| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10013714 |
| Family | CBM57 |
| Protein Properties | Length: 1147 Molecular Weight: 126749 Isoelectric Point: 8.437 |
| Chromosome | Chromosome/Scaffold: 1168 Start: 188835 End: 193633 |
| Description | Di-glucose binding protein with Kinesin motor domain |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 169 | 315 | 9.3e-29 |
| SINVGYTDDQTVTKDGLSYMKDSCFLGGDTVRTNAIIGDGLEEDESLCLYQAARMGDFSYCFRSLEPGDYDVALHFAEIVFTNGPPGLRVFDVFLQEKKV VSNLDIFARVGANNPLVISDLKASVGLGEKLSIRLEGVTGTPILSAI | |||
| Full Sequence |
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| Protein Sequence Length: 1147 Download |
| MADPVSSTSP SCPSFSNGKG FLSLSLSLSL HGTFFSRLVK IRSGLASWKC DCVFCLFSPF 60 PGRSLLGFSL SSPDLVICAS SPEMESSICG VSPEIVGSRK KQCMDLSLDN GIAGFESGAR 120 ETSRSVKFSP FCQTFYNKEL SPDSSIELLA HPVKGEKIVG DVPAPGWISI NVGYTDDQTV 180 TKDGLSYMKD SCFLGGDTVR TNAIIGDGLE EDESLCLYQA ARMGDFSYCF RSLEPGDYDV 240 ALHFAEIVFT NGPPGLRVFD VFLQEKKVVS NLDIFARVGA NNPLVISDLK ASVGLGEKLS 300 IRLEGVTGTP ILSAISVAKD DSASTGEASF PEHIKRSRAA KIESQKNADC EMEDDYQKLL 360 TAYECQQREL TEMRKTVEEL NRGNQVKTKE CQNALKSMQD LQSELMRKSM HVGSLAFAVE 420 GQVKEKSRWF SALKDLTEKL EIMKGDQIKL SEEARSYKAC FREMSEIAST IQSTVKQQSG 480 LHGDLMKKYM EGVRERKELY NKVLELKGNI RVFCRCRPLN SEEIAAGAAM AIDFESAKDG 540 ELTVFSNGVP RKTFKFDSIF SPQANQADVF EDTAAFATSV LDGYNVCIFA YGQTGTGKTF 600 TMEGTKEARG VNYKTLNELF HMIKEREKLF KYEVSVSVLE VYNEQIRDLL VSNSQPATVK 660 RLEIRPAGDG LHCVQGLVEA RVNNVNEAWE VLQTGSNARA VGSTSANDHS SRSHCIHCVM 720 VKGENLLNKE CTRSKLWLVD LAGSERVAKT EVQGERLKET QNINRSLSAL GDVIFSLATK 780 SPHIPFRNSK LTHLLQDSLG GDSKALMFVQ ISPNESDLSE TLCSLNFASR VRGIELGPAK 840 RQFDMPELVR YKQLAEKTRQ ELKLKDVQIR KMDDTVQGLE LKVKEKDIKN KHLQEKIKEL 900 ESQLLVERKL ARQHVDTKIA EQHSKQSDDQ TCPPPRPPLG TRLLGNISNK ASSNGSANGA 960 LNKETMDAEN FLPSTDVIFK IADPMEKENN PDMAENLGMQ KRTAGRFSIC PAPRRNSFIP 1020 FPSPSPLPLL PVSLNQDAEK GVCESPKEGK TGTRKRNSVL RRSVHKKLQS RSPMQQQIAR 1080 KGGINVGMEK VRLSIGSRGR MAQRVVLHGS AAAKRVGSKE ITTQQKQVSH KEKERGWNSA 1140 TTTARL* 1200 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd01371 | KISc_KIF3 | 4.0e-96 | 509 | 834 | 339 | + Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. 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 this group 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 | 2.0e-118 | 509 | 832 | 332 | + 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. | ||
| pfam00225 | Kinesin | 1.0e-134 | 515 | 834 | 329 | + Kinesin motor domain. | ||
| smart00129 | KISc | 1.0e-137 | 509 | 840 | 339 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
| cd01366 | KISc_C_terminal | 3.0e-172 | 507 | 837 | 332 | + Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. 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 this subgroup the motor domain is found at the C-terminus (C-type). 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. | ||
| Gene Ontology | |
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| GO Term | Description |
| GO:0003777 | microtubule motor activity |
| GO:0005524 | ATP binding |
| GO:0007018 | microtubule-based movement |
| Annotations - NR Download unfiltered results here | |||||||
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| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | NP_177370.1 | 0 | 62 | 1025 | 72 | 1012 | kinesin motor protein-related [Arabidopsis thaliana] |
| RefSeq | NP_177370.1 | 4e-24 | 979 | 1127 | 1040 | 1191 | kinesin motor protein-related [Arabidopsis thaliana] |
| RefSeq | XP_002300478.1 | 0 | 60 | 1127 | 3 | 1083 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002317602.1 | 0 | 62 | 1142 | 28 | 1124 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532828.1 | 0 | 62 | 1141 | 47 | 1141 | ATP binding 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 | 2h58_A | 0 | 507 | 836 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
| PDB | 3h4s_A | 0 | 496 | 855 | 1 | 355 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_C | 0 | 505 | 861 | 2 | 353 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_A | 0 | 505 | 861 | 2 | 353 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cnz_B | 0 | 505 | 861 | 2 | 353 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| DW067034 | 268 | 482 | 748 | 0 |
| DV990845 | 300 | 565 | 863 | 0 |
| ES865056 | 284 | 579 | 861 | 0 |
| GW337702 | 237 | 695 | 930 | 0 |
| FQ433065 | 222 | 699 | 920 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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