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Conserved domains on  [gi|24431939|ref|NP_079178|]
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dnaJ homolog subfamily C member 22 [Homo sapiens]

Protein Classification

J domain-containing protein( domain architecture ID 10644999)

J domain-containing protein similar to the N-terminal conserved domain (called J domain) of DnaJ-like proteins, which is involved in regulating the ATPase activity of heat shock protein 70 (Hsp70) by ATP hydrolysis

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ smart00271
DnaJ molecular chaperone homology domain;
278-335 3.09e-18

DnaJ molecular chaperone homology domain;


:

Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 77.27  E-value: 3.09e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24431939    278 AYQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:smart00271   3 YYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
 
Name Accession Description Interval E-value
DnaJ smart00271
DnaJ molecular chaperone homology domain;
278-335 3.09e-18

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 77.27  E-value: 3.09e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24431939    278 AYQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:smart00271   3 YYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 279-335 5.78e-18

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: 79.36  E-value: 5.78e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939 279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:COG0484   3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD-PEAEEKFKEINEAYEVLSDPEK 58
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 279-335 3.56e-17

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: 74.43  E-value: 3.56e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939   279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:pfam00226   3 YEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD-PEAEEKFKEINEAYEVLSDPEK 58
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 279-335 7.85e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 80.61  E-value: 7.85e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14282   7 YEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQK 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 279-331 3.84e-16

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: 71.42  E-value: 3.84e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24431939 279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQtEEAQRHFLEIQAAYEVLS 331
Cdd:cd06257   3 YDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLS 54
 
Name Accession Description Interval E-value
DnaJ smart00271
DnaJ molecular chaperone homology domain;
278-335 3.09e-18

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 77.27  E-value: 3.09e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 24431939    278 AYQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:smart00271   3 YYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 279-335 5.78e-18

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: 79.36  E-value: 5.78e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939 279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:COG0484   3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD-PEAEEKFKEINEAYEVLSDPEK 58
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 279-335 3.56e-17

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: 74.43  E-value: 3.56e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939   279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:pfam00226   3 YEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD-PEAEEKFKEINEAYEVLSDPEK 58
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
278-335 4.40e-17

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 75.14  E-value: 4.40e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24431939 278 AYQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:COG2214   7 HYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPER 64
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 279-335 7.85e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 80.61  E-value: 7.85e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14282   7 YEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQK 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 279-331 3.84e-16

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: 71.42  E-value: 3.84e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24431939 279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQtEEAQRHFLEIQAAYEVLS 331
Cdd:cd06257   3 YDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLS 54
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 279-335 2.24e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 70.08  E-value: 2.24e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDqtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14278   6 YGLLGVSRNASDAEIKRAYRKLARELHPDVNPD--EEAQEKFKEISVAYEVLSDPEK 60
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 279-335 4.29e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 69.19  E-value: 4.29e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14290   6 YKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQK 62
PRK14280 PRK14280
molecular chaperone DnaJ;
279-335 3.47e-12

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 66.67  E-value: 3.47e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNldQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14280   7 YEVLGVSKSASKDEIKKAYRKLSKKYHPDIN--KEEGADEKFKEISEAYEVLSDDQK 61
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 279-335 6.36e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 65.98  E-value: 6.36e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTeEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14277   8 YEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDK-EAEQKFKEINEAYEILSDPQK 63
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 279-335 1.54e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 64.79  E-value: 1.54e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQteEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14291   6 YEILGVSRNATQEEIKKAYRRLARKYHPDFNKNP--EAEEKFKEINEAYQVLSDPEK 60
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 279-335 2.23e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 64.01  E-value: 2.23e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQK 62
PRK14297 PRK14297
molecular chaperone DnaJ;
279-335 1.05e-10

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 62.11  E-value: 1.05e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTeEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14297   7 YEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNK-EAEEKFKEINEAYQVLSDPQK 62
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
278-334 1.64e-10

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 56.34  E-value: 1.64e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24431939 278 AYQVLGLSEGATNEEIHRSYQELVKVWHPD-HNLDQTEEAQRHFLE----IQAAYEVLSQPR 334
Cdd:COG1076   6 AFELLGLPPDADDAELKRAYRKLQREHHPDrLAAGLPEEEQRLALQkaaaINEAYETLKDPR 67
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 279-335 2.09e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 61.40  E-value: 2.09e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTeEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14284   4 YTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDA-EAEKRFKEVSEAYEVLSDAQK 59
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 279-335 2.42e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 60.98  E-value: 2.42e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14281   6 YEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDN-KEAEEHFKEVNEAYEVLSNDDK 61
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 279-335 1.02e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 58.80  E-value: 1.02e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDqtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14299   7 YAILGVPKNASQDEIKKAFKKLARKYHPDVNKS--PGAEEKFKEINEAYTVLSDPEK 61
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 279-335 2.95e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 57.69  E-value: 2.95e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNlDQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKN-KGNKESEEKFKEATEAYEILRDPKK 62
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 279-335 2.96e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 57.79  E-value: 2.96e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDhnLDQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14276   7 YDRLGVSKDASQDEIKKAYRKLSKKYHPD--INKEPGAEEKYKEVQEAYETLSDPQK 61
PRK14295 PRK14295
molecular chaperone DnaJ;
279-335 4.12e-09

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 57.55  E-value: 4.12e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRhFLEIQAAYEVLSQPRK 335
Cdd:PRK14295  12 YKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEER-FKEISEAYDVLSDEKK 67
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 279-335 4.40e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 57.06  E-value: 4.40e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRhFLEIQAAYEVLSQPRK 335
Cdd:PRK14301   7 YEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQK-FKEAAEAYEVLRDAEK 62
PRK14293 PRK14293
molecular chaperone DnaJ;
279-333 6.90e-09

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 56.54  E-value: 6.90e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTeeAQRHFLEIQAAYEVLSQP 333
Cdd:PRK14293   6 YEILGVSRDADKDELKRAYRRLARKYHPDVNKEPG--AEDRFKEINRAYEVLSDP 58
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 279-335 1.26e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 56.01  E-value: 1.26e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDqtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14298   8 YEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE--PDAEEKFKEISEAYAVLSDAEK 62
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 279-335 1.53e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 55.38  E-value: 1.53e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14285   6 YEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGN-KEAESIFKEATEAYEVLIDDNK 61
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 279-335 3.79e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 54.24  E-value: 3.79e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNldQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14287   7 YEVLGVDRNASVDEVKKAYRKLARKYHPDVN--KAPDAEDKFKEVKEAYDTLSDPQK 61
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 273-335 4.98e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 54.00  E-value: 4.98e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24431939  273 EKRQLaYQVLGLSEGATNEEIHRSYQELVKVWHPDHNlDQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14294   2 VKRDY-YEILGVTRDASEEEIKKSYRKLAMKYHPDRN-PGDKEAEELFKEAAEAYEVLSDPKK 62
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 273-335 8.60e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 53.29  E-value: 8.60e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24431939  273 EKRQLaYQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDqtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14283   3 EKRDY-YEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE--EGAEEKFKEISEAYAVLSDDEK 62
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 276-335 9.21e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 53.09  E-value: 9.21e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24431939  276 QLAYQVLGLSEGATNEEIHRSYQELVKVWHPDHNldQTEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14300   3 QDYYQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKDEQK 60
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 279-335 2.11e-07

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 52.13  E-value: 2.11e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEeaqrhFLEIQAAYEVLSQPRK 335
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEK-----FKEISRAYEVLSDPEK 82
PRK14279 PRK14279
molecular chaperone DnaJ;
279-335 3.97e-07

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 51.27  E-value: 3.97e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQTEEAQRhFLEIQAAYEVLSQPRK 335
Cdd:PRK14279  12 YKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEER-FKAVSEAHDVLSDPAK 67
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 274-330 3.73e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 48.02  E-value: 3.73e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  274 KRQLAYQVLGLSEGATNEEIHRSYQELVKVWHPDhnLDQTEEAQRHFLEIQAAYEVL 330
Cdd:PRK14296   2 KKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPD--LNKSPDAHDKMVEINEAADVL 56
djlA PRK09430
co-chaperone DjlA;
278-330 1.19e-05

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 45.96  E-value: 1.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24431939  278 AYQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQ----------TEEAQrhflEIQAAYEVL 330
Cdd:PRK09430 202 AYKVLGVSESDDDQEIKRAYRKLMSEHHPDKLVAKglppemmemaKEKAQ----EIQAAYELI 260
PRK14288 PRK14288
molecular chaperone DnaJ;
279-335 5.86e-04

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 41.21  E-value: 5.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24431939  279 YQVLGLSEGATNEEIHRSYQELVKVWHPDHNLDQtEEAQRHFLEIQAAYEVLSQPRK 335
Cdd:PRK14288   6 YEILEVEKHSNQETIKKSYRKLALKYHPDRNAGD-KEAEEKFKLINEAYGVLSDEKK 61
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 268-335 1.16e-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: 40.40  E-value: 1.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24431939 268 HSFQDEKRQLAYQVLGLSE---GATNEEIHRSYQELVKVWHPDHNLDQTEEAQRH-FLEIQAAYEVLSQPRK 335
Cdd:COG5269  35 EDFKNWKKVDLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEfFKLIQKAREVLGDRKL 106
 
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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