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Conserved domains on  [gi|1796958718|ref|NP_001364405|]
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kinesin-like protein KIF9 isoform 5 [Homo sapiens]

Protein Classification

myosin/kinesin family protein( domain architecture ID 366212)

myosin/kinesin family protein; contains an ATPase-containing motor domain found in myosins and kinesins that provides the driving force in myosin and kinesin mediated processes

Graphical summary

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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 ...
 6-89 1.22e-50

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 cd01375:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 334  Bit Score: 161.98  E-value: 1.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958718   6 KVHAFVRVKPTDDFAHEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLHDASQDLVYETVAKDVVSQALDGY 85
Cdd:cd01375     1 KVQAFVRVRPTDDFAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDWSFKFDGVLHNASQELVYETVAKDVVSSALAGY 80


                  ....
gi 1796958718  86 NGNL 89
Cdd:cd01375    81 NGTI 84
 
Name Accession Description Interval E-value
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 6-89 1.22e-50

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. 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: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 161.98  E-value: 1.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958718   6 KVHAFVRVKPTDDFAHEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLHDASQDLVYETVAKDVVSQALDGY 85
Cdd:cd01375     1 KVQAFVRVRPTDDFAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDWSFKFDGVLHNASQELVYETVAKDVVSSALAGY 80


                  ....
gi 1796958718  86 NGNL 89
Cdd:cd01375    81 NGTI 84
Kinesin pfam00225
Kinesin motor domain;
12-87 7.77e-11

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 56.43  E-value: 7.77e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796958718  12 RVKPTDDFahEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLH-DASQDLVYETVAKDVVSQALDGYNG 87
Cdd:pfam00225   1 RVRPLNER--EKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDpEATQEDVYEETAKPLVESVLEGYNV 75
 
Name Accession Description Interval E-value
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 6-89 1.22e-50

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. 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: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 161.98  E-value: 1.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958718   6 KVHAFVRVKPTDDFAHEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLHDASQDLVYETVAKDVVSQALDGY 85
Cdd:cd01375     1 KVQAFVRVRPTDDFAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDWSFKFDGVLHNASQELVYETVAKDVVSSALAGY 80


                  ....
gi 1796958718  86 NGNL 89
Cdd:cd01375    81 NGTI 84
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 6-87 2.86e-14

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: 65.74  E-value: 2.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958718   6 KVHAFVRVKPT----DDFAHEMIRYgDDKRSIDIHLKKdirrgvvNNQQTDWSFKLDGVLHD-ASQDLVYETVAKDVVSQ 80
Cdd:cd00106     1 NVRVAVRVRPLngreARSAKSVISV-DGGKSVVLDPPK-------NRVAPPKTFAFDAVFDStSTQEEVYEGTAKPLVDS 72


                  ....*..
gi 1796958718  81 ALDGYNG 87
Cdd:cd00106    73 ALEGYNG 79
Kinesin pfam00225
Kinesin motor domain;
12-87 7.77e-11

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 56.43  E-value: 7.77e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796958718  12 RVKPTDDFahEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLH-DASQDLVYETVAKDVVSQALDGYNG 87
Cdd:pfam00225   1 RVRPLNER--EKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDpEATQEDVYEETAKPLVESVLEGYNV 75
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 54-87 2.01e-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: 40.78  E-value: 2.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1796958718  54 SFKLDGVLHDASQDL-VYETVAKDVVSQALDGYNG 87
Cdd:cd01374    40 SFTFDHVFGGDSTNReVYELIAKPVVKSALEGYNG 74
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 10-86 3.89e-04

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: 37.19  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796958718  10 FVRVKP------TDDFAHemIRYGDDKRSIDIHLKKDIRRgvvnnqqtdWSFKLDGVLH-DASQDLVYETVAKDVVSqAL 82
Cdd:cd01366     7 FCRVRPllpseeNEDTSH--ITFPDEDGQTIELTSIGAKQ---------KEFSFDKVFDpEASQEDVFEEVSPLVQS-AL 74


                  ....
gi 1796958718  83 DGYN 86
Cdd:cd01366    75 DGYN 78
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 13-86 2.89e-03

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: 35.01  E-value: 2.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796958718  13 VKPTDDfahEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVL-HDASQDLVYETVAKDVVSQALDGYN 86
Cdd:cd01370    24 VKVMDN---HMLVFDPKDEEDGFFHGGSNNRDRRKRRNKELKYVFDRVFdETSTQEEVYEETTKPLVDGVLNGYN 95
 
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.
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