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Conserved domains on  [gi|488296884|ref|WP_002368092|]
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MULTISPECIES: J domain-containing protein [Bacteria]

Protein Classification

J domain-containing protein( domain architecture ID 11422315)

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
SCOP:  4000605

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
9-50 2.05e-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: 47.77  E-value: 2.05e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKE----MAQINNEYEALFDKLK 50
Cdd:COG0484   13 SAEEIKKAYRKLAKKYHPDRNPGDPEaeekFKEINEAYEVLSDPEK 58
 
Name Accession Description Interval E-value
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
9-50 2.05e-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: 47.77  E-value: 2.05e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKE----MAQINNEYEALFDKLK 50
Cdd:COG0484   13 SAEEIKKAYRKLAKKYHPDRNPGDPEaeekFKEINEAYEVLSDPEK 58
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
9-50 2.41e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 49.03  E-value: 2.41e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKEMAQ----INNEYEALFDKLK 50
Cdd:PRK14277  18 TEEEIKKAYRRLAKKYHPDLNPGDKEAEQkfkeINEAYEILSDPQK 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
9-50 2.86e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 45.30  E-value: 2.86e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 488296884     9 TLEELKRVYKKLALKYHPDMGGTDKEMA-----QINNEYEALFDKLK 50
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
9-47 1.13e-06

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: 43.69  E-value: 1.13e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKE----MAQINNEYEALFD 47
Cdd:cd06257   13 SDEEIKKAYRKLALKYHPDKNPDDPEaeekFKEINEAYEVLSD 55
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
9-50 3.15e-06

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: 42.46  E-value: 3.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 488296884    9 TLEELKRVYKKLALKYHPDMGGTDKEMA----QINNEYEALFDKLK 50
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPGDPEAEekfkEINEAYEVLSDPEK 58
 
Name Accession Description Interval E-value
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
9-50 2.05e-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: 47.77  E-value: 2.05e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKE----MAQINNEYEALFDKLK 50
Cdd:COG0484   13 SAEEIKKAYRKLAKKYHPDRNPGDPEaeekFKEINEAYEVLSDPEK 58
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
9-50 2.41e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 49.03  E-value: 2.41e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKEMAQ----INNEYEALFDKLK 50
Cdd:PRK14277  18 TEEEIKKAYRRLAKKYHPDLNPGDKEAEQkfkeINEAYEILSDPQK 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
9-50 2.86e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 45.30  E-value: 2.86e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 488296884     9 TLEELKRVYKKLALKYHPDMGGTDKEMA-----QINNEYEALFDKLK 50
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
9-47 1.13e-06

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: 43.69  E-value: 1.13e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKE----MAQINNEYEALFD 47
Cdd:cd06257   13 SDEEIKKAYRKLALKYHPDKNPDDPEaeekFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
11-50 1.29e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 46.68  E-value: 1.29e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488296884  11 EELKRVYKKLALKYHPDMGGTDKEMAQ----INNEYEALFDKLK 50
Cdd:PRK10767  19 DEIKKAYRKLAMKYHPDRNPGDKEAEEkfkeIKEAYEVLSDPQK 62
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
11-58 1.57e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 46.81  E-value: 1.57e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488296884  11 EELKRVYKKLALKYHPDMG---GTDKEMAQINNEYEALFDKLKNTHKNKEG 58
Cdd:PRK14292  17 DEIKSAYRKLALKYHPDRNkekGAAEKFAQINEAYAVLSDAEKRAHYDRFG 67
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
9-59 2.60e-06

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 45.97  E-value: 2.60e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKEMAQINNEYEALFDKLKNTHKNKEGE 59
Cdd:PTZ00037  41 TTSEIKKAYRKLAIKHHPDKGGDPEKFKEISRAYEVLSDPEKRKIYDEYGE 91
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
9-50 3.15e-06

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: 42.46  E-value: 3.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 488296884    9 TLEELKRVYKKLALKYHPDMGGTDKEMA----QINNEYEALFDKLK 50
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPGDPEAEekfkEINEAYEVLSDPEK 58
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
11-50 3.47e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 45.46  E-value: 3.47e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488296884  11 EELKRVYKKLALKYHPDMG---GTDKEMAQINNEYEALFDKLK 50
Cdd:PRK14276  19 DEIKKAYRKLSKKYHPDINkepGAEEKYKEVQEAYETLSDPQK 61
PRK14293 PRK14293
molecular chaperone DnaJ;
11-47 3.59e-06

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 45.37  E-value: 3.59e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 488296884  11 EELKRVYKKLALKYHPDMG---GTDKEMAQINNEYEALFD 47
Cdd:PRK14293  18 DELKRAYRRLARKYHPDVNkepGAEDRFKEINRAYEVLSD 57
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
9-73 6.70e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 44.54  E-value: 6.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488296884   9 TLEELKRVYKKLALKYHPDMG---GTDKEMAQINNEYEALFDKLKNTHKNKEGeyyqkeTTETPQEWQ 73
Cdd:PRK14299  17 SQDEIKKAFKKLARKYHPDVNkspGAEEKFKEINEAYTVLSDPEKRRIYDTYG------TTAASAGWQ 78
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
5-50 9.97e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 44.37  E-value: 9.97e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488296884   5 KDVTTlEELKRVYKKLALKYHPDMGGTDKEMAQINNE----YEALFDKLK 50
Cdd:PRK14294  14 RDASE-EEIKKSYRKLAMKYHPDRNPGDKEAEELFKEaaeaYEVLSDPKK 62
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
11-45 1.06e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 44.41  E-value: 1.06e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 488296884  11 EELKRVYKKLALKYHPDMGGTDKE----MAQINNEYEAL 45
Cdd:PRK14281  18 DEIKKAYRKLALKYHPDKNPDNKEaeehFKEVNEAYEVL 56
PRK14297 PRK14297
molecular chaperone DnaJ;
11-50 1.54e-05

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 43.62  E-value: 1.54e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488296884  11 EELKRVYKKLALKYHPDMGGTDKE----MAQINNEYEALFDKLK 50
Cdd:PRK14297  19 DEIKKAFRKLAIKYHPDKNKGNKEaeekFKEINEAYQVLSDPQK 62
PRK14280 PRK14280
molecular chaperone DnaJ;
11-58 1.68e-05

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 43.56  E-value: 1.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488296884  11 EELKRVYKKLALKYHPDMG---GTDKEMAQINNEYEALFDKLKNTHKNKEG 58
Cdd:PRK14280  19 DEIKKAYRKLSKKYHPDINkeeGADEKFKEISEAYEVLSDDQKRAQYDQFG 69
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
9-50 3.81e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 42.52  E-value: 3.81e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTD----KEMAQINNEYEALFDKLK 50
Cdd:PRK14284  14 SPEEIKKAYRKLAVKYHPDKNPGDaeaeKRFKEVSEAYEVLSDAQK 59
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
5-58 4.98e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 42.14  E-value: 4.98e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488296884   5 KDVTTlEELKRVYKKLALKYHPDMG---GTDKEMAQINNEYEALFDKLKNTHKNKEG 58
Cdd:PRK14298  15 KDASV-EDIKKAYRKLAMKYHPDKNkepDAEEKFKEISEAYAVLSDAEKRAQYDRFG 70
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
11-63 4.99e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 42.28  E-value: 4.99e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488296884  11 EELKRVYKKLALKYHPDMGGTDKEMAQINNEYEALFDKLKNTHKNKEGEYYQK 63
Cdd:PRK14286  19 EEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGK 71
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
9-50 1.13e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 41.19  E-value: 1.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKEMA---QINNEYEALFDKLK 50
Cdd:PRK14278  16 SDAEIKRAYRKLARELHPDVNPDEEAQEkfkEISVAYEVLSDPEK 60
PRK14289 PRK14289
molecular chaperone DnaJ;
9-62 1.72e-04

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 40.58  E-value: 1.72e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKEMAQINNEYEALFDKLKNThkNKEGEYYQ 62
Cdd:PRK14289  18 TVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDP--DKRSRYDQ 69
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
11-54 1.76e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 40.50  E-value: 1.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488296884  11 EELKRVYKKLALKYHPDMGGTDKEMAQINNEYEALFDKLKNTHK 54
Cdd:PRK14301  19 DEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEK 62
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
9-58 3.13e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 39.99  E-value: 3.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488296884   9 TLEELKRVYKKLALKYHPDMG---GTDKEMAQINNEYEALFDKLKNTHKNKEG 58
Cdd:PRK14287  17 SVDEVKKAYRKLARKYHPDVNkapDAEDKFKEVKEAYDTLSDPQKKAHYDQFG 69
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
9-50 3.70e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 39.75  E-value: 3.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488296884   9 TLEELKRVYKKLALKYHPDMG---GTDKEMAQINNEYEALFDKLK 50
Cdd:PRK14291  16 TQEEIKKAYRRLARKYHPDFNknpEAEEKFKEINEAYQVLSDPEK 60
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
11-58 3.99e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 39.59  E-value: 3.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488296884  11 EELKRVYKKLALKYHPDMGGTDKEMAQINNE----YEALFDKLKNTHKNKEG 58
Cdd:PRK14285  18 DEIKKAYRKIAIKYHPDKNKGNKEAESIFKEateaYEVLIDDNKRAQYDRFG 69
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
4-58 6.45e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 39.16  E-value: 6.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488296884   4 IKDVTTLEELKRVYKKLALKYHPDMG---GTDKEMAQINNEYEALFDKLKNTHKNKEG 58
Cdd:PRK14296  12 VSKTASEQEIRQAYRKLAKQYHPDLNkspDAHDKMVEINEAADVLLDKDKRKQYDQFG 69
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
9-45 7.27e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 36.31  E-value: 7.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488296884   9 TLEELKRVYKKLALKYHPD--MGGTDKEM--------AQINNEYEAL 45
Cdd:COG1076   17 DDAELKRAYRKLQREHHPDrlAAGLPEEEqrlalqkaAAINEAYETL 63
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
12-58 8.64e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 38.46  E-value: 8.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488296884  12 ELKRVYKKLALKYHPD---MGGTDKEMAQINNEYEALFDKLKNTHKNKEG 58
Cdd:PRK14300  19 DLKKAYLKLAKQYHPDttdAKDAEKKFKEINAAYDVLKDEQKRAAYDRFG 68
PRK14288 PRK14288
molecular chaperone DnaJ;
11-59 1.05e-03

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 38.52  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488296884  11 EELKRVYKKLALKYHPDMGGTDKEMAQ----INNEYEALFDKLKNTHKNKEGE 59
Cdd:PRK14288  18 ETIKKSYRKLALKYHPDRNAGDKEAEEkfklINEAYGVLSDEKKRALYDRYGK 70
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
9-66 1.06e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 38.24  E-value: 1.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKEMAQ-----INNEYEALFDKLKNTHKNK-----EGEYYQKETT 66
Cdd:PRK14282  17 TQEEIKRAYKRLVKEWHPDRHPENRKEAEqkfkeIQEAYEVLSDPQKRAMYDRfgyvgEQPPYQETES 84
PRK14295 PRK14295
molecular chaperone DnaJ;
5-57 1.27e-03

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 38.29  E-value: 1.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488296884   5 KDVTTlEELKRVYKKLALKYHPDMGGTDKEMAQINNEYEALFDKLKNTHKNKE 57
Cdd:PRK14295  19 KDATE-AEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKE 70
PHA03102 PHA03102
Small T antigen; Reviewed
9-59 1.84e-03

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 36.96  E-value: 1.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488296884   9 TLEELKRVYKKLALKYHPDMGGTDKEMAQINNEYEALFDKLKNTHKNKEGE 59
Cdd:PHA03102  20 NLPLMRKAYLRKCLEFHPDKGGDEEKMKELNTLYKKFRESVKSLRDLDGEE 70
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
11-50 3.14e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 37.11  E-value: 3.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488296884  11 EELKRVYKKLALKYHPDMG---GTDKEMAQINNEYEALFDKLK 50
Cdd:PRK14283  20 KEIKKAYRKLARKYHPDVSeeeGAEEKFKEISEAYAVLSDDEK 62
 
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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