Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.002G110600.1 |
Family | CBM57 |
Protein Properties | Length: 1049 Molecular Weight: 117853 Isoelectric Point: 8.2171 |
Chromosome | Chromosome/Scaffold: 02 Start: 8165053 End: 8171552 |
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 | 29 | 167 | 5.5e-22 |
IFVNAGGGAIKKEGDINLDIEKDCCFEGGDVIRTDESIINGGDIPSVYQSARFGTNLSYKFNDMPAGEYLVDLHFAEIVYTNGPKGMRVFDVISELDVYS IVGDNKPLQVVDVRVSVGEDGVIFMRFDGVVGSPIVSGI |
Full Sequence |
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Protein Sequence Length: 1049 Download |
MDSMLCVSGS RSIQSGLTNT NNFKERPVIF VNAGGGAIKK EGDINLDIEK DCCFEGGDVI 60 RTDESIINGG DIPSVYQSAR FGTNLSYKFN DMPAGEYLVD LHFAEIVYTN GPKGMRVFDV 120 ISELDVYSIV GDNKPLQVVD VRVSVGEDGV IFMRFDGVVG SPIVSGIYIK QATELPSKAI 180 VSVLYLPYWS VLIGSLTSLR CFLSYKLNAE SSVKQELSLC NNCAAEVKVS SDQNRVMRTN 240 SLARYEKKIE ELKAQCQLKT DECHEAWMSL TAANEELEKI RMELDNRFFR NMQLDQAMQK 300 QKAELRDVSR RYECDKKLWA AAIDDFEKKI KMMKIEHSQL FHDAHACANT IPELNKMIIA 360 VRDIVAQHED LKLKLNEEQA KSKKLYNQAL EAKGNIRVFC RCRPLTKEEM SIGCQTVVDF 420 SAAKDGDLTV ITNGSTKKNF KFDRVYAPKD DQVDVFADAS ALVTSVLDGY NVCIFAYGQT 480 GTGKTFTMEG TKQNRGVNYR TLHQLFKIAQ QRKETVTYDI SVSVLEVYNE QIRDLLATST 540 TTTKRLDIKQ VSDGVQHVPG IVEAKVENIK QAWDVLQAGS NARAVGSNNV NERSSRSHCM 600 LCTMVRAKNL VNDECTMSKL WLVDLAGSER LAKTEVQGER LKEAQNINRS LSALGDVISC 660 LANKSSHIPY RNSKLTHLLQ DSLGGDSKTL MLVQISPSEH DIGETLSSLN FATRVRGVEL 720 GPAKKQIDMG ELQKFKTMLD KAKQELRSKD DAMRKLEEGF QNVEGKAKVK DQLFKNQQEK 780 VNELESQLAS KTELCRQLEK QLLQLSEGKK EKEEICSDFQ QKVNELEKKL KEQEEAASMN 840 LHCKVKELEN RMKERTQEFE LHTKSLQQKL KEAENKLWEK ENSESQSLQH KINVLGEGLR 900 QHEQGDCLPR PPSAEKSEAT PVLSRMENIY DVDPLGQKSL NSTNRTINQE PSLLHGNTSL 960 RELRRKGDIK SRGMENNFLI SASSLEKKRL PSESSKAKHL DSSRASAKIT TSTKSIRGAQ 1020 KTTSNTANRI NKDQGAGARD NKFKVWLR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01372 | KISc_KIF4 | 8.0e-100 | 396 | 716 | 341 | + Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during 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 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 | 3.0e-114 | 395 | 716 | 332 | + 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-130 | 395 | 724 | 337 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
pfam00225 | Kinesin | 9.0e-132 | 401 | 718 | 327 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 9.0e-176 | 393 | 721 | 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 | 831 | 51 | 884 | hypothetical protein [Vitis vinifera] |
EMBL | CBI40845.1 | 0 | 51 | 1048 | 6 | 979 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0 | 1 | 959 | 51 | 963 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002302362.1 | 0 | 1 | 1048 | 1 | 1046 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002527363.1 | 0 | 1 | 1048 | 9 | 1031 | 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 | 392 | 720 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 383 | 745 | 2 | 361 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 391 | 751 | 2 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 391 | 751 | 2 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 391 | 751 | 2 | 359 | 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 |
EL442930 | 266 | 481 | 745 | 0 |
DV990845 | 300 | 449 | 745 | 0 |
FL921658 | 259 | 485 | 743 | 0 |
ES865056 | 287 | 462 | 745 | 0 |
EH194227 | 292 | 528 | 819 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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