y
Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_99230g0010 |
Family | GT92 |
Protein Properties | Length: 317 Molecular Weight: 37394 Isoelectric Point: 5.8667 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT92 | 168 | 309 | 3.7e-36 |
SSLYGDLNPQRMREWMAYHAKFFGPRLHFVFHDAGGVHPKVREVLEPWIHAGCVTLQDIIEQEQFDGYYHNRFLIVNDFFHRHKFMVNWTFFFDVDEYVY ISLGNTLQSILNDLSSYTQFAIEQYSMSNKLYLRNNLGNDST |
Full Sequence |
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Protein Sequence Length: 317 Download |
MHLEPKDLLV RVNGELVTQF LKLETVLDES VGKTYTMSDI ADRAVMDIYK YINKHLERIS 60 DDPERGTVVE KLVEEIVQDK YHLRRFFSIC EAHRQVGETS LNDSSSISHQ IVRLTIESSI 120 RETRPEVNTL HGDEFGKPKR IVSLKEEDTY NASSYNQAPL YYYFYRGSSL YGDLNPQRMR 180 EWMAYHAKFF GPRLHFVFHD AGGVHPKVRE VLEPWIHAGC VTLQDIIEQE QFDGYYHNRF 240 LIVNDFFHRH KFMVNWTFFF DVDEYVYISL GNTLQSILND LSSYTQFAIE QYSMSNKLYL 300 RNNLGNDSTN DTYSREW 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00106 | KISc | 6.0e-9 | 32 | 123 | 130 | + 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 | 3.0e-12 | 32 | 122 | 126 | + Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division. | ||
pfam01697 | Glyco_transf_92 | 2.0e-12 | 168 | 307 | 147 | + Glycosyltransferase family 92. Members of this family act as galactosyltransferases, belonging to glycosyltransferase family 92. The aligned region contains several conserved cysteine residues and several charged residues that may be catalytic residues. This is supported by the inclusion of this family in the GT-A glycosyl transferase superfamily. | ||
pfam00225 | Kinesin | 2.0e-16 | 32 | 129 | 138 | + Kinesin motor domain. | ||
cd01374 | KISc_CENP_E | 3.0e-25 | 30 | 123 | 128 | + Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation 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. |
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_001758982.1 | 0 | 131 | 317 | 92 | 275 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002263686.1 | 0 | 144 | 305 | 245 | 408 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299381.1 | 0 | 151 | 317 | 115 | 275 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002307008.1 | 0 | 127 | 317 | 196 | 381 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002510749.1 | 0 | 127 | 317 | 188 | 373 | conserved hypothetical protein [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 | 1t5c_B | 0.002 | 32 | 118 | 90 | 212 | A Chain A, Crystal Structure Of The Motor Domain Of Human Kinetochore Protein Cenp-E |
PDB | 1t5c_A | 0.002 | 32 | 118 | 90 | 212 | A Chain A, Crystal Structure Of The Motor Domain Of Human Kinetochore Protein Cenp-E |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
BF609207 | 166 | 134 | 298 | 0 |
GE480447 | 192 | 127 | 317 | 0 |
DT630473 | 147 | 171 | 317 | 0 |
DN633485 | 146 | 172 | 317 | 0 |
BF516971 | 153 | 134 | 285 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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