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Conserved domains on  [gi|212375004|pdb|3EAB|A]
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Chain A, Spastin

Protein Classification

protein kinase family protein( domain architecture ID 10119387)

protein kinase family protein, may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates; may contain an MIT (microtubule interacting and transport) domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
9-88 1.47e-27

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear.


:

Pssm-ID: 239142  Cd Length: 79  Bit Score: 95.04  E-value: 1.47e-27
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EAB_A       9 VRVFHKQAFEYISIALRIDEDekaGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 86
Cdd:cd02679  1 IRGYYKQAFEEISKALRADEW---GDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQ 77

               ..
3EAB_A      87 LL 88
Cdd:cd02679 78 VL 79
 
Name Accession Description Interval E-value
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
9-88 1.47e-27

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear.


Pssm-ID: 239142  Cd Length: 79  Bit Score: 95.04  E-value: 1.47e-27
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EAB_A       9 VRVFHKQAFEYISIALRIDEDekaGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 86
Cdd:cd02679  1 IRGYYKQAFEEISKALRADEW---GDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQ 77

               ..
3EAB_A      87 LL 88
Cdd:cd02679 78 VL 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
9-86 1.93e-13

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 59.24  E-value: 1.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EAB_A          9 VRVFHKQAFEYISIALRIDEdekAGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 86
Cdd:smart00745  1 TRDYLSKAKELISKALKADE---AGNYEEALELYKKAIEYLLEGIKVESdsKRREALKAKAAEYLDRAEEIKKSLLERLA 77
 
Name Accession Description Interval E-value
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
9-88 1.47e-27

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in the AAA protein spastin, a probable ATPase involved in the assembly or function of nuclear protein complexes; spastins might also be involved in microtubule dynamics. The molecular function of the MIT domain is unclear.


Pssm-ID: 239142  Cd Length: 79  Bit Score: 95.04  E-value: 1.47e-27
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EAB_A       9 VRVFHKQAFEYISIALRIDEDekaGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 86
Cdd:cd02679  1 IRGYYKQAFEEISKALRADEW---GDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQ 77

               ..
3EAB_A      87 LL 88
Cdd:cd02679 78 VL 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
9-86 1.93e-13

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 59.24  E-value: 1.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3EAB_A          9 VRVFHKQAFEYISIALRIDEdekAGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 86
Cdd:smart00745  1 TRDYLSKAKELISKALKADE---AGNYEEALELYKKAIEYLLEGIKVESdsKRREALKAKAAEYLDRAEEIKKSLLERLA 77
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
11-86 3.05e-10

MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.


Pssm-ID: 239121  Cd Length: 75  Bit Score: 51.16  E-value: 3.05e-10
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3EAB_A      11 VFHKQAFEYISIALRIDEDekaGQKEQAVEWYKKGIEELEKGIAVIV--TGQGEQCERARRLQAKMMTNLVMAKDRLQ 86
Cdd:cd02656  1 ELLQQAKELIKQAVKEDED---GNYEEALELYKEALDYLLQALKAEKepKLRKLLRKKVKEYLDRAEFLKELLKKQKQ 75
 
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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