Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.001G436200.4 |
Family | CBM57 |
Protein Properties | Length: 1083 Molecular Weight: 120796 Isoelectric Point: 7.9753 |
Chromosome | Chromosome/Scaffold: 01 Start: 46763015 End: 46768360 |
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 | 71 | 213 | 2.8e-26 |
INAGCTGGAVFLGGVEFVEDDCFAGGDTVRTDATIGDGQDGGLSLYQTARYGNFSYCFRGLEPGTYDVSLHLAEIVFTEGPPGLRVFDVFIHEKKVVSCL DIYAQVGANKPLVVSDLKAFVEGDEGLLIRFEGVMGKPIVCGI |
Full Sequence |
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Protein Sequence Length: 1083 Download |
MDKNKCSIEV SLENGIDGSG IKDSSKTPCV KFSPVFQTFN KELSPESSFE LLPQTEKEEK 60 LVKVFVPGVS INAGCTGGAV FLGGVEFVED DCFAGGDTVR TDATIGDGQD GGLSLYQTAR 120 YGNFSYCFRG LEPGTYDVSL HLAEIVFTEG PPGLRVFDVF IHEKKVVSCL DIYAQVGANK 180 PLVVSDLKAF VEGDEGLLIR FEGVMGKPIV CGISVTKDSS AHTGEAQLLK PVEMSQVAEC 240 ESPKEDNGHL QVEGDYEKLL RDYECQRREL TEMRRTMDEL KRENRLKSRE CQDALKSLQE 300 LQNELMRKSM HVGSLAFAIE GQVKEKSRWF TSLRDLTRKL KLMKMEHIKL SEEALAYKNC 360 VADMEDMRFT IVSTMKQQVE LHEDIKIKFV EGAKERKELY NKVLELKGNI RVFCRCRPLK 420 PEEVAAGALV TIDFESAKDG ELTVMSNGLP RKTFKFDAVF GPQANQADVF EDTASFASSI 480 LDGYNVCVFA YGQTGTGKTF TMEGTEEDRG VNFRTLEQVF CMIKEREELF RYDVSVSVLE 540 VYNEQIRDLL VSDSQPGVAA KRLEIRQAGE GLHHVPGLVE ARVHNMSEVW EVLQTGSNAR 600 AIGSTNANEH SSRSHCIHCV MVKGENLLNG ECTKNKLWLV DLAGSERISK TEVQGERLRE 660 TQNINKSLSA LGDVISALAT KSPHIPFRNS KLTHLLQDSL GGDSKTFMFV QISPNENDLG 720 ETLCSLNFAS RVRGIELGPA KRQLDNAELL RYKQMSEKSK QDLKSKDVQI KKMEDTINGL 780 DLKTKEKDLK YMMLQDKVKE LEAQLLVERK LARQHVDTKI AEQQQQQQMK QQQAEHIIAP 840 PRPPLPNRIL GSNWIYNEPA NGALNKQQIN PTQPLAGNTS NKSTIPLPST DGIVKLIDST 900 EKENNPDMAN QPRLPKRTGR ASICTTAGQV LAAPAPRRNS MIPLPSIPSL VQLPSIPSSF 960 LLCQVDMKQD LEGTETNCLH KQTHCDSPKG IRNGSKRLNT MLKRSLQKKA NMKSPMQQHT 1020 RRGGINVGME KVRVSIGSRG RMAHRVLLGN GRRAGMRETH QKQMLGEKER RWNSGTVART 1080 PI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01369 | KISc_KHC_KIF5 | 3.0e-99 | 409 | 735 | 332 | + 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-121 | 409 | 733 | 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-136 | 415 | 735 | 330 | + Kinesin motor domain. | ||
smart00129 | KISc | 5.0e-138 | 409 | 741 | 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 | 5.0e-175 | 407 | 738 | 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 | |
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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 |
RefSeq | XP_002270779.1 | 0.00001 | 7 | 124 | 118 | 226 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002270779.1 | 0 | 215 | 1082 | 201 | 1061 | PREDICTED: similar to kinesin motor protein-related [Vitis vinifera] |
RefSeq | XP_002300478.1 | 0 | 1 | 1063 | 39 | 1083 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317602.1 | 0 | 1 | 1082 | 62 | 1129 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532828.1 | 0 | 7 | 1082 | 82 | 1147 | 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 | 407 | 737 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 396 | 755 | 1 | 354 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 405 | 775 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 405 | 775 | 2 | 368 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 405 | 775 | 2 | 368 | 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 |
DV990845 | 300 | 465 | 764 | 0 |
DW067034 | 268 | 382 | 649 | 0 |
ES865056 | 284 | 479 | 762 | 0 |
GW337702 | 300 | 596 | 895 | 0 |
FQ433065 | 257 | 600 | 852 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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