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Conserved domains on  [gi|2309466023|ref|XP_050641685|]
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dnaJ homolog subfamily B member 6 isoform X1 [Macaca thibetana thibetana]

Protein Classification

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 3.19e-37

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: 127.59  E-value: 3.19e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDP-EAEEKFKEINEAYEVLSDPEKRAIYD 63
terminal_TopJ super family cl41578
terminal organelle assembly protein TopJ;
3-151 5.98e-28

terminal organelle assembly protein TopJ;


The actual alignment was detected with superfamily member NF037946:

Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 112.99  E-value: 5.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYgkeglnggggggSH 82
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKA--PDAAEIFAEINEAYEVLSNPEKRANYDKY------------GH 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309466023  83 FDSPFEFGFTFrNPDDVFREFFGG----------RDPFSFEFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFG 151
Cdd:NF037946   72 DGVDGEGGFGF-DAFDVFSSFFETinksgaflddSVDESVSADDDLDRLFDDSKEPSFTSGLDEIVQFWEAFIGNPDYG 149
flhF super family cl35529
flagellar biosynthesis protein FlhF;
229-322 1.97e-03

flagellar biosynthesis protein FlhF;


The actual alignment was detected with superfamily member PRK06995:

Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 39.95  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023 229 INGVADEDALAEERTRRGQNALPAQPASLRPPKPPRPA--------SLLRHAPHSLYEEEGEQDRPRAPGPWDPLASAAG 300
Cdd:PRK06995   40 IVALADSDLAALAPPAAAAPAAAQPPPAAAPAAVSRPAapaaepapWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAP 119

                          90       100
                  ....*....|....*....|..
gi 2309466023 301 VQREAAEEQAQRETPVGARGQR 322
Cdd:PRK06995  120 AERAAAENAARRLARAAAAAPR 141
 
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 3.19e-37

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: 127.59  E-value: 3.19e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDP-EAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 3-106 1.16e-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: 135.04  E-value: 1.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSH 82
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGG 78

                          90       100
                  ....*....|....*....|....
gi 2309466023  83 FDSPFEFGFtFRNPDDVFREFFGG 106
Cdd:TIGR02349  79 GFNGFDIGF-FGDFGDIFGDFFGG 101
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 3-107 3.64e-36

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 134.12  E-value: 3.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSh 82
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDK-EAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGGGGG- 82

                          90       100
                  ....*....|....*....|....*
gi 2309466023  83 FDSPFEFGFTFrnpDDVFREFFGGR 107
Cdd:PRK10767   83 FGGGGGFGDIF---GDIFGDIFGGG 104
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 3-68 2.97e-33

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: 119.81  E-value: 2.97e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDP-EAEEKFKEINEAYEVLSDPEKRAAYDRF 65
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-61 3.72e-32

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 114.25  E-value: 3.72e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023    2 VDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKK 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 6.32e-29

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: 105.71  E-value: 6.32e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENkEEAERKFKQVAEAYEVLSD 58
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
3-151 5.98e-28

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 112.99  E-value: 5.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYgkeglnggggggSH 82
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKA--PDAAEIFAEINEAYEVLSNPEKRANYDKY------------GH 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309466023  83 FDSPFEFGFTFrNPDDVFREFFGG----------RDPFSFEFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFG 151
Cdd:NF037946   72 DGVDGEGGFGF-DAFDVFSSFFETinksgaflddSVDESVSADDDLDRLFDDSKEPSFTSGLDEIVQFWEAFIGNPDYG 149
flhF PRK06995
flagellar biosynthesis protein FlhF;
229-322 1.97e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 39.95  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023 229 INGVADEDALAEERTRRGQNALPAQPASLRPPKPPRPA--------SLLRHAPHSLYEEEGEQDRPRAPGPWDPLASAAG 300
Cdd:PRK06995   40 IVALADSDLAALAPPAAAAPAAAQPPPAAAPAAVSRPAapaaepapWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAP 119

                          90       100
                  ....*....|....*....|..
gi 2309466023 301 VQREAAEEQAQRETPVGARGQR 322
Cdd:PRK06995  120 AERAAAENAARRLARAAAAAPR 141
 
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 3.19e-37

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: 127.59  E-value: 3.19e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDP-EAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 3-106 1.16e-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: 135.04  E-value: 1.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSH 82
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGG 78

                          90       100
                  ....*....|....*....|....
gi 2309466023  83 FDSPFEFGFtFRNPDDVFREFFGG 106
Cdd:TIGR02349  79 GFNGFDIGF-FGDFGDIFGDFFGG 101
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 3-107 3.64e-36

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 134.12  E-value: 3.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSh 82
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDK-EAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQGGGGGG- 82

                          90       100
                  ....*....|....*....|....*
gi 2309466023  83 FDSPFEFGFTFrnpDDVFREFFGGR 107
Cdd:PRK10767   83 FGGGGGFGDIF---GDIFGDIFGGG 104
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 3-68 2.97e-33

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: 119.81  E-value: 2.97e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDP-EAEEKFKEINEAYEVLSDPEKRAAYDRF 65
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-61 3.72e-32

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 114.25  E-value: 3.72e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023    2 VDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKK 61
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 3-105 2.29e-30

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 118.33  E-value: 2.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEG-LNGGGGGGS 81
Cdd:PRK14294    5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDK-EAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGlSGTGFSGFS 83

                          90       100
                  ....*....|....*....|....*
gi 2309466023  82 HFDSPF-EFGftfrnpdDVFREFFG 105
Cdd:PRK14294   84 GFDDIFsSFG-------DIFEDFFG 101
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 3-107 5.49e-30

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 117.20  E-value: 5.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKY----GKEGLNGGGG 78
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFgyvgEQPPYQETES 84

                          90       100       110
                  ....*....|....*....|....*....|
gi 2309466023  79 GGSHFDSPF-EFGFTFRNpdDVFREFFGGR 107
Cdd:PRK14282   85 GGGFFEDIFkDFENIFNR--DIFDIFFGER 112
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 3-106 1.19e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 116.18  E-value: 1.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKygkEGLNGGGGGGSH 82
Cdd:PRK14290    4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYDQ---TGTVDFGAGGSN 80

                          90       100
                  ....*....|....*....|....*
gi 2309466023  83 FDSPfefGFT-FRNPDDVFREFFGG 106
Cdd:PRK14290   81 FNWD---NFThFSDINDIFNQIFGG 102
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 3-58 6.32e-29

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: 105.71  E-value: 6.32e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENkEEAERKFKQVAEAYEVLSD 58
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
PRK14280 PRK14280
molecular chaperone DnaJ;
3-109 2.75e-28

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 112.89  E-value: 2.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSH 82
Cdd:PRK14280    5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKE--EGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGGGGF 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2309466023  83 FDSPFEFGFTFrnpDDVFREFFGG----RDP 109
Cdd:PRK14280   83 GGGDFGGGFGF---EDIFSSFFGGggrrRDP 110
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
3-151 5.98e-28

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 112.99  E-value: 5.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYgkeglnggggggSH 82
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKA--PDAAEIFAEINEAYEVLSNPEKRANYDKY------------GH 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309466023  83 FDSPFEFGFTFrNPDDVFREFFGG----------RDPFSFEFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFG 151
Cdd:NF037946   72 DGVDGEGGFGF-DAFDVFSSFFETinksgaflddSVDESVSADDDLDRLFDDSKEPSFTSGLDEIVQFWEAFIGNPDYG 149
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 3-106 1.64e-27

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 110.63  E-value: 1.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSH 82
Cdd:PRK14291    4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKN--PEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAFSGSGQQQQG 81

                          90       100
                  ....*....|....*....|....
gi 2309466023  83 FDSpfEFGFTFRNPDDVFREFFGG 106
Cdd:PRK14291   82 QEG--FSDFGGGNIEDILEDVFDI 103
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 3-105 7.71e-27

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 109.16  E-value: 7.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKeglnggggggsh 82
Cdd:PRK14284    2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDA-EAEKRFKEVSEAYEVLSDAQKRESYDRYGK------------ 68

                          90       100
                  ....*....|....*....|....*...
gi 2309466023  83 fDSPFEF-----GFTFRNPDDVFREFFG 105
Cdd:PRK14284   69 -DGPFAGaggfgGAGMGNMEDALRTFMG 95
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 3-106 7.81e-27

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 108.78  E-value: 7.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYgkeglnggggGGSH 82
Cdd:PRK14298    6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE--PDAEEKFKEISEAYAVLSDAEKRAQYDRF----------GHAG 73

                          90       100
                  ....*....|....*....|....*....
gi 2309466023  83 FDSPFEFGFTFRNPD-----DVFREFFGG 106
Cdd:PRK14298   74 IDNQYSAEDIFRGADfggfgDIFEMFFGG 102
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 3-62 1.67e-26

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 99.69  E-value: 1.67e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKR 62
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDP-KAEERFKEINEAYELLSDAEKR 59
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 3-68 2.31e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 107.97  E-value: 2.31e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:PRK14281    4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNK-EAEEHFKEVNEAYEVLSNDDKRRRYDQF 68
PRK14297 PRK14297
molecular chaperone DnaJ;
3-106 3.19e-26

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 107.18  E-value: 3.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSH 82
Cdd:PRK14297    5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNK-EAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGAGGFGSG 83

                          90       100
                  ....*....|....*....|....
gi 2309466023  83 FDSPFEFgFTFRNPDDVFREFFGG 106
Cdd:PRK14297   84 GFGGFDF-SDMGGFGDIFDSFFGG 106
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 3-109 3.31e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 107.10  E-value: 3.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNG----GGG 78
Cdd:PRK14276    5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKE--PGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGgfggGAG 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2309466023  79 GGSHFDSPFEFG-FtfrnpDDVFREFFGG----RDP 109
Cdd:PRK14276   83 GFGGFDGSGGFGgF-----EDIFSSFFGGggarRNP 113
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 3-105 6.70e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 106.42  E-value: 6.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSH 82
Cdd:PRK14277    6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDK-EAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFDPGGFGQGG 84

                          90       100
                  ....*....|....*....|....*..
gi 2309466023  83 FD----SPFEFGFTFRNPDDVFREFFG 105
Cdd:PRK14277   85 FGqggfGGGGFDFDFGGFGDIFEDIFG 111
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 3-105 8.14e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 105.98  E-value: 8.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENkEEAERKFKQVAEAYEVLSDAKKRDIYDKYgKEGLNGGGGGGSH 82
Cdd:PRK14301    5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDN-PEAEQKFKEAAEAYEVLRDAEKRARYDRF-GHAGVNGNGGFGG 82

                          90       100
                  ....*....|....*....|...
gi 2309466023  83 FDSPFEFgftFRNPDDVFREFFG 105
Cdd:PRK14301   83 FSSAEDI---FSHFSDIFGDLFG 102
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
1-66 4.00e-25

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 96.71  E-value: 4.00e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2309466023   1 MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:COG2214     4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14289 PRK14289
molecular chaperone DnaJ;
3-68 1.61e-24

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 102.60  E-value: 1.61e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDK-EAEEKFKEAAEAYDVLSDPDKRSRYDQF 70
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 3-106 5.71e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 100.67  E-value: 5.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSH 82
Cdd:PRK14283    6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE--EGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGMDGFSQEDIF 83

                          90       100
                  ....*....|....*....|....*....
gi 2309466023  83 FDSPFE-----FGFTFRNPDDVFRefFGG 106
Cdd:PRK14283   84 NNINFEdifqgFGFGIGNIFDMFG--FGG 110
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 3-106 6.69e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 100.51  E-value: 6.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDkygkeglNGGGGGGSH 82
Cdd:PRK14278    4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPD--EEAQEKFKEISVAYEVLSDPEKRRIVD-------LGGDPLESA 74

                          90       100
                  ....*....|....*....|....
gi 2309466023  83 FDSPFEFGFTFRNPDDVFREFFGG 106
Cdd:PRK14278   75 GGGGGGFGGGFGGLGDVFEAFFGG 98
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 1-106 2.45e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 98.81  E-value: 2.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   1 MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGG 80
Cdd:PRK14292    1 MMDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKE--KGAAEKFAQINEAYAVLSDAEKRAHYDRFGTAPGAGMPGGD 78

                          90       100
                  ....*....|....*....|....*.
gi 2309466023  81 ShfdspfeFGFTFRNPDDVFREFFGG 106
Cdd:PRK14292   79 P-------FGGMGFDPMDIFEQLFGG 97
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 4-106 5.08e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 98.14  E-value: 5.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   4 YYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSHf 83
Cdd:PRK14286    6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNK-ESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGGFGQ- 83

                          90       100
                  ....*....|....*....|...
gi 2309466023  84 DSPFEFGFTFRNPDDVFREFFGG 106
Cdd:PRK14286   84 GAYTDFSDIFGDFGDIFGDFFGG 106
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 3-107 1.41e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 96.60  E-value: 1.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYDKYgKEGLNGGGGGGSH 82
Cdd:PRK14285    4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNK-EAESIFKEATEAYEVLIDDNKRAQYDRF-GHTAFEGGGGFEG 81

                          90       100
                  ....*....|....*....|....*..
gi 2309466023  83 FDSPFEfGFT--FRNPDDVFREFFGGR 107
Cdd:PRK14285   82 FSGGFS-GFSdiFEDFGDIFDSFFTGN 107
PRK14279 PRK14279
molecular chaperone DnaJ;
3-66 1.30e-21

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 94.41  E-value: 1.30e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERkFKQVAEAYEVLSDAKKRDIYD 66
Cdd:PRK14279   10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEER-FKAVSEAHDVLSDPAKRKEYD 72
PRK14293 PRK14293
molecular chaperone DnaJ;
1-68 7.76e-21

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 91.98  E-value: 7.76e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2309466023   1 MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:PRK14293    2 AADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKE--PGAEDRFKEINRAYEVLSDPETRARYDQF 67
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 3-107 9.55e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 90.38  E-value: 9.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSH 82
Cdd:PRK14299    5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKS--PGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQGPPP 82

                          90       100
                  ....*....|....*....|....*...
gi 2309466023  83 fDSPFEFGFTFRNPDD---VFREFFGGR 107
Cdd:PRK14299   83 -GPPGGGDFSGFNVGDfsdFFQQLFGGR 109
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
 3-104 1.40e-19

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: 89.87  E-value: 1.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNpeNKEEAERKFKQVAEAYEVLSDAKKRDIYDKYgkeglnggggggSH 82
Cdd:TIGR03835   3 DYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRN--KAPDAASIFAEINEANDVLSNPKKRANYDKY------------GH 68

                          90       100
                  ....*....|....*....|..
gi 2309466023  83 FDSPFEFGFTFRnpDDVFREFF 104
Cdd:TIGR03835  69 DGVDREDDFDFQ--ADVFNSFF 88
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 4-106 6.92e-19

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 86.80  E-value: 6.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   4 YYEVLGVQRHASPEDIKKAYRKLALKWHPDK--NPEnkeeaerKFKQVAEAYEVLSDAKKRDIYDKYGkeglnggggggs 81
Cdd:PTZ00037   30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKggDPE-------KFKEISRAYEVLSDPEKRKIYDEYG------------ 90

                          90       100
                  ....*....|....*....|....*
gi 2309466023  82 hfDSPFEFGFTFRNPDDVFREFFGG 106
Cdd:PTZ00037   91 --EEGLEGGEQPADASDLFDLIFGG 113
PRK14295 PRK14295
molecular chaperone DnaJ;
3-66 7.72e-19

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 86.44  E-value: 7.72e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKeEAERKFKQVAEAYEVLSDAKKRDIYD 66
Cdd:PRK14295   10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDA-KAEERFKEISEAYDVLSDEKKRKEYD 72
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 3-106 7.85e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 86.22  E-value: 7.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPEnkEEAERKFKQVAEAYEVLSDAKKRDIYDKYgkeglnggggggSH 82
Cdd:PRK14287    5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKA--PDAEDKFKEVKEAYDTLSDPQKKAHYDQF------------GH 70

                          90       100
                  ....*....|....*....|....*...
gi 2309466023  83 FDSPFEFGFT----FRNPDDVFREFFGG 106
Cdd:PRK14287   71 TDPNQGFGGGgagdFGGFSDIFDMFFGG 98
PRK14288 PRK14288
molecular chaperone DnaJ;
2-94 8.60e-19

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 85.90  E-value: 8.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   2 VDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEeAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGS 81
Cdd:PRK14288    3 LSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKE-AEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGASQS 81

                          90       100
                  ....*....|....*....|..
gi 2309466023  82 HFDSPFE---------FGFTFR 94
Cdd:PRK14288   82 DFSDFFEdlgsffedaFGFGAR 103
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 3-105 4.30e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 84.23  E-value: 4.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENkeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSH 82
Cdd:PRK14296    5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSP--DAHDKMVEINEAADVLLDKDKRKQYDQFGHAAFDGSSGFSSN 82

                          90       100
                  ....*....|....*....|....*....
gi 2309466023  83 FdSPFEFGFT------FRNPDDVFREFFG 105
Cdd:PRK14296   83 F-GDFEDLFSnmgssgFSSFTNIFSDFFG 110
PRK10266 PRK10266
curved DNA-binding protein;
3-105 5.50e-17

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 80.25  E-value: 5.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENkeEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSH 82
Cdd:PRK10266    5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEP--DAEARFKEVAEAWEVLSDEQRRAEYDQLWQHRNDPQFNRQFQ 82

                          90       100
                  ....*....|....*....|...
gi 2309466023  83 FDSPFEFGftFRNPDDVFREFFG 105
Cdd:PRK10266   83 HGDGQSFN--AEDFDDIFSSIFG 103
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 3-68 5.71e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 77.75  E-value: 5.71e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNpeNKEEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:PRK14300    4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKDEQKRAAYDRF 67
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1-64 5.95e-16

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 71.37  E-value: 5.95e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309466023   1 MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDK-----NPENKEEAERKFKQVAEAYEVLSDAKKRDI 64
Cdd:COG1076     3 LDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaglPEEEQRLALQKAAAINEAYETLKDPRGIDL 71
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 4-68 3.76e-10

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 61.34  E-value: 3.76e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2309466023    4 YYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENkeEAERKFKQVAEAYEVLSDAKKRDIYDKY 68
Cdd:PTZ00341   575 FYDILGVGVNADMKEISERYFKLAENYYPPKRSGN--EGFHKFKKINEAYQILGDIDKKKMYNKF 637
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 2-66 6.57e-08

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 53.50  E-value: 6.57e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309466023   2 VDYYEVLGVQRH---ASPEDIKKAYRKLALKWHPDKNPENKEEAERK-FKQVAEAYEVLSDAKKRDIYD 66
Cdd:COG5269    43 VDLYALLGLSKYrtkAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEfFKLIQKAREVLGDRKLRLQYD 111
djlA PRK09430
co-chaperone DjlA;
3-61 3.37e-07

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 50.58  E-value: 3.37e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2309466023   3 DYYEVLGVQRHASPEDIKKAYRKLALKWHPDK------NPENKEEAERKFKQVAEAYEVLSDAKK 61
Cdd:PRK09430  201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvakglPPEMMEMAKEKAQEIQAAYELIKKQKG 265
hscB PRK01356
co-chaperone HscB; Provisional
 1-65 1.01e-04

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 42.17  E-value: 1.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023   1 MVDYYEVLGVQRHASP--EDIKKAYRKLALKWHPDKnPENKEEAERKFKQVAE---AYEVLSDAKKRDIY 65
Cdd:PRK01356    1 MQNYFQLLGLPQEYNIdlKILEKQYFAMQVKYHPDK-AKTLQEKEQNLIIASElnnAYSTLKDALKRAEY 69
PHA03102 PHA03102
Small T antigen; Reviewed
 6-37 1.79e-03

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 38.50  E-value: 1.79e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2309466023   6 EVLGVQRHA--SPEDIKKAYRKLALKWHPDK--NPE 37
Cdd:PHA03102    9 DLLGLPRSAwgNLPLMRKAYLRKCLEFHPDKggDEE 44
flhF PRK06995
flagellar biosynthesis protein FlhF;
229-322 1.97e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 39.95  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309466023 229 INGVADEDALAEERTRRGQNALPAQPASLRPPKPPRPA--------SLLRHAPHSLYEEEGEQDRPRAPGPWDPLASAAG 300
Cdd:PRK06995   40 IVALADSDLAALAPPAAAAPAAAQPPPAAAPAAVSRPAapaaepapWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAP 119

                          90       100
                  ....*....|....*....|..
gi 2309466023 301 VQREAAEEQAQRETPVGARGQR 322
Cdd:PRK06995  120 AERAAAENAARRLARAAAAAPR 141
 
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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