Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29235.m000232 |
Family | CBM57 |
Protein Properties | Length: 1074 Molecular Weight: 121937 Isoelectric Point: 6.6769 |
Chromosome | Chromosome/Scaffold: 29235 Start: 20689 End: 28078 |
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 | 78 | 220 | 4.4e-30 |
MFINAGSEATIEADLEVKFLGDTNFEGGNVLRTDELINEAGDYQFIYQSARFGSFSYRFDNLPPGSYFVDLHFVEIINTNGPRGLRVFDVFIQEEKVLSE FDIFSVVGANKPLQLVDSRVSVKEDGVILIRFEGIIGSPVVSG |
Full Sequence |
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Protein Sequence Length: 1074 Download |
MEDMQLDNFY QNQETHLPNS SISRVFEWEK DVKFDQEFKD SAVLEDWDSL VDSMLCDSNS 60 RLIPSGFSRS SCTDELVMFI NAGSEATIEA DLEVKFLGDT NFEGGNVLRT DELINEAGDY 120 QFIYQSARFG SFSYRFDNLP PGSYFVDLHF VEIINTNGPR GLRVFDVFIQ EEKVLSEFDI 180 FSVVGANKPL QLVDSRVSVK EDGVILIRFE GIIGSPVVSG LCIRKAPEVS VPCQTQDYLK 240 CNNCATEIEI SSDQKKILRA RATDKYEKRI QELITECQHK SNECHEAWMS LTAANEQLEK 300 VRMELDNKTF QSRSLDQTVG KQAENLRNIT NMYERDKQYW AAAVENLQNK VKMMKEEHSR 360 LSYEAHECAD SIPELSKMVT AVQALVAQCE DLKAKYSEEQ AKRKELYNQI QEAKGNIRVF 420 CRCRPLSKAE SSAGCTTVVD FDAAKDGDLG IITGGSTRKT FKFDRVFTPR DNQVDVFADA 480 SPLVLSVLDG YNVCIFAYGQ TGTGKTFTME GTEQSRGVNY RTLEQLFKIA KERSETFTYS 540 ISVSVLEVYN EQIRDLLATS PTSKKLEIKQ SSEGSHHVPG IVEAKVDNLK EVWNVLQAGS 600 NARAVGSNNV NEHSSRSHCM LCVMVKAKNL MNGECTKSKL WLVDLAGSER LAKTDVQGER 660 LKEAQNINRS LSALGDVIYA LATKSSHIPY RNSKLTHLLQ DSLGGDSKTL MFVQISPTEQ 720 DVSETLSSLN FATRVRGIEF GPAKRQIDTS ELQKMKLLLD KARQECKSKE ESLRKLEENL 780 QNLENKARGK DQVYKNQQEK IKELEGQLEF KSTLHSQLGK QISQLSDRLK GKEDICNGLL 840 QKVKELDNKL RERQQSDSTA FQQKVKELEN KLKEQVQESE SYSFALQHKI KELERKLKEQ 900 ENNSETLLLH QKIKDLEDKL NEQEKQLQCK QLLDPHDFPG SVRATPTEQK TCVRDDGFLS 960 DIESHVLRNS NSMKRPFSQG STLMKENNNN NNNTLHDQTR KKRQSGETEN NFMQASFHDN 1020 RVRKSDPPKI GRVMTSRAAR PASVAQGPLT HKRVIRDQGQ GGFRERDAKK KIWC 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 | 4.0e-104 | 416 | 738 | 328 | + 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 | 2.0e-122 | 416 | 736 | 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-139 | 416 | 744 | 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-141 | 422 | 738 | 326 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 0 | 414 | 741 | 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 - 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 | 413 | 740 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 403 | 779 | 1 | 377 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 411 | 778 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 411 | 778 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 411 | 778 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
Sequence Alignments (This image is cropped. Click for full image.) |
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