Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna26561.1-v1.0-hybrid |
Family | CBM57 |
Protein Properties | Length: 1017 Molecular Weight: 114894 Isoelectric Point: 7.1311 |
Chromosome | Chromosome/Scaffold: 1 Start: 3783247 End: 3789033 |
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 | 76 | 208 | 8.3e-22 |
MFVNAGGEGLLETSNVGFQVEGDKFFQGGNVIRTDEAIEGSDMPSIYQSARFGNFAYRFENWCPGDYFVDLHFSEIVYTNGPKGMRVFDVFMQEEKATNK ALQVVDVRVSVGEDGVLVIRFEGVNGSPIVSGI |
Full Sequence |
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Protein Sequence Length: 1017 Download |
MAEPHSTTTA SHPPQFYETL TSSSPFSSTD LRRDTEPPKP ADHDGDEPLS SLCIPGSKLV 60 RTGSVLSACS DNEPVMFVNA GGEGLLETSN VGFQVEGDKF FQGGNVIRTD EAIEGSDMPS 120 IYQSARFGNF AYRFENWCPG DYFVDLHFSE IVYTNGPKGM RVFDVFMQEE KATNKALQVV 180 DVRVSVGEDG VLVIRFEGVN GSPIVSGICI KRPRLSASKV NCGNLVCNNC AAEIEISSGQ 240 EKYIRMQFIA KYEKKIEELK TWFQLKTDEC HEAWMSLTTA NKQLQDITME LDNKSYTIHC 300 LGQAREETEA KFRDISGKYE HDKRMWTAVV DKLERGVRLM KQEYYQLYCE VHKCADAVPE 360 LSNMVSAVQA MGNIRVFCRC RPLRKEESPA GHATVVQFDA AKDGELGIIS SGSNKKIFKF 420 DRVYTPEDDQ ADVFADASPM ITSVLDGYNV CIFAYGQTGT GKTFTMEGPE SNRGVNYRTL 480 EQLFIAAEER KEIFTYNISV SVLEVYNEQI RDLLATSSTS KKLEMRQSSE GTHHMPGLIE 540 AKVENIKEVW RILQAGSNAR ATGSNNVNEH SSRSHCILCI MVRAKNMMTG NCTMSKLWLV 600 DLAGSERLAK TEVQGERLKE AQNINRSLSA LGDVISALAA KKSHIPYRNS KLTRLLQDSL 660 GGDAKTLMFV QISPSEQDLN ETLSSLNFAA RVRGVELGPA KKQVDTGEVQ KLRNQNDKLK 720 QELRSKEDAL RKVEENFQNL ENKAKGDYQM CRSQQDKIDE LEKQIALKID LSRRLENQLL 780 QANEKAEAYL DLQRKVKELE HKQKENEHAY PMILHEKVKD LENKLKERTR ELEHHSAVAQ 840 WKVQELEEKL AMKENNKGFQ LLQQKVKELE EKLRWHERER ASLAFSTENS EATPIQTTCL 900 RHETVGDVNP LSQRSFSYIN QMTDHGSALL KVPESLHEIR RKREFQSKGH ENFVQPATLT 960 DGKMFSGEPN RGKSGTHKAL ARITRSIKPG TTQKSYPNIR NDRDQVPSVK SRIWLR* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01369 | KISc_KHC_KIF5 | 7.0e-105 | 371 | 691 | 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-128 | 373 | 693 | 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 | 8.0e-140 | 373 | 701 | 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 | 6.0e-140 | 379 | 695 | 326 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 0 | 371 | 698 | 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 | 372 | 697 | 4 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3cob_C | 0 | 372 | 713 | 5 | 344 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3cob_A | 0 | 372 | 713 | 5 | 344 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3cnz_B | 0 | 372 | 713 | 5 | 344 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3cnz_A | 0 | 372 | 713 | 5 | 344 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
Sequence Alignments (This image is cropped. Click for full image.) |
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