| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT2G22610.2 |
| Family | CBM57 |
| Protein Properties | Length: 1063 Molecular Weight: 120509 Isoelectric Point: 6.3318 |
| Chromosome | Chromosome/Scaffold: 2 Start: 9599550 End: 9604776 |
| Description | kinesin motor domain containing protein, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 80 | 222 | 2.9e-23 |
| MFINAGGDDSKVLDSELNISRDDYFEGGDVLRTEESIVEAGDFPFIYQSARVGNFCYQLNNLLPGEYLIDFHFAEIINTNGPKGIRVFNVYVQDEKATEF DIFSVVGANRPLLLVDLRVMVMDDGLIRVRFEGINGSPVVCGI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1063 Download |
| MDDVQIDDTF PVDLNGVTSL CSPEIPSFDF VSDETEKLEI GDTSIDDCDD ALGDSMVCDP 60 NSRLVPTGLT RTNRTDETIM FINAGGDDSK VLDSELNISR DDYFEGGDVL RTEESIVEAG 120 DFPFIYQSAR VGNFCYQLNN LLPGEYLIDF HFAEIINTNG PKGIRVFNVY VQDEKATEFD 180 IFSVVGANRP LLLVDLRVMV MDDGLIRVRF EGINGSPVVC GICLRKAPQV SVPRTSQDFI 240 KCENCATEIE ISPTRKRLMR AKAHDKYEKK IAELSERYEH KTNECHEAWM SLTSANEQLE 300 KVMMELNNKI YQARSLDQTV ITQADCLKSI TRKYENDKRH WATAIDSLQE KIEIMKREQS 360 QLSQEAHECV EGIPELYKMV GGVQALVSQC EDLKQKYSEE QAKRKELYNH IQETKGNIRV 420 FCRCRPLNTE ETSTKSATIV DFDGAKDGEL GVITGNNSKK SFKFDRVYTP KDGQVDVFAD 480 ASPMVVSVLD GYNVCIFAYG QTGTGKTFTM EGTPQNRGVN YRTVEQLFEV ARERRETISY 540 NISVSVLEVY NEQIRDLLAT SPGSKKLEIK QSSDGSHHVP GLVEANVENI NEVWNVLQAG 600 SNARSVGSNN VNEHSSRSHC MLSIMVKAKN LMNGDCTKSK LWLVDLAGSE RLAKTDVQGE 660 RLKEAQNINR SLSALGDVIY ALATKSSHIP YRNSKLTHLL QDSLGGDSKT LMFVQISPSE 720 HDVSETLSSL NFATRVRGVE LGPARKQVDT GEIQKLKAMV EKARQESRSK DESIKKMEEN 780 IQNLEGKNKG RDNSYRSLQE KNKDLQNQLD SVHNQSEKQY AQLQERLKSR DEICSNLQQK 840 VKELECKLRE RHQSDSAANN QKVKDYENKL KESEGNSLVW QQKIKELEIK HKDEQSQEAV 900 LLRQKIKELE MRLKEQEKHI QEMATTREFP EVANATPNEV KTCFKEDNFG NENMESNTNI 960 LRTSNRLKTK RHDSLNLNEM TRKKRASRSG ETENNGDDPQ MKEKRIRKSD PPKVFSRVVR 1020 PTRTASGSSS QVPVAQKRVI KREQQEVPVV KERDSKKKIW SR* 1080 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd01369 | KISc_KHC_KIF5 | 9.0e-106 | 417 | 735 | 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 | 4.0e-123 | 417 | 737 | 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 | 4.0e-137 | 417 | 745 | 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 | 6.0e-140 | 423 | 739 | 326 | + Kinesin motor domain. | ||
| cd01366 | KISc_C_terminal | 0 | 415 | 742 | 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 | |
|---|---|
| GO Term | Description |
| GO:0003777 | microtubule motor activity |
| GO:0005524 | ATP binding |
| GO:0007018 | microtubule-based movement |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAD15569.1 | 0 | 1 | 1062 | 1 | 1068 | putative kinesin heavy chain [Arabidopsis thaliana] |
| EMBL | CBI40845.1 | 0 | 101 | 1062 | 6 | 979 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_179846.2 | 0 | 1 | 1062 | 1 | 1093 | kinesin motor protein-related [Arabidopsis thaliana] |
| RefSeq | XP_002266404.1 | 0 | 1 | 851 | 1 | 865 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002266404.1 | 0.000000006 | 828 | 1062 | 773 | 982 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2h58_A | 0 | 414 | 741 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
| PDB | 3h4s_A | 0 | 404 | 785 | 1 | 375 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_C | 0 | 412 | 779 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_A | 0 | 412 | 779 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cnz_B | 0 | 412 | 779 | 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 | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| DV990845 | 302 | 471 | 768 | 0 |
| ES865056 | 289 | 483 | 766 | 0 |
| EH194227 | 312 | 550 | 858 | 0 |
| EL442930 | 266 | 503 | 766 | 0 |
| FL921658 | 258 | 507 | 764 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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