Basic Information | |
---|---|
Species | Populus trichocarpa |
Cazyme ID | Potri.011G140000.1 |
Family | CBM57 |
Protein Properties | Length: 1193 Molecular Weight: 132902 Isoelectric Point: 7.0099 |
Chromosome | Chromosome/Scaffold: 11 Start: 16220775 End: 16226905 |
Description | Di-glucose binding protein with Kinesin motor domain |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
CBM57 | 192 | 334 | 5.9e-26 |
INAGCTDRAVVFGGVEFLGDDCFLGGDTVRTDATIGDGQDGGLSLYQTARYGNFSYCFRALEPGNYDVSLHLAEIVFTDGPPGLRVFDVFVQEKKVMSCL DIYAQVGANKPLVVSGLKAFVEGDEGLLIRFEGVMGKPIVCGI |
Full Sequence |
---|
Protein Sequence Length: 1193 Download |
MEDSNSTNEQ PPHWHDPLLL TDVHHQQQHN TSPLSCSSKT GLISSKSQTL AMVDSDSNED 60 MCWQESQSVE SVTMKKLIDR VENDAIDGRS MLGFSLTSPD LVICAGSPDI SRTGYGDSPE 120 LLDGNKCSIE LSLENGIDGS DMKDSIKTPC VKFSSVFQTF NKELSPESSF ELLPQQEKEE 180 KLVKDFVPGV CINAGCTDRA VVFGGVEFLG DDCFLGGDTV RTDATIGDGQ DGGLSLYQTA 240 RYGNFSYCFR ALEPGNYDVS LHLAEIVFTD GPPGLRVFDV FVQEKKVMSC LDIYAQVGAN 300 KPLVVSGLKA FVEGDEGLLI RFEGVMGKPI VCGISVTKDF SANIAEARLL KPIGMSQVAE 360 CDSPKDNGHL EVEGDYQKLL RDHEFQRREL TEMRRAMDEL KRENRLKSRE CQDALKSLQE 420 LQNELMRKSM HVGSLAFAIE GQVKEKGRWF TSLRDLTRKL KIMKMEHIKL SEEALAYKNC 480 VVDMDEIRST ILSKMKQQVD LHEDLKIKFV EGAKERKELY NKVLELKGNI RVFCRCRPLK 540 SEEVAAGALM TIDFESAKDG ELTVMSNGLP KKTFKFDAVF GPQANQADVF EDTAPFASSV 600 LDGYNVCIFA YGQTGTGKTF TMEGTEEDRG VNFRTLEQVF HMIKEREKLF RYDVSVSVLE 660 VYNEQIKDLL VSDSQPGVAA KRLEIRQAGD GLHHVPGLVE AKVHNMSEVW QVLRTGSNAR 720 AVGSTNANEH SSRSHCIHCV MVKGENLLNG ECTKSKLWLV DLAGSERIAK TEVQGERLKE 780 TQNINKSLSA LGDVISALAT KSPHIPFRNS KLTHLLQDSL GGDSKTLMFL QISPNENDLG 840 ETLCSLNFAS RVRGIELGPA KRQMDNAELL RYKQMAEKSK QDLKSKDVQI KKLEDTINGL 900 DLKTKEKDFK YKILQDKVKE LEAQLLVERK LARQHVDTKI AEQQQQQQQD EQIIAPPRPP 960 LANRILGSNK NFDEPVNGAL NKEQINLTLP PMGNTSYKST IPLPSTEGVV KLTDSTEKEN 1020 NPAMADQPRL LKRTGRASIC TTARHVLAAP APRRNSMIPL PSVPSIPSSF PLCQVDMKED 1080 SEGSETNCLP EQTQCDSPKE IRYGSKRIST MLKRSLQKKV NMKSPLQQHM RRGGINVGME 1140 KVRVSIGSRG RTAHRVLLGN GRRTGMRETQ QKQMLGEKER RWNSGTVART PV* 1200 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01371 | KISc_KIF3 | 1.0e-100 | 529 | 855 | 339 | + Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and 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 this group 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 | 4.0e-123 | 529 | 853 | 333 | + 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. | ||
pfam00225 | Kinesin | 1.0e-138 | 535 | 855 | 330 | + Kinesin motor domain. | ||
smart00129 | KISc | 2.0e-140 | 529 | 861 | 340 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
cd01366 | KISc_C_terminal | 6.0e-178 | 527 | 858 | 333 | + 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 - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002270779.1 | 1e-27 | 13 | 245 | 9 | 226 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002270779.1 | 0 | 336 | 1192 | 201 | 1061 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002300478.1 | 0 | 86 | 1173 | 3 | 1083 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317602.1 | 0 | 61 | 1192 | 1 | 1129 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532828.1 | 0 | 58 | 1192 | 17 | 1147 | ATP binding protein, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2h58_A | 0 | 527 | 857 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 516 | 881 | 1 | 360 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 525 | 895 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 525 | 895 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 525 | 895 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
DV990845 | 300 | 585 | 884 | 0 |
DW067034 | 268 | 502 | 769 | 0 |
ES865056 | 288 | 595 | 882 | 0 |
GW337702 | 296 | 716 | 1011 | 0 |
FQ433065 | 267 | 720 | 978 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|