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Conserved domains on  [gi|3738163|emb|CAA21299|]
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DNAJ protein, splicing factor Spf31 [Schizosaccharomyces pombe]

Protein Classification

J domain-containing protein( domain architecture ID 13623259)

J domain-containing protein similar to Schizosaccharomyces pombe J domain-containing protein Spf31

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
PubMed:  8016869|10542335|35729039|9585179|15170475|9644977
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 ...
 31-93 3.31e-14

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: 64.42  E-value: 3.31e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3738163     31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ super family cl33903
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 31-162 9.42e-06

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


The actual alignment was detected with superfamily member COG0484:

Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 43.92  E-value: 9.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3738163   31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIREsldsAYTAARNQLLKEKKLS 110
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRA----AYDRFGHAAELLLATE 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 3738163  111 PNSEDVHSDQFLFDLKVRWREILIADEVARRRARQLDLANQQREQARQDEIA 162
Cdd:COG0484  77 LAESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELAL 128
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 31-93 3.31e-14

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: 64.42  E-value: 3.31e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3738163     31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 31-83 3.13e-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: 59.10  E-value: 3.13e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 3738163   31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDL 83
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVL 53
DnaJ smart00271
DnaJ molecular chaperone homology domain;
31-87 9.91e-10

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 52.62  E-value: 9.91e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 3738163      31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAAD-AFDILKKAESDLVNDK 87
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEeKFKEINEAYEVLSDPE 59
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 29-80 1.28e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 50.90  E-value: 1.28e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 3738163    29 KLNAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNP-------KAADAFDILKKAE 80
Cdd:PRK14301   3 QRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPeaeqkfkEAAEAYEVLRDAE 61
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 31-73 2.21e-07

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 46.15  E-value: 2.21e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 3738163   31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAF 73
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERF 43
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 31-162 9.42e-06

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: 43.92  E-value: 9.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3738163   31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIREsldsAYTAARNQLLKEKKLS 110
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRA----AYDRFGHAAELLLATE 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 3738163  111 PNSEDVHSDQFLFDLKVRWREILIADEVARRRARQLDLANQQREQARQDEIA 162
Cdd:COG0484  77 LAESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELAL 128
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 33-82 4.12e-04

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: 40.28  E-value: 4.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3738163     33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDnPKAAD-------AFDIL----KKAESD 82
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD-KEAEEkfkeineAYEVLsdpeKRAQYD 62
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 31-93 3.31e-14

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: 64.42  E-value: 3.31e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3738163     31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 31-83 3.13e-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: 59.10  E-value: 3.13e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 3738163   31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDL 83
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVL 53
DnaJ smart00271
DnaJ molecular chaperone homology domain;
31-87 9.91e-10

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 52.62  E-value: 9.91e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 3738163      31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAAD-AFDILKKAESDLVNDK 87
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEeKFKEINEAYEVLSDPE 59
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 29-80 1.28e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 50.90  E-value: 1.28e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 3738163    29 KLNAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNP-------KAADAFDILKKAE 80
Cdd:PRK14301   3 QRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPeaeqkfkEAAEAYEVLRDAE 61
PRK14295 PRK14295
molecular chaperone DnaJ;
33-95 1.69e-07

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 50.62  E-value: 1.69e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3738163    33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLDSA 95
Cdd:PRK14295  12 YKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDEA 74
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 31-73 2.21e-07

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 46.15  E-value: 2.21e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 3738163   31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAF 73
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERF 43
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 29-93 3.14e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 49.60  E-value: 3.14e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3738163    29 KLNAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:PRK14285   2 KRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 29-93 4.87e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 49.04  E-value: 4.87e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3738163    29 KLNAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:PRK14281   2 KRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYD 66
PRK14289 PRK14289
molecular chaperone DnaJ;
29-76 1.71e-06

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 47.52  E-value: 1.71e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 3738163    29 KLNAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKA-------ADAFDIL 76
Cdd:PRK14289   4 KRDYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAeekfkeaAEAYDVL 58
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 33-93 2.79e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 46.91  E-value: 2.79e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3738163    33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYD 67
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 33-93 2.82e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 46.76  E-value: 2.82e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3738163    33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:PRK14284   4 YTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 33-93 4.01e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 46.38  E-value: 4.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3738163    33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDnPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:PRK14298   8 YEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE-PDAEEKFKEISEAYAVLSDAEKRAQYD 67
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 31-162 9.42e-06

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: 43.92  E-value: 9.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3738163   31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIREsldsAYTAARNQLLKEKKLS 110
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRA----AYDRFGHAAELLLATE 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 3738163  111 PNSEDVHSDQFLFDLKVRWREILIADEVARRRARQLDLANQQREQARQDEIA 162
Cdd:COG0484  77 LAESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELAL 128
PRK14297 PRK14297
molecular chaperone DnaJ;
33-82 3.10e-05

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 43.62  E-value: 3.10e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3738163    33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAA-------DAFDIL----KKAESD 82
Cdd:PRK14297   7 YEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEekfkeinEAYQVLsdpqKKAQYD 67
PRK14279 PRK14279
molecular chaperone DnaJ;
33-93 1.08e-04

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 42.03  E-value: 1.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3738163    33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:PRK14279  12 YKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
31-103 1.36e-04

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 39.32  E-value: 1.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3738163   31 NAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAAD--------AFDILKK----AESDLVNDKIRESLDSAYTA 98
Cdd:COG2214   6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEelfqrlneAYEVLSDperrAEYDRELGQSGKGSASQPSA 85


                ....*
gi 3738163   99 ARNQL 103
Cdd:COG2214  86 AAQRL 90
PRK14280 PRK14280
molecular chaperone DnaJ;
29-93 1.59e-04

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 41.63  E-value: 1.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3738163    29 KLNAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDnPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:PRK14280   3 KRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKE-EGADEKFKEISEAYEVLSDDQKRAQYD 66
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 29-79 2.07e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 41.28  E-value: 2.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 3738163    29 KLNAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKA 79
Cdd:PRK10767   3 KRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEA 53
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 33-98 2.09e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 41.41  E-value: 2.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3738163    33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDnPKAADAFDILKKAESDLVNDKIRESLDSAYTA 98
Cdd:PRK14292   5 YELLGVSRTASADEIKSAYRKLALKYHPDRNKE-KGAAEKFAQINEAYAVLSDAEKRAHYDRFGTA 69
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 33-82 4.12e-04

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: 40.28  E-value: 4.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3738163     33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDnPKAAD-------AFDIL----KKAESD 82
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD-KEAEEkfkeineAYEVLsdpeKRAQYD 62
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 29-102 6.50e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 39.99  E-value: 6.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3738163    29 KLNAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDnPKAADAFDILKKAESDLVNDKIRESLDSAYTAARNQ 102
Cdd:PRK14287   3 KRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKA-PDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTDPNQ 75
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 33-102 2.67e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 38.15  E-value: 2.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3738163    33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDnPKAADAFDILKKAESDLVNDKIRESLDSAYTAARNQ 102
Cdd:PRK14276   7 YDRLGVSKDASQDEIKKAYRKLSKKYHPDINKE-PGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANG 75
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 33-93 2.90e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 37.82  E-value: 2.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3738163    33 YDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLD 93
Cdd:PRK14294   7 YEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYD 67
PRK14288 PRK14288
molecular chaperone DnaJ;
29-102 3.84e-03

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 37.36  E-value: 3.84e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3738163    29 KLNAYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAADAFDILKKAESDLVNDKIRESLDSAYTAARNQ 102
Cdd:PRK14288   2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQ 75
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 17-99 8.77e-03

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 36.34  E-value: 8.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3738163    17 RGREIDrilsSFKLnaYDVLDILPGMSVDDIRNLYRKKSLMIHPDKNRDNPKAAD---AFDILKKAESDLVNDKI-RESL 92
Cdd:PTZ00037  21 RKREVD----NEKL--YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEKFKEisrAYEVLSDPEKRKIYDEYgEEGL 94


                 ....*..
gi 3738163    93 DSAYTAA 99
Cdd:PTZ00037  95 EGGEQPA 101
 
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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