| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10035954 |
| Family | CBM57 |
| Protein Properties | Length: 1059 Molecular Weight: 119226 Isoelectric Point: 7.379 |
| Chromosome | Chromosome/Scaffold: 76 Start: 423232 End: 428622 |
| 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 | 80 | 223 | 2.2e-27 |
| MIVNSGNESSVETESTLKFVGDSYYEGGTVLRTDEDIADAGDFPFIYKSARFGNFCYRFHGLPSGDYFVDLHFAEIINTNGPKGIRVFDVFIHEDKVLSE FDIFSIVGANKPLQLVDVRVSVKEDGILLLRFEGLSGSPMLSAI | |||
| Full Sequence |
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| Protein Sequence Length: 1059 Download |
| MEDLQFSNRV SETVLSGSSS SCFPPIGNNG DAGYGPTESA FEDADAGKSL VDSMICDSNS 60 RLVLSGFSRS NCSETDGVFM IVNSGNESSV ETESTLKFVG DSYYEGGTVL RTDEDIADAG 120 DFPFIYKSAR FGNFCYRFHG LPSGDYFVDL HFAEIINTNG PKGIRVFDVF IHEDKVLSEF 180 DIFSIVGANK PLQLVDVRVS VKEDGILLLR FEGLSGSPML SAICIRKASE VTATQQQKEF 240 LRCNHCASEM EVSSAQKRLV RTKVTDKYEK RIQDLTALCQ RKTNECHEAW MSLTAANEQL 300 EKVRMELDNK TYQTRSLDQT VGEQADNLRN ITTMYGRDKK SWSQAINNMQ EKIRIMKEEH 360 IRLSRDAHGC IDSIPELNNM VSGVQALVAQ CEELKLKYSE EQAKRKQLYN QIQETKGNIR 420 VFCRCRPLSK EEASTGYATV VDFDAAKDGD LGVLTGGSNK KIFKFDRVYT PRDGQVDVFS 480 DASPMVVSVL DGYNVCIFAY GQTGTGKTFT MEGPEHNRGV NYRTLEQLFT VARERSDTFT 540 YNISVSVLEV YNEQIRDLLT TSTTSKKLEI KQTAEGSHHV PGVVEAKVDN IKDVWSVLQA 600 GSNARAVGSN NVNEHSSRSH CMLCIMVKTK NLMNGECTKS KLWLVDLAGS ERLAKTDAQG 660 ERLKEAQNIN KSLSALGDVI YALATKSSHI PYRNSKLTHL LQDSLGGDSK TLMFVQISPS 720 EHDLSETLSS LNFATRVRGV ELGPPKKQLD TSEIQRLKTL LEKTRQESRS KDESLRKLEE 780 NLQNLENKTR SKDHVYKSQL EKIRELEGQL EQKGNLHGQS EKYVSQLSER LKGREEICNE 840 LQQKVKELES KLKQREQSDS ETFQHKVREM EKKMNEQAQE SESQSFTLQQ KIKELESRLH 900 EQNQNSEAVA LHVKIKELEE KLREHEQKLQ NRRVSNAVDG IRASPTGKNT CAKDDERMTD 960 VEANILKCSN SINRPSDVKG YSTAKAAGDE ARKKRHSRNG ETENCNTQAC FNDYRGRKSD 1020 PPKIARVTSQ ATLTHKRINR ETTRLAIKDR DPKKRTWC* 1080 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd01369 | KISc_KHC_KIF5 | 1.0e-99 | 418 | 736 | 324 | + 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 | 1.0e-113 | 418 | 738 | 329 | + 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. | ||
| smart00129 | KISc | 6.0e-125 | 418 | 746 | 336 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
| pfam00225 | Kinesin | 7.0e-131 | 424 | 740 | 326 | + Kinesin motor domain. | ||
| cd01366 | KISc_C_terminal | 5.0e-177 | 416 | 743 | 330 | + 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 |
| EMBL | CAN63715.1 | 0 | 47 | 899 | 47 | 883 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI40845.1 | 0 | 96 | 901 | 1 | 785 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI40845.1 | 0.00000003 | 955 | 1057 | 863 | 977 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002266404.1 | 0 | 47 | 836 | 47 | 840 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002532381.1 | 0 | 39 | 1058 | 42 | 1074 | 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 | 415 | 742 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
| PDB | 3h4s_A | 0 | 405 | 793 | 1 | 382 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_C | 0 | 413 | 780 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_A | 0 | 413 | 780 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cnz_B | 0 | 413 | 780 | 1 | 368 | 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 |
| EL442930 | 266 | 504 | 767 | 0 |
| EH194227 | 312 | 551 | 862 | 0 |
| DV990845 | 301 | 473 | 769 | 0 |
| ES827277 | 257 | 578 | 833 | 0 |
| FL921658 | 258 | 508 | 765 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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