| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01003948001 |
| Family | CBM57 |
| Protein Properties | Length: 980 Molecular Weight: 111240 Isoelectric Point: 8.0533 |
| Chromosome | Chromosome/Scaffold: Start: 13962625 End: 13968360 |
| Description | Di-glucose binding protein with Kinesin motor domain |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 2 | 126 | 2.6e-23 |
| KFLADTFFQGGDVLRTEECITEGGDCPLIYQSARLGNFSYRFENLHPGDYFVDLHFVEIINTDGPKGMRVFNVFVQEEKANFDIFSIVGANKPVQLVDLR VPVKEDGLIVIRFEGVNGSPMVSGI | |||
| Full Sequence |
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| Protein Sequence Length: 980 Download |
| MKFLADTFFQ GGDVLRTEEC ITEGGDCPLI YQSARLGNFS YRFENLHPGD YFVDLHFVEI 60 INTDGPKGMR VFNVFVQEEK ANFDIFSIVG ANKPVQLVDL RVPVKEDGLI VIRFEGVNGS 120 PMVSGICIRK APMLSVPPAS PEYLICNHCS AEIEVSPIQK KLKQTKFTVK YEKKIEELTM 180 QCQRKTDECY EAWMSLTAAN EQLEKVRMEL DNKLFQTYSL DQTVEKQAEK LRHISSKYEH 240 DKKVWVAALN DLDDKIKMMK QEHSQLSREA HECADSIPEL NQMVVAVQAL VAQCEDFKMK 300 YIEEQTKRKK LYNQVQEAKG MFCNIRVFCR CRPFRKEELS AGSATVVDLD GAKDGDLGIL 360 TGGSTRKNFK FDRVYTPKDD QVDVFADASP MVISVLDGYN VCIFAYGQTG TGKTFTMEGT 420 QQNRGVNYRT LEELFKVAEE RSDTFTYSLS VSVLEVYNEQ IRDLLATSPA SKKLEIKQSS 480 EGFHHVPGIV EAKVENIKEV WKVLQAGSNA RAVGSNNVNE HSSRSHCMLC IMVKAKNLMN 540 GDCTKSKLWL VDLAGSERLA KTDVQGERLK EAQNINRSLS ALGDVISALA TKSSHVPYRN 600 SKLTHLLQDS LGGDSKTLMF VQISPSEHDL GETLSSLNFA SRVRGVELGP AKRQIDTGEL 660 QKMKTMLDKA RQESRSKDES LRKLEESLQH LEGKARGKDQ IYKTQQEKIK ELEGQLELKT 720 SLHGQSEKQI SQLSERLKGR EEVCSSLQHK VKDLESKLKE QVKESESHSF ILQQKIKELD 780 RKLKDQEQSS EAASSLQQKV NELERKLREQ EESSEVAALL HLKIKELEEK LREQEQQSEC 840 LTYQDCASVS RVTPIEVKPR VRDEFMSDVE PNILRNSNTM NRPMSQGSTF LRGTDSLSDK 900 RKRREFRSTE MENNTIVSNS SNDNRTRQSD PPKPFARLTK AVKPVGAANR RPFLTHSKTS 960 RDQVQGIKER DTKKRIWSR* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd01369 | KISc_KHC_KIF5 | 1.0e-101 | 323 | 642 | 325 | + 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-122 | 324 | 644 | 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 | 1.0e-135 | 324 | 652 | 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 | 3.0e-138 | 330 | 646 | 326 | + Kinesin motor domain. | ||
| cd01366 | KISc_C_terminal | 0 | 319 | 649 | 333 | + 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 |
| EMBL | CAN63715.1 | 0 | 1 | 963 | 94 | 1063 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI40845.1 | 0 | 1 | 979 | 1 | 979 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_179846.2 | 0 | 6 | 979 | 111 | 1093 | kinesin motor protein-related [Arabidopsis thaliana] |
| RefSeq | XP_002266404.1 | 0 | 1 | 979 | 94 | 982 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002532381.1 | 0 | 1 | 761 | 94 | 853 | ATP binding protein, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2h58_A | 0 | 324 | 648 | 5 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
| PDB | 3h4s_A | 0 | 308 | 700 | 1 | 383 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_C | 0 | 321 | 686 | 3 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cob_A | 0 | 321 | 686 | 3 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 3cnz_B | 0 | 321 | 686 | 3 | 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 |
| EH194227 | 318 | 457 | 774 | 0 |
| FL921658 | 258 | 414 | 671 | 0 |
| DV990845 | 302 | 378 | 675 | 0 |
| EL442930 | 266 | 410 | 673 | 0 |
| ES865056 | 289 | 390 | 673 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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