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Conserved domains on  [gi|15231204|ref|NP_187939|]
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Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

Protein Classification

J domain-containing protein( domain architecture ID 10446266)

J domain-containing protein containing a similar domain as DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70.

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
PubMed:  35729039|9644977|8016869|15170475
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 64-123 5.34e-21

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: 80.59  E-value: 5.34e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231204    64 SLYELLKVNETASLTEIKTAYRSLAKVYHPDASESD---GRDFMEIHKAYATLADPTTRAIYD 123
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDpeaEEKFKEINEAYEVLSDPEKRAIYD 63
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 64-123 5.34e-21

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: 80.59  E-value: 5.34e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231204    64 SLYELLKVNETASLTEIKTAYRSLAKVYHPDASESD---GRDFMEIHKAYATLADPTTRAIYD 123
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDpeaEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-154 6.17e-17

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: 72.43  E-value: 6.17e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204  66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD---FMEIHKAYATLADPTTRAIYDSTLRVPRRRVHAGAMGRSG 142
Cdd:COG0484   3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAeekFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAESAA 82

                        90
                ....*....|..
gi 15231204 143 RVYATTRRWETD 154
Cdd:COG0484  83 AEAAAAEAKEEA 94
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 66-149 2.70e-16

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: 74.17  E-value: 2.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204    66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD--FMEIHKAYATLADPTTRAIYDstlrvprRRVHAGAMGRSGR 143
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEekFKEINEAYEVLSDPEKRAQYD-------QFGHAGFNGGGGG 75


                  ....*.
gi 15231204   144 VYATTR 149
Cdd:TIGR02349  76 GGGGFN 81
DnaJ smart00271
DnaJ molecular chaperone homology domain;
64-117 2.73e-16

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 68.42  E-value: 2.73e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231204     64 SLYELLKVNETASLTEIKTAYRSLAKVYHPD----ASESDGRDFMEIHKAYATLADPT 117
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDknpgDKEEAEEKFKEINEAYEVLSDPE 59
PRK14293 PRK14293
molecular chaperone DnaJ;
66-123 4.70e-15

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 70.79  E-value: 4.70e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD--FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14293   6 YEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEdrFKEINRAYEVLSDPETRARYD 65
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-115 2.11e-14

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.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 63.33  E-value: 2.11e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15231204  66 YELLKVNETASLTEIKTAYRSLAKVYHPD---ASESDGRDFMEIHKAYATLAD 115
Cdd:cd06257   3 YDILGVPPDASDEEIKKAYRKLALKYHPDknpDDPEAEEKFKEINEAYEVLSD 55
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 64-123 5.34e-21

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: 80.59  E-value: 5.34e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231204    64 SLYELLKVNETASLTEIKTAYRSLAKVYHPDASESD---GRDFMEIHKAYATLADPTTRAIYD 123
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDpeaEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-154 6.17e-17

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: 72.43  E-value: 6.17e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204  66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD---FMEIHKAYATLADPTTRAIYDSTLRVPRRRVHAGAMGRSG 142
Cdd:COG0484   3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAeekFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAESAA 82

                        90
                ....*....|..
gi 15231204 143 RVYATTRRWETD 154
Cdd:COG0484  83 AEAAAAEAKEEA 94
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 66-149 2.70e-16

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: 74.17  E-value: 2.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204    66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD--FMEIHKAYATLADPTTRAIYDstlrvprRRVHAGAMGRSGR 143
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEekFKEINEAYEVLSDPEKRAQYD-------QFGHAGFNGGGGG 75


                  ....*.
gi 15231204   144 VYATTR 149
Cdd:TIGR02349  76 GGGGFN 81
DnaJ smart00271
DnaJ molecular chaperone homology domain;
64-117 2.73e-16

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 68.42  E-value: 2.73e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231204     64 SLYELLKVNETASLTEIKTAYRSLAKVYHPD----ASESDGRDFMEIHKAYATLADPT 117
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDknpgDKEEAEEKFKEINEAYEVLSDPE 59
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
64-130 4.61e-15

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 66.28  E-value: 4.61e-15
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231204  64 SLYELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD----FMEIHKAYATLADPTTRAIYDSTLRVPR 130
Cdd:COG2214   6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALaeelFQRLNEAYEVLSDPERRAEYDRELGQSG 76
PRK14293 PRK14293
molecular chaperone DnaJ;
66-123 4.70e-15

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 70.79  E-value: 4.70e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD--FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14293   6 YEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEdrFKEINRAYEVLSDPETRARYD 65
PRK14280 PRK14280
molecular chaperone DnaJ;
66-123 5.21e-15

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 70.91  E-value: 5.21e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD--FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14280   7 YEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADekFKEISEAYEVLSDDQKRAQYD 66
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 65-123 9.33e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 70.21  E-value: 9.33e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231204   65 LYELLKVNETASLTEIKTAYRSLAKVYHPDASESDG---RDFMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14277   7 YYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKeaeQKFKEINEAYEILSDPQKRAQYD 68
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 66-123 1.02e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 69.79  E-value: 1.02e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPD------ASEsdgRDFMEIHKAYATLADPTTRAIYD 123
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDrnpgdkEAE---EKFKEIKEAYEVLSDPQKRAAYD 67
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 66-140 1.14e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 69.88  E-value: 1.14e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDAS-ESDGRD-FMEIHKAYATLADPTTRAIYDstlrvprRRVHAGAMGR 140
Cdd:PRK14298   8 YEILGLSKDASVEDIKKAYRKLAMKYHPDKNkEPDAEEkFKEISEAYAVLSDAEKRAQYD-------RFGHAGIDNQ 77
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-115 2.11e-14

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.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 63.33  E-value: 2.11e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15231204  66 YELLKVNETASLTEIKTAYRSLAKVYHPD---ASESDGRDFMEIHKAYATLAD 115
Cdd:cd06257   3 YDILGVPPDASDEEIKKAYRKLALKYHPDknpDDPEAEEKFKEINEAYEVLSD 55
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 66-141 3.46e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 68.31  E-value: 3.46e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDG--RDFMEIHKAYATLADPTTRAIYDstlrvprRRVHAGAMGRS 141
Cdd:PRK14283   8 YEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGaeEKFKEISEAYAVLSDDEKRQRYD-------QFGHAGMDGFS 78
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 66-120 1.20e-13

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 61.94  E-value: 1.20e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231204  66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGR---DFMEIHKAYATLADPTTRA 120
Cdd:COG5407   3 YEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKaeeRFKEINEAYELLSDAEKRA 60
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 63-123 1.27e-13

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 66.77  E-value: 1.27e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231204   63 SSLYELLKVNETASLTEIKTAYRSLAKVYHPDASeSDGRDFMEIHKAYATLADPTTRAIYD 123
Cdd:PTZ00037  28 EKLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKG-GDPEKFKEISRAYEVLSDPEKRKIYD 87
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 66-123 1.63e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 66.72  E-value: 1.63e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD--FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14291   6 YEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEekFKEINEAYQVLSDPEKRKLYD 65
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 65-123 2.32e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 66.26  E-value: 2.32e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231204   65 LYELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD--FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14276   6 YYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEekYKEVQEAYETLSDPQKRAAYD 66
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 66-123 5.82e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 64.91  E-value: 5.82e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDG--RDFMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14292   5 YELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGaaEKFAQINEAYAVLSDAEKRAHYD 64
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 66-123 7.83e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 64.65  E-value: 7.83e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDAS-ESDGRD-FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14287   7 YEVLGVDRNASVDEVKKAYRKLARKYHPDVNkAPDAEDkFKEVKEAYDTLSDPQKKAHYD 66
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 66-124 2.32e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 63.03  E-value: 2.32e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD--FMEIHKAYATLADPTTRAIYDS 124
Cdd:PRK14299   7 YAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEekFKEINEAYTVLSDPEKRRIYDT 67
PRK10266 PRK10266
curved DNA-binding protein;
66-123 4.07e-12

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 62.15  E-value: 4.07e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDAS-ESDGRD-FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK10266   7 YAIMGVKPTDDLKTIKTAYRRLARKYHPDVSkEPDAEArFKEVAEAWEVLSDEQRRAEYD 66
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 66-142 4.42e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 62.55  E-value: 4.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDG---RDFMEIHKAYATLADPTTRAIYDstlRVPRRRVHAGAMGRSG 142
Cdd:PRK14284   4 YTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAeaeKRFKEVSEAYEVLSDAQKRESYD---RYGKDGPFAGAGGFGG 80
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 66-125 7.47e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 61.87  E-value: 7.47e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD----FMEIHKAYATLADPTTRAIYDST 125
Cdd:PRK14290   6 YKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEaeekFKEISEAYEVLSDPQKRRQYDQT 69
PRK14289 PRK14289
molecular chaperone DnaJ;
66-142 1.04e-11

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 61.39  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDG---RDFMEIHKAYATLADPTTRAIYDstlrvprRRVHAGAMGRSG 142
Cdd:PRK14289   8 YEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKeaeEKFKEAAEAYDVLSDPDKRSRYD-------QFGHAGVGGAAG 80
PRK14295 PRK14295
molecular chaperone DnaJ;
66-123 1.08e-11

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 61.40  E-value: 1.08e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGR---DFMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14295  12 YKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKaeeRFKEISEAYDVLSDEKKRKEYD 72
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 66-123 1.52e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 60.96  E-value: 1.52e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD----FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14282   7 YEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEaeqkFKEIQEAYEVLSDPQKRAMYD 68
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 64-145 2.98e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 60.00  E-value: 2.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   64 SLYELLKVNETASLTEIKTAYRSLAKVYHPDASESDG---RDFMEIHKAYATLADPTTRAIYDstlRVPRRRVHAGAMGR 140
Cdd:PRK14286   5 SYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKeseEKFKEATEAYEILRDPKKRQAYD---QFGKAGVNAGAGGF 81


                 ....*
gi 15231204  141 SGRVY 145
Cdd:PRK14286  82 GQGAY 86
PRK14297 PRK14297
molecular chaperone DnaJ;
66-123 3.19e-11

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 60.18  E-value: 3.19e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGR---DFMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14297   7 YEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEaeeKFKEINEAYQVLSDPQKKAQYD 67
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 66-123 3.66e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 59.96  E-value: 3.66e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDAS-ESDGRD-FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14296   7 YEVLGVSKTASEQEIRQAYRKLAKQYHPDLNkSPDAHDkMVEINEAADVLLDKDKRKQYD 66
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 66-123 6.85e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 58.91  E-value: 6.85e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDG--RDFMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14278   6 YGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEaqEKFKEISVAYEVLSDPEKRRIVD 65
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 66-123 1.21e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 58.49  E-value: 1.21e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDG--RDFMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14300   6 YQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDaeKKFKEINAAYDVLKDEQKRAAYD 65
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 66-123 2.06e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 57.47  E-value: 2.06e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD---FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14294   7 YEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAeelFKEAAEAYEVLSDPKKRGIYD 67
PRK14279 PRK14279
molecular chaperone DnaJ;
66-142 4.52e-10

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 56.66  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESD---GRDFMEIHKAYATLADPTTRAIYDSTlrvpRRRVHAGAMGRSG 142
Cdd:PRK14279  12 YKELGVSSDASAEEIKKAYRKLARELHPDANPGDpaaEERFKAVSEAHDVLSDPAKRKEYDET----RRLFAGGGFGGRR 87
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 66-142 7.76e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 55.90  E-value: 7.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDG---RDFMEIHKAYATLADPTTRAIYDstlrvprRRVHAGAMGRSG 142
Cdd:PRK14301   7 YEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPeaeQKFKEAAEAYEVLRDAEKRARYD-------RFGHAGVNGNGG 79
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 66-123 2.94e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 54.43  E-value: 2.94e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDAS--ESDGRD-FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14281   6 YEVLGVSRSADKDEIKKAYRKLALKYHPDKNpdNKEAEEhFKEVNEAYEVLSNDDKRRRYD 66
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
66-116 4.71e-08

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 47.48  E-value: 4.71e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231204  66 YELLKVNETASLTEIKTAYRSLAKVYHPD-----ASESDGRDFME----IHKAYATLADP 116
Cdd:COG1076   7 FELLGLPPDADDAELKRAYRKLQREHHPDrlaagLPEEEQRLALQkaaaINEAYETLKDP 66
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 66-123 5.34e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 50.76  E-value: 5.34e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPDASESDGRD---FMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14285   6 YEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAesiFKEATEAYEVLIDDNKRAQYD 66
PRK14288 PRK14288
molecular chaperone DnaJ;
64-123 1.28e-07

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 49.69  E-value: 1.28e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231204   64 SLYELLKVNETASLTEIKTAYRSLAKVYHPDASESDG---RDFMEIHKAYATLADPTTRAIYD 123
Cdd:PRK14288   4 SYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKeaeEKFKLINEAYGVLSDEKKRALYD 66
djlA PRK09430
co-chaperone DjlA;
66-94 8.63e-05

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 41.34  E-value: 8.63e-05
                         10        20
                 ....*....|....*....|....*....
gi 15231204   66 YELLKVNETASLTEIKTAYRSLAKVYHPD 94
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPD 231
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 84-122 2.68e-04

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: 39.10  E-value: 2.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15231204    84 YRSLAKVYHPDASES--DGRDFM----EIHKAYATLADPTTRAIY 122
Cdd:TIGR00714  12 YRQLQAQYHPDASGMaqEQLAASqqstTLNQAYHTLKDPLRRAEY 56
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 65-124 6.87e-04

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 38.86  E-value: 6.87e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231204  65 LYELL---KVNETASLTEIKTAYRSLAKVYHPD---ASESDGRD--FMEIHKAYATLADPTTRAIYDS 124
Cdd:COG5269  45 LYALLglsKYRTKAIPPQILKAHKKKVYKYHPDktaAGGNKGCDefFKLIQKAREVLGDRKLRLQYDS 112
hscB PRK00294
co-chaperone HscB; Provisional
 77-122 1.70e-03

co-chaperone HscB; Provisional


Pssm-ID: 166894 [Multi-domain]  Cd Length: 173  Bit Score: 37.14  E-value: 1.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15231204   77 LTEIKTAYRSLAKVYHPD----ASESDGRDFME----IHKAYATLADPTTRAIY 122
Cdd:PRK00294  20 LDQLATRYRELAREVHPDrfadAPEREQRLALErsasLNEAYQTLKSPPRRARY 73
 
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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