Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.002G032500.1 |
Family | CBM57 |
Protein Properties | Length: 1174 Molecular Weight: 131020 Isoelectric Point: 7.547 |
Chromosome | Chromosome/Scaffold: 02 Start: 2427626 End: 2433929 |
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 | 184 | 325 | 4.2e-24 |
SINAGCLNGAVELDGVIYSNDDCFVGGDVIIADRIVGDGGGNSLYNTARLGDFSYNFLTLECGFYAIDLHFAEIVFTTGPPGIRVFDVFVQEEKVVTSLD IYGQVGANKPLVISNIRTFVDSGGGLLIRFEGLMGSPIVCGI |
Full Sequence |
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Protein Sequence Length: 1174 Download |
MEDSNNFHHL RTDPLLLTDV SWQQNTSFYT DAAMASHSEN PSLSDLVSSP KQDSADVVDP 60 RQSQSPNVIS TPIREFDGRS MLGFSLTSPD LVICAGSPDI PSKAYGDSPE FLEKHRCSIE 120 VSLENGIEGS DNSKAKQKSP TVKFSTVCET FHKELSPESS FELLPLRETA DYSQHKHEDY 180 PAISINAGCL NGAVELDGVI YSNDDCFVGG DVIIADRIVG DGGGNSLYNT ARLGDFSYNF 240 LTLECGFYAI DLHFAEIVFT TGPPGIRVFD VFVQEEKVVT SLDIYGQVGA NKPLVISNIR 300 TFVDSGGGLL IRFEGLMGSP IVCGITVRKD SLESFKEAGS EEIMGMDKVG GHESPRDISD 360 CEIEVKYQIL QMDYERQKKE LAEMRSALEG LKRENKLKTK ECQEACKSLQ ELQNELMRKS 420 MHVGSLAFAI EGQVKEKSRW FSSLRDMTRK LKIMKMERIK LSEEVSHYKN CIMDINDFGT 480 KIQSRINQQA DLHEDLKTKY LKGAKERKEL YNKVLELKGN IRVFCRCRPL NSEEIAAGAS 540 LAIDFESAKD GELTVISNGA PKKTFRFDAV FGPHAEQADV FQDTAPFATS VLDGYNVCIF 600 AYGQTGTGKT FTMEGTKEAR GVNFRTLEEL FRVINERQKL YRYEISVSAL EVYNEQIRDL 660 LVSGSQQSTM AKRLEIRQVG EGMHHVPGLV EAHVNNMNEV WEVLQTGSNA RAVGSTNANE 720 HSSRSHCIHC VMVKGENLLN GECTKSKLWL VDLAGSERVA KTDVLGERLK ETQNINRSLS 780 ALGDVISALA TKSSHIPFRN SKLTHLLQDS LGGDSKALMF VQISPNENDL GETLCSLNFA 840 SRVRGIELGP AKKQMDTSEL LRWKQMVEKS KQDMKIKDLQ IRKMEETIHG LDLKMKDKDL 900 KNKNLQEKVK ELESQLLIER KLARQHVDTR IAEQQQKQQN EDVRPPLATR LLGTNKSSNE 960 VKNGTLMKEQ VNLTRPLTEN SFRPSMPLSV TDGSFKHIDP VEKENNPEVA EQLRLPTRTG 1020 RASMCPTIRR MPASSAPRRN SLIPLPSTPS SAQLAPPFHP LPSQPDIIEE VDEFIPEQTV 1080 CNSPKGTKSG GKKLSSILRR SLQKKVQLKS PMQQHLRRGL NVGMERVRVS IGSRGRMASR 1140 VLVGNGRKGG KEIQQKQNQK EKERAWNIGR TAI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01371 | KISc_KIF3 | 1.0e-97 | 520 | 846 | 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-121 | 520 | 844 | 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 | 2.0e-139 | 526 | 846 | 330 | + Kinesin motor domain. | ||
smart00129 | KISc | 1.0e-140 | 520 | 852 | 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 | 1.0e-177 | 518 | 849 | 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 | NP_177370.1 | 0 | 13 | 1157 | 6 | 1191 | kinesin motor protein-related [Arabidopsis thaliana] |
RefSeq | XP_002300478.1 | 0 | 76 | 1157 | 3 | 1083 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317602.1 | 0 | 76 | 1172 | 26 | 1125 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002532828.1 | 0 | 76 | 331 | 45 | 300 | ATP binding protein, putative [Ricinus communis] |
RefSeq | XP_002532828.1 | 0 | 402 | 1173 | 362 | 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 | 518 | 848 | 3 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 507 | 872 | 1 | 360 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 516 | 872 | 2 | 352 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 516 | 872 | 2 | 352 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 516 | 872 | 2 | 352 | 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 | 299 | 577 | 875 | 0 |
ES865056 | 288 | 586 | 873 | 0 |
DW067034 | 268 | 493 | 760 | 0 |
GW337702 | 295 | 707 | 996 | 0 |
FG136150 | 231 | 653 | 883 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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