Basic Information | |
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Species | Mimulus guttatus |
Cazyme ID | mgv1a000533m |
Family | CBM57 |
Protein Properties | Length: 1092 Molecular Weight: 122304 Isoelectric Point: 6.6167 |
Chromosome | Chromosome/Scaffold: 174 Start: 248069 End: 252634 |
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 | |||
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Family | Start | End | Evalue |
CBM57 | 89 | 234 | 6.8e-30 |
IGINVGSSTSVEFQDSIRFSEDGSFNGGDTIRTENPIIGDDDTKDVRLYQTARFGSFSYHFENLVSGEYLVDLHFSEIVFTDGPSGMRIFDVFLQDDKVV SCLDIYAQVGAHVPLVISDLKTCVNGDEGLSVRFEGVIGSPIVSGI |
Full Sequence |
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Protein Sequence Length: 1092 Download |
MLGFSLTSPD LVCMGSPDIT NQRYEESPNF FTGGRIDVSL ENGIEGSETI DPFKDPSANM 60 EDLCTEASFE LVAPPLVEEN LTKDSTTVIG INVGSSTSVE FQDSIRFSED GSFNGGDTIR 120 TENPIIGDDD TKDVRLYQTA RFGSFSYHFE NLVSGEYLVD LHFSEIVFTD GPSGMRIFDV 180 FLQDDKVVSC LDIYAQVGAH VPLVISDLKT CVNGDEGLSV RFEGVIGSPI VSGIFIRKDS 240 SASSEEVRLS EQVGFTCIPQ CDSLNDDENG SFNDNEFHRL RTEHAIQKEE LSKTKRILEG 300 IKREYEEKSR ECHEAWKSLK DLQNELMRKS MHVGSLAFAI EGQVKEKTRW FSSLRDLTRK 360 LKILKMEHIS LTEEAAVLKH YVGEMEGVQS IVQSTMNQQV ELHEDIKNKY LQEVKQRKEL 420 YNKVLELKGN IRVFCRCRPL NTEEINGGVS VAVDFEASKD GELTILSNGI SKKTFKFDAV 480 FSPENNQCDV FEETAPLAIS VLDGFNVCVF AYGQTGTGKT FTMEGTNEAR GVNYRTLEKL 540 FDIIEERKNT HRYEVSVSVL EVYNEQIKDL LVSDSQPGLN AKRLEIKQVG EGGHHVPGLV 600 EANVNNVREV WEVLRTGSNG RAVGSTNANE HSSRSHCMHC VMVKGENLLN GECTRSKLWL 660 VDLAGSERIA KTEVQGERLK ETQNINRSLS ALGDVISALA NRSPHIPFRN SKLTHLLQDS 720 LGGDSKTLMF VQISPNENDL TETICSLNFA SRVRGIELGP AKKQMDKTEL VKYKQMVEKL 780 RQEMKSKDSH VRKLEDTNYG LEVKIKDRDS KNRSLQEKIK ELESQLLVER KLARQHVDSR 840 ILAEMKQHQE EQVNSESTRP PLAPTKILGV HKSQSETKPQ PSNNIPRLSA ENDDFSFFPL 900 SMDENPKMDK ENNPEIAEQL LKPPKQTGRA SLCPIVPRVS APRRNSLIPL PSLHGQAKLA 960 PSFLPLTPIQ ADKSEEGGET CLPLQVHSPK DQKNRGKRLG SALRRSLQKK IYVKTPMQPP 1020 VRRIGVNVGM DKLRVSIGSR GRIGQRVFLG NARRGVATRD ANNSNNNTQL KQNHRDKERG 1080 WNTGTVTRNL L* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01371 | KISc_KIF3 | 2.0e-99 | 430 | 756 | 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 | 3.0e-116 | 430 | 754 | 335 | + 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 | 5.0e-137 | 436 | 756 | 330 | + Kinesin motor domain. | ||
smart00129 | KISc | 2.0e-137 | 430 | 762 | 340 | + 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 | 8.0e-177 | 428 | 759 | 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 | |
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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 | XP_002270779.1 | 0.0000000000005 | 1 | 156 | 76 | 240 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002270779.1 | 0 | 312 | 1088 | 276 | 1058 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002300478.1 | 0 | 1 | 1055 | 8 | 1074 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317602.1 | 0 | 1 | 1088 | 31 | 1126 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532828.1 | 0 | 1 | 1091 | 50 | 1147 | 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 | 428 | 758 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 417 | 787 | 1 | 365 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 426 | 796 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 426 | 796 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 426 | 796 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GR071387 | 235 | 618 | 852 | 0 |
DV990845 | 302 | 484 | 785 | 0 |
ES865056 | 288 | 496 | 783 | 0 |
DW067034 | 268 | 403 | 670 | 0 |
FG136150 | 246 | 563 | 808 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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