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Conserved domains on  [gi|214830187|ref|NP_001135768|]
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spartin [Homo sapiens]

Protein Classification

senescence-associated domain-containing protein( domain architecture ID 11553080)

senescence-associated domain-containing protein similar to Arabidopsis thaliana chloroplastic protein EARLY-RESPONSIVE TO DEHYDRATION 7 that accumulates during dehydration stress and is induced by abscisic acid

Graphical summary

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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 ...
 427-617 5.35e-65

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: 212.49  E-value: 5.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214830187  427 ILSGASWVSWGLVKGAEITGKAIQKGASKLRERIQPEEKPVEVSPAVTKGLYIAKQATGGAAKVSQFLVDGVCTVANCVG 506
Cdd:pfam06911   3 IVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGNVG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214830187  507 KELAPHVKKHGSKLVPESLKKdkdgksplDGAMVVAASSVQGFSTVWQGLECAAKCIVNNVSAETVQTVRYKYGYNAGEA 586
Cdd:pfam06911  83 AKLAPHVKKTGTGKPPESKKG--------NGKPGVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEV 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 214830187  587 THHAVDSAVNVGVTAYNINNIGIKAMVKKTA 617
Cdd:pfam06911 155 TDDLLGTAGNVGLVAIDASGVSRRAVLKSAA 185
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 16-95 1.24e-29

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: 111.99  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214830187  16 IREAYKKAFLFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISISSKeSEHTGPGWESARQMQQKMKETLQNVRTRLEIL 95
Cdd:cd02679    1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVP-SAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
 
Name Accession Description Interval E-value
Senescence pfam06911
Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of ...
 427-617 5.35e-65

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: 212.49  E-value: 5.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214830187  427 ILSGASWVSWGLVKGAEITGKAIQKGASKLRERIQPEEKPVEVSPAVTKGLYIAKQATGGAAKVSQFLVDGVCTVANCVG 506
Cdd:pfam06911   3 IVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGNVG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214830187  507 KELAPHVKKHGSKLVPESLKKdkdgksplDGAMVVAASSVQGFSTVWQGLECAAKCIVNNVSAETVQTVRYKYGYNAGEA 586
Cdd:pfam06911  83 AKLAPHVKKTGTGKPPESKKG--------NGKPGVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEV 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 214830187  587 THHAVDSAVNVGVTAYNINNIGIKAMVKKTA 617
Cdd:pfam06911 155 TDDLLGTAGNVGLVAIDASGVSRRAVLKSAA 185
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 16-95 1.24e-29

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: 111.99  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214830187  16 IREAYKKAFLFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISISSKeSEHTGPGWESARQMQQKMKETLQNVRTRLEIL 95
Cdd:cd02679    1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVP-SAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
16-92 2.65e-18

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 79.66  E-value: 2.65e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 214830187    16 IREAYKKAFLFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISISSkESEHTGPGWESARQMQQKMKETLQNVRTRL 92
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVES-DSKRREALKAKAAEYLDRAEEIKKSLLERL 76
 
Name Accession Description Interval E-value
Senescence pfam06911
Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of ...
 427-617 5.35e-65

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: 212.49  E-value: 5.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214830187  427 ILSGASWVSWGLVKGAEITGKAIQKGASKLRERIQPEEKPVEVSPAVTKGLYIAKQATGGAAKVSQFLVDGVCTVANCVG 506
Cdd:pfam06911   3 IVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGNVG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214830187  507 KELAPHVKKHGSKLVPESLKKdkdgksplDGAMVVAASSVQGFSTVWQGLECAAKCIVNNVSAETVQTVRYKYGYNAGEA 586
Cdd:pfam06911  83 AKLAPHVKKTGTGKPPESKKG--------NGKPGVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEV 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 214830187  587 THHAVDSAVNVGVTAYNINNIGIKAMVKKTA 617
Cdd:pfam06911 155 TDDLLGTAGNVGLVAIDASGVSRRAVLKSAA 185
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 16-95 1.24e-29

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: 111.99  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214830187  16 IREAYKKAFLFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISISSKeSEHTGPGWESARQMQQKMKETLQNVRTRLEIL 95
Cdd:cd02679    1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVP-SAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
16-92 2.65e-18

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 79.66  E-value: 2.65e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 214830187    16 IREAYKKAFLFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGISISSkESEHTGPGWESARQMQQKMKETLQNVRTRL 92
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVES-DSKRREALKAKAAEYLDRAEEIKKSLLERL 76
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 18-104 2.16e-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: 39.98  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 214830187  18 EAYKKAFLFVNKGLNTDELGQKEEAKNYYKQGIGHLLRGIsisskesehTGPGWESARQ-MQQKMKETLqnvrTRLEILE 96
Cdd:cd02656    1 ELLQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQAL---------KAEKEPKLRKlLRKKVKEYL----DRAEFLK 67


                 ....*...
gi 214830187  97 KGLATSLQ 104
Cdd:cd02656   68 ELLKKQKQ 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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