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Conserved domains on  [gi|37362651|ref|NP_011387|]
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U2-type spliceosomal complex subunit CWC23 [Saccharomyces cerevisiae S288C]

Protein Classification

J domain-containing protein( domain architecture ID 10446266)

J domain-containing protein containing a similar domain as DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70.

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
SCOP:  4000605

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
15-84 1.29e-15

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: 69.81  E-value: 1.29e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362651    15 NLYDVLELPTPLDvhtiyDDlpQIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYD 84
Cdd:pfam00226   1 DYYEILGVSPDAS-----DE--EIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
15-84 1.29e-15

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: 69.81  E-value: 1.29e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362651    15 NLYDVLELPTPLDvhtiyDDlpQIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYD 84
Cdd:pfam00226   1 DYYEILGVSPDAS-----DE--EIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
15-76 1.95e-12

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: 60.64  E-value: 1.95e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37362651  15 NLYDVLELPTPLDvhtiyddLPQIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTN 76
Cdd:cd06257   1 DYYDILGVPPDAS-------DEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
15-85 1.15e-11

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: 61.26  E-value: 1.15e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37362651  15 NLYDVLELPTPldvhtiyDDLPQIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDR 85
Cdd:COG0484   1 DYYEILGVSRD-------ASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDR 64
DnaJ smart00271
DnaJ molecular chaperone homology domain;
15-78 7.60e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 56.47  E-value: 7.60e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37362651     15 NLYDVLELPTPLDvhtiyddLPQIKRKYRTLALKYHPDKHPDNPSII-HKFHLLSTATNILTNAD 78
Cdd:smart00271   2 DYYEILGVPRDAS-------LDEIKKAYRKLALKYHPDKNPGDKEEAeEKFKEINEAYEVLSDPE 59
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
37-86 3.90e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 59.76  E-value: 3.90e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14301  20 EIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRF 69
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
15-84 1.29e-15

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: 69.81  E-value: 1.29e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362651    15 NLYDVLELPTPLDvhtiyDDlpQIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYD 84
Cdd:pfam00226   1 DYYEILGVSPDAS-----DE--EIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
15-76 1.95e-12

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: 60.64  E-value: 1.95e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37362651  15 NLYDVLELPTPLDvhtiyddLPQIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTN 76
Cdd:cd06257   1 DYYDILGVPPDAS-------DEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
15-85 1.15e-11

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: 61.26  E-value: 1.15e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37362651  15 NLYDVLELPTPldvhtiyDDLPQIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDR 85
Cdd:COG0484   1 DYYEILGVSRD-------ASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDR 64
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
15-87 5.64e-11

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 57.81  E-value: 5.64e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37362651  15 NLYDVLELPTpldvhtiYDDLPQIKRKYRTLALKYHPDKHPDNPSII-HKFHLLSTATNILTNADVRPHYDRWL 87
Cdd:COG2214   6 DHYAVLGVPP-------DASLEEIRQAYRRLAKLLHPDRGGELKALAeELFQRLNEAYEVLSDPERRAEYDREL 72
DnaJ smart00271
DnaJ molecular chaperone homology domain;
15-78 7.60e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 56.47  E-value: 7.60e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37362651     15 NLYDVLELPTPLDvhtiyddLPQIKRKYRTLALKYHPDKHPDNPSII-HKFHLLSTATNILTNAD 78
Cdd:smart00271   2 DYYEILGVPRDAS-------LDEIKKAYRKLALKYHPDKNPGDKEEAeEKFKEINEAYEVLSDPE 59
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
37-86 3.90e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 59.76  E-value: 3.90e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14301  20 EIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRF 69
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
37-86 4.65e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 59.44  E-value: 4.65e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14281  19 EIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQF 68
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
38-85 9.81e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 58.62  E-value: 9.81e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 37362651   38 IKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDR 85
Cdd:PRK10767  21 IKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYDQ 68
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
37-86 7.61e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 55.67  E-value: 7.61e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDnPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14292  18 EIKSAYRKLALKYHPDRNKE-KGAAEKFAQINEAYAVLSDAEKRAHYDRF 66
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
37-86 2.80e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 54.08  E-value: 2.80e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDnPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14298  21 DIKKAYRKLAMKYHPDKNKE-PDAEEKFKEISEAYAVLSDAEKRAQYDRF 69
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
37-94 5.45e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 53.23  E-value: 5.45e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRWLIEFLRKT 94
Cdd:PRK14294  20 EIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGT 77
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
37-86 1.19e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 52.15  E-value: 1.19e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14284  17 EIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDRY 66
PRK14279 PRK14279
molecular chaperone DnaJ;
37-84 2.63e-07

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 51.27  E-value: 2.63e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYD 84
Cdd:PRK14279  25 EIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
PRK14288 PRK14288
molecular chaperone DnaJ;
14-86 5.91e-07

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 50.07  E-value: 5.91e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37362651   14 LNLYDVLELPTPLDVHTIyddlpqiKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14288   3 LSYYEILEVEKHSNQETI-------KKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRY 68
PRK14297 PRK14297
molecular chaperone DnaJ;
37-86 6.51e-07

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 49.78  E-value: 6.51e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14297  20 EIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQF 69
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
37-86 1.10e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 49.41  E-value: 1.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14277  21 EIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQF 70
PRK14289 PRK14289
molecular chaperone DnaJ;
17-86 1.96e-06

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 48.67  E-value: 1.96e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362651   17 YDVLELPTpldvhTIYDDlpQIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14289   8 YEVLGVSK-----TATVD--EIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQF 70
PRK10266 PRK10266
curved DNA-binding protein;
33-87 4.02e-06

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 47.51  E-value: 4.02e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 37362651   33 DDLPQIKRKYRTLALKYHPD--KHPDNPSiihKFHLLSTATNILTNADVRPHYDR-WL 87
Cdd:PRK10266  16 DDLKTIKTAYRRLARKYHPDvsKEPDAEA---RFKEVAEAWEVLSDEQRRAEYDQlWQ 70
PRK14295 PRK14295
molecular chaperone DnaJ;
37-84 4.84e-06

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 47.15  E-value: 4.84e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYD 84
Cdd:PRK14295  25 EIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYD 72
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
37-84 6.58e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 46.97  E-value: 6.58e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 37362651   37 QIKRKYRTLALKYHPDKHPDnPSIIHKFHLLSTATNILTNADVRPHYD 84
Cdd:PRK14278  19 EIKRAYRKLARELHPDVNPD-EEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
37-86 7.50e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 46.52  E-value: 7.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14285  19 EIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDRF 68
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
3-84 1.09e-05

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 46.35  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37362651    3 GHELEDVINQRLnlYDVLELPTPLDvhtiyddLPQIKRKYRTLALKYHPDKHPDNpsiiHKFHLLSTATNILTNADVRPH 82
Cdd:PTZ00037  19 GRRKREVDNEKL--YEVLNLSKDCT-------TSEIKKAYRKLAIKHHPDKGGDP----EKFKEISRAYEVLSDPEKRKI 85

                 ..
gi 37362651   83 YD 84
Cdd:PTZ00037  86 YD 87
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
34-86 1.15e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 45.97  E-value: 1.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 37362651   34 DLPQIKRKYRTLALKYHPDKHpDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14283  18 DKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYDQF 69
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
37-85 2.84e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 44.92  E-value: 2.84e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDN-PSIIHKFHLLSTATNILTNADVRPHYDR 85
Cdd:PRK14290  19 DIKKAFRELAKKWHPDLHPGNkAEAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
37-86 2.86e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 44.98  E-value: 2.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14286  20 EIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQF 69
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
37-86 3.42e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 44.76  E-value: 3.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPdNPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14291  19 EIKKAYRRLARKYHPDFNK-NPEAEEKFKEINEAYQVLSDPEKRKLYDQF 67
PRK14280 PRK14280
molecular chaperone DnaJ;
37-86 1.01e-04

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 43.17  E-value: 1.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 37362651   37 QIKRKYRTLALKYHPD--KHPDnpsIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14280  20 EIKKAYRKLSKKYHPDinKEEG---ADEKFKEISEAYEVLSDDQKRAQYDQF 68
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
37-86 1.33e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 42.62  E-value: 1.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 37362651   37 QIKRKYRTLALKYHPDKHPDnPSIIHKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14299  20 EIKKAFKKLARKYHPDVNKS-PGAEEKFKEINEAYTVLSDPEKRRIYDTY 68
PRK14293 PRK14293
molecular chaperone DnaJ;
38-85 1.36e-04

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 42.67  E-value: 1.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 37362651   38 IKRKYRTLALKYHPDKHPDnPSIIHKFHLLSTATNILTNADVRPHYDR 85
Cdd:PRK14293  20 LKRAYRRLARKYHPDVNKE-PGAEDRFKEINRAYEVLSDPETRARYDQ 66
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
12-54 1.64e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 39.39  E-value: 1.64e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 37362651  12 QRLNLYDVLELPTPLDvhtiyddLPQIKRKYRTLALKYHPDKH 54
Cdd:COG1076   2 QLDDAFELLGLPPDAD-------DAELKRAYRKLQREHHPDRL 37
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
37-86 3.73e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 41.32  E-value: 3.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 37362651   37 QIKRKYRTLALKYHPDKHPDNPSII-HKFHLLSTATNILTNADVRPHYDRW 86
Cdd:PRK14282  20 EIKRAYKRLVKEWHPDRHPENRKEAeQKFKEIQEAYEVLSDPQKRAMYDRF 70
PHA03102 PHA03102
Small T antigen; Reviewed
16-53 2.93e-03

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 37.34  E-value: 2.93e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 37362651   16 LYDVLELPTpldvhTIYDDLPQIKRKYRTLALKYHPDK 53
Cdd:PHA03102   7 LMDLLGLPR-----SAWGNLPLMRKAYLRKCLEFHPDK 39
 
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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