NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|578816480|ref|XP_006716827|]
View 

kinesin-like protein KIF24 isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Motor_domain super family cl22853
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 47-86 1.58e-17

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


The actual alignment was detected with superfamily member cd01367:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 328  Bit Score: 84.65  E-value: 1.58e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 578816480  47 KVLKDSFIGN-AKTCMIANISPSHVATEHTLNTLRYADRVK 86
Cdd:cd01367  288 QVLKDSFIGEnSKTCMIATISPGASSCEHTLNTLRYADRVK 328
 
Name Accession Description Interval E-value
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 47-86 1.58e-17

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. 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 in the middle (M-type) of the protein chain. M-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 (KIF2 may be slower). 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.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 84.65  E-value: 1.58e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 578816480  47 KVLKDSFIGN-AKTCMIANISPSHVATEHTLNTLRYADRVK 86
Cdd:cd01367  288 QVLKDSFIGEnSKTCMIATISPGASSCEHTLNTLRYADRVK 328
Kinesin pfam00225
Kinesin motor domain;
48-87 7.52e-15

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 76.84  E-value: 7.52e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 578816480   48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKE 87
Cdd:pfam00225 286 LLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKN 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 48-89 6.09e-14

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 74.15  E-value: 6.09e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 578816480    48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELK 89
Cdd:smart00129 288 LLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIK 329
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
48-101 2.58e-07

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 54.36  E-value: 2.58e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578816480  48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELK-KGIKCCTSVTSR 101
Cdd:COG5059  296 LLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKnKIQVNSSSDSSR 350
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 48-89 2.80e-03

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 41.46  E-value: 2.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 578816480   48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELK 89
Cdd:PLN03188  394 LLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
 
Name Accession Description Interval E-value
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 47-86 1.58e-17

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. 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 in the middle (M-type) of the protein chain. M-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 (KIF2 may be slower). 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.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 84.65  E-value: 1.58e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 578816480  47 KVLKDSFIGN-AKTCMIANISPSHVATEHTLNTLRYADRVK 86
Cdd:cd01367  288 QVLKDSFIGEnSKTCMIATISPGASSCEHTLNTLRYADRVK 328
Kinesin pfam00225
Kinesin motor domain;
48-87 7.52e-15

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 76.84  E-value: 7.52e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 578816480   48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKE 87
Cdd:pfam00225 286 LLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKN 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 48-89 6.09e-14

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 74.15  E-value: 6.09e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 578816480    48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELK 89
Cdd:smart00129 288 LLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIK 329
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 47-88 4.29e-12

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. 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.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 68.52  E-value: 4.29e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 578816480  47 KVLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKEL 88
Cdd:cd01370  304 RLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 48-86 3.91e-11

Kinesin motor domain; 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.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 65.35  E-value: 3.91e-11
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 578816480  48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVK 86
Cdd:cd00106  288 LLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 49-89 1.78e-10

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed 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 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. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 63.53  E-value: 1.78e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 578816480  49 LKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELK 89
Cdd:cd01365  315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIV 355
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 47-89 3.85e-09

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation 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.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 59.27  E-value: 3.85e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 578816480  47 KVLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELK 89
Cdd:cd01372  299 RLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 47-86 8.46e-09

Kinesin motor domain, kinesins II or KIF3_like proteins; 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.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 58.24  E-value: 8.46e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 578816480  47 KVLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVK 86
Cdd:cd01371  293 RLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAK 332
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
48-101 2.58e-07

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 54.36  E-value: 2.58e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578816480  48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELK-KGIKCCTSVTSR 101
Cdd:COG5059  296 LLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKnKIQVNSSSDSSR 350
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 48-89 6.15e-07

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; 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.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 52.60  E-value: 6.15e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 578816480  48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELK 89
Cdd:cd01366  287 LLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCE 328
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 48-89 3.47e-06

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. 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.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 50.20  E-value: 3.47e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 578816480  48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELK 89
Cdd:cd01373  297 LLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIK 338
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 47-88 1.66e-05

Kinesin motor domain, CENP-E/KIP2-like subgroup; 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.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 47.71  E-value: 1.66e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 578816480  47 KVLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKEL 88
Cdd:cd01374  280 RILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 31-86 2.47e-05

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; 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.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 47.32  E-value: 2.47e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578816480  31 MQKKQHWIYLEVTMgVKVLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVK 86
Cdd:cd01369  269 DGKKTHIPYRDSKL-TRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAK 323
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 48-89 2.80e-03

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 41.46  E-value: 2.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 578816480   48 VLKDSFIGNAKTCMIANISPSHVATEHTLNTLRYADRVKELK 89
Cdd:PLN03188  394 LLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIK 435
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH