Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.009G228400.1 |
Family | CBM57 |
Protein Properties | Length: 1115 Molecular Weight: 125685 Isoelectric Point: 8.3029 |
Chromosome | Chromosome/Scaffold: 09 Start: 17918158 End: 17924778 |
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 | 126 | 270 | 6.5e-27 |
MFVNAGGGALKNEGASGVDVCGDKFFEGGDVLRTIESINGGGDMPPIYQSARFGNVTYRFNDFPPGDYLVDLHFAEIVNTNGPKGMRVFDVFIQEDKVLS ELDVYSIVGANKPLQVVDIRASVGASREIVVRFESVCGSPIVNGI |
Full Sequence |
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Protein Sequence Length: 1115 Download |
MSYYNISVHK TSVVFIVSYI VKKVKETLSK ILKNTGPPTN SLLFFFLVGL SPMAESQIPK 60 SHLQLSKIQS PNSRPCSLLN CEQDTMNSEF ENENQEDEVD STLCFSGSRL IKSGFETSEF 120 SDTAVMFVNA GGGALKNEGA SGVDVCGDKF FEGGDVLRTI ESINGGGDMP PIYQSARFGN 180 VTYRFNDFPP GDYLVDLHFA EIVNTNGPKG MRVFDVFIQE DKVLSELDVY SIVGANKPLQ 240 VVDIRASVGA SREIVVRFES VCGSPIVNGI CIKRATELAD KVSRLNCDYL VCNNCDAEIE 300 ISSPLKKHMK MKSTVKYEKK IEELKNLCQL KTDECYEAWM SLTTSNEQLE KVRMELDNKF 360 FQNLNLDRAL EQQAAKLKDI STKYQCDKRL WVDSVIELER KIKIIKQEHS LLSNKAHDCA 420 DSIPELNKMI FAVQALVAQC EDLKLRLNEE QAMRKKLHNQ IQEAKGKIRV FCRCRPLRDD 480 EASAGHTTIV DFTAAKDGDI GILTGSSMKK IFKFDRVYTP KDDQVSVFAD ASPVVTSVLD 540 GYNVCIFAYG QTGTGKTFTM EGTGQNRGVN YRTLEQLFKL IEERKEISTF SISVSVLEVY 600 NEQIRDLLAT EPASKRLGIR QASEGFHHVP GIVEAKVENI KEVWNVLQAG NNARAIGSNN 660 VNEHSSRSHC MLCILVKAKN LITGECTKSK LWLVDLAGSE RLAKTEVQGD RLKEAQNINR 720 SLSALGDVIS ALANKSSHIP YRNSKLTHLL QDSLGGDSKT LMFVQISPSE QDLGETLSSL 780 NFASRVRGVE LGPTKKQVDT AELQKLKQML DKAKQELKSK DDALRKSVEN FHNLEDKAKA 840 KGQLCKTQEE KLNELENQLS SKAELCKQLE RQLWQLSERM MEKEEICSNS QLKVVELENK 900 LKEHVQNQTA SLSLQRKVKK LEDILKERTR EFELHSGTLQ QKVKELENKL KMERESGGSQ 960 QKGNELEQKL RQHQEQTMRP GLSYSAEKSQ VTPIETIYGM NPTTRRSLNS NGRRMNEMGS 1020 DLLKGTESLR ELRRKRQIES KGIENNVLLS SAFVEKKVWS ETNKARQIEQ WPCRITRSGK 1080 SVNSVEKSFT GNRINWDQGK EPRESSNKLK MWLR* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd01369 | KISc_KHC_KIF5 | 6.0e-102 | 467 | 785 | 324 | + 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-123 | 467 | 787 | 331 | + 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-133 | 468 | 795 | 335 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
pfam00225 | Kinesin | 1.0e-137 | 473 | 789 | 326 | + Kinesin motor domain. | ||
cd01366 | KISc_C_terminal | 6.0e-178 | 465 | 792 | 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI40845.1 | 0 | 147 | 927 | 5 | 785 | unnamed protein product [Vitis vinifera] |
EMBL | CBI40845.1 | 0.0007 | 986 | 1114 | 847 | 979 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0 | 92 | 885 | 44 | 840 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002266404.1 | 0.000000005 | 911 | 1114 | 772 | 982 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002527363.1 | 0 | 90 | 1114 | 1 | 1031 | 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 | 464 | 791 | 2 | 330 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
PDB | 3h4s_A | 0 | 454 | 816 | 1 | 361 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_C | 0 | 462 | 822 | 1 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cob_A | 0 | 462 | 822 | 1 | 359 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
PDB | 3cnz_B | 0 | 462 | 822 | 1 | 359 | 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 |
ES805371 | 324 | 791 | 1112 | 0 |
FL921658 | 258 | 557 | 814 | 0 |
DV990845 | 302 | 521 | 818 | 0 |
EL442930 | 266 | 553 | 816 | 0 |
EH194227 | 308 | 600 | 907 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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