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Conserved domains on  [gi|1175554460|ref|WP_082096159|]
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DnaJ domain-containing protein [Candidatus Nitrosotenuis cloacae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DnaJ_bact super family cl37091
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
125-193 1.66e-30

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.


The actual alignment was detected with superfamily member TIGR02349:

Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 114.23  E-value: 1.66e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175554460 125 YYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKYYKASFG 193
Cdd:TIGR02349   2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFN 70
 
Name Accession Description Interval E-value
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
125-193 1.66e-30

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: 114.23  E-value: 1.66e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175554460 125 YYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKYYKASFG 193
Cdd:TIGR02349   2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFN 70
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
124-192 1.23e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 104.07  E-value: 1.23e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAE-RFAEINEAYDTLSDAETRAEYDKYYKASF 192
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEeKFKEIKEAYEVLSDPQKRAAYDQYGHAAF 74
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
124-187 1.54e-25

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 101.82  E-value: 1.54e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKY 187
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKY 69
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
124-190 1.87e-24

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: 93.23  E-value: 1.87e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTK-DQGSAERFAEINEAYDTLSDAETRAEYDKYYKA 190
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHA 68
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
124-185 2.80e-23

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: 87.53  E-value: 2.80e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDR-TKDQGSAERFAEINEAYDTLSDAETRAEYD 185
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
124-177 5.10e-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: 5.10e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQ-GSAERFAEINEAYDTLSD 177
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
123-179 3.68e-18

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 74.58  E-value: 3.68e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1175554460  123 PNYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQ--GSAERFAEINEAYDTLSDAE 179
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkeEAEEKFKEINEAYEVLSDPE 59
 
Name Accession Description Interval E-value
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
125-193 1.66e-30

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: 114.23  E-value: 1.66e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175554460 125 YYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKYYKASFG 193
Cdd:TIGR02349   2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFN 70
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
124-192 1.23e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 104.07  E-value: 1.23e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAE-RFAEINEAYDTLSDAETRAEYDKYYKASF 192
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEeKFKEIKEAYEVLSDPQKRAAYDQYGHAAF 74
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
124-187 1.54e-25

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 101.82  E-value: 1.54e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKY 187
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKY 69
PRK14293 PRK14293
molecular chaperone DnaJ;
116-193 1.24e-24

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 98.52  E-value: 1.24e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1175554460 116 MMQDsslpnYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKYYKASFG 193
Cdd:PRK14293    1 MAAD-----YYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQFGEAGVS 73
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
124-190 1.87e-24

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: 93.23  E-value: 1.87e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTK-DQGSAERFAEINEAYDTLSDAETRAEYDKYYKA 190
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHA 68
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
125-187 4.80e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 97.08  E-value: 4.80e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175554460 125 YYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKY 187
Cdd:PRK14276    6 YYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQY 68
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
124-187 2.05e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 95.30  E-value: 2.05e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKY 187
Cdd:PRK14298    6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRF 69
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
124-185 2.80e-23

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: 87.53  E-value: 2.80e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDR-TKDQGSAERFAEINEAYDTLSDAETRAEYD 185
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
124-190 2.90e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 94.96  E-value: 2.90e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKYYKA 190
Cdd:PRK14292    3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDRFGTA 69
PRK14295 PRK14295
molecular chaperone DnaJ;
124-193 2.86e-22

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 92.22  E-value: 2.86e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTK-DQGSAERFAEINEAYDTLSDAETRAEYDKyYKASFG 193
Cdd:PRK14295   10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYDE-ARSLFG 79
PRK14280 PRK14280
molecular chaperone DnaJ;
124-187 2.90e-22

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 92.09  E-value: 2.90e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKY 187
Cdd:PRK14280    5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQF 68
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
124-192 9.91e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 90.98  E-value: 9.91e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKYYKASF 192
Cdd:PRK14291    4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAF 72
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
124-187 1.89e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 88.84  E-value: 1.89e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKY 187
Cdd:PRK14299    5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDTY 68
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
122-185 2.34e-21

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 83.61  E-value: 2.34e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1175554460 122 LPNYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQG--SAERFAEINEAYDTLSDAETRAEYD 185
Cdd:COG2214     4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
124-185 4.34e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 86.26  E-value: 4.34e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYD 185
Cdd:PRK14278    4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVD 65
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
124-183 4.42e-20

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 79.27  E-value: 4.42e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTK-DQGSAERFAEINEAYDTLSDAETRAE 183
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKgDPKAEERFKEINEAYELLSDAEKRAR 61
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
124-192 5.82e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 86.01  E-value: 5.82e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAE-RFAEINEAYDTLSDAETRAEYDKYYKASF 192
Cdd:PRK14277    6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEqKFKEINEAYEILSDPQKRAQYDQFGHAAF 75
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
124-193 6.16e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 85.95  E-value: 6.16e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAE-RFAEINEAYDTLSDAETRAEYDKYYKASFG 193
Cdd:PRK14301    5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEqKFKEAAEAYEVLRDAEKRARYDRFGHAGVN 75
PRK14297 PRK14297
molecular chaperone DnaJ;
124-192 2.47e-19

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 84.06  E-value: 2.47e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTK-DQGSAERFAEINEAYDTLSDAETRAEYDKYYKASF 192
Cdd:PRK14297    5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKgNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADF 74
PRK14279 PRK14279
molecular chaperone DnaJ;
124-185 3.17e-19

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 84.01  E-value: 3.17e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTK-DQGSAERFAEINEAYDTLSDAETRAEYD 185
Cdd:PRK14279   10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPgDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
124-177 5.10e-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: 5.10e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQ-GSAERFAEINEAYDTLSD 177
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpEAEEKFKEINEAYEVLSD 55
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
124-192 6.83e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 83.07  E-value: 6.83e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKYYKASF 192
Cdd:PRK14296    5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHAAF 73
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
124-187 1.38e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 82.15  E-value: 1.38e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDR-TKDQGSAE-RFAEINEAYDTLSDAETRAEYDKY 187
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRhPENRKEAEqKFKEIQEAYEVLSDPQKRAMYDRF 70
DnaJ smart00271
DnaJ molecular chaperone homology domain;
123-179 3.68e-18

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 74.58  E-value: 3.68e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1175554460  123 PNYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQ--GSAERFAEINEAYDTLSDAE 179
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkeEAEEKFKEINEAYEVLSDPE 59
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
124-190 4.88e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 80.64  E-value: 4.88e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKYYKA 190
Cdd:PRK14283    6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQFGHA 72
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
125-187 9.10e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 79.81  E-value: 9.10e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175554460 125 YYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTK-DQGSAERFAEINEAYDTLSDAETRAEYDKY 187
Cdd:PRK14294    6 YYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPgDKEAEELFKEAAEAYEVLSDPKKRGIYDQY 69
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
124-193 2.01e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 79.08  E-value: 2.01e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAE-RFAEINEAYDTLSDAETRAEYDKYYKASFG 193
Cdd:PRK14281    4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEeHFKEVNEAYEVLSNDDKRRRYDQFGHAGVG 74
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
124-189 6.98e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 77.19  E-value: 6.98e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAE-RFAEINEAYDTLSDAETRAEYDKYYK 189
Cdd:PRK14284    2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEkRFKEVSEAYEVLSDAQKRESYDRYGK 68
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
125-190 7.74e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 76.95  E-value: 7.74e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175554460 125 YYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTK-DQGSAERFAEINEAYDTLSDAETRAEYDKYYKA 190
Cdd:PRK14286    6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKgNKESEEKFKEATEAYEILRDPKKRQAYDQFGKA 72
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
124-187 1.33e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 76.59  E-value: 1.33e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKY 187
Cdd:PRK14287    5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQF 68
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
124-193 1.88e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 76.12  E-value: 1.88e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKD--QGSAERFAEINEAYDTLSDAETRAEYDKYYKASFG 193
Cdd:PRK14290    4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGnkAEAEEKFKEISEAYEVLSDPQKRRQYDQTGTVDFG 75
PRK14289 PRK14289
molecular chaperone DnaJ;
124-193 2.48e-16

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 75.64  E-value: 2.48e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTK-DQGSAERFAEINEAYDTLSDAETRAEYDKYYKASFG 193
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPgDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVG 76
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
124-192 4.92e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 75.05  E-value: 4.92e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKYYKASF 192
Cdd:PRK14300    4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAF 72
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
121-178 5.19e-16

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 69.06  E-value: 5.19e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1175554460 121 SLPNYYHVLGVSQDATQEEIKSKFRQLAKEHHPDR------TKDQGSA-ERFAEINEAYDTLSDA 178
Cdd:COG1076     2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaglpEEEQRLAlQKAAAINEAYETLKDP 66
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
125-187 6.14e-15

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 71.78  E-value: 6.14e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175554460 125 YYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQgsaERFAEINEAYDTLSDAETRAEYDKY 187
Cdd:PTZ00037   30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDP---EKFKEISRAYEVLSDPEKRKIYDEY 89
PRK10266 PRK10266
curved DNA-binding protein;
122-186 1.38e-14

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 70.24  E-value: 1.38e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1175554460 122 LPNYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDK 186
Cdd:PRK10266    3 LKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQ 67
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
124-192 8.11e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 68.48  E-value: 8.11e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAER-FAEINEAYDTLSDAETRAEYDKYYKASF 192
Cdd:PRK14285    4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESiFKEATEAYEVLIDDNKRAQYDRFGHTAF 73
PRK14288 PRK14288
molecular chaperone DnaJ;
124-189 1.58e-10

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 58.93  E-value: 1.58e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175554460 124 NYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTK-DQGSAERFAEINEAYDTLSDAETRAEYDKYYK 189
Cdd:PRK14288    4 SYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAgDKEAEEKFKLINEAYGVLSDEKKRALYDRYGK 70
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
125-187 1.78e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 47.47  E-value: 1.78e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175554460  125 YYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQGSAERFAEINEAYDTLSDAETRAEYDKY 187
Cdd:PTZ00341   575 FYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKF 637
djlA PRK09430
co-chaperone DjlA;
118-173 5.98e-06

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 45.19  E-value: 5.98e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175554460 118 QDSSLPNYYHVLGVSQDATQEEIKSKFRQLAKEHHPDRTKDQG--------SAERFAEINEAYD 173
Cdd:PRK09430  195 RGPTLEDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKLVAKGlppemmemAKEKAQEIQAAYE 258
hscB PRK00294
co-chaperone HscB; Provisional
137-184 2.18e-05

co-chaperone HscB; Provisional


Pssm-ID: 166894 [Multi-domain]  Cd Length: 173  Bit Score: 42.92  E-value: 2.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1175554460 137 QEEIKSKFRQLAKEHHPDRTKDQG------SAERFAEINEAYDTLSDAETRAEY 184
Cdd:PRK00294   20 LDQLATRYRELAREVHPDRFADAPereqrlALERSASLNEAYQTLKSPPRRARY 73
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
137-184 2.19e-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: 39.87  E-value: 2.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1175554460 137 QEEIKSKFRQLAKEHHPDRTKDQ----GSAERFAEINEAYDTLSDAETRAEY 184
Cdd:TIGR00714   5 QSRLRKRYRQLQAQYHPDASGMAqeqlAASQQSTTLNQAYHTLKDPLRRAEY 56
hscB PRK05014
co-chaperone HscB; Provisional
142-184 2.20e-04

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 39.89  E-value: 2.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1175554460 142 SKFRQLAKEHHPDRTKDQGSAERF------AEINEAYDTLSDAETRAEY 184
Cdd:PRK05014   22 SRYQELQRQFHPDKFANASERERLlavqqaATINDAYQTLKHPLKRAEY 70
hscB PRK01356
co-chaperone HscB; Provisional
124-184 3.02e-04

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 39.86  E-value: 3.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175554460 124 NYYHVLGVSQDAT--QEEIKSKFRQLAKEHHPDRTKDQGSAERF----AEINEAYDTLSDAETRAEY 184
Cdd:PRK01356    3 NYFQLLGLPQEYNidLKILEKQYFAMQVKYHPDKAKTLQEKEQNliiaSELNNAYSTLKDALKRAEY 69
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
144-184 4.47e-03

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 36.54  E-value: 4.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1175554460 144 FRQLAKEHHPDRTKDQGSAER------FAEINEAYDTLSDAETRAEY 184
Cdd:PRK03578   29 YRTVQAQVHPDRFAAAGDAEKrvamqwATRANEAYQTLRDPLKRARY 75
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
114-175 4.48e-03

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 35.60  E-value: 4.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1175554460 114 RKMmqdsSLPNYYHVLGVSQDATQEEIKSKFRQLAKEHHPDrtkDQGSAERFAEINEAYDTL 175
Cdd:PTZ00100   60 NPM----SKSEAYKILNISPTASKERIREAHKQLMLRNHPD---NGGSTYIASKVNEAKDLL 114
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
124-185 6.64e-03

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 36.55  E-value: 6.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1175554460 124 NYYHVLGVSQ---DATQEEIKSKFRQLAKEHHPDRTKDQGSA---ERFAEINEAYDTLSDAETRAEYD 185
Cdd:COG5269    44 DLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAAGGNKgcdEFFKLIQKAREVLGDRKLRLQYD 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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