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Conserved domains on  [gi|499868728|ref|WP_011549462|]
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MULTISPECIES: Fe-S protein assembly co-chaperone HscB [Burkholderia]

Protein Classification

Fe-S protein assembly co-chaperone HscB( domain architecture ID 11479991)

Fe-S protein assembly co-chaperone HscB acts as a co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
1-175 8.70e-93

Fe-S protein assembly co-chaperone HscB;


:

Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 267.27  E-value: 8.70e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728   1 MVSLKDSHFDLFHLPAQFALDEAALDAAYRTVQTQVHPDRFAAAGDAQKRIAMQWATRANEAYRTLRDPLKRASYLLSLR 80
Cdd:PRK03578   1 MVSLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLHLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728  81 GVDIGAENNTAMEPAFLMQQMEWREGIEDAAAARNVDALDALLAELRDEKRVRVERLGTLLDS-GADQAAAEAVRQLMFI 159
Cdd:PRK03578  81 GVDVQAENNTAMPPAFLMQQMEWREAIEDARAARDVDALDALLAELRDERRERYAELGALLDSrGDDQAAAEAVRQLMFI 160

                        170
                 ....*....|....*.
gi 499868728 160 ERVASEVGAQIERLET 175
Cdd:PRK03578 161 EKLAQEIGAAIERLED 176
 
Name Accession Description Interval E-value
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
1-175 8.70e-93

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 267.27  E-value: 8.70e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728   1 MVSLKDSHFDLFHLPAQFALDEAALDAAYRTVQTQVHPDRFAAAGDAQKRIAMQWATRANEAYRTLRDPLKRASYLLSLR 80
Cdd:PRK03578   1 MVSLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLHLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728  81 GVDIGAENNTAMEPAFLMQQMEWREGIEDAAAARNVDALDALLAELRDEKRVRVERLGTLLDS-GADQAAAEAVRQLMFI 159
Cdd:PRK03578  81 GVDVQAENNTAMPPAFLMQQMEWREAIEDARAARDVDALDALLAELRDERRERYAELGALLDSrGDDQAAAEAVRQLMFI 160

                        170
                 ....*....|....*.
gi 499868728 160 ERVASEVGAQIERLET 175
Cdd:PRK03578 161 EKLAQEIGAAIERLED 176
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 29-173 5.07e-23

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 89.17  E-value: 5.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728   29 YRTVQTQVHPDrfAAAGDAQKRIAMQWATRANEAYRTLRDPLKRASYLLSLRGVDIGAENNTAMEPAFLMQQMEWREGIE 108
Cdd:TIGR00714  12 YRQLQAQYHPD--ASGMAQEQLAASQQSTTLNQAYHTLKDPLRRAEYMLKLLNIDLTQEQTSERDTAFPMELLKVRDELD 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499868728  109 DAAAARNVDALDALLAELRDEKRVRVERLGTLLDSGADQAAAEAVRQLMFIERVASEVGAQIERL 173
Cdd:TIGR00714  90 EIEQMDDEAGLELLEKQNKEMIQDIEAQLGQCLNDQDWAAAVKYTVKLKYWYKLASAFEDWEEGK 154
HSCB_C pfam07743
HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization ...
 92-166 4.43e-17

HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization domain and is found on co-chaperone proteins.


Pssm-ID: 462252  Cd Length: 75  Bit Score: 71.40  E-value: 4.43e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499868728   92 MEPAFLMQQMEWREGIEDAAAaRNVDALDALLAELRDEKRVRVERLGTLLDSGADQAAAEAVRQLMFIERVASEV 166
Cdd:pfam07743   1 MDPEFLMEQMEWREELEEAEA-RDEEELEELKAENKERIKELEAELEEAFDEQDLEAAADLVRRLRYLEKIQEEI 74
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
6-69 6.19e-13

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 60.58  E-value: 6.19e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499868728   6 DSHFDLFHLPAQfaLDEAALDAAYRTVQTQVHPDRFAA-AGDAQKRIAMQWATRANEAYRTLRDP 69
Cdd:COG1076    4 DDAFELLGLPPD--ADDAELKRAYRKLQREHHPDRLAAgLPEEEQRLALQKAAAINEAYETLKDP 66
DnaJ smart00271
DnaJ molecular chaperone homology domain;
29-71 4.14e-03

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 34.13  E-value: 4.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 499868728    29 YRTVQTQVHPDRFAaagdAQKRIAMQWATRANEAYRTLRDPLK 71
Cdd:smart00271  22 YRKLALKYHPDKNP----GDKEEAEEKFKEINEAYEVLSDPEK 60
 
Name Accession Description Interval E-value
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
1-175 8.70e-93

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 267.27  E-value: 8.70e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728   1 MVSLKDSHFDLFHLPAQFALDEAALDAAYRTVQTQVHPDRFAAAGDAQKRIAMQWATRANEAYRTLRDPLKRASYLLSLR 80
Cdd:PRK03578   1 MVSLKDDHFSLFGLPARFALDEAALDAAYRTVQAQVHPDRFAAAGDAEKRVAMQWATRANEAYQTLRDPLKRARYLLHLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728  81 GVDIGAENNTAMEPAFLMQQMEWREGIEDAAAARNVDALDALLAELRDEKRVRVERLGTLLDS-GADQAAAEAVRQLMFI 159
Cdd:PRK03578  81 GVDVQAENNTAMPPAFLMQQMEWREAIEDARAARDVDALDALLAELRDERRERYAELGALLDSrGDDQAAAEAVRQLMFI 160

                        170
                 ....*....|....*.
gi 499868728 160 ERVASEVGAQIERLET 175
Cdd:PRK03578 161 EKLAQEIGAAIERLED 176
hscB PRK05014
co-chaperone HscB; Provisional
 8-174 1.26e-47

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 152.75  E-value: 1.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728   8 HFDLFHLPAQFALDEAALDAAYRTVQTQVHPDRFAAAGDAQKRIAMQWATRANEAYRTLRDPLKRASYLLSLRGVDIGAE 87
Cdd:PRK05014   3 YFTLFGLPARYDIDTQLLASRYQELQRQFHPDKFANASERERLLAVQQAATINDAYQTLKHPLKRAEYLLSLHGFDLAHE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728  88 NNTAMEPAFLMQQMEWREGIEDAAAARNVD-ALDALLAELRDEKRVRVERLGTLLDSGADQAAAEAVRQLMFIERVASEV 166
Cdd:PRK05014  83 QHTVRDTAFLMEQMELREELEDIEQSKDPEaALESFIKRVKKMFKTRLQQMVEQLDNEAWDAAADTVRKLKFLDKLRSEV 162


                 ....*...
gi 499868728 167 gaqiERLE 174
Cdd:PRK05014 163 ----EQLE 166
hscB PRK01773
Fe-S protein assembly co-chaperone HscB;
9-174 7.80e-30

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 179335 [Multi-domain]  Cd Length: 173  Bit Score: 107.14  E-value: 7.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728   9 FDLFHLPAQFALDEAALDAAYRTVQTQVHPDRFAAAGDAQKRIAMQWATRANEAYRTLRDPLKRASYLLSLR-GVDIGAE 87
Cdd:PRK01773   5 FALFDLPVDFQLDNALLSERYLALQKSLHPDNFANSSAQEQRLAMQKSAEVNDALQILKDPILRAEAIIALNtGEQQNLE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728  88 NNTAMEPAFLMQQMEWREGIEDAAAARNVDALDALLAELRDEKRVRVERLGTLLDSGADQAAAEAVRQLMFIERVASEvg 167
Cdd:PRK01773  85 EKSTQDMAFLMQQMEWREQLEEIEQQQDEDALTAFSKEIKQEQQAILTELSTALNSQQWQQASQINDRLRFIKKLIIE-- 162


                 ....*..
gi 499868728 168 aqIERLE 174
Cdd:PRK01773 163 --IERVE 167
hscB PRK00294
co-chaperone HscB; Provisional
 7-174 3.86e-28

co-chaperone HscB; Provisional


Pssm-ID: 166894 [Multi-domain]  Cd Length: 173  Bit Score: 103.01  E-value: 3.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728   7 SHFDLFHLPAQFALDEAALDAAYRTVQTQVHPDRFAAAGDAQKRIAMQWATRANEAYRTLRDPLKRASYLLSLRGVDIGA 86
Cdd:PRK00294   5 CHFALFDLQPSFRLDLDQLATRYRELAREVHPDRFADAPEREQRLALERSASLNEAYQTLKSPPRRARYLLALSGHEVPL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728  87 EnNTAMEPAFLMQQMEWREGIEDAAAARNVDALDALLAELRDEKRVRVERLGTLLDSGADQAAAEA-VRQLMFIERVASE 165
Cdd:PRK00294  85 E-VTVHDPEFLLQQMQLREELEELQDEADLAGVATFKRRLKAAQDELNESFAACWDDAARREEAERlMRRMQFLDKLAQE 163


                 ....*....
gi 499868728 166 VGAQIERLE 174
Cdd:PRK00294 164 VRQLEERLD 172
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 29-173 5.07e-23

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 89.17  E-value: 5.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728   29 YRTVQTQVHPDrfAAAGDAQKRIAMQWATRANEAYRTLRDPLKRASYLLSLRGVDIGAENNTAMEPAFLMQQMEWREGIE 108
Cdd:TIGR00714  12 YRQLQAQYHPD--ASGMAQEQLAASQQSTTLNQAYHTLKDPLRRAEYMLKLLNIDLTQEQTSERDTAFPMELLKVRDELD 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499868728  109 DAAAARNVDALDALLAELRDEKRVRVERLGTLLDSGADQAAAEAVRQLMFIERVASEVGAQIERL 173
Cdd:TIGR00714  90 EIEQMDDEAGLELLEKQNKEMIQDIEAQLGQCLNDQDWAAAVKYTVKLKYWYKLASAFEDWEEGK 154
HSCB_C pfam07743
HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization ...
 92-166 4.43e-17

HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization domain and is found on co-chaperone proteins.


Pssm-ID: 462252  Cd Length: 75  Bit Score: 71.40  E-value: 4.43e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499868728   92 MEPAFLMQQMEWREGIEDAAAaRNVDALDALLAELRDEKRVRVERLGTLLDSGADQAAAEAVRQLMFIERVASEV 166
Cdd:pfam07743   1 MDPEFLMEQMEWREELEEAEA-RDEEELEELKAENKERIKELEAELEEAFDEQDLEAAADLVRRLRYLEKIQEEI 74
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
6-69 6.19e-13

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 60.58  E-value: 6.19e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499868728   6 DSHFDLFHLPAQfaLDEAALDAAYRTVQTQVHPDRFAA-AGDAQKRIAMQWATRANEAYRTLRDP 69
Cdd:COG1076    4 DDAFELLGLPPD--ADDAELKRAYRKLQREHHPDRLAAgLPEEEQRLALQKAAAINEAYETLKDP 66
hscB PRK01356
co-chaperone HscB; Provisional
 7-97 1.27e-11

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 59.51  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728   7 SHFDLFHLPAQFALDEAALDAAYRTVQTQVHPDRfaAAGDAQKRIAMQWATRANEAYRTLRDPLKRASYLLSLRGVDIGA 86
Cdd:PRK01356   3 NYFQLLGLPQEYNIDLKILEKQYFAMQVKYHPDK--AKTLQEKEQNLIIASELNNAYSTLKDALKRAEYMLLLQNINLND 80

                         90
                 ....*....|..
gi 499868728  87 EN-NTAMEPAFL 97
Cdd:PRK01356  81 EKtRSLLSPLEL 92
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 29-156 1.40e-05

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 42.77  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499868728  29 YRTVQTQVHPDRFAAAGDAQKRIAmqwatRANEAYRTLRDPLKRASYllslrgvDIGAENNTAMEPAFLMQQMEWREGIE 108
Cdd:COG0484   21 YRKLAKKYHPDRNPGDPEAEEKFK-----EINEAYEVLSDPEKRAAY-------DRFGHAAELLLATELAESAAAEAAAA 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499868728 109 DAAAARNVDALDALLAELRDEKRVRVERLGTLLDSGADQAAAEAVRQL 156
Cdd:COG0484   89 EAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELALAAVLGLLL 136
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
29-91 5.22e-04

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 37.39  E-value: 5.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499868728  29 YRTVQTQVHPDRFAaagdAQKRIAMQWATRANEAYRTLRDPLKRASYLLSLRGVDIGAENNTA 91
Cdd:COG2214   26 YRRLAKLLHPDRGG----ELKALAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKGSASQPS 84
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 29-75 6.23e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 39.34  E-value: 6.23e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499868728  29 YRTVQTQVHPDRFAAAGDAQKRIamqwaTRANEAYRTLRDPLKRASY 75
Cdd:PRK14301  25 YRKLALQYHPDRNPDNPEAEQKF-----KEAAEAYEVLRDAEKRARY 66
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 29-86 9.99e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 38.82  E-value: 9.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499868728  29 YRTVQTQVHPDRFAAAGDAQKRIamqwaTRANEAYRTLRDPLKRASY-LLSLRGVDIGA 86
Cdd:PRK14286  25 YRKLAIKYHPDKNKGNKESEEKF-----KEATEAYEILRDPKKRQAYdQFGKAGVNAGA 78
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 29-75 1.15e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 38.33  E-value: 1.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499868728  29 YRTVQTQVHPDRFAAAGDAQKriamqwATRANEAYRTLRDPLKRASY 75
Cdd:PRK14292  23 YRKLALKYHPDRNKEKGAAEK------FAQINEAYAVLSDAEKRAHY 63
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 29-75 1.39e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 38.29  E-value: 1.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499868728  29 YRTVQTQVHPDRFAAAGDAQKRIamqwaTRANEAYRTLRDPLKRASY 75
Cdd:PRK14284  22 YRKLAVKYHPDKNPGDAEAEKRF-----KEVSEAYEVLSDAQKRESY 63
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 29-75 1.63e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 37.86  E-value: 1.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499868728  29 YRTVQTQVHPDrfAAAGDAQkriAMQWATRANEAYRTLRDPLKRASY 75
Cdd:PRK14277  26 YRRLAKKYHPD--LNPGDKE---AEQKFKEINEAYEILSDPQKRAQY 67
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 29-75 2.43e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 37.37  E-value: 2.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499868728  29 YRTVQTQVHPDRFAAAGDAQKriamqwATRANEAYRTLRDPLKRASY 75
Cdd:PRK14276  25 YRKLSKKYHPDINKEPGAEEK------YKEVQEAYETLSDPQKRAAY 65
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 29-75 3.04e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 37.30  E-value: 3.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499868728  29 YRTVQTQVHPDRfAAAGDAQKRIamqwaTRANEAYRTLRDPLKRASY 75
Cdd:PRK14300  24 YLKLAKQYHPDT-TDAKDAEKKF-----KEINAAYDVLKDEQKRAAY 64
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 35-75 3.96e-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: 34.37  E-value: 3.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 499868728   35 QVHPDR---FAAAGDAQKRIamqwatraNEAYRTLRDPLKRASY 75
Cdd:pfam00226  27 KYHPDKnpgDPEAEEKFKEI--------NEAYEVLSDPEKRAIY 62
DnaJ smart00271
DnaJ molecular chaperone homology domain;
29-71 4.14e-03

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 34.13  E-value: 4.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 499868728    29 YRTVQTQVHPDRFAaagdAQKRIAMQWATRANEAYRTLRDPLK 71
Cdd:smart00271  22 YRKLALKYHPDKNP----GDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 29-75 5.83e-03

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 36.42  E-value: 5.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 499868728   29 YRTVQTQVHPDRFAAAGDAQ--KRIamqwatraNEAYRTLRDPLKRASY 75
Cdd:TIGR02349  21 YRKLAKKYHPDRNKDKEAEEkfKEI--------NEAYEVLSDPEKRAQY 61
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 29-75 8.75e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 35.89  E-value: 8.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499868728  29 YRTVQTQVHPDRfaAAGDAQ-----KRIamqwatraNEAYRTLRDPLKRASY 75
Cdd:PRK10767  25 YRKLAMKYHPDR--NPGDKEaeekfKEI--------KEAYEVLSDPQKRAAY 66
PRK14297 PRK14297
molecular chaperone DnaJ;
29-75 9.90e-03

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 35.53  E-value: 9.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499868728  29 YRTVQTQVHPDRFAAAGDAQKRIamqwaTRANEAYRTLRDPLKRASY 75
Cdd:PRK14297  25 FRKLAIKYHPDKNKGNKEAEEKF-----KEINEAYQVLSDPQKKAQY 66
 
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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