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Conserved domains on  [gi|21280963|gb|AAM44977|]
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putative DnaJ 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 ...
 66-130 1.16e-24

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: 91.38  E-value: 1.16e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963    66 SFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDrvEEYTDRFIRVQEAYETLSDPRRRVLYD 130
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD--PEAEEKFKEINEAYEVLSDPEKRAIYD 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 ...
 66-130 1.16e-24

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: 91.38  E-value: 1.16e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963    66 SFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDrvEEYTDRFIRVQEAYETLSDPRRRVLYD 130
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD--PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-160 1.09e-23

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: 91.30  E-value: 1.09e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963  66 SFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDrvEEYTDRFIRVQEAYETLSDPRRRVLYDRDLSMGFSFSFSGRR 145
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD--PEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELA 78

                        90
                ....*....|....*
gi 21280963 146 QNRYDQEVVEEKSEW 160
Cdd:COG0484  79 ESAAAEAAAAEAKEE 93
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 66-143 7.03e-22

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: 91.12  E-value: 7.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963    66 SFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYDR----DLSMGFSFSF 141
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEE---KFKEINEAYEVLSDPEKRAQYDQfghaGFNGGGGGGG 77


                  ..
gi 21280963   142 SG 143
Cdd:TIGR02349  78 GG 79
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-125 1.61e-20

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 80.74  E-value: 1.61e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963     66 SFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSpPDRVEEYTDRFIRVQEAYETLSDPRR 125
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKN-PGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 67-122 6.00e-19

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: 76.43  E-value: 6.00e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21280963  67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDrvEEYTDRFIRVQEAYETLSD 122
Cdd:cd06257   2 YYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD--PEAEEKFKEINEAYEVLSD 55
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 60-131 8.96e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 82.53  E-value: 8.96e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21280963   60 KQSEDlsFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRvEEYTDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14282   1 REKKD--YYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENR-KEAEQKFKEIQEAYEVLSDPQKRAMYDR 69
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
67-139 1.04e-13

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 68.69  E-value: 1.04e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYDR------DLSMGFSF 139
Cdd:NF037946   7 YYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAE---IFAEINEAYEVLSNPEKRANYDKyghdgvDGEGGFGF 82
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-130 1.16e-24

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: 91.38  E-value: 1.16e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963    66 SFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDrvEEYTDRFIRVQEAYETLSDPRRRVLYD 130
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD--PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-160 1.09e-23

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: 91.30  E-value: 1.09e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963  66 SFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDrvEEYTDRFIRVQEAYETLSDPRRRVLYDRDLSMGFSFSFSGRR 145
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD--PEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELA 78

                        90
                ....*....|....*
gi 21280963 146 QNRYDQEVVEEKSEW 160
Cdd:COG0484  79 ESAAAEAAAAEAKEE 93
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 66-143 7.03e-22

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: 91.12  E-value: 7.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963    66 SFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYDR----DLSMGFSFSF 141
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEE---KFKEINEAYEVLSDPEKRAQYDQfghaGFNGGGGGGG 77


                  ..
gi 21280963   142 SG 143
Cdd:TIGR02349  78 GG 79
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-125 1.61e-20

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 80.74  E-value: 1.61e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963     66 SFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSpPDRVEEYTDRFIRVQEAYETLSDPRR 125
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKN-PGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 67-122 6.00e-19

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: 76.43  E-value: 6.00e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21280963  67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDrvEEYTDRFIRVQEAYETLSD 122
Cdd:cd06257   2 YYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD--PEAEEKFKEINEAYEVLSD 55
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 60-131 8.96e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 82.53  E-value: 8.96e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21280963   60 KQSEDlsFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRvEEYTDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14282   1 REKKD--YYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENR-KEAEQKFKEIQEAYEVLSDPQKRAMYDR 69
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
62-134 1.62e-18

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 76.30  E-value: 1.62e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21280963  62 SEDLSFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRvEEYTDRFIRVQEAYETLSDPRRRVLYDRDLS 134
Cdd:COG2214   2 PDLKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELK-ALAEELFQRLNEAYEVLSDPERRAEYDRELG 73
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 67-153 1.91e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 81.74  E-value: 1.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYDRdlsMGFSfSFSGRRQ 146
Cdd:PRK14291   5 YYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEE---KFKEINEAYQVLSDPEKRKLYDQ---FGHA-AFSGSGQ 77


                 ....*..
gi 21280963  147 NRYDQEV 153
Cdd:PRK14291  78 QQQGQEG 84
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 67-126 2.72e-18

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 75.04  E-value: 2.72e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963  67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytDRFIRVQEAYETLSDPRRR 126
Cdd:COG5407   2 PYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAE--ERFKEINEAYELLSDAEKR 59
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 67-131 9.65e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 79.80  E-value: 9.65e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK10767   6 YYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAE--EKFKEIKEAYEVLSDPQKRAAYDQ 68
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 67-131 1.23e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 79.46  E-value: 1.23e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14277   7 YYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAE--QKFKEINEAYEILSDPQKRAQYDQ 69
PRK14293 PRK14293
molecular chaperone DnaJ;
67-131 1.35e-17

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 79.26  E-value: 1.35e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEeytDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14293   5 YYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAE---DRFKEINRAYEVLSDPETRARYDQ 66
PRK14279 PRK14279
molecular chaperone DnaJ;
67-147 1.38e-17

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 79.39  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytDRFIRVQEAYETLSDPRRRVLYDRDLSMGFSFSFSGRRQ 146
Cdd:PRK14279  11 FYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAE--ERFKAVSEAHDVLSDPAKRKEYDETRRLFAGGGFGGRRF 88


                 .
gi 21280963  147 N 147
Cdd:PRK14279  89 D 89
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 67-143 1.55e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 79.36  E-value: 1.55e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVS-PPDRVEEYTDrfirVQEAYETLSDPRRRVLYDRDLSMGFSFSFSG 143
Cdd:PRK14276   6 YYDRLGVSKDASQDEIKKAYRKLSKKYHPDINkEPGAEEKYKE----VQEAYETLSDPQKRAAYDQYGAAGANGGFGG 79
PRK14280 PRK14280
molecular chaperone DnaJ;
67-143 2.53e-17

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 78.61  E-value: 2.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSppdRVEEYTDRFIRVQEAYETLSDPRRRVLYDR----DLSMGFSFSFS 142
Cdd:PRK14280   6 YYEVLGVSKSASKDEIKKAYRKLSKKYHPDIN---KEEGADEKFKEISEAYEVLSDDQKRAQYDQfghaGPNQGFGGGGF 82


                 .
gi 21280963  143 G 143
Cdd:PRK14280  83 G 83
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 67-137 4.70e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 77.74  E-value: 4.70e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVsppDRVEEYTDRFIRVQEAYETLSDPRRRVLYDR----DLSMGF 137
Cdd:PRK14287   6 YYEVLGVDRNASVDEVKKAYRKLARKYHPDV---NKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQfghtDPNQGF 77
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 67-131 6.55e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 77.58  E-value: 6.55e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14284   3 YYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAE--KRFKEVSEAYEVLSDAQKRESYDR 65
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 67-131 1.01e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 76.73  E-value: 1.01e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRveEYTDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14294   6 YYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDK--EAEELFKEAAEAYEVLSDPKKRGIYDQ 68
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 67-130 1.05e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 77.01  E-value: 1.05e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYD 130
Cdd:PRK14278   5 YYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQE---KFKEISVAYEVLSDPEKRRIVD 65
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 67-131 2.86e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 74.98  E-value: 2.86e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14299   6 YYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEE---KFKEINEAYTVLSDPEKRRIYDT 67
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 65-131 9.43e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 74.16  E-value: 9.43e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21280963   65 LSFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14292   2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAE---KFAQINEAYAVLSDAEKRAHYDR 65
PRK14295 PRK14295
molecular chaperone DnaJ;
67-145 1.14e-15

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 74.11  E-value: 1.14e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytDRFIRVQEAYETLSDPRRRVLYDRDLSMgfsFSFSGRR 145
Cdd:PRK14295  11 YYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAE--ERFKEISEAYDVLSDEKKRKEYDEARSL---FGNGGFR 84
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 64-149 2.03e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 73.10  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963   64 DLSFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRveEYTDRFIRVQEAYETLSDPRRRVLYDRDLSMGFSFSFSG 143
Cdd:PRK14286   3 ERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNK--ESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGG 80


                 ....*.
gi 21280963  144 RRQNRY 149
Cdd:PRK14286  81 FGQGAY 86
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 67-143 2.51e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 73.04  E-value: 2.51e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRvEEYTDRFIRVQEAYETLSDPRRRVLYDRDLSMGFSFSFSG 143
Cdd:PRK14290   5 YYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNK-AEAEEKFKEISEAYEVLSDPQKRRQYDQTGTVDFGAGGSN 80
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 67-131 2.88e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 72.92  E-value: 2.88e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytDRFIRVQEAYETLS--DPRRRvlYDR 131
Cdd:PRK14281   5 YYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAE--EHFKEVNEAYEVLSndDKRRR--YDQ 67
PRK14289 PRK14289
molecular chaperone DnaJ;
67-131 3.59e-15

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 72.56  E-value: 3.59e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14289   7 YYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAE--EKFKEAAEAYDVLSDPDKRSRYDQ 69
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
67-125 7.58e-15

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 66.36  E-value: 7.58e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21280963  67 FYDLLGVTESVTLPEIKQAYKQLARKYHPD----VSPPDRVEEYTDRFIRVQEAYETLSDPRR 125
Cdd:COG1076   6 AFELLGLPPDADDAELKRAYRKLQREHHPDrlaaGLPEEEQRLALQKAAAINEAYETLKDPRG 68
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 67-131 1.02e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 71.39  E-value: 1.02e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPdrvEEYTDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14283   7 YYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE---EGAEEKFKEISEAYAVLSDDEKRQRYDQ 68
PRK10266 PRK10266
curved DNA-binding protein;
67-131 2.16e-14

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 69.85  E-value: 2.16e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK10266   6 YYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEA---RFKEVAEAWEVLSDEQRRAEYDQ 67
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 67-152 4.72e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 69.49  E-value: 4.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYDRdlsmgfsFSFSGrRQ 146
Cdd:PRK14298   7 YYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEE---KFKEISEAYAVLSDAEKRAQYDR-------FGHAG-ID 75


                 ....*.
gi 21280963  147 NRYDQE 152
Cdd:PRK14298  76 NQYSAE 81
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
67-139 1.04e-13

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 68.69  E-value: 1.04e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYDR------DLSMGFSF 139
Cdd:NF037946   7 YYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAE---IFAEINEAYEVLSNPEKRANYDKyghdgvDGEGGFGF 82
PRK14297 PRK14297
molecular chaperone DnaJ;
67-143 1.53e-13

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 67.89  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRveEYTDRFIRVQEAYETLSDPRRRVLYDR----DLSMGFSFSFS 142
Cdd:PRK14297   6 YYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNK--EAEEKFKEINEAYQVLSDPQKKAQYDQfgtaDFNGAGGFGSG 83


                 .
gi 21280963  143 G 143
Cdd:PRK14297  84 G 84
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 67-131 1.96e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 67.46  E-value: 1.96e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDrvEEYTDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14301   6 YYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDN--PEAEQKFKEAAEAYEVLRDAEKRARYDR 68
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 67-143 7.78e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 65.74  E-value: 7.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEeytDRFIRVQEAYETLSDPRRRVLYDR------DLSMGFSFS 140
Cdd:PRK14296   6 YYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAH---DKMVEINEAADVLLDKDKRKQYDQfghaafDGSSGFSSN 82


                 ...
gi 21280963  141 FSG 143
Cdd:PRK14296  83 FGD 85
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 67-130 3.56e-11

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 60.99  E-value: 3.56e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPdrveeyTDRFIRVQEAYETLSDPRRRVLYD 130
Cdd:PTZ00037  30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD------PEKFKEISRAYEVLSDPEKRKIYD 87
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 67-143 5.48e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 60.39  E-value: 5.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDrvEEYTDRFIRVQEAYETLSDPRRRVLYDR---------DLSMGF 137
Cdd:PRK14285   5 YYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGN--KEAESIFKEATEAYEVLIDDNKRAQYDRfghtafeggGGFEGF 82


                 ....*.
gi 21280963  138 SFSFSG 143
Cdd:PRK14285  83 SGGFSG 88
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 67-131 1.65e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 59.26  E-value: 1.65e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963   67 FYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRVEEytdRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14300   5 YYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEK---KFKEINAAYDVLKDEQKRAAYDR 66
PRK14288 PRK14288
molecular chaperone DnaJ;
64-131 4.75e-10

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 57.78  E-value: 4.75e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21280963   64 DLSFYDLLGVTESVTLPEIKQAYKQLARKYHPDVSPPDRveEYTDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PRK14288   2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDK--EAEEKFKLINEAYGVLSDEKKRALYDR 67
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 57-131 1.43e-08

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 53.64  E-value: 1.43e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21280963    57 DPVKQSEDLSFYDLLGVTESVTLPEIKQAYKQLARKYHPdvsPPDRVEEYTDRFIRVQEAYETLSDPRRRVLYDR 131
Cdd:PTZ00341  565 APTIEIPDTLFYDILGVGVNADMKEISERYFKLAENYYP---PKRSGNEGFHKFKKINEAYQILGDIDKKKMYNK 636
djlA PRK09430
co-chaperone DjlA;
68-118 3.18e-06

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 46.34  E-value: 3.18e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 21280963   68 YDLLGVTESVTLPEIKQAYKQLARKYHPD--VS---PPDRVEEYTDRFIRVQEAYE 118
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDklVAkglPPEMMEMAKEKAQEIQAAYE 258
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 53-130 8.68e-06

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 45.41  E-value: 8.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21280963  53 LTHDDPVKQSEDLsfYDLLGVTE---SVTLPEIKQAYKQLARKYHPDVSPPDRVEEYTDRFIRVQEAYETLSDPRRRVLY 129
Cdd:COG5269  33 TREDFKNWKKVDL--YALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEFFKLIQKAREVLGDRKLRLQY 110


                .
gi 21280963 130 D 130
Cdd:COG5269 111 D 111
 
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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