Basic Information | |
---|---|
Species | Fragaria vesca |
Cazyme ID | mrna20704.1-v1.0-hybrid |
Family | CBM57 |
Protein Properties | Length: 1087 Molecular Weight: 123289 Isoelectric Point: 6.8217 |
Chromosome | Chromosome/Scaffold: 1 Start: 17213306 End: 17219310 |
Description | Di-glucose binding protein with Kinesin motor domain |
View CDS |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
CBM57 | 64 | 200 | 2.3e-26 |
MFVNAGTEDLYESDSGVTFLGDSYFVGGNVLRTNEQIGDGGDYPHIYQSARVGNFSYRFNYLPPGEYYIDIHFTEIINTNGPKGMRVFNVLSDFDIYAIV GANKPLQLVDSRVSVKEDGVVVIRFEGVIGSPLVSGI |
Full Sequence |
---|
Protein Sequence Length: 1087 Download |
MEETQFDPDF QDSEQAQQPN PDLKDSSMDE DDESLVDSML CDSGSRLIPT GFTRPNSTSG 60 EYVMFVNAGT EDLYESDSGV TFLGDSYFVG GNVLRTNEQI GDGGDYPHIY QSARVGNFSY 120 RFNYLPPGEY YIDIHFTEII NTNGPKGMRV FNVLSDFDIY AIVGANKPLQ LVDSRVSVKE 180 DGVVVIRFEG VIGSPLVSGI GIRRPPSDSV TGKIVELLKC NNCDAEIEVS SAQKKLMQKK 240 STAKYEKKIQ ELNTRCELKA KECYEAWMSL TVANEQLDKV RMELDNTAFK TLTQDQAMQK 300 QAEDIRNLSS KYEHDKKYWA AAVNDLQLKI KLMQKEHLHL SREAHACADS IPDLNNMISA 360 VQGLVAECED LKVKYNEEQA KRKKLFNEVQ EAKGNIRVFC RCRPLSKEEI TTGCKAVVDF 420 EAAQDGCLGF VTGASTKKSF KFDRVYTPKD DQADVYVDAS PMVISVLDGY NVCIFAYGQT 480 GTGKTFTMEG TEKNRGVNYR TLEQLFEIAN ERRETFTYNI SVSVLEVYNE QIRDLLDTSP 540 HPSKKLEIKQ APEGSHHVPG IVEAKVESIK EVWSVLQAGS NARAVGSNNV NEHSSRSHCL 600 LCIMVKAKNL INGESTKSKL WLVDLAGSER LAKTDVQGER LKEAQNINRS LSALGDVISA 660 LANKSGHIPY RNSKLTHLLQ DSLGGDSKTL MFVQISPSDK DLGETMSSLN FATRVRGIEL 720 GPVKKQVDTS ELQKTKLMLE RARQEARSKD DSLRKLEENL QNLESKNKGK DQIYKNQQEK 780 IKDLEGKLEL KTALLIQLEK QISQLSDRLR GKEETCSCLK QKELYLMKVE ELEADLRQQQ 840 KSESESANLR QKVKDLQSKL DEQMQESEFI STTLQHKVKE LEIKLKEEEQ KSDPSSLHQK 900 IKELEDKLRE QEKQLTEEKL RVVQEKQLLE EKLREKERQL VEDKLRGQEN QSQCTQVLTE 960 MVRATPHEGK SRIRDEIMND VDPCILRTSN SLNRRMSQGS TLLKGNESVH EKRRKREFKS 1020 GETENFHRLS TSLYDNKSRK SDPPKIARIT RPVKPVTATQ GPLIHKRIIR DQVQVKERDN 1080 KKKIWS* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01372 | KISc_KIF4 | 7.0e-103 | 396 | 719 | 344 | + 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-122 | 395 | 716 | 330 | + 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-137 | 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 | 3.0e-140 | 401 | 718 | 327 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 0 | 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 | |
---|---|
GO Term | Description |
GO:0003777 | microtubule motor activity |
GO:0005524 | ATP binding |
GO:0007018 | microtubule-based movement |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
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 | 382 | 772 | 1 | 383 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 390 | 751 | 1 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 390 | 751 | 1 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 390 | 751 | 1 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
Sequence Alignments (This image is cropped. Click for full image.) |
---|