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Conserved domains on  [gi|491227401|ref|NP_001264984|]
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sacsin isoform 2 [Homo sapiens]

Protein Classification

DnaJ and HEPN domain-containing protein( domain architecture ID 10245166)

DnaJ and HEPN domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HEPN smart00748
Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;
4304-4420 5.08e-22

Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;


:

Pssm-ID: 214800  Cd Length: 113  Bit Score: 93.90  E-value: 5.08e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227401   4304 LRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAADYAVRGKSDKDVKPTALAQKIEEYSQQLEGLTNDVHTLEAYG 4383
Cdd:smart00748    1 LRRAKRFLEAAKLDLEKGFYDLAAFLSQQAAELALKALLLALGGEPPKTHSLRELLSELEKLLRLPEFIDEIRECLNLLE 80
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 491227401   4384 VDSLKTRYPDLLPfpqiPNDRFTSEVAMRVMECTACI 4420
Cdd:smart00748   81 EAYIKSRYPDAGE----PLEWYTKEDAEELLKCAEEI 113
DnaJ super family cl02542
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
4175-4210 1.10e-03

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


The actual alignment was detected with superfamily member pfam00226:

Pssm-ID: 413365 [Multi-domain]  Cd Length: 63  Bit Score: 40.15  E-value: 1.10e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 491227401  4175 ESERKKIIRRLYLKWHPDKNPENHDiANEVFKHLQN 4210
Cdd:pfam00226   14 DEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINE 48
 
Name Accession Description Interval E-value
HEPN smart00748
Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;
4304-4420 5.08e-22

Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;


Pssm-ID: 214800  Cd Length: 113  Bit Score: 93.90  E-value: 5.08e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227401   4304 LRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAADYAVRGKSDKDVKPTALAQKIEEYSQQLEGLTNDVHTLEAYG 4383
Cdd:smart00748    1 LRRAKRFLEAAKLDLEKGFYDLAAFLSQQAAELALKALLLALGGEPPKTHSLRELLSELEKLLRLPEFIDEIRECLNLLE 80
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 491227401   4384 VDSLKTRYPDLLPfpqiPNDRFTSEVAMRVMECTACI 4420
Cdd:smart00748   81 EAYIKSRYPDAGE----PLEWYTKEDAEELLKCAEEI 113
HEPN COG2250
HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];
4304-4430 3.90e-06

HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];


Pssm-ID: 441851  Cd Length: 121  Bit Score: 48.79  E-value: 3.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227401 4304 LRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAADYAVRGKSDK--DVkpTALAQKIEEYSQQLEGLTNDVHTLEA 4381
Cdd:COG2250     1 LRRAERDLEAAELLLEEGRYDLACFHAQQAAEKALKALLLALGGEPPKthDL--RELLELLEKLLPEPEELRDLLRLLDK 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 491227401 4382 YGVDSlktRYPDLLPfpqIPNDRFTSEVAMRVMECTACIIIKLENFMQQ 4430
Cdd:COG2250    79 AYIPA---RYPDALP---EGPEEYTREEAEEALELAEEVLEFVEKLLKE 121
HEPN pfam05168
HEPN domain;
4300-4417 4.05e-06

HEPN domain;


Pssm-ID: 398711  Cd Length: 117  Bit Score: 48.77  E-value: 4.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227401  4300 ARRWLRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAAdYAVRGKSDK---DVkpTALAQKIEEYSQQLEGLTNDV 4376
Cdd:pfam05168    1 AEDWLRRAEEDLEAAELLLEEGDYDWACFHAQQAAEKALKAL-LLKLGGDPPkthDL--RELLGELKKGLGLPEELREIL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 491227401  4377 HTLEAYGVDSlktRYPDLLPfpqipndrFTSEVAMRVMECT 4417
Cdd:pfam05168   78 DELEKAYIES---RYPDADE--------GTEEDAEEALKDA 107
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
4175-4210 1.10e-03

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 40.15  E-value: 1.10e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 491227401  4175 ESERKKIIRRLYLKWHPDKNPENHDiANEVFKHLQN 4210
Cdd:pfam00226   14 DEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINE 48
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
4162-4223 1.70e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 44.03  E-value: 1.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227401 4162 EVTSVVEQAWKlpeSERKKIIRRLYLKWHPDKNPENHDI------ANEVFKHLQNEinrlEKQAFLDQ 4223
Cdd:PRK14281    7 EVLGVSRSADK---DEIKKAYRKLALKYHPDKNPDNKEAeehfkeVNEAYEVLSND----DKRRRYDQ 67
DnaJ smart00271
DnaJ molecular chaperone homology domain;
4175-4213 1.74e-03

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 39.53  E-value: 1.74e-03
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 491227401   4175 ESERKKIIRRLYLKWHPDKNPENHDIANEVFKhlqnEIN 4213
Cdd:smart00271   15 LDEIKKAYRKLALKYHPDKNPGDKEEAEEKFK----EIN 49
 
Name Accession Description Interval E-value
HEPN smart00748
Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;
4304-4420 5.08e-22

Higher Eukarytoes and Prokaryotes Nucleotide-binding domain;


Pssm-ID: 214800  Cd Length: 113  Bit Score: 93.90  E-value: 5.08e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227401   4304 LRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAADYAVRGKSDKDVKPTALAQKIEEYSQQLEGLTNDVHTLEAYG 4383
Cdd:smart00748    1 LRRAKRFLEAAKLDLEKGFYDLAAFLSQQAAELALKALLLALGGEPPKTHSLRELLSELEKLLRLPEFIDEIRECLNLLE 80
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 491227401   4384 VDSLKTRYPDLLPfpqiPNDRFTSEVAMRVMECTACI 4420
Cdd:smart00748   81 EAYIKSRYPDAGE----PLEWYTKEDAEELLKCAEEI 113
HEPN COG2250
HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];
4304-4430 3.90e-06

HEPN domain protein, predicted toxin of MNT-HEPN system [Defense mechanisms];


Pssm-ID: 441851  Cd Length: 121  Bit Score: 48.79  E-value: 3.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227401 4304 LRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAADYAVRGKSDK--DVkpTALAQKIEEYSQQLEGLTNDVHTLEA 4381
Cdd:COG2250     1 LRRAERDLEAAELLLEEGRYDLACFHAQQAAEKALKALLLALGGEPPKthDL--RELLELLEKLLPEPEELRDLLRLLDK 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 491227401 4382 YGVDSlktRYPDLLPfpqIPNDRFTSEVAMRVMECTACIIIKLENFMQQ 4430
Cdd:COG2250    79 AYIPA---RYPDALP---EGPEEYTREEAEEALELAEEVLEFVEKLLKE 121
HEPN pfam05168
HEPN domain;
4300-4417 4.05e-06

HEPN domain;


Pssm-ID: 398711  Cd Length: 117  Bit Score: 48.77  E-value: 4.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227401  4300 ARRWLRQARANFSAARNDLHKNANEWVCFKCYLSTKLALIAAdYAVRGKSDK---DVkpTALAQKIEEYSQQLEGLTNDV 4376
Cdd:pfam05168    1 AEDWLRRAEEDLEAAELLLEEGDYDWACFHAQQAAEKALKAL-LLKLGGDPPkthDL--RELLGELKKGLGLPEELREIL 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 491227401  4377 HTLEAYGVDSlktRYPDLLPfpqipndrFTSEVAMRVMECT 4417
Cdd:pfam05168   78 DELEKAYIES---RYPDADE--------GTEEDAEEALKDA 107
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
4175-4210 1.10e-03

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 40.15  E-value: 1.10e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 491227401  4175 ESERKKIIRRLYLKWHPDKNPENHDiANEVFKHLQN 4210
Cdd:pfam00226   14 DEEIKKAYRKLALKYHPDKNPGDPE-AEEKFKEINE 48
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
4162-4223 1.70e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 44.03  E-value: 1.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227401 4162 EVTSVVEQAWKlpeSERKKIIRRLYLKWHPDKNPENHDI------ANEVFKHLQNEinrlEKQAFLDQ 4223
Cdd:PRK14281    7 EVLGVSRSADK---DEIKKAYRKLALKYHPDKNPDNKEAeehfkeVNEAYEVLSND----DKRRRYDQ 67
DnaJ smart00271
DnaJ molecular chaperone homology domain;
4175-4213 1.74e-03

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 39.53  E-value: 1.74e-03
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 491227401   4175 ESERKKIIRRLYLKWHPDKNPENHDIANEVFKhlqnEIN 4213
Cdd:smart00271   15 LDEIKKAYRKLALKYHPDKNPGDKEEAEEKFK----EIN 49
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
4175-4223 2.60e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 43.63  E-value: 2.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 491227401 4175 ESERKKIIRRLYLKWHPDKNPENHDIANEVFKHLQNEINRL---EKQAFLDQ 4223
Cdd:PRK14282   18 QEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLsdpQKRAMYDR 69
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
4175-4213 5.43e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 42.44  E-value: 5.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 491227401 4175 ESERKKIIRRLYLKWHPDKNPENHDiANEVFKhlqnEIN 4213
Cdd:PRK10767   18 EDEIKKAYRKLAMKYHPDRNPGDKE-AEEKFK----EIK 51
 
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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