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Conserved domains on  [gi|15227905|ref|NP_179374|]
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Senescence/dehydration-associated protein-like protein [Arabidopsis thaliana]

Protein Classification

senescence-associated domain-containing protein( domain architecture ID 12072735)

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 ...
256-434 1.65e-48

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: 164.34  E-value: 1.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227905   256 KLIATGSGHLIKGILWCGDVTMDRLIWGNGFMKRRLSKAEKESEVHPDTLKRIRRVKRMTKMTESVANSILSGVLKVSGF 335
Cdd:pfam06911   1 SGIVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227905   336 FTSSVANtKVGKKFFSLLPGE--------VILASLDGFNKVCDAVEVAGRNVMSTSSTVTTELVDHKYGGKAAEATNEGL 407
Cdd:pfam06911  81 VGAKLAP-HVKKTGTGKPPESkkgngkpgVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEVTDDLL 159
                         170       180
                  ....*....|....*....|....*..
gi 15227905   408 DAAGYALGTAWVAfkirKAINPKSVLK 434
Cdd:pfam06911 160 GTAGNVGLVAIDA----SGVSRRAVLK 182
 
Name Accession Description Interval E-value
Senescence pfam06911
Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of ...
256-434 1.65e-48

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: 164.34  E-value: 1.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227905   256 KLIATGSGHLIKGILWCGDVTMDRLIWGNGFMKRRLSKAEKESEVHPDTLKRIRRVKRMTKMTESVANSILSGVLKVSGF 335
Cdd:pfam06911   1 SGIVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227905   336 FTSSVANtKVGKKFFSLLPGE--------VILASLDGFNKVCDAVEVAGRNVMSTSSTVTTELVDHKYGGKAAEATNEGL 407
Cdd:pfam06911  81 VGAKLAP-HVKKTGTGKPPESkkgngkpgVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEVTDDLL 159
                         170       180
                  ....*....|....*....|....*..
gi 15227905   408 DAAGYALGTAWVAfkirKAINPKSVLK 434
Cdd:pfam06911 160 GTAGNVGLVAIDA----SGVSRRAVLK 182
 
Name Accession Description Interval E-value
Senescence pfam06911
Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of ...
256-434 1.65e-48

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: 164.34  E-value: 1.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227905   256 KLIATGSGHLIKGILWCGDVTMDRLIWGNGFMKRRLSKAEKESEVHPDTLKRIRRVKRMTKMTESVANSILSGVLKVSGF 335
Cdd:pfam06911   1 SGIVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227905   336 FTSSVANtKVGKKFFSLLPGE--------VILASLDGFNKVCDAVEVAGRNVMSTSSTVTTELVDHKYGGKAAEATNEGL 407
Cdd:pfam06911  81 VGAKLAP-HVKKTGTGKPPESkkgngkpgVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEVTDDLL 159
                         170       180
                  ....*....|....*....|....*..
gi 15227905   408 DAAGYALGTAWVAfkirKAINPKSVLK 434
Cdd:pfam06911 160 GTAGNVGLVAIDA----SGVSRRAVLK 182
 
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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