 5 | 380 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002328416.1 | 0.00000000007 | 348 | 400 | 26 | 78 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002328416.1 | 0 | 410 | 783 | 7 | 380 | predicted protein [Populus trichocarpa] |
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 | 2p4n_K | 0 | 3 | 274 | 8 | 319 | A Chain A, Lip5(mit)2 |
PDB | 1bg2_A | 0 | 3 | 274 | 8 | 319 | A Chain A, Human Ubiquitous Kinesin Motor Domain |
PDB | 1mkj_A | 0 | 3 | 274 | 8 | 319 | A Chain A, Human Kinesin Motor Domain With Docked Neck Linker |
PDB | 4atx_C | 0 | 3 | 274 | 8 | 319 | C Chain C, Rigor Kinesin Motor Domain With An Ordered Neck-Linker, Docked On Tubulin Dimer, Modelled Into The 8a Cryo-Em Map Of Doublecortin-Microtubules Decorated With Kinesin |
PDB | 2y65_D | 0 | 3 | 274 | 12 | 327 | W Chain W, Crystal Structure Of Drosophila Melanogaster Kinesin-1 Motor Domain Dimer-Tail Complex |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HE645682 | 335 | 424 | 755 | 0 |
DW488858 | 302 | 470 | 771 | 0 |
DT521718 | 276 | 509 | 784 | 0 |
GR716280 | 283 | 481 | 763 | 0 |
HE645682 | 53 | 348 | 400 | 0.0000000003 |
Sequence Alignments (This image is cropped. Click for full image.) |
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