| Basic Information | |
|---|---|
| Species | Citrus clementina |
| Cazyme ID | Ciclev10000365m |
| Family | CE16 |
| Protein Properties | Length: 765 Molecular Weight: 84441.8 Isoelectric Point: 8.5534 |
| Chromosome | Chromosome/Scaffold: 5 Start: 31863796 End: 31870938 |
| 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 | 478 | 742 | 7.4e-21 |
| IGLPSFQKGCNFAAAGSTIHQATPTSVCPFSFDIQVNQFLHFKARVVELLAKGKRLDKYIPAVDYFSKGLYTFDIGQNDLAGAFYSKTIDQVLASIPKIL EEFETGLRRLYDEGARNFWIHNTGPLGCLAQNVAKFGTDLSMLDELGCVSGHNQAAKLFNLQLHALCKKLQGDYTDSNITYVDIYTIKYSLIANYSRYGF EQPIMACCGVGGAPLNYNSGISCGQTKVINGTSVTAKACSDSTEYVNWDGIHYTEAANQYVSTQI | |||
| Full Sequence |
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| Protein Sequence Length: 765 Download |
| MSNITVCARF RPLSSKERSN HGDSVCIHGI DNESFIFKDD KEENFKFGFD RVFYEKSEQA 60 EVFEFLALPI VRDAFNGMNG TVITYGQTGA GKTFSMESGI SNRAVGETQM NMASSRSHCI 120 YIFTVQQELT KEKRVKAGKL LLVDLAGSEK AEKTGAEGKV LEEAKTINKS LSALGNVISA 180 LTCGSPGKAF HIPYRDSKLT RILQDALGGN SRTALLCCCS PSTSNSAESL STLRFGTRYQ 240 NDLKIKINNV WNCFKKFYFF AMSFLNFFLL GFSNDILILL THGRAKHIKA SPHAHCSKES 300 NAKKHGVYEA TKDESMERIL NKLKSENKAL KTRIAAAGKI DAFHKEAGEN GYASIVHKIS 360 DRLSHLVSWI WPFSSIKLLP LLAKMTTKIL IVQILTLCSI ILPKANSLVF KYPAVFNFGD 420 SNSDTGELSA GLGFTLDPVY GRTHFKASSG RFCDGRLIVD FLMDAMKLPF LNAYLDSIGL 480 PSFQKGCNFA AAGSTIHQAT PTSVCPFSFD IQVNQFLHFK ARVVELLAKG KRLDKYIPAV 540 DYFSKGLYTF DIGQNDLAGA FYSKTIDQVL ASIPKILEEF ETGLRRLYDE GARNFWIHNT 600 GPLGCLAQNV AKFGTDLSML DELGCVSGHN QAAKLFNLQL HALCKKLQGD YTDSNITYVD 660 IYTIKYSLIA NYSRYGFEQP IMACCGVGGA PLNYNSGISC GQTKVINGTS VTAKACSDST 720 EYVNWDGIHY TEAANQYVST QILTGKYSDP PFADKMPFLL DLKF* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00225 | Kinesin | 5.0e-25 | 9 | 106 | 101 | + Kinesin motor domain. | ||
| cd01369 | KISc_KHC_KIF5 | 2.0e-30 | 1 | 100 | 100 | + 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. | ||
| pfam00225 | Kinesin | 2.0e-64 | 96 | 238 | 145 | + Kinesin motor domain. | ||
| cd01369 | KISc_KHC_KIF5 | 5.0e-81 | 96 | 241 | 146 | + 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. | ||
| cd01837 | SGNH_plant_lipase_like | 1.0e-105 | 413 | 745 | 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 | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | NP_564668.1 | 0 | 387 | 764 | 4 | 382 | GDSL-motif lipase/hydrolase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002284922.1 | 0 | 385 | 764 | 1 | 380 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002319029.1 | 0 | 385 | 764 | 1 | 380 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002328416.1 | 0 | 385 | 764 | 1 | 380 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002512338.1 | 0 | 385 | 764 | 1 | 380 | Alpha-L-fucosidase 2 precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1goj_A | 0 | 96 | 248 | 187 | 337 | A Chain A, Structure Of A Fast Kinesin: Implications For Atpase Mechanism And Interactions With Microtubu |
| PDB | 1goj_A | 0.0000000000001 | 2 | 96 | 6 | 98 | A Chain A, Structure Of A Fast Kinesin: Implications For Atpase Mechanism And Interactions With Microtubu |
| PDB | 2p4n_K | 0 | 95 | 238 | 182 | 321 | A Chain A, Structure Of A Fast Kinesin: Implications For Atpase Mechanism And Interactions With Microtubu |
| PDB | 2p4n_K | 0.0000000001 | 3 | 97 | 8 | 96 | A Chain A, Structure Of A Fast Kinesin: Implications For Atpase Mechanism And Interactions With Microtubu |
| PDB | 1bg2_A | 0 | 95 | 238 | 182 | 321 | A Chain A, Human Ubiquitous Kinesin Motor Domain |
