Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_000724m |
Family | CBM57 |
Protein Properties | Length: 1061 Molecular Weight: 120049 Isoelectric Point: 7.3316 |
Chromosome | Chromosome/Scaffold: 09466 Start: 12567 End: 18874 |
Description | Di-glucose binding protein with Kinesin motor domain |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 78 | 221 | 2e-28 |
MFVNAGDEASIEADSTIKVLGDTNFEGGNVLRTNELINEAGDYPFIYQSARLGNFCYRFNNLPSGVYLVDLHFAEIINTNGPKGMRVFNVFMQEEKVLTE FDIFAIVGANKPLQLVESRVSVKEDGILVIRFEGIIGSPVVSGI |
Full Sequence |
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Protein Sequence Length: 1061 Download |
MEDSRLDNLY QDPETLFPIS SASKVFEWEN DVKLDEERKD SAIGGDWDDL VDSMICDSNS 60 RLIPSGFARS NCTDEIVMFV NAGDEASIEA DSTIKVLGDT NFEGGNVLRT NELINEAGDY 120 PFIYQSARLG NFCYRFNNLP SGVYLVDLHF AEIINTNGPK GMRVFNVFMQ EEKVLTEFDI 180 FAIVGANKPL QLVESRVSVK EDGILVIRFE GIIGSPVVSG ICIRKARKLS VPCRSQEYLK 240 CNNCAAEIEV SSDQKKLMRT KATDKYEKKI QELITECQRK TNECHEAWMS LTTANEQLEK 300 IRMELDNKTF QTRSLDQTVG KQSENLRNLT SIYERDKKYW AAAVKNLQQE IKIMKEEHCQ 360 LSREAHECAD SIPQLNNMVT GVKALVAQCE DLKAKYSQEQ AKRKELYNQI QEAKGNIRVF 420 CRCRPLSKEE TSAGYTTVVD FEAAKDGELA ILTGGSTRKT FKFDRVYTPK DNQVDVFADA 480 SPLVVSVLDG YNVCIFAYGQ TGTGKTFTME GTEQNRGVNY RTLGQLFETA KERSETFAYS 540 LSVSVLEVYN EQIRDLLATS PTSKKLEIKQ SSEGSHHVPG IVEAKVDNLK EVWNVLQAGS 600 NARSVGSNNV NEHSSRSHCM LCVMVKAKNL MNGECTKSKL WLVDLAGSER LAKTEVQGER 660 LKEAQNINRS LSAIGDVIYA LATKSSHIPY RNSKLTHLLQ DSLGGDSKTL MFVQISPSEQ 720 DLSETLSSLN FATRVRGIEL GPAKKQIDTS ELQRMKLMLD KARQESKAKD ESLRKIEENL 780 QNMENKARSK DHIYKVQQEK IKELEGQLEL KSNLNSQSEK QVLQLSDKLK GREEICNALQ 840 QKVKELENKL RERQQSDSAA FQQKVKELEN KLKEQVQESE FHSLTLQNKV KELERKLMEQ 900 EQSSETLLLQ QKIKELEEKL REQEKQLQWM QNQDISGMIR ATPSAGKIRT RDDEVMSEIE 960 CHVLRSSNSI NHPLSHGSAQ SKGNDSLLHE TRKNRQYRSG EIENIIHRKS DPPRIARVMR 1020 TAKPVTAAVA APGPLTHKRI SRDQGPGIKE RDAKKKIWSR * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01369 | KISc_KHC_KIF5 | 5.0e-102 | 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 | 9.0e-120 | 416 | 736 | 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 | 422 | 738 | 326 | + Kinesin motor domain. | ||
smart00129 | KISc | 9.0e-138 | 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. | ||
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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAN63715.1 | 0 | 1 | 1045 | 1 | 1064 | hypothetical protein [Vitis vinifera] |
EMBL | CBI40845.1 | 0 | 94 | 1060 | 1 | 979 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_179846.2 | 0 | 1 | 1060 | 1 | 1093 | kinesin motor protein-related [Arabidopsis thaliana] |
RefSeq | XP_002266404.1 | 0 | 1 | 834 | 1 | 840 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002532381.1 | 0 | 1 | 1058 | 1 | 1073 | 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 | 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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EH194227 | 312 | 549 | 860 | 0 |
EL442930 | 266 | 502 | 765 | 0 |
FL921658 | 258 | 506 | 763 | 0 |
DV990845 | 302 | 470 | 767 | 0 |
ES865056 | 289 | 482 | 765 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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