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Conserved domains on  [gi|124512886|ref|XP_001349799|]
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DnaJ protein, putative [Plasmodium falciparum 3D7]

Protein Classification

J domain-containing protein( domain architecture ID 10154716)

J domain-containing protein similar to molecular chaperone 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 cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 102-152 1.60e-09

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: 52.93  E-value: 1.60e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 124512886 102 PFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAA-EAFHILTRAYEEL 152
Cdd:cd06257    2 YYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAeEKFKEINEAYEVL 53
 
Name Accession Description Interval E-value
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 102-152 1.60e-09

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: 52.93  E-value: 1.60e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 124512886 102 PFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAA-EAFHILTRAYEEL 152
Cdd:cd06257    2 YYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAeEKFKEINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 101-161 2.16e-09

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: 52.86  E-value: 2.16e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124512886  101 SPFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDK-AAEAFHILTRAYEELQKDEIKEQY 161
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPeAEEKFKEINEAYEVLSDPEKRAIY 62
DnaJ smart00271
DnaJ molecular chaperone homology domain;
101-156 2.46e-09

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 52.62  E-value: 2.46e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 124512886   101 SPFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDK--AAEAFHILTRAYEELQKDE 156
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKeeAEEKFKEINEAYEVLSDPE 59
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 103-161 6.34e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 53.45  E-value: 6.34e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDK-AAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKeSEEKFKEATEAYEILRDPKKRQAY 66
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 101-161 2.83e-07

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: 48.93  E-value: 2.83e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124512886 101 SPFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEA-FHILTRAYEELQKDEIKEQY 161
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEkFKEINEAYEVLSDPEKRAAY 62
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 103-161 1.03e-05

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: 46.44  E-value: 1.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886  103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQY 61
 
Name Accession Description Interval E-value
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 102-152 1.60e-09

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: 52.93  E-value: 1.60e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 124512886 102 PFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAA-EAFHILTRAYEEL 152
Cdd:cd06257    2 YYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAeEKFKEINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 101-161 2.16e-09

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: 52.86  E-value: 2.16e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124512886  101 SPFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDK-AAEAFHILTRAYEELQKDEIKEQY 161
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPeAEEKFKEINEAYEVLSDPEKRAIY 62
DnaJ smart00271
DnaJ molecular chaperone homology domain;
101-156 2.46e-09

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 52.62  E-value: 2.46e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 124512886   101 SPFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDK--AAEAFHILTRAYEELQKDE 156
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKeeAEEKFKEINEAYEVLSDPE 59
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 103-161 6.34e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 53.45  E-value: 6.34e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDK-AAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKeSEEKFKEATEAYEILRDPKKRQAY 66
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 101-161 2.83e-07

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: 48.93  E-value: 2.83e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124512886 101 SPFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEA-FHILTRAYEELQKDEIKEQY 161
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEkFKEINEAYEVLSDPEKRAAY 62
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 103-161 4.36e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 51.00  E-value: 4.36e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14298   8 YEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQY 66
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
101-161 6.30e-07

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 46.63  E-value: 6.30e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124512886 101 SPFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDK--AAEAFHILTRAYEELQKDEIKEQY 161
Cdd:COG2214    6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalAEELFQRLNEAYEVLSDPERRAEY 68
PRK14280 PRK14280
molecular chaperone DnaJ;
103-161 1.41e-06

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 49.33  E-value: 1.41e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14280   7 YEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQY 65
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 103-161 3.74e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 47.96  E-value: 3.74e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14292   5 YELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHY 63
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 103-161 4.01e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 47.88  E-value: 4.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEA-FHILTRAYEELQKDEIKEQY 161
Cdd:PRK14281   6 YEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEhFKEVNEAYEVLSNDDKRRRY 65
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 102-160 4.86e-06

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 43.45  E-value: 4.86e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 102 PFEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAE-AFHILTRAYEELQKDEIKEQ 160
Cdd:COG5407    2 PYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEeRFKEINEAYELLSDAEKRAR 61
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 103-161 1.03e-05

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: 46.44  E-value: 1.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886  103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQY 61
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
102-132 2.69e-05

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 41.71  E-value: 2.69e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 124512886 102 PFEIFGIYENINMDLIKSRYRKLSILIHPDK 132
Cdd:COG1076    6 AFELLGLPPDADDAELKRAYRKLQREHHPDR 36
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 103-161 2.74e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 45.22  E-value: 2.74e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEA-FHILTRAYEELQKDEIKEQY 161
Cdd:PRK14284   4 YTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKrFKEVSEAYEVLSDAQKRESY 63
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 103-161 4.72e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 44.76  E-value: 4.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAE-AFHILTRAYEEL---QKDEIKEQY 161
Cdd:PRK14294   7 YEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEeLFKEAAEAYEVLsdpKKRGIYDQY 69
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 103-161 6.64e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 44.21  E-value: 6.64e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEA-FHILTRAYEELQKDEIKEQY 161
Cdd:PRK14285   6 YEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESiFKEATEAYEVLIDDNKRAQY 65
PRK14293 PRK14293
molecular chaperone DnaJ;
103-161 7.06e-05

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 44.21  E-value: 7.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14293   6 YEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARY 64
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 103-161 1.04e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 43.66  E-value: 1.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14283   8 YEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRY 66
PRK14297 PRK14297
molecular chaperone DnaJ;
103-161 1.20e-04

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 43.23  E-value: 1.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEA-FHILTRAYEELQKDEIKEQY 161
Cdd:PRK14297   7 YEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEkFKEINEAYQVLSDPQKKAQY 66
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 103-158 1.81e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 42.82  E-value: 1.81e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEA-FHILTRAYEELqKDEIK 158
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEkFKEIKEAYEVL-SDPQK 62
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 103-161 2.36e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 42.45  E-value: 2.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14291   6 YEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLY 64
PRK14289 PRK14289
molecular chaperone DnaJ;
103-161 2.47e-04

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 42.51  E-value: 2.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEA-FHILTRAYEELQKDEIKEQY 161
Cdd:PRK14289   8 YEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEkFKEAAEAYDVLSDPDKRSRY 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 103-161 3.44e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 42.10  E-value: 3.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEA-FHILTRAYEELQKDEIKEQY 161
Cdd:PRK14277   8 YEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQkFKEINEAYEILSDPQKRAQY 67
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 103-161 6.98e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 40.84  E-value: 6.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14276   7 YDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAY 65
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 103-161 7.88e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 40.76  E-value: 7.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14287   7 YEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHY 65
PRK14295 PRK14295
molecular chaperone DnaJ;
103-161 9.04e-04

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 40.60  E-value: 9.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKID-KAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PRK14295  12 YKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDaKAEERFKEISEAYDVLSDEKKRKEY 71
ThyX COG1351
Thymidylate synthase ThyX, FAD-dependent family [Nucleotide transport and metabolism]; ...
 70-154 1.49e-03

Thymidylate synthase ThyX, FAD-dependent family [Nucleotide transport and metabolism]; Thymidylate synthase ThyX, FAD-dependent family is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440962  Cd Length: 197  Bit Score: 39.12  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886  70 TSNKEKNVEEKKLNKGDAGKEINRILEHKHSSPFE----IFGIyENINMDLIK--------------SRYRKLSIL--IH 129
Cdd:COG1351   24 YSSKSLRELLKELSEEKAEKLIRRLLRHGHESPFEhasfTFAI-EGVSRAVTHqlvrhriasysqqsQRYVKLDDKeyYI 102

                         90       100
                 ....*....|....*....|....*
gi 124512886 130 PDkcKIDKAAEAFHILTRAYEELQK 154
Cdd:COG1351  103 PP--EIAKNEELLEEYEEAMEKAFE 125
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 103-161 1.56e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 39.73  E-value: 1.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKCKIDKAAEA-FHILTRAYEELQKDEIKEQY 161
Cdd:PRK14301   7 YEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQkFKEAAEAYEVLRDAEKRARY 66
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 103-161 3.95e-03

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 38.65  E-value: 3.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 124512886 103 FEIFGIYENINMDLIKSRYRKLSILIHPDKckiDKAAEAFHILTRAYEELQKDEIKEQY 161
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDK---GGDPEKFKEISRAYEVLSDPEKRKIY 86
 
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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