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Conserved domains on  [gi|2025811512|ref|XP_040594068|]
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dnaJ homolog subfamily B member 6 [Mesocricetus auratus]

Protein Classification

molecular chaperone DnaJ( domain architecture ID 1000952)

molecular chaperone DnaJ, part of the DnaK-DnaJ-GrpE system, prevents the aggregation of unfolded substrate and acts primarily by stimulating the ATPase activity of Hsp70

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10767 super family cl35946
chaperone protein DnaJ; Provisional
3-108 6.34e-40

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK10767:

Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 141.05  E-value: 6.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGs 82
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDK-EAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGGGGG- 82
                          90       100
                  ....*....|....*....|....*.
gi 2025811512  83 hFDSPFEFGFTFrnpDDVFREFFGGR 108
Cdd:PRK10767   83 -FGGGGGFGDIF---GDIFGDIFGGG 104
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
3-108 6.34e-40

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 141.05  E-value: 6.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGs 82
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDK-EAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGGGGG- 82
                          90       100
                  ....*....|....*....|....*.
gi 2025811512  83 hFDSPFEFGFTFrnpDDVFREFFGGR 108
Cdd:PRK10767   83 -FGGGGGFGDIF---GDIFGDIFGGG 104
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
3-107 3.49e-39

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: 138.89  E-value: 3.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGG 78
                          90       100
                  ....*....|....*....|....*
gi 2025811512  83 HFdSPFEFGFtFRNPDDVFREFFGG 107
Cdd:TIGR02349  79 GF-NGFDIGF-FGDFGDIFGDFFGG 101
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
3-74 9.07e-37

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: 126.36  E-value: 9.07e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLN 74
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDP-EAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL 71
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
3-66 1.52e-36

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: 123.35  E-value: 1.52e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDP-EAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-61 2.09e-31

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 110.02  E-value: 2.09e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512    2 VDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKK 61
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
3-58 1.86e-28

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: 102.24  E-value: 1.86e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENkEEAERKFKQVAEAYEVLSD 58
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
3-107 7.26e-28

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 109.91  E-value: 7.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLngggggggs 82
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKA--PDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGV--------- 74
                          90       100
                  ....*....|....*....|....*
gi 2025811512  83 hfDSPFEFGFtfrNPDDVFREFFGG 107
Cdd:NF037946   75 --DGEGGFGF---DAFDVFSSFFET 94
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
3-108 6.34e-40

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 141.05  E-value: 6.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGs 82
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDK-EAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGGGGG- 82
                          90       100
                  ....*....|....*....|....*.
gi 2025811512  83 hFDSPFEFGFTFrnpDDVFREFFGGR 108
Cdd:PRK10767   83 -FGGGGGFGDIF---GDIFGDIFGGG 104
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
3-107 3.49e-39

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: 138.89  E-value: 3.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGG 78
                          90       100
                  ....*....|....*....|....*
gi 2025811512  83 HFdSPFEFGFtFRNPDDVFREFFGG 107
Cdd:TIGR02349  79 GF-NGFDIGF-FGDFGDIFGDFFGG 101
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
3-74 9.07e-37

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: 126.36  E-value: 9.07e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLN 74
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDP-EAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL 71
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
3-66 1.52e-36

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: 123.35  E-value: 1.52e-36
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDP-EAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
3-106 4.00e-36

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 131.04  E-value: 4.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEeAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:PRK14294    5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKE-AEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGTGFSGFS 83
                          90       100
                  ....*....|....*....|....*
gi 2025811512  83 HFDSPF-EFGftfrnpdDVFREFFG 106
Cdd:PRK14294   84 GFDDIFsSFG-------DIFEDFFG 101
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-61 2.09e-31

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 110.02  E-value: 2.09e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512    2 VDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKK 61
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
3-106 2.46e-31

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 118.31  E-value: 2.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNggGGGGGS 82
Cdd:PRK14301    5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDN-PEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVN--GNGGFG 81
                          90       100
                  ....*....|....*....|....
gi 2025811512  83 HFDSPFEFgftFRNPDDVFREFFG 106
Cdd:PRK14301   82 GFSSAEDI---FSHFSDIFGDLFG 102
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
3-108 3.51e-31

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 117.97  E-value: 3.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEG---LNGGGGG 79
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGeqpPYQETES 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 2025811512  80 GGSHFDSPF-EFGFTFRNpdDVFREFFGGR 108
Cdd:PRK14282   85 GGGFFEDIFkDFENIFNR--DIFDIFFGER 112
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
3-107 6.62e-30

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 114.26  E-value: 6.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGggggs 82
Cdd:PRK14290    4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYDQTGTVDFGAGG----- 78
                          90       100
                  ....*....|....*....|....*..
gi 2025811512  83 hfdSPFEF-GFT-FRNPDDVFREFFGG 107
Cdd:PRK14290   79 ---SNFNWdNFThFSDINDIFNQIFGG 102
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
3-107 1.66e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 113.78  E-value: 1.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:PRK14284    2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDA-EAEKRFKEVSEAYEVLSDAQKRESYDRYGKDGPFAGAGGFGG 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2025811512  83 HFDSPFE---------FGFTFRNPDDVFREFFGG 107
Cdd:PRK14284   81 AGMGNMEdalrtfmgaFGGEFGGGGSFFEGLFGG 114
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
3-107 4.27e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 112.56  E-value: 4.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGgs 82
Cdd:PRK14291    4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKN--PEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAFSGSGQQQ-- 79
                          90       100
                  ....*....|....*....|....*
gi 2025811512  83 hFDSPFEFGFTFRNPDDVFREFFGG 107
Cdd:PRK14291   80 -QGQEGFSDFGGGNIEDILEDVFDI 103
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
3-58 1.86e-28

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: 102.24  E-value: 1.86e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENkEEAERKFKQVAEAYEVLSD 58
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
PRK14280 PRK14280
molecular chaperone DnaJ;
3-110 2.37e-28

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 110.20  E-value: 2.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:PRK14280    5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKE--EGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGGGGF 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2025811512  83 HfDSPFEFGFTFrnpDDVFREFFGG----RDP 110
Cdd:PRK14280   83 G-GGDFGGGFGF---EDIFSSFFGGggrrRDP 110
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
3-107 2.49e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 110.32  E-value: 2.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLngggggggs 82
Cdd:PRK14298    6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE--PDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGI--------- 74
                          90       100       110
                  ....*....|....*....|....*....|
gi 2025811512  83 hfDSPFEFGFTFRNPD-----DVFREFFGG 107
Cdd:PRK14298   75 --DNQYSAEDIFRGADfggfgDIFEMFFGG 102
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
3-110 4.89e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 109.41  E-value: 4.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:PRK14276    5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKE--PGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFGGGAG 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2025811512  83 HFdSPFEFGFTFRNPDDVFREFFGG----RDP 110
Cdd:PRK14276   83 GF-GGFDGSGGFGGFEDIFSSFFGGggarRNP 113
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
3-107 7.26e-28

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 109.91  E-value: 7.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLngggggggs 82
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKA--PDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGV--------- 74
                          90       100
                  ....*....|....*....|....*
gi 2025811512  83 hfDSPFEFGFtfrNPDDVFREFFGG 107
Cdd:NF037946   75 --DGEGGFGF---DAFDVFSSFFET 94
PRK14289 PRK14289
molecular chaperone DnaJ;
3-154 4.21e-27

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 107.22  E-value: 4.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGs 82
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDK-EAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVGGAAGGGG- 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2025811512  83 hfdspfeFGFTFRNPDDVFREF---FGGrdpfsfdffedpfddffgsrrgsrgnrsrgtgsFFSAFSGFPAFGGG 154
Cdd:PRK14289   84 -------FSGEGMSMEDIFSMFgdiFGG---------------------------------HGGGFGGFGGFGGG 118
PRK14297 PRK14297
molecular chaperone DnaJ;
3-107 5.38e-27

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 106.79  E-value: 5.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:PRK14297    5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNK-EAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGAGGFGSG 83
                          90       100
                  ....*....|....*....|....*
gi 2025811512  83 HFDSpFEFgFTFRNPDDVFREFFGG 107
Cdd:PRK14297   84 GFGG-FDF-SDMGGFGDIFDSFFGG 106
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
3-73 8.72e-27

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 106.43  E-value: 8.72e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGL 73
Cdd:PRK14281    4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNK-EAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAGV 73
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
3-62 1.26e-26

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 97.76  E-value: 1.26e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKR 62
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDP-KAEERFKEINEAYELLSDAEKR 59
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
3-106 1.45e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 105.65  E-value: 1.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:PRK14277    6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDK-EAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFDPGGFGQGG 84
                          90       100
                  ....*....|....*....|....*..
gi 2025811512  83 HFDSPFE---FGFTFRNPDDVFREFFG 106
Cdd:PRK14277   85 FGQGGFGgggFDFDFGGFGDIFEDIFG 111
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
1-66 1.63e-26

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 98.25  E-value: 1.63e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2025811512   1 MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:COG2214     4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
4-107 3.24e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 104.69  E-value: 3.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   4 YYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEeAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGSh 83
Cdd:PRK14286    6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKE-SEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGGFGQ- 83
                          90       100
                  ....*....|....*....|....
gi 2025811512  84 fDSPFEFGFTFRNPDDVFREFFGG 107
Cdd:PRK14286   84 -GAYTDFSDIFGDFGDIFGDFFGG 106
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
3-107 6.29e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 103.98  E-value: 6.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGkeglngggggggs 82
Cdd:PRK14278    4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPD--EEAQEKFKEISVAYEVLSDPEKRRIVDLGG------------- 68
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2025811512  83 hfdSPFE--------FGFTFRNPDDVFREFFGG 107
Cdd:PRK14278   69 ---DPLEsaggggggFGGGFGGLGDVFEAFFGG 98
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
3-107 2.29e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 102.21  E-value: 2.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGG--- 79
Cdd:PRK14283    6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE--EGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGMDGFSQEdif 83
                          90       100
                  ....*....|....*....|....*....
gi 2025811512  80 GGSHFDSPFE-FGFTFRNPDDVFRefFGG 107
Cdd:PRK14283   84 NNINFEDIFQgFGFGIGNIFDMFG--FGG 110
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
1-107 7.46e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 100.73  E-value: 7.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   1 MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGkeglngggGGG 80
Cdd:PRK14292    1 MMDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKE--KGAAEKFAQINEAYAVLSDAEKRAHYDRFG--------TAP 70
                          90       100
                  ....*....|....*....|....*..
gi 2025811512  81 GSHFDSPFEFGFTFRNPDDVFREFFGG 107
Cdd:PRK14292   71 GAGMPGGDPFGGMGFDPMDIFEQLFGG 97
PRK14293 PRK14293
molecular chaperone DnaJ;
1-107 8.79e-24

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 97.75  E-value: 8.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   1 MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGG 80
Cdd:PRK14293    2 AADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKE--PGAEDRFKEINRAYEVLSDPETRARYDQFGEAGVSGAAGFP 79
                          90       100
                  ....*....|....*....|....*..
gi 2025811512  81 gshfDSPFEFGFTfrnpdDVFREFFGG 107
Cdd:PRK14293   80 ----DMGDMGGFA-----DIFETFFSG 97
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
3-108 2.29e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 95.39  E-value: 2.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:PRK14299    5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKS--PGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQGPPP 82
                          90       100
                  ....*....|....*....|....*..
gi 2025811512  83 HFDSPFEF-GFTFRNPDDVFREFFGGR 108
Cdd:PRK14299   83 GPPGGGDFsGFNVGDFSDFFQQLFGGR 109
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
3-105 2.84e-22

terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ homolog and probable assembly protein of the Mycoplasma terminal organelle. The terminal organelle is involved in both cytadherence and gliding motility. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274808 [Multi-domain]  Cd Length: 871  Bit Score: 95.27  E-value: 2.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNpeNKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGggggggs 82
Cdd:TIGR03835   3 DYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRN--KAPDAASIFAEINEANDVLSNPKKRANYDKYGHDGVDR------- 73
                          90       100
                  ....*....|....*....|...
gi 2025811512  83 hfdspfEFGFTFRnpDDVFREFF 105
Cdd:TIGR03835  74 ------EDDFDFQ--ADVFNSFF 88
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
3-108 4.15e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 93.13  E-value: 4.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNggGGGGGS 82
Cdd:PRK14285    4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNK-EAESIFKEATEAYEVLIDDNKRAQYDRFGHTAFE--GGGGFE 80
                          90       100
                  ....*....|....*....|....*..
gi 2025811512  83 HFDSPFE-FGFTFRNPDDVFREFFGGR 108
Cdd:PRK14285   81 GFSGGFSgFSDIFEDFGDIFDSFFTGN 107
PRK14279 PRK14279
molecular chaperone DnaJ;
3-66 6.51e-22

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 92.87  E-value: 6.51e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:PRK14279   10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDP-AAEERFKAVSEAHDVLSDPAKRKEYD 72
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
4-107 2.25e-21

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 91.81  E-value: 2.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   4 YYEVLGVQRHASPEDIKKAYRKQALKWHPDK--NPEnkeeaerKFKQVAEAYEVLSDAKKRDIYDKYGKEGLnggggggg 81
Cdd:PTZ00037   30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKggDPE-------KFKEISRAYEVLSDPEKRKIYDEYGEEGL-------- 94
                          90       100
                  ....*....|....*....|....*.
gi 2025811512  82 shfdspfEFGFTFRNPDDVFREFFGG 107
Cdd:PTZ00037   95 -------EGGEQPADASDLFDLIFGG 113
PRK14288 PRK14288
molecular chaperone DnaJ;
2-95 1.33e-20

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 88.98  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   2 VDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNgGGGGGG 81
Cdd:PRK14288    3 LSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDK-EAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLN-QAGASQ 80
                          90       100
                  ....*....|....*....|...
gi 2025811512  82 SHFDSPFE---------FGFTFR 95
Cdd:PRK14288   81 SDFSDFFEdlgsffedaFGFGAR 103
PRK14295 PRK14295
molecular chaperone DnaJ;
3-66 3.42e-19

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 85.29  E-value: 3.42e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:PRK14295   10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDA-KAEERFKEISEAYDVLSDEKKRKEYD 72
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
3-107 4.76e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 84.68  E-value: 4.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGkeglngggggggs 82
Cdd:PRK14287    5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKA--PDAEDKFKEVKEAYDTLSDPQKKAHYDQFG------------- 69
                          90       100
                  ....*....|....*....|....*....
gi 2025811512  83 HFDSPFEFGFT----FRNPDDVFREFFGG 107
Cdd:PRK14287   70 HTDPNQGFGGGgagdFGGFSDIFDMFFGG 98
PRK10266 PRK10266
curved DNA-binding protein;
3-106 4.70e-17

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 78.32  E-value: 4.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENkeEAERKFKQVAEAYEVLSDAKKRDIYDkygkeglNGGGGGGGS 82
Cdd:PRK10266    5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEP--DAEARFKEVAEAWEVLSDEQRRAEYD-------QLWQHRNDP 75
                          90       100
                  ....*....|....*....|....*...
gi 2025811512  83 HFDSPFEFG----FTFRNPDDVFREFFG 106
Cdd:PRK10266   76 QFNRQFQHGdgqsFNAEDFDDIFSSIFG 103
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
3-105 1.23e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 78.13  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNpeNKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:PRK14300    4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQNQQSRGGG 81
                          90       100
                  ....*....|....*....|....*
gi 2025811512  83 HFDSPFefgftfrNPD--DVFREFF 105
Cdd:PRK14300   82 GNHGGF-------HPDinDIFGDFF 99
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
3-106 4.42e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 76.52  E-value: 4.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENkeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGS 82
Cdd:PRK14296    5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSP--DAHDKMVEINEAADVLLDKDKRKQYDQFGHAAFDGSSGFSSN 82
                          90       100       110
                  ....*....|....*....|....*....|
gi 2025811512  83 HFDspFEFGFT------FRNPDDVFREFFG 106
Cdd:PRK14296   83 FGD--FEDLFSnmgssgFSSFTNIFSDFFG 110
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1-64 4.70e-16

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 70.60  E-value: 4.70e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2025811512   1 MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDK-----NPENKEEAERKFKQVAEAYEVLSDAKKRDI 64
Cdd:COG1076     3 LDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaglPEEEQRLALQKAAAINEAYETLKDPRGIDL 71
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
4-73 1.48e-11

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 63.65  E-value: 1.48e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512    4 YYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENkeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGL 73
Cdd:PTZ00341   575 FYDILGVGVNADMKEISERYFKLAENYYPPKRSGN--EGFHKFKKINEAYQILGDIDKKKMYNKFGYDGI 642
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
2-66 6.34e-09

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 55.42  E-value: 6.34e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2025811512   2 VDYYEVLGVQRH---ASPEDIKKAYRKQALKWHPDKNPENKEEAERK-FKQVAEAYEVLSDAKKRDIYD 66
Cdd:COG5269    43 VDLYALLGLSKYrtkAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEfFKLIQKAREVLGDRKLRLQYD 111
djlA PRK09430
co-chaperone DjlA;
3-61 2.39e-06

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 47.11  E-value: 2.39e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2025811512   3 DYYEVLGVQRHASPEDIKKAYRKQALKWHPDK------NPENKEEAERKFKQVAEAYEVLSDAKK 61
Cdd:PRK09430  201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvakglPPEMMEMAKEKAQEIQAAYELIKKQKG 265
PHA03102 PHA03102
Small T antigen; Reviewed
6-37 2.06e-04

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 40.42  E-value: 2.06e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2025811512   6 EVLGVQRHA--SPEDIKKAYRKQALKWHPDK--NPE 37
Cdd:PHA03102    9 DLLGLPRSAwgNLPLMRKAYLRKCLEFHPDKggDEE 44
hscB PRK01356
co-chaperone HscB; Provisional
1-65 2.84e-04

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 40.25  E-value: 2.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025811512   1 MVDYYEVLGVQRHASP--EDIKKAYRKQALKWHPDKnPENKEEAERKFKQVAE---AYEVLSDAKKRDIY 65
Cdd:PRK01356    1 MQNYFQLLGLPQEYNIdlKILEKQYFAMQVKYHPDK-AKTLQEKEQNLIIASElnnAYSTLKDALKRAEY 69
PHA02624 PHA02624
large T antigen; Provisional
6-62 1.82e-03

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 39.20  E-value: 1.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2025811512   6 EVLGVQRHA--SPEDIKKAYRKQALKWHPDK--NPEnkeeaerKFKQVAEAYEVLSDAKKR 62
Cdd:PHA02624   15 DLLGLPMAAwgNLPLMRKAYLRKCKEYHPDKggDEE-------KMKRLNSLYKKLQEGVKS 68
 
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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