Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29591.m000139 |
Family | CBM57 |
Protein Properties | Length: 1147 Molecular Weight: 128232 Isoelectric Point: 6.9317 |
Chromosome | Chromosome/Scaffold: 29591 Start: 72883 End: 78394 |
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 | |||
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Family | Start | End | Evalue |
CBM57 | 149 | 294 | 5.1e-31 |
SINVGSTNEGVVLNGVQFLEDTCYTGGDTVKTNATIGDLDREEDGLSLYQTARFGNFSYCIPAMEPGNYVVTLHLAEIVFTDGPPGRRVFDVFIQEKKVV SSLDIYAQVGANKPLVISQLKTCVDGEEGLTIRFQGVIGSPIVCGI |
Full Sequence |
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Protein Sequence Length: 1147 Download |
MADPDPYSSS STSDIPHNDV SWNSNQILES VDTQMLIDPV ANNGIDGRSV LGFSLTSPDL 60 VICAGSCGDS PEFFNRTTKN YSFELSLENG INGTNTKDTQ KIQSVKFSPI CQTFNKQLSP 120 ESSLEELVAE PSRMRNDDNL LKDPLIGVSI NVGSTNEGVV LNGVQFLEDT CYTGGDTVKT 180 NATIGDLDRE EDGLSLYQTA RFGNFSYCIP AMEPGNYVVT LHLAEIVFTD GPPGRRVFDV 240 FIQEKKVVSS LDIYAQVGAN KPLVISQLKT CVDGEEGLTI RFQGVIGSPI VCGISITEDS 300 SARKDEYVVF LFVSAPISCE QEPDGDHQKL ERHVEFQEKE LTEMRRALEE LKRENQLKNR 360 ECQDAWNSLH ELQNELMRKS MHVGSLGKEI SFFCCHQFRQ FLKMVIMRIE HLKISEEALA 420 YKKCLRDMEE MRSTIQSTMK QQVDLHEDLK IKFIEGEKKR KELYNRVLEL KGNIKVFCRC 480 RPLNAEEVAS GDSMAIDFES AKDGELTVIS NGLPRKTFKF DAVFSPEADQ ADVFGDTAPF 540 ATSVLDGYNV CIFAYGQTGT GKTFTMEGSE EARGVNFRTL EEIFRIIKER YKLFRYDIFV 600 SVLEVYNEQI RDLLGSGSQP GVATKRLEIR QAGEGLHHVP GLVEAQVNNI SEAWEVLQTG 660 SNARAIGSTN ANEHSSRSHC IHCVMVKGEN LLNGECTKSK LWLVDLAGSE RVAKTEVQGD 720 RLKETQNINR SLSALGDVIS ALATKSPHIP FRNSKLTHLL QDSLGGDSKT LMFVQISPSE 780 NDLGETVCSL NFASRVRGIE LGPARRQLDN TELQRYKQMA EKSKQDMKSK DIQIKKMEET 840 INGLVLRIKE KDLRNKNLQE KLKELESQLL IERKLARQHV DTKIAEQQQQ QQMKQQQDEQ 900 SSAPPRPPLA NRLLGSNKNF SEAASTATTK EQVNSWQPLV ENNSYRPTLC ILPTDGMVKY 960 IDPTEKENNP GMAEHPRLPK RTGRASICTT AQRIPVAPAP RRTSMIPLPS VPGLAHLPSP 1020 LAPLSLCEID IKEEDTGGSE INCLPEQTHC NSPKGIKHGT RKLSTILRQS LQKKMQLNSP 1080 MQQHLRKRGI NVGMEKVRVS IGSRGRMAHR VLLGNGRRTG IKDTQQNRSH REKERGWNIG 1140 TAGRTAI |
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-98 | 473 | 799 | 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 | 9.0e-121 | 473 | 797 | 333 | + 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 | 5.0e-137 | 473 | 805 | 340 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
pfam00225 | Kinesin | 4.0e-139 | 479 | 799 | 330 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 8.0e-179 | 471 | 802 | 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 | 0.000000000002 | 1 | 205 | 37 | 229 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002270779.1 | 0 | 362 | 1147 | 276 | 1061 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002300478.1 | 0 | 47 | 1128 | 5 | 1083 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317602.1 | 0 | 20 | 1147 | 1 | 1129 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532828.1 | 0 | 1 | 1147 | 1 | 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 | 471 | 801 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 460 | 825 | 1 | 360 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 469 | 825 | 2 | 352 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 469 | 825 | 2 | 352 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 469 | 825 | 2 | 352 | 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 |
DV990845 | 302 | 527 | 828 | 0 |
DW067034 | 268 | 446 | 713 | 0 |
ES865056 | 288 | 539 | 826 | 0 |
DT575110 | 289 | 530 | 817 | 0 |
FG136150 | 231 | 606 | 836 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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