NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568922458|ref|XP_006501383|]
View 

spartin isoform X1 [Mus musculus]

Protein Classification

MIT_spastin and Senescence domain-containing protein( domain architecture ID 11553080)

MIT_spastin and Senescence domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Senescence pfam06911
Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of ...
 431-622 5.70e-66

Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of plant senescence-associated proteins and spartin. In Hemerocallis, petals a genetically based program that leads to senescence and cell death approximately 24 hours after the flower opens, and it is believed that senescence proteins produced around that time have a role in this program. This domain is also present at the C-terminal of Spartin, a protein from higher vertebrates associated with mitochondrial membranes and transportation along microtubules. Spartin functions presynaptically with endocytic adaptor Eps15 to regulate synaptic growth and function. Mutations in human spartin gene cause Troyer syndrome, a hereditary spastic paraplegia. This AAA ATPase domain, similar to other AAA proteins contain an alpha/beta nucleotide-binding domain (NBD) and a smaller four-helix bundle domain (HBD). Uniquely among AAA structures, spastin has two helices (N-terminal alpha1 and C-terminal alpha11) hat embrace the NBD.


:

Pssm-ID: 462037  Cd Length: 186  Bit Score: 215.19  E-value: 5.70e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458  431 ILSGASWVSWGLVKGAEFTGKAIQKGASKLRERIQPEEKPVEVSPAVTRGLYIAKQATGGAAKVSQLLVDGVCTVANCVG 510
Cdd:pfam06911   3 IVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGNVG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458  511 KELAPHVKKHGSKLVPESLKRdkdgksalDGAMVVAASSVQGFSTVWQGLECAAKCIVNNVSAETVQTVRYKYGHNAGEA 590
Cdd:pfam06911  83 AKLAPHVKKTGTGKPPESKKG--------NGKPGVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEV 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568922458  591 THNAVDSAINVGLTAYNIDNIGIKAMVKKTAK 622
Cdd:pfam06911 155 TDDLLGTAGNVGLVAIDASGVSRRAVLKSAAK 186
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 16-95 1.41e-26

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: 103.13  E-value: 1.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458  16 IKEAYEKAFMFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISIaAAEPGHTGPAWEAARQMQQKMKETLQNVRTRLEIL 95
Cdd:cd02679    1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAV-PVPSAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
PRK14954 super family cl33039
DNA polymerase III subunits gamma and tau; Provisional
 109-212 5.63e-03

DNA polymerase III subunits gamma and tau; Provisional


The actual alignment was detected with superfamily member PRK14954:

Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 39.93  E-value: 5.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458 109 DVPKLYPEFPPKDACKKSPEQESvsTAPQRAEVDGSASAACAGPSG-APSALPVPSPSCPAEAPPaysPQAAEGHYTVSY 187
Cdd:PRK14954 389 DVKKKAPEPDLPQPDRHPGPAKP--EAPGARPAELPSPASAPTPEQqPPVARSAPLPPSPQASAP---RNVASGKPGVDL 463

                         90       100
                 ....*....|....*....|....*
gi 568922458 188 GTDSGEFSSvgedFYRNRSQPPPLE 212
Cdd:PRK14954 464 GSWQGKFMN----FTRNGSRKQPVQ 484
 
Name Accession Description Interval E-value
Senescence pfam06911
Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of ...
 431-622 5.70e-66

Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of plant senescence-associated proteins and spartin. In Hemerocallis, petals a genetically based program that leads to senescence and cell death approximately 24 hours after the flower opens, and it is believed that senescence proteins produced around that time have a role in this program. This domain is also present at the C-terminal of Spartin, a protein from higher vertebrates associated with mitochondrial membranes and transportation along microtubules. Spartin functions presynaptically with endocytic adaptor Eps15 to regulate synaptic growth and function. Mutations in human spartin gene cause Troyer syndrome, a hereditary spastic paraplegia. This AAA ATPase domain, similar to other AAA proteins contain an alpha/beta nucleotide-binding domain (NBD) and a smaller four-helix bundle domain (HBD). Uniquely among AAA structures, spastin has two helices (N-terminal alpha1 and C-terminal alpha11) hat embrace the NBD.


Pssm-ID: 462037  Cd Length: 186  Bit Score: 215.19  E-value: 5.70e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458  431 ILSGASWVSWGLVKGAEFTGKAIQKGASKLRERIQPEEKPVEVSPAVTRGLYIAKQATGGAAKVSQLLVDGVCTVANCVG 510
Cdd:pfam06911   3 IVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGNVG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458  511 KELAPHVKKHGSKLVPESLKRdkdgksalDGAMVVAASSVQGFSTVWQGLECAAKCIVNNVSAETVQTVRYKYGHNAGEA 590
Cdd:pfam06911  83 AKLAPHVKKTGTGKPPESKKG--------NGKPGVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEV 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568922458  591 THNAVDSAINVGLTAYNIDNIGIKAMVKKTAK 622
Cdd:pfam06911 155 TDDLLGTAGNVGLVAIDASGVSRRAVLKSAAK 186
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 16-95 1.41e-26

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: 103.13  E-value: 1.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458  16 IKEAYEKAFMFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISIaAAEPGHTGPAWEAARQMQQKMKETLQNVRTRLEIL 95
Cdd:cd02679    1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAV-PVPSAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
16-92 6.95e-16

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 72.73  E-value: 6.95e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568922458    16 IKEAYEKAFMFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISIaAAEPGHTGPAWEAARQMQQKMKETLQNVRTRL 92
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKV-ESDSKRREALKAKAAEYLDRAEEIKKSLLERL 76
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
 109-212 5.63e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 39.93  E-value: 5.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458 109 DVPKLYPEFPPKDACKKSPEQESvsTAPQRAEVDGSASAACAGPSG-APSALPVPSPSCPAEAPPaysPQAAEGHYTVSY 187
Cdd:PRK14954 389 DVKKKAPEPDLPQPDRHPGPAKP--EAPGARPAELPSPASAPTPEQqPPVARSAPLPPSPQASAP---RNVASGKPGVDL 463

                         90       100
                 ....*....|....*....|....*
gi 568922458 188 GTDSGEFSSvgedFYRNRSQPPPLE 212
Cdd:PRK14954 464 GSWQGKFMN----FTRNGSRKQPVQ 484
 
Name Accession Description Interval E-value
Senescence pfam06911
Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of ...
 431-622 5.70e-66

Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of plant senescence-associated proteins and spartin. In Hemerocallis, petals a genetically based program that leads to senescence and cell death approximately 24 hours after the flower opens, and it is believed that senescence proteins produced around that time have a role in this program. This domain is also present at the C-terminal of Spartin, a protein from higher vertebrates associated with mitochondrial membranes and transportation along microtubules. Spartin functions presynaptically with endocytic adaptor Eps15 to regulate synaptic growth and function. Mutations in human spartin gene cause Troyer syndrome, a hereditary spastic paraplegia. This AAA ATPase domain, similar to other AAA proteins contain an alpha/beta nucleotide-binding domain (NBD) and a smaller four-helix bundle domain (HBD). Uniquely among AAA structures, spastin has two helices (N-terminal alpha1 and C-terminal alpha11) hat embrace the NBD.


Pssm-ID: 462037  Cd Length: 186  Bit Score: 215.19  E-value: 5.70e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458  431 ILSGASWVSWGLVKGAEFTGKAIQKGASKLRERIQPEEKPVEVSPAVTRGLYIAKQATGGAAKVSQLLVDGVCTVANCVG 510
Cdd:pfam06911   3 IVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGNVG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458  511 KELAPHVKKHGSKLVPESLKRdkdgksalDGAMVVAASSVQGFSTVWQGLECAAKCIVNNVSAETVQTVRYKYGHNAGEA 590
Cdd:pfam06911  83 AKLAPHVKKTGTGKPPESKKG--------NGKPGVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEV 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568922458  591 THNAVDSAINVGLTAYNIDNIGIKAMVKKTAK 622
Cdd:pfam06911 155 TDDLLGTAGNVGLVAIDASGVSRRAVLKSAAK 186
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 16-95 1.41e-26

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: 103.13  E-value: 1.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458  16 IKEAYEKAFMFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISIaAAEPGHTGPAWEAARQMQQKMKETLQNVRTRLEIL 95
Cdd:cd02679    1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAV-PVPSAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
16-92 6.95e-16

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 72.73  E-value: 6.95e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568922458    16 IKEAYEKAFMFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISIaAAEPGHTGPAWEAARQMQQKMKETLQNVRTRL 92
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKV-ESDSKRREALKAKAAEYLDRAEEIKKSLLERL 76
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 18-97 1.74e-04

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: 40.37  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458  18 EAYEKAFMFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGIsiaAAEPGhtgpawEAARQ-MQQKMKETLqnvrTRLEILE 96
Cdd:cd02656    1 ELLQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQAL---KAEKE------PKLRKlLRKKVKEYL----DRAEFLK 67


                 .
gi 568922458  97 K 97
Cdd:cd02656   68 E 68
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
 109-212 5.63e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 39.93  E-value: 5.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922458 109 DVPKLYPEFPPKDACKKSPEQESvsTAPQRAEVDGSASAACAGPSG-APSALPVPSPSCPAEAPPaysPQAAEGHYTVSY 187
Cdd:PRK14954 389 DVKKKAPEPDLPQPDRHPGPAKP--EAPGARPAELPSPASAPTPEQqPPVARSAPLPPSPQASAP---RNVASGKPGVDL 463

                         90       100
                 ....*....|....*....|....*
gi 568922458 188 GTDSGEFSSvgedFYRNRSQPPPLE 212
Cdd:PRK14954 464 GSWQGKFMN----FTRNGSRKQPVQ 484
 
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