Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa014706m |
Family | CBM57 |
Protein Properties | Length: 1064 Molecular Weight: 120095 Isoelectric Point: 6.6658 |
Chromosome | Chromosome/Scaffold: 1 Start: 46075301 End: 46081726 |
Description | Di-glucose binding protein with Kinesin motor domain |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 71 | 207 | 4e-25 |
LFVNAGGEALNENRNIGIQVEPDRFFQGGNVLRTDETIDGSDVPSIYQSARFGNFSYRFENLSPGDYFVDLHFAEIVYTNGPKGMRVFDVLSGIDIYSIV GANKALQLVDVRVSVWEDESISIRFVGVNGSPIVGGI |
Full Sequence |
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Protein Sequence Length: 1064 Download |
MEETQSTNSH HEFPETPIPC SVLGPEKHPK QLDYGDDNDD DDSTLSALCV PGSRLVRTGF 60 VHSTCSDNLV LFVNAGGEAL NENRNIGIQV EPDRFFQGGN VLRTDETIDG SDVPSIYQSA 120 RFGNFSYRFE NLSPGDYFVD LHFAEIVYTN GPKGMRVFDV LSGIDIYSIV GANKALQLVD 180 VRVSVWEDES ISIRFVGVNG SPIVGGICIK RAATLPDSFL LSYNLNEASK VEHGRLVCNN 240 CTAEIEISSA QEKYIRLEYT AKYEKKIEEL GTQCQVKTDE SHEAWMSLTS ANKQLQNVTM 300 QLDNKMYESH CLDQAREETA AKLRDISGKY EHDKRLWTAV ADNLERKVKS IKKEYSQLYS 360 EVHEFTDAIP ELNNMVSAVQ AMVAQSDDLK LKFSEEQAKR KILYNQIQEA KGNIRVFCRC 420 RPLRKEDLLA GQATVVQFDV AKDGELGILT SGSTKKIFRF DRIYTPKDDQ VDVFADASPM 480 IISVLDGYNV CILAYGQTGT GKTFTMEGSD TNRGVNYRTL EQLFKIADER KETFIYNISV 540 SVLEVYNEQI RDLLATSPTS KRLEMRQAPE GVHHIPGIVE AKVEGIKEAW NVLQAGSSAR 600 AVGSNNVNEH SSRSHCILCI MVKAKNLISG ECTMSKLWLV DLAGSERLAK TEVQGERLKE 660 AQNINRSLSA LGDVISALAT KRSHIPYRNS KLTHLLHDSL GGDAKTLMFV QISPSEQDLS 720 ETLSSLNFAT RVRGVELGPA RKQIDMGEVQ KLRQMLDKLK QELRFKDDAL QKLEENFQNL 780 EDKAKEECQL SRSQQERINE LEDHIAVKID LCRRLENQLL KLSEEANGKS ETCLNLQKKV 840 KELEDKLNEQ EHVDSMILQN KVKELENKLK ERTQVYEHHS AIVQGKVQEL EKKLIMEENN 900 KGTQLLQQKV KELEEKLRRN EQGHVISTFS AEKSGATPKE RKTWFRCDTI SDIDPLRLRS 960 LSYSNQMTNQ ESVLLKGTNS LRALRRRREL QSKGNENLMF PATLVDRKML SAESRTEMSG 1020 DQKALARITR SIKPSTSAQK AGPNNKNYKD QVPAVKQSRI WLR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01369 | KISc_KHC_KIF5 | 8.0e-98 | 413 | 731 | 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-119 | 413 | 733 | 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 | 3.0e-131 | 413 | 741 | 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 | 2.0e-131 | 419 | 735 | 326 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 2.0e-173 | 411 | 738 | 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 | CBI40845.1 | 0 | 93 | 871 | 6 | 785 | unnamed protein product [Vitis vinifera] |
EMBL | CBI40845.1 | 0.00000003 | 931 | 1063 | 847 | 979 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0 | 1 | 837 | 1 | 847 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0.0000000000002 | 858 | 1063 | 782 | 982 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002527363.1 | 0 | 37 | 1063 | 2 | 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 | 410 | 737 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 400 | 762 | 1 | 361 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 408 | 775 | 1 | 365 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 408 | 775 | 1 | 365 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 408 | 775 | 1 | 365 | 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 |
FY998134 | 246 | 351 | 596 | 0 |
DV990845 | 300 | 467 | 762 | 0 |
EL442930 | 266 | 499 | 762 | 0 |
FL921658 | 258 | 503 | 760 | 0 |
ES865056 | 289 | 479 | 762 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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