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Conserved domains on  [gi|2080281572|ref|XP_042832443|]
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dnaJ homolog subfamily B member 6 isoform X3 [Panthera tigris]

Protein Classification

J domain-containing protein( domain architecture ID 1000550)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
3-66 4.06e-38

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: 127.20  E-value: 4.06e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDP-EAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK10767 super family cl35946
chaperone protein DnaJ; Provisional
3-133 8.57e-38

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK10767:

Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 135.27  E-value: 8.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGkeglnggggggvH 82
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDK-EAEEKFKEIKEAYEVLSDPQKRAAYDQYG------------H 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2080281572  83 -----------FDHPFDFGFTFrnpDDVFREFFGGRdpfsfdffedpfedffGSRRGPRGSR 133
Cdd:PRK10767   72 aafeqggggggFGGGGGFGDIF---GDIFGDIFGGG----------------RGGGRQRARR 114
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
3-66 4.06e-38

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: 127.20  E-value: 4.06e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDP-EAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
3-133 8.57e-38

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 135.27  E-value: 8.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGkeglnggggggvH 82
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDK-EAEEKFKEIKEAYEVLSDPQKRAAYDQYG------------H 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2080281572  83 -----------FDHPFDFGFTFrnpDDVFREFFGGRdpfsfdffedpfedffGSRRGPRGSR 133
Cdd:PRK10767   72 aafeqggggggFGGGGGFGDIF---GDIFGDIFGGG----------------RGGGRQRARR 114
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
3-68 7.49e-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: 126.74  E-value: 7.49e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDP-EAEEKFKEINEAYEVLSDPEKRAAYDRF 65
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
3-136 7.17e-36

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: 130.03  E-value: 7.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGVH 82
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2080281572  83 FDHPFDFGFtFRNPDDVFREFFGGrdpfsfdffedpfedFFGSRRGPRGSRNQG 136
Cdd:TIGR02349  79 GFNGFDIGF-FGDFGDIFGDFFGG---------------GGGSGRRRRSGPRRG 116
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-61 5.79e-33

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 113.87  E-value: 5.79e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572    2 VDYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKK 61
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
3-105 7.85e-31

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 116.79  E-value: 7.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGgggvh 82
Cdd:PRK14294    5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDK-EAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGTG----- 78
                          90       100
                  ....*....|....*....|...
gi 2080281572  83 FDHPFDFGFTFRNPDDVFREFFG 105
Cdd:PRK14294   79 FSGFSGFDDIFSSFGDIFEDFFG 101
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
3-58 9.94e-30

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: 105.32  E-value: 9.94e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENkEEAERKFKQVAEAYEVLSD 58
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
3-106 1.80e-27

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 108.75  E-value: 1.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGlnggggggvh 82
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKA--PDAAEIFAEINEAYEVLSNPEKRANYDKYGHDG---------- 73
                          90       100
                  ....*....|....*....|....
gi 2080281572  83 FDHPFDFGFtfrNPDDVFREFFGG 106
Cdd:NF037946   74 VDGEGGFGF---DAFDVFSSFFET 94
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
3-104 3.17e-21

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: 92.18  E-value: 3.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNpeNKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGlnggggggvh 82
Cdd:TIGR03835   3 DYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRN--KAPDAASIFAEINEANDVLSNPKKRANYDKYGHDG---------- 70
                          90       100
                  ....*....|....*....|..
gi 2080281572  83 FDHPFDFGFTfrnpDDVFREFF 104
Cdd:TIGR03835  71 VDREDDFDFQ----ADVFNSFF 88
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
3-66 4.06e-38

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: 127.20  E-value: 4.06e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDP-EAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
3-133 8.57e-38

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 135.27  E-value: 8.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGkeglnggggggvH 82
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDK-EAEEKFKEIKEAYEVLSDPQKRAAYDQYG------------H 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2080281572  83 -----------FDHPFDFGFTFrnpDDVFREFFGGRdpfsfdffedpfedffGSRRGPRGSR 133
Cdd:PRK10767   72 aafeqggggggFGGGGGFGDIF---GDIFGDIFGGG----------------RGGGRQRARR 114
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
3-68 7.49e-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: 126.74  E-value: 7.49e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDP-EAEEKFKEINEAYEVLSDPEKRAAYDRF 65
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
3-136 7.17e-36

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: 130.03  E-value: 7.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGVH 82
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2080281572  83 FDHPFDFGFtFRNPDDVFREFFGGrdpfsfdffedpfedFFGSRRGPRGSRNQG 136
Cdd:TIGR02349  79 GFNGFDIGF-FGDFGDIFGDFFGG---------------GGGSGRRRRSGPRRG 116
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-61 5.79e-33

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 113.87  E-value: 5.79e-33
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572    2 VDYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKK 61
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
3-105 7.85e-31

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 116.79  E-value: 7.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGgggvh 82
Cdd:PRK14294    5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDK-EAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGTG----- 78
                          90       100
                  ....*....|....*....|...
gi 2080281572  83 FDHPFDFGFTFRNPDDVFREFFG 105
Cdd:PRK14294   79 FSGFSGFDDIFSSFGDIFEDFFG 101
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
3-107 3.23e-30

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 115.28  E-value: 3.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKY----GKEGLNGGGG 78
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFgyvgEQPPYQETES 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 2080281572  79 GGVHFDHPF-DFGFTFRNpdDVFREFFGGR 107
Cdd:PRK14282   85 GGGFFEDIFkDFENIFNR--DIFDIFFGER 112
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
3-58 9.94e-30

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: 105.32  E-value: 9.94e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENkEEAERKFKQVAEAYEVLSD 58
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
3-106 1.30e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 113.49  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKyGKEGLNGGGGGGVH 82
Cdd:PRK14290    4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYDQ-TGTVDFGAGGSNFN 82
                          90       100
                  ....*....|....*....|....*
gi 2080281572  83 FDHpfdfgFT-FRNPDDVFREFFGG 106
Cdd:PRK14290   83 WDN-----FThFSDINDIFNQIFGG 102
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
3-62 7.49e-29

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 103.54  E-value: 7.49e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKR 62
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDP-KAEERFKEINEAYELLSDAEKR 59
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
3-130 8.31e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 111.37  E-value: 8.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGgggvh 82
Cdd:PRK14301    5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDN-PEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVNGNG----- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2080281572  83 fdhpfdFGFTFRNPDDVFREF---FGGRDPFSfdffedpfedFFGSRRGPR 130
Cdd:PRK14301   79 ------GFGGFSSAEDIFSHFsdiFGDLFGFS----------GGGSRRGPR 113
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
3-133 9.34e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 111.48  E-value: 9.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGlnggggggvh 82
Cdd:PRK14298    6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE--PDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAG---------- 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2080281572  83 FDHPFDFGFTFRNPD-----DVFREFFGGrdpfsfdffedpfedffGSRRGPRGSR 133
Cdd:PRK14298   74 IDNQYSAEDIFRGADfggfgDIFEMFFGG-----------------GGRRGRMGPR 112
PRK14280 PRK14280
molecular chaperone DnaJ;
3-109 2.04e-28

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 110.58  E-value: 2.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGVH 82
Cdd:PRK14280    5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKE--EGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGGGGF 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2080281572  83 FDHPFDFGFTFrnpDDVFREFFGG----RDP 109
Cdd:PRK14280   83 GGGDFGGGFGF---EDIFSSFFGGggrrRDP 110
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
3-106 6.48e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 109.09  E-value: 6.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGVH 82
Cdd:PRK14291    4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKN--PEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAFSGSGQQQQG 81
                          90       100
                  ....*....|....*....|....
gi 2080281572  83 FDHPFDFGFTfrNPDDVFREFFGG 106
Cdd:PRK14291   82 QEGFSDFGGG--NIEDILEDVFDI 103
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
3-106 1.80e-27

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 108.75  E-value: 1.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGlnggggggvh 82
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKA--PDAAEIFAEINEAYEVLSNPEKRANYDKYGHDG---------- 73
                          90       100
                  ....*....|....*....|....
gi 2080281572  83 FDHPFDFGFtfrNPDDVFREFFGG 106
Cdd:NF037946   74 VDGEGGFGF---DAFDVFSSFFET 94
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
1-66 2.57e-27

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 100.56  E-value: 2.57e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2080281572   1 MVDYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:COG2214     4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
3-68 7.52e-27

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 106.43  E-value: 7.52e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:PRK14281    4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNK-EAEEHFKEVNEAYEVLSNDDKRRRYDQF 68
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
1-106 1.77e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 105.36  E-value: 1.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   1 MVDYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGG 80
Cdd:PRK14292    1 MMDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKE--KGAAEKFAQINEAYAVLSDAEKRAHYDRFGTAPGAGMPGGD 78
                          90       100
                  ....*....|....*....|....*.
gi 2080281572  81 VhfdhpfdFGFTFRNPDDVFREFFGG 106
Cdd:PRK14292   79 P-------FGGMGFDPMDIFEQLFGG 97
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
3-133 1.89e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 105.31  E-value: 1.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKeglnggggggvh 82
Cdd:PRK14284    2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDA-EAEKRFKEVSEAYEVLSDAQKRESYDRYGK------------ 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2080281572  83 fDHPFDF-----GFTFRNPDDVFREF-------FGGRDPFsFDFFEDPFEDFFGSRRGPRGSR 133
Cdd:PRK14284   69 -DGPFAGaggfgGAGMGNMEDALRTFmgafggeFGGGGSF-FEGLFGGLGEAFGMRGGPAGAR 129
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
3-131 3.84e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 104.36  E-value: 3.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGvh 82
Cdd:PRK14278    4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPD--EEAQEKFKEISVAYEVLSDPEKRRIVDLGGDPLESAGGGGG-- 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2080281572  83 fdhpfDFGFTFRNPDDVFREFFGGrdpfsfdffedpfedfFGSRRGPRG 131
Cdd:PRK14278   80 -----GFGGGFGGLGDVFEAFFGG----------------GAASRGPRG 107
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
3-109 5.05e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 104.01  E-value: 5.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGVH 82
Cdd:PRK14276    5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKE--PGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFGGGAG 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2080281572  83 FDHPFDFGFTFRNPDDVFREFFGG----RDP 109
Cdd:PRK14276   83 GFGGFDGSGGFGGFEDIFSSFFGGggarRNP 113
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
3-107 7.15e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 103.73  E-value: 7.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGVH 82
Cdd:PRK14277    6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDK-EAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFDPGGFGQGG 84
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2080281572  83 FDH--------PFDFGFTFRNPDDVFREFFGGR 107
Cdd:PRK14277   85 FGQggfggggfDFDFGGFGDIFEDIFGDFFGTG 117
PRK14297 PRK14297
molecular chaperone DnaJ;
3-106 1.03e-25

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 103.32  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGVH 82
Cdd:PRK14297    5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNK-EAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGAGGFGSG 83
                          90       100
                  ....*....|....*....|....
gi 2080281572  83 FDHPFDFgFTFRNPDDVFREFFGG 106
Cdd:PRK14297   84 GFGGFDF-SDMGGFGDIFDSFFGG 106
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
3-130 3.78e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 101.82  E-value: 3.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEG----LNGGGG 78
Cdd:PRK14283    6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE--EGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGmdgfSQEDIF 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2080281572  79 GGVHFDHPFD-FGFTFRNPDDVFRefFGGrdpfsfdffedpfedffGSRRGPR 130
Cdd:PRK14283   84 NNINFEDIFQgFGFGIGNIFDMFG--FGG-----------------GSRHGPQ 117
PRK14289 PRK14289
molecular chaperone DnaJ;
3-68 5.93e-25

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 101.45  E-value: 5.93e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDK-EAEEKFKEAAEAYDVLSDPDKRSRYDQF 70
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
4-132 4.79e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 98.52  E-value: 4.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   4 YYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGVHF 83
Cdd:PRK14286    6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNK-ESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGGFGQG 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2080281572  84 DHPfDFGFTFRNPDDVFREFFGGrdpfsfdffEDPFEDFFGSRRGP-RGS 132
Cdd:PRK14286   85 AYT-DFSDIFGDFGDIFGDFFGG---------GRGGGSGGGRRSGPqRGS 124
PRK14279 PRK14279
molecular chaperone DnaJ;
3-66 1.34e-22

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 94.80  E-value: 1.34e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKEEAERkFKQVAEAYEVLSDAKKRDIYD 66
Cdd:PRK14279   10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEER-FKAVSEAHDVLSDPAKRKEYD 72
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
3-110 1.61e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 93.08  E-value: 1.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGggggvh 82
Cdd:PRK14299    5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKS--PGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAG------ 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2080281572  83 FDHP-------FDF-GFTFRNPDDVFREFFGGRDPF 110
Cdd:PRK14299   77 WQGPppgppggGDFsGFNVGDFSDFFQQLFGGRGGF 112
PRK14293 PRK14293
molecular chaperone DnaJ;
1-68 8.55e-22

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 92.36  E-value: 8.55e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2080281572   1 MVDYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:PRK14293    2 AADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKE--PGAEDRFKEINRAYEVLSDPETRARYDQF 67
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
3-104 3.17e-21

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: 92.18  E-value: 3.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNpeNKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGlnggggggvh 82
Cdd:TIGR03835   3 DYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRN--KAPDAASIFAEINEANDVLSNPKKRANYDKYGHDG---------- 70
                          90       100
                  ....*....|....*....|..
gi 2080281572  83 FDHPFDFGFTfrnpDDVFREFF 104
Cdd:TIGR03835  71 VDREDDFDFQ----ADVFNSFF 88
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
3-107 5.15e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 90.05  E-value: 5.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGvH 82
Cdd:PRK14285    4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNK-EAESIFKEATEAYEVLIDDNKRAQYDRFGHTAFEGGGGFE-G 81
                          90       100
                  ....*....|....*....|....*.
gi 2080281572  83 FDHPFD-FGFTFRNPDDVFREFFGGR 107
Cdd:PRK14285   82 FSGGFSgFSDIFEDFGDIFDSFFTGN 107
PRK14295 PRK14295
molecular chaperone DnaJ;
3-66 1.92e-20

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 88.75  E-value: 1.92e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:PRK14295   10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDA-KAEERFKEISEAYDVLSDEKKRKEYD 72
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
3-201 6.64e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 86.99  E-value: 6.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGkeglnggggggvH 82
Cdd:PRK14287    5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKA--PDAEDKFKEVKEAYDTLSDPQKKAHYDQFG------------H 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572  83 FDHPFDFGFT----FRNPDDVFREFFGGrdpfsfdffedpfedfFGSRRGPRGSRnQGTGSFFSAFSGFPS--FGGG--- 153
Cdd:PRK14287   71 TDPNQGFGGGgagdFGGFSDIFDMFFGG----------------GGGRRNPNAPR-QGADLQYTMTLEFKEavFGKEtei 133
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2080281572 154 -FSSLDTGFTSFGSAGHGGLTSFSSTAFGGSGMGSFKSISTSTKMVNGR 201
Cdd:PRK14287  134 eIPREETCGTCHGSGAKPGTKPETCSHCGGSGQLNVEQNTPFGRVVNRR 182
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
4-106 4.82e-19

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 85.26  E-value: 4.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   4 YYEVLGVQRHASAEDIKKAYRKLALKWHPDK--NPEnkeeaerKFKQVAEAYEVLSDAKKRDIYDKYGkeglnggggggv 81
Cdd:PTZ00037   30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKggDPE-------KFKEISRAYEVLSDPEKRKIYDEYG------------ 90
                          90       100
                  ....*....|....*....|....*
gi 2080281572  82 hfDHPFDFGFTFRNPDDVFREFFGG 106
Cdd:PTZ00037   91 --EEGLEGGEQPADASDLFDLIFGG 113
PRK10266 PRK10266
curved DNA-binding protein;
3-105 9.10e-19

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 83.33  E-value: 9.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENkeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGgvH 82
Cdd:PRK10266    5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEP--DAEARFKEVAEAWEVLSDEQRRAEYDQLWQHRNDPQFNR--Q 80
                          90       100
                  ....*....|....*....|...
gi 2080281572  83 FDHPFDFGFTFRNPDDVFREFFG 105
Cdd:PRK10266   81 FQHGDGQSFNAEDFDDIFSSIFG 103
PRK14288 PRK14288
molecular chaperone DnaJ;
2-68 5.61e-18

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 81.66  E-value: 5.61e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2080281572   2 VDYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:PRK14288    3 LSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDK-EAEEKFKLINEAYGVLSDEKKRALYDRY 68
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1-64 9.19e-17

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 72.14  E-value: 9.19e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2080281572   1 MVDYYEVLGVQRHASAEDIKKAYRKLALKWHPDK-----NPENKEEAERKFKQVAEAYEVLSDAKKRDI 64
Cdd:COG1076     3 LDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaglPEEEQRLALQKAAAINEAYETLKDPRGIDL 71
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
3-105 2.59e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 76.91  E-value: 2.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENkeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGVH 82
Cdd:PRK14296    5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSP--DAHDKMVEINEAADVLLDKDKRKQYDQFGHAAFDGSSGFSSN 82
                          90       100
                  ....*....|....*....|....*...
gi 2080281572  83 FDHPFDF-----GFTFRNPDDVFREFFG 105
Cdd:PRK14296   83 FGDFEDLfsnmgSSGFSSFTNIFSDFFG 110
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
3-184 3.34e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 76.59  E-value: 3.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDKNpeNKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGVH 82
Cdd:PRK14300    4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDAFQNQQSRGGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572  83 FDHPfdfGFtfrNPD------DVFREFFGGrdpfsfdffedpfedffGSRRGPRGSRNQG-------TGSFFSAFSGFPS 149
Cdd:PRK14300   82 GNHG---GF---HPDindifgDFFSDFMGG-----------------SRRSRPTSSKVRGsdlkynlTINLEEAFHGIEK 138
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2080281572 150 fGGGFSSLDTGFTSFGSAGHGGLTSFSSTAFGGSG 184
Cdd:PRK14300  139 -NISFSSEVKCDTCHGSGSEKGETVTTCDACSGVG 172
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
4-86 6.05e-11

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 62.11  E-value: 6.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572    4 YYEVLGVQRHASAEDIKKAYRKLALKWHPDKNPENkeEAERKFKQVAEAYEVLSDAKKRDIYDKYgkeglNGGGGGGVHF 83
Cdd:PTZ00341   575 FYDILGVGVNADMKEISERYFKLAENYYPPKRSGN--EGFHKFKKINEAYQILGDIDKKKMYNKF-----GYDGIKGVNF 647

                   ...
gi 2080281572   84 DHP 86
Cdd:PTZ00341   648 IHP 650
djlA PRK09430
co-chaperone DjlA;
3-61 7.33e-08

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 51.74  E-value: 7.33e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2080281572   3 DYYEVLGVQRHASAEDIKKAYRKLALKWHPDK------NPENKEEAERKFKQVAEAYEVLSDAKK 61
Cdd:PRK09430  201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvakglPPEMMEMAKEKAQEIQAAYELIKKQKG 265
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
2-66 2.35e-07

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 50.80  E-value: 2.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2080281572   2 VDYYEVLGVQRH---ASAEDIKKAYRKLALKWHPDKNPENKEEAERK-FKQVAEAYEVLSDAKKRDIYD 66
Cdd:COG5269    43 VDLYALLGLSKYrtkAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEfFKLIQKAREVLGDRKLRLQYD 111
hscB PRK01356
co-chaperone HscB; Provisional
1-65 3.77e-05

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 42.94  E-value: 3.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080281572   1 MVDYYEVLGVQRHASA--EDIKKAYRKLALKWHPDKnPENKEEAERKFKQVAE---AYEVLSDAKKRDIY 65
Cdd:PRK01356    1 MQNYFQLLGLPQEYNIdlKILEKQYFAMQVKYHPDK-AKTLQEKEQNLIIASElnnAYSTLKDALKRAEY 69
PHA03102 PHA03102
Small T antigen; Reviewed
6-37 2.70e-04

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 40.04  E-value: 2.70e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2080281572   6 EVLGVQRHA--SAEDIKKAYRKLALKWHPDK--NPE 37
Cdd:PHA03102    9 DLLGLPRSAwgNLPLMRKAYLRKCLEFHPDKggDEE 44
PHA02624 PHA02624
large T antigen; Provisional
6-62 1.23e-03

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 39.58  E-value: 1.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2080281572   6 EVLGVQRHA--SAEDIKKAYRKLALKWHPDK--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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