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Conserved domains on  [gi|14423730|sp|P78983|]
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RecName: Full=Heat shock 70 kDa protein; AltName: Allergen=Alt a 3

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00009 super family cl36495
heat shock 70 kDa protein; Provisional
1-115 3.72e-51

heat shock 70 kDa protein; Provisional


The actual alignment was detected with superfamily member PTZ00009:

Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 172.29  E-value: 3.72e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423730    1 KTNKIVITNDKGRLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSDSKVDEKLDAGDKQKLTAEIDK 80
Cdd:PTZ00009 499 KSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKVKGKLSDSDKATIEKAIDE 578
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 14423730   81 TVQWLDDNQTATKDEYESQQKELEGVANPIMMKFY 115
Cdd:PTZ00009 579 ALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMY 613
 
Name Accession Description Interval E-value
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
1-115 3.72e-51

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 172.29  E-value: 3.72e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423730    1 KTNKIVITNDKGRLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSDSKVDEKLDAGDKQKLTAEIDK 80
Cdd:PTZ00009 499 KSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKVKGKLSDSDKATIEKAIDE 578
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 14423730   81 TVQWLDDNQTATKDEYESQQKELEGVANPIMMKFY 115
Cdd:PTZ00009 579 ALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMY 613
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
1-115 9.25e-24

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 95.79  E-value: 9.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423730     1 KTNKIVITNDKGrLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSDSKvdEKLDAGDKQKLTAEIDk 80
Cdd:pfam00012 489 KEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEG--DKVPEAEKSKVESAIE- 564
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 14423730    81 tvqWLDDN-QTATKDEYESQQKELEGVANPIMMKFY 115
Cdd:pfam00012 565 ---WLKDElEGDDKEEIEAKTEELAQVSQKIGERMY 597
 
Name Accession Description Interval E-value
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
1-115 3.72e-51

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 172.29  E-value: 3.72e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423730    1 KTNKIVITNDKGRLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSDSKVDEKLDAGDKQKLTAEIDK 80
Cdd:PTZ00009 499 KSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKVKGKLSDSDKATIEKAIDE 578
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 14423730   81 TVQWLDDNQTATKDEYESQQKELEGVANPIMMKFY 115
Cdd:PTZ00009 579 ALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMY 613
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
1-115 9.25e-24

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 394970 [Multi-domain]  Cd Length: 598  Bit Score: 95.79  E-value: 9.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423730     1 KTNKIVITNDKGrLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSDSKvdEKLDAGDKQKLTAEIDk 80
Cdd:pfam00012 489 KEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEG--DKVPEAEKSKVESAIE- 564
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 14423730    81 tvqWLDDN-QTATKDEYESQQKELEGVANPIMMKFY 115
Cdd:pfam00012 565 ---WLKDElEGDDKEEIEAKTEELAQVSQKIGERMY 597
dnaK PRK00290
molecular chaperone DnaK; Provisional
1-115 1.70e-17

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 77.83  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423730    1 KTNKIVITNDKGrLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSDSKvdEKLDAGDKQKLTAEIDK 80
Cdd:PRK00290 488 KEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELG--DKVPADEKEKIEAAIKE 564
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 14423730   81 TVQWLDDNQtatKDEYESQQKELEGVANPIMMKFY 115
Cdd:PRK00290 565 LKEALKGED---KEAIKAKTEELTQASQKLGEAMY 596
dnaK CHL00094
heat shock protein 70
1-111 4.75e-11

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 59.36  E-value: 4.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423730    1 KTNKIVITNdKGRLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSDskVDEKLDAGDKQKLTAEIDK 80
Cdd:CHL00094 490 KEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKE--LKDKISEEKKEKIENLIKK 566
                         90       100       110
                 ....*....|....*....|....*....|.
gi 14423730   81 TVQWLDdnqtatKDEYESQQKELEGVANPIM 111
Cdd:CHL00094 567 LRQALQ------NDNYESIKSLLEELQKALM 591
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
1-115 6.32e-10

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 56.37  E-value: 6.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423730    1 KTNKIVITNDKGrLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSDSKvdEKLDAGDKQKLTAEIDK 80
Cdd:PTZ00400 529 KKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLK--DKISDADKDELKQKITK 605
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 14423730   81 TVQWLddnQTATKDEYESQQKELEGVANPIMMKFY 115
Cdd:PTZ00400 606 LRSTL---SSEDVDSIKDKTKQLQEASWKISQQAY 637
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
5-74 7.95e-07

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 47.44  E-value: 7.95e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14423730    5 IVITNdKGRLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSD--SKVDEKLDAGDKQKL 74
Cdd:PRK13411 494 IRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKEngELISEELKQRAEQKV 564
PLN03184 PLN03184
chloroplast Hsp70; Provisional
1-103 5.14e-06

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 44.84  E-value: 5.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423730    1 KTNKIVITNdKGRLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSDskVDEKLDAGDKQKLTAEIDK 80
Cdd:PLN03184 527 KKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKE--LGDKVPADVKEKVEAKLKE 603
                         90       100
                 ....*....|....*....|....
gi 14423730   81 TVQWLD-DNQTATKDEYESQQKEL 103
Cdd:PLN03184 604 LKDAIAsGSTQKMKDAMAALNQEV 627
PTZ00186 PTZ00186
heat shock 70 kDa precursor protein; Provisional
1-104 8.09e-06

heat shock 70 kDa precursor protein; Provisional


Pssm-ID: 140213 [Multi-domain]  Cd Length: 657  Bit Score: 44.29  E-value: 8.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14423730    1 KTNKIVITNDKGrLSKEEIERMLAEAEKYKAEDEAEAARISAKNALESYAYSLRNTLSDSKVDEKLDAGDKQKLTAEIDK 80
Cdd:PTZ00186 515 KTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWKYVSDAEKENVKTLVAELRK 593
                         90       100
                 ....*....|....*....|....
gi 14423730   81 TVQwlddNQTATKDEYESQQKELE 104
Cdd:PTZ00186 594 AME----NPNVAKDDLAAATDKLQ 613
PRK13410 PRK13410
molecular chaperone DnaK; Provisional
14-44 1.39e-03

molecular chaperone DnaK; Provisional


Pssm-ID: 184038 [Multi-domain]  Cd Length: 668  Bit Score: 37.68  E-value: 1.39e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 14423730   14 LSKEEIERMLAEAEKYKAEDEAEAARISAKN 44
Cdd:PRK13410 502 LSEQEVNRMIQEAEAKADEDRRRRERIEKRN 532
 
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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