Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10022542m |
Family | CBM57 |
Protein Properties | Length: 1087 Molecular Weight: 123282 Isoelectric Point: 6.6366 |
Chromosome | Chromosome/Scaffold: 4 Start: 674169 End: 679962 |
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 | 80 | 224 | 7.2e-26 |
MFINAGGDDDAKVLDSELNILKDAYFEGGDVMRTEESIVEAGDFPFLYQSARVGNFCYRLNNLVPGEYLIDFHFAEIINTNGPKGIRVFNVYVQDEKVLA EFDIFSVVGANRPLLLVDLRVMVMDDGLIRVKFEGINGSPVVCGI |
Full Sequence |
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Protein Sequence Length: 1087 Download |
MEDVQIDATV PVDPGAITKI CSPEIPYSQF VNDATENLEI GDTSVDDCED SLGDSMVCDP 60 NSRLVPTGFT RPNSTDETIM FINAGGDDDA KVLDSELNIL KDAYFEGGDV MRTEESIVEA 120 GDFPFLYQSA RVGNFCYRLN NLVPGEYLID FHFAEIINTN GPKGIRVFNV YVQDEKVLAE 180 FDIFSVVGAN RPLLLVDLRV MVMDDGLIRV KFEGINGSPV VCGICLRKAP KVSVPRTSQD 240 YIKCENCATE IEISPKRKRL MRAKAHEKYE KKIAELSERY EHKTNECHEA WMSLTSANEQ 300 LEKVLMELDN KMYEARSLDQ TVVTQADCLK SITSKYEIDK RHWATALDAL QEKIEIMKRE 360 QSQLSHEAHE CVEGIPELYK MVDGVQALVS QCEDLKQKYS EEQAKRKELY NHIQETKGNI 420 RVFCRCRPLN KDETSTKSAT IVDFDGAKDG ELGIITGNNS KKSFKFDRVY TPKDGQVDVF 480 ADASPMVVSV LDGYNVCIFA YGQTGTGKTF TMEGTPQNRG VNYRTVEQLF EVARERRETI 540 TYNISVSVLE VYNEQIRDLL ATSPASKKLE IKQSSDGSHQ VPGLIEANVE NINEVWNVLQ 600 AGSNARAVGS NNVNEHSSRS HCMLSIMVKA KNLMNGDCTK SKLWLVDLAG SERLAKTDVQ 660 GERLKEAQNI NRSLSALGDV IYALATKSSH IPYRNSKLTH LLQDSLGGDS KTLMFVQISP 720 SEHDVSETLS SLNFATRVRG VELGPARRQL DTGELQKMKA MVEKARQESR SKDESIKKLE 780 ENIQSLEGKN KGRDHSYRSL QEKNKELETQ LDLLNSQSEK QNAQLQERLK SRDDICSNLQ 840 QKVKELEYKL RERHQSDSAA YHQKAKDLEN KLKESEGNSL VWQQKVKYFE NKLKESEGNS 900 LVWQQKIKEL EIKHKAEQSQ EAVLLRQKIK ELEMRLKEQE QHIQQMATTR EFPDVANATP 960 NEVRTCFKDD NFEKENMESN NNILRTSNRL KNKRPDSLNL NEMTRKKRAS RSGETENNGD 1020 DPHMKEKRIR KSDPPKVLLS RVVRPTRPVS GSSNPVPVAH KRVIKREQQD VPVGKERDPK 1080 KKIWSR* |
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-107 | 419 | 737 | 324 | + 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-123 | 419 | 739 | 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 | 4.0e-137 | 419 | 747 | 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-139 | 425 | 741 | 326 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 0 | 417 | 744 | 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 |
GenBank | AAD15569.1 | 0 | 1 | 1086 | 1 | 1068 | putative kinesin heavy chain [Arabidopsis thaliana] |
EMBL | CBI40845.1 | 0 | 97 | 1086 | 1 | 979 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_179846.2 | 0 | 1 | 1086 | 1 | 1093 | kinesin motor protein-related [Arabidopsis thaliana] |
RefSeq | XP_002266404.1 | 0 | 1 | 834 | 1 | 840 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0.00000001 | 841 | 1086 | 759 | 982 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 416 | 743 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 406 | 774 | 1 | 367 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 414 | 781 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 414 | 781 | 1 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 414 | 781 | 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 |
DV990845 | 302 | 473 | 770 | 0 |
EL442930 | 266 | 505 | 768 | 0 |
ES865056 | 289 | 485 | 768 | 0 |
FL921658 | 258 | 509 | 766 | 0 |
EH194227 | 312 | 552 | 860 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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