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Conserved domains on  [gi|25144380|ref|NP_491888|]
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Inheritance of peroxisomes protein 1 [Caenorhabditis elegans]

Protein Classification

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 ...
 260-444 1.01e-46

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: 160.11  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144380   260 NFLIKGGQKIAWGVETTTVRVISRVEDNGEQYRTTLIATDKPMQVSPVIKGSVVYMHKGTKTVAKCTRYLLDKIGDMGVS 339
Cdd:pfam06911   1 SGIVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144380   340 MGKKLADSAQRRFGDGKSGGLVS-GTIEILGGGITGVATVWMSLEDGSRHLCRSIANQTVQNVKLKYGDDASDTTHHALF 418
Cdd:pfam06911  81 VGAKLAPHVKKTGTGKPPESKKGnGKPGVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEVTDDLLG 160

                         170       180
                  ....*....|....*....|....*.
gi 25144380   419 AAGHGTLAAAQLWDLGPRSVAGRMAR 444
Cdd:pfam06911 161 TAGNVGLVAIDASGVSRRAVLKSAAK 186
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 14-90 3.29e-22

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: 90.03  E-value: 3.29e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25144380  14 VDAVFSGAYASIEQGLCYDEVNDWENTLAMYEKGLNLIVEGEKMKN--ARKSEMWKMLQESKSSVQHRINVLKKEGPKQ 90
Cdd:cd02679   1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
Inp1 pfam12634
Inheritance of peroxisomes protein 1; Inp1 is a family of peripheral membrane proteins of ...
 117-237 2.55e-14

Inheritance of peroxisomes protein 1; Inp1 is a family of peripheral membrane proteins of peroxisomes. Inp1p binds Pex25p, Pex30p, and Vps1p, all of which are involved in controlling peroxisome division. The levels of Inp1p vary with the cell cycle, and Inp1 acts as a factor that retains peroxisomes in cells and controls peroxisome division. Inp1p promotes the retention of peroxisomes in mother cells and buds of budding yeast by attaching peroxisomes to as-yet-unidentified cortical structures.


:

Pssm-ID: 432685  Cd Length: 137  Bit Score: 69.62  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144380   117 FGSQEADLIYFLPEG-----------------------VQLFTIDGEKTTAPTAptsLQILRFPQPTdggassdtlAFMQ 173
Cdd:pfam12634   6 FKHPNVKIVSFTPPGsssssssssptssdvdypsgsieTLPWRSKTERTIAVGP---LEIYRIPGSV---------AFLS 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25144380   174 VGPWAYPLMgAKTPVLRNE--FGAYLVanpTPENPNMTVAILL--SSDIERRLIEELHIVLREFTDFK 237
Cdd:pfam12634  74 CGNIVHPIL-PKSQCWCVDdgESKFVL---RIRRPERYWRIEFpvETEEDKEKVEEFKEVLSKILQFE 137
 
Name Accession Description Interval E-value
Senescence pfam06911
Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of ...
 260-444 1.01e-46

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: 160.11  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144380   260 NFLIKGGQKIAWGVETTTVRVISRVEDNGEQYRTTLIATDKPMQVSPVIKGSVVYMHKGTKTVAKCTRYLLDKIGDMGVS 339
Cdd:pfam06911   1 SGIVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144380   340 MGKKLADSAQRRFGDGKSGGLVS-GTIEILGGGITGVATVWMSLEDGSRHLCRSIANQTVQNVKLKYGDDASDTTHHALF 418
Cdd:pfam06911  81 VGAKLAPHVKKTGTGKPPESKKGnGKPGVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEVTDDLLG 160

                         170       180
                  ....*....|....*....|....*.
gi 25144380   419 AAGHGTLAAAQLWDLGPRSVAGRMAR 444
Cdd:pfam06911 161 TAGNVGLVAIDASGVSRRAVLKSAAK 186
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 14-90 3.29e-22

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: 90.03  E-value: 3.29e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25144380  14 VDAVFSGAYASIEQGLCYDEVNDWENTLAMYEKGLNLIVEGEKMKN--ARKSEMWKMLQESKSSVQHRINVLKKEGPKQ 90
Cdd:cd02679   1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
14-81 1.49e-14

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 68.49  E-value: 1.49e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25144380     14 VDAVFSGAYASIEQGLCYDEVNDWENTLAMYEKGLNLIVEGEKMKN---------ARKSEMWKMLQESKSSVQHRIN 81
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESdskrrealkAKAAEYLDRAEEIKKSLLERLA 77
Inp1 pfam12634
Inheritance of peroxisomes protein 1; Inp1 is a family of peripheral membrane proteins of ...
 117-237 2.55e-14

Inheritance of peroxisomes protein 1; Inp1 is a family of peripheral membrane proteins of peroxisomes. Inp1p binds Pex25p, Pex30p, and Vps1p, all of which are involved in controlling peroxisome division. The levels of Inp1p vary with the cell cycle, and Inp1 acts as a factor that retains peroxisomes in cells and controls peroxisome division. Inp1p promotes the retention of peroxisomes in mother cells and buds of budding yeast by attaching peroxisomes to as-yet-unidentified cortical structures.


Pssm-ID: 432685  Cd Length: 137  Bit Score: 69.62  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144380   117 FGSQEADLIYFLPEG-----------------------VQLFTIDGEKTTAPTAptsLQILRFPQPTdggassdtlAFMQ 173
Cdd:pfam12634   6 FKHPNVKIVSFTPPGsssssssssptssdvdypsgsieTLPWRSKTERTIAVGP---LEIYRIPGSV---------AFLS 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25144380   174 VGPWAYPLMgAKTPVLRNE--FGAYLVanpTPENPNMTVAILL--SSDIERRLIEELHIVLREFTDFK 237
Cdd:pfam12634  74 CGNIVHPIL-PKSQCWCVDdgESKFVL---RIRRPERYWRIEFpvETEEDKEKVEEFKEVLSKILQFE 137
 
Name Accession Description Interval E-value
Senescence pfam06911
Senescence domain; This is the AAA ATPase senescence domain (SC) found at the C-terminal of ...
 260-444 1.01e-46

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: 160.11  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144380   260 NFLIKGGQKIAWGVETTTVRVISRVEDNGEQYRTTLIATDKPMQVSPVIKGSVVYMHKGTKTVAKCTRYLLDKIGDMGVS 339
Cdd:pfam06911   1 SGIVKGAGTISRGIVTGSEYTAKGLQSGGELLKSKTKPNEKPMEVSPATKKRVRRAKKFTGMAAKVSAKTVGGVGKVAGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144380   340 MGKKLADSAQRRFGDGKSGGLVS-GTIEILGGGITGVATVWMSLEDGSRHLCRSIANQTVQNVKLKYGDDASDTTHHALF 418
Cdd:pfam06911  81 VGAKLAPHVKKTGTGKPPESKKGnGKPGVLNASLDAFSTVLDGLEAAAKNLLSSTSDATTTVVGHKYGEEAGEVTDDLLG 160

                         170       180
                  ....*....|....*....|....*.
gi 25144380   419 AAGHGTLAAAQLWDLGPRSVAGRMAR 444
Cdd:pfam06911 161 TAGNVGLVAIDASGVSRRAVLKSAAK 186
MIT_spastin cd02679
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 14-90 3.29e-22

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: 90.03  E-value: 3.29e-22
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25144380  14 VDAVFSGAYASIEQGLCYDEVNDWENTLAMYEKGLNLIVEGEKMKN--ARKSEMWKMLQESKSSVQHRINVLKKEGPKQ 90
Cdd:cd02679   1 IRGYYKQAFEEISKALRADEWGDKEQALAHYRKGLRELEEGIAVPVpsAGVGSQWERARRLQQKMKTNLNMVKTRLQVL 79
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
14-81 1.49e-14

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 68.49  E-value: 1.49e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25144380     14 VDAVFSGAYASIEQGLCYDEVNDWENTLAMYEKGLNLIVEGEKMKN---------ARKSEMWKMLQESKSSVQHRIN 81
Cdd:smart00745   1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESdskrrealkAKAAEYLDRAEEIKKSLLERLA 77
Inp1 pfam12634
Inheritance of peroxisomes protein 1; Inp1 is a family of peripheral membrane proteins of ...
 117-237 2.55e-14

Inheritance of peroxisomes protein 1; Inp1 is a family of peripheral membrane proteins of peroxisomes. Inp1p binds Pex25p, Pex30p, and Vps1p, all of which are involved in controlling peroxisome division. The levels of Inp1p vary with the cell cycle, and Inp1 acts as a factor that retains peroxisomes in cells and controls peroxisome division. Inp1p promotes the retention of peroxisomes in mother cells and buds of budding yeast by attaching peroxisomes to as-yet-unidentified cortical structures.


Pssm-ID: 432685  Cd Length: 137  Bit Score: 69.62  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25144380   117 FGSQEADLIYFLPEG-----------------------VQLFTIDGEKTTAPTAptsLQILRFPQPTdggassdtlAFMQ 173
Cdd:pfam12634   6 FKHPNVKIVSFTPPGsssssssssptssdvdypsgsieTLPWRSKTERTIAVGP---LEIYRIPGSV---------AFLS 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25144380   174 VGPWAYPLMgAKTPVLRNE--FGAYLVanpTPENPNMTVAILL--SSDIERRLIEELHIVLREFTDFK 237
Cdd:pfam12634  74 CGNIVHPIL-PKSQCWCVDdgESKFVL---RIRRPERYWRIEFpvETEEDKEKVEEFKEVLSKILQFE 137
 
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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