NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|27261818|ref|NP_758841|]
View 

dnaJ homolog subfamily C member 16 precursor [Mus musculus]

Protein Classification

DnaJ and TRX_DnaJ domain-containing protein( domain architecture ID 13534556)

DnaJ and TRX_DnaJ domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 134-243 3.26e-59

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


:

Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 195.67  E-value: 3.26e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818 134 DSGDEKYLLHFSHYVNEVLPESFKRPYLIKITSDWCFSCIHIEPVWKEVVQELEGLGVGIGVVHAGYERRLAHHLGAHST 213
Cdd:cd02963   1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 27261818 214 PSILGVISGKITFFHNAVVH-ENLRQFVESL 243
Cdd:cd02963  81 PAIVGIINGQVTFYHDSSFTkQHVVDFVRKL 111
DnaJ_bact super family cl37091
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 29-140 2.48e-34

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.


The actual alignment was detected with superfamily member TIGR02349:

Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 134.65  E-value: 2.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818    29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQQREh 108
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGGG- 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 27261818   109 rFRHFHENFyFD------ESFFHFPFNAERRDSGDEKY 140
Cdd:TIGR02349  80 -FNGFDIGF-FGdfgdifGDFFGGGGGSGRRRRSGPRR 115
 
Name Accession Description Interval E-value
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 134-243 3.26e-59

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 195.67  E-value: 3.26e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818 134 DSGDEKYLLHFSHYVNEVLPESFKRPYLIKITSDWCFSCIHIEPVWKEVVQELEGLGVGIGVVHAGYERRLAHHLGAHST 213
Cdd:cd02963   1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 27261818 214 PSILGVISGKITFFHNAVVH-ENLRQFVESL 243
Cdd:cd02963  81 PAIVGIINGQVTFYHDSSFTkQHVVDFVRKL 111
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 29-140 2.48e-34

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: 134.65  E-value: 2.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818    29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQQREh 108
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGGG- 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 27261818   109 rFRHFHENFyFD------ESFFHFPFNAERRDSGDEKY 140
Cdd:TIGR02349  80 -FNGFDIGF-FGdfgdifGDFFGGGGGSGRRRRSGPRR 115
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 29-123 9.03e-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: 123.27  E-value: 9.03e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQQRE 107
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80

                        90
                ....*....|....*.
gi 27261818 108 HRFRHFHENFYFDESF 123
Cdd:COG0484  81 AAAEAAAAEAKEEAAE 96
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 29-90 2.82e-31

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: 116.42  E-value: 2.82e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27261818    29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKN-KDPGAEDRFIQISKAYEILSNEEKRTNYD 90
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 29-135 2.57e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 120.64  E-value: 2.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQQREH 108
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAFSGSGQQQQGQE 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 27261818  109 RF------------RHFHENFYFDESFFHFPFNAERRDS 135
Cdd:PRK14291  84 GFsdfgggniedilEDVFDIFGFGDIFGRRRATRERRKT 122
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
29-168 7.11e-25

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 108.37  E-value: 7.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAG-ENQGYQKQQRE 107
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGvDGEGGFGFDAF 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27261818  108 HRFRHFHENFYFDESFFHFPFNAERRDSGDEKYLLHFShyvnevlPESFKRPYLIKITSDW 168
Cdd:NF037946  86 DVFSSFFETINKSGAFLDDSVDESVSADDDLDRLFDDS-------KEPSFTSGLDEIVQFW 139
DnaJ smart00271
DnaJ molecular chaperone homology domain;
29-85 1.91e-23

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 93.84  E-value: 1.91e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 27261818     29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD--PGAEDRFIQISKAYEILSNEEK 85
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGdkEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 29-82 2.56e-23

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: 93.38  E-value: 2.56e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27261818  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDRFIQISKAYEILSN 82
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 149-244 2.13e-04

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 41.98  E-value: 2.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818 149 NEVLPESFK-RPYLIKITSDWCFSCIHIEPVWKEVVQELEGLGVgIGV---------------------VHAGYERRLAH 206
Cdd:COG0526  19 KPLSLADLKgKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVF-VGVdvdenpeavkaflkelglpypVLLDPDGELAK 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 27261818 207 HLGAHSTPSILgVIS--GKITFFHN-AVVHENLRQFVESLL 244
Cdd:COG0526  98 AYGVRGIPTTV-LIDkdGKIVARHVgPLSPEELEEALEKLL 137
 
Name Accession Description Interval E-value
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 134-243 3.26e-59

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 195.67  E-value: 3.26e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818 134 DSGDEKYLLHFSHYVNEVLPESFKRPYLIKITSDWCFSCIHIEPVWKEVVQELEGLGVGIGVVHAGYERRLAHHLGAHST 213
Cdd:cd02963   1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 27261818 214 PSILGVISGKITFFHNAVVH-ENLRQFVESL 243
Cdd:cd02963  81 PAIVGIINGQVTFYHDSSFTkQHVVDFVRKL 111
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 29-140 2.48e-34

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: 134.65  E-value: 2.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818    29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQQREh 108
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGGG- 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 27261818   109 rFRHFHENFyFD------ESFFHFPFNAERRDSGDEKY 140
Cdd:TIGR02349  80 -FNGFDIGF-FGdfgdifGDFFGGGGGSGRRRRSGPRR 115
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 29-123 9.03e-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: 123.27  E-value: 9.03e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQQRE 107
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80

                        90
                ....*....|....*.
gi 27261818 108 HRFRHFHENFYFDESF 123
Cdd:COG0484  81 AAAEAAAAEAKEEAAE 96
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 29-90 2.82e-31

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: 116.42  E-value: 2.82e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27261818    29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKN-KDPGAEDRFIQISKAYEILSNEEKRTNYD 90
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 29-135 2.57e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 120.64  E-value: 2.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQQREH 108
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAFSGSGQQQQGQE 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 27261818  109 RF------------RHFHENFYFDESFFHFPFNAERRDS 135
Cdd:PRK14291  84 GFsdfgggniedilEDVFDIFGFGDIFGRRRATRERRKT 122
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 29-100 2.46e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 117.55  E-value: 2.46e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQG 100
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPgDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQG 77
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 29-101 5.92e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 116.73  E-value: 5.92e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGY 101
Cdd:PRK14276   5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGF 77
PRK14280 PRK14280
molecular chaperone DnaJ;
29-134 9.59e-28

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 115.97  E-value: 9.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQQREH 108
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGGGGFGG 84

                         90       100
                 ....*....|....*....|....*...
gi 27261818  109 rfRHFHENFYFDESFFHFpFN--AERRD 134
Cdd:PRK14280  85 --GDFGGGFGFEDIFSSF-FGggGRRRD 109
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 29-86 1.34e-27

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 105.85  E-value: 1.34e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27261818  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKR 86
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKgDPKAEERFKEINEAYELLSDAEKR 59
PRK14293 PRK14293
molecular chaperone DnaJ;
29-96 4.84e-27

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 113.55  E-value: 4.84e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAG 96
Cdd:PRK14293   4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQFGEAG 71
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 29-124 5.83e-27

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 113.41  E-value: 5.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQQ--R 106
Cdd:PRK14298   6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSAEDifR 85

                         90
                 ....*....|....*...
gi 27261818  107 EHRFRHFHENFyfdESFF 124
Cdd:PRK14298  86 GADFGGFGDIF---EMFF 100
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 29-102 2.57e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 106.95  E-value: 2.57e-25
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQ 102
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQ 78
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
29-168 7.11e-25

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 108.37  E-value: 7.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAG-ENQGYQKQQRE 107
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGvDGEGGFGFDAF 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27261818  108 HRFRHFHENFYFDESFFHFPFNAERRDSGDEKYLLHFShyvnevlPESFKRPYLIKITSDW 168
Cdd:NF037946  86 DVFSSFFETINKSGAFLDDSVDESVSADDDLDRLFDDS-------KEPSFTSGLDEIVQFW 139
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 29-133 5.49e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 104.91  E-value: 5.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAG-----ENQGYQK 103
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGmdgfsQEDIFNN 85

                         90       100       110
                 ....*....|....*....|....*....|
gi 27261818  104 QQREHRFRHFheNFYFDESFFHFPFNAERR 133
Cdd:PRK14283  86 INFEDIFQGF--GFGIGNIFDMFGFGGGSR 113
PRK14295 PRK14295
molecular chaperone DnaJ;
23-90 1.28e-23

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 103.78  E-value: 1.28e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27261818   23 LSALDF---DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKRTNYD 90
Cdd:PRK14295   1 MSTKDYiekDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYD 72
DnaJ smart00271
DnaJ molecular chaperone homology domain;
29-85 1.91e-23

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 93.84  E-value: 1.91e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 27261818     29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD--PGAEDRFIQISKAYEILSNEEK 85
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGdkEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 29-82 2.56e-23

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: 93.38  E-value: 2.56e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27261818  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDRFIQISKAYEILSN 82
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 29-100 7.66e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 101.28  E-value: 7.66e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQG 100
Cdd:PRK14278   4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVDLGGDPLESAG 75
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 29-140 9.68e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 100.64  E-value: 9.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD--PGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQQR 106
Cdd:PRK14282   5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPEnrKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPPYQETES 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 27261818  107 -----EHRFRHFhENFyFDESFFHFPFNAERRDSGDEKY 140
Cdd:PRK14282  85 gggffEDIFKDF-ENI-FNRDIFDIFFGERRTQEEQREY 121
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 29-95 1.15e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 100.73  E-value: 1.15e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDA 95
Cdd:PRK14292   3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDRFGTA 69
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 29-133 2.01e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 99.82  E-value: 2.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGEN-----QGYQ 102
Cdd:PRK14301   5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDnPEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVNgnggfGGFS 84

                         90       100       110
                 ....*....|....*....|....*....|.
gi 27261818  103 KQqrEHRFRHFHENFyfdESFFHFPFNAERR 133
Cdd:PRK14301  85 SA--EDIFSHFSDIF---GDLFGFSGGGSRR 110
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 29-104 2.14e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 100.26  E-value: 2.14e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNkdPG---AEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQ 104
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLN--PGdkeAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFDPGGFGQ 82
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 29-96 3.46e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 99.50  E-value: 3.46e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDRFIQISKAYEILSNEEKRTNYDHYGDAG 96
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDnKEAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAG 72
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 29-133 6.44e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 98.30  E-value: 6.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNkdPG---AEDRFIQISKAYEILSNEEKRTNYDHYGDAG-ENQGYQkq 104
Cdd:PRK14294   5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRN--PGdkeAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGlSGTGFS-- 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 27261818  105 qrehRFRHFHENF--YFD--ESFFHFPFNAERR 133
Cdd:PRK14294  81 ----GFSGFDDIFssFGDifEDFFGFGGGRRGR 109
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
29-90 4.17e-21

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 88.24  E-value: 4.17e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27261818  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPG--AEDRFIQISKAYEILSNEEKRTNYD 90
Cdd:COG2214   6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 29-101 1.01e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 94.69  E-value: 1.01e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGY 101
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTDPNQGF 77
PRK14279 PRK14279
molecular chaperone DnaJ;
29-90 3.49e-20

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 93.64  E-value: 3.49e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKRTNYD 90
Cdd:PRK14279  10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPgDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 29-100 3.57e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 93.37  E-value: 3.57e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQG 100
Cdd:PRK14284   2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPgDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKDGPFAG 74
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 29-139 1.14e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 91.61  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYG-DAGENQGYQKQQRE 107
Cdd:PRK14300   4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGhDAFQNQQSRGGGGN 83

                         90       100       110
                 ....*....|....*....|....*....|..
gi 27261818  108 HRFRHFHENFYFDESFFHFPFNAERRDSGDEK 139
Cdd:PRK14300  84 HGGFHPDINDIFGDFFSDFMGGSRRSRPTSSK 115
PRK14289 PRK14289
molecular chaperone DnaJ;
29-96 1.16e-18

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 88.73  E-value: 1.16e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAG 96
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPgDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAG 74
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 31-102 1.63e-18

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 88.72  E-value: 1.63e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27261818   31 YRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPgaeDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQ 102
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDP---EKFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQ 99
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 29-95 1.64e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 88.08  E-value: 1.64e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDA 95
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHA 71
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 29-123 2.02e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 87.68  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD--PGAEDRFIQISKAYEILSNEEKRTNYDH-----YGDAGENQGY 101
Cdd:PRK14290   4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGnkAEAEEKFKEISEAYEVLSDPQKRRQYDQtgtvdFGAGGSNFNW 83

                         90       100
                 ....*....|....*....|...
gi 27261818  102 QKqqrehrFRHFHE-NFYFDESF 123
Cdd:PRK14290  84 DN------FTHFSDiNDIFNQIF 100
PRK14297 PRK14297
molecular chaperone DnaJ;
29-100 3.76e-18

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 87.15  E-value: 3.76e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQG 100
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKgNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGA 77
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 31-100 1.24e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 85.43  E-value: 1.24e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27261818   31 YRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQG 100
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKgNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAG 77
PRK10266 PRK10266
curved DNA-binding protein;
29-124 2.78e-17

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 83.33  E-value: 2.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYD----HYGDAGENQGYQKQ 104
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDqlwqHRNDPQFNRQFQHG 84

                         90       100
                 ....*....|....*....|
gi 27261818  105 QREHRFRHFHENFYfdESFF 124
Cdd:PRK10266  85 DGQSFNAEDFDDIF--SSIF 102
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 29-93 1.63e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 75.80  E-value: 1.63e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDRFIQISKAYEILSNEEKRTNYDHYG 93
Cdd:PRK14285   4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGnKEAESIFKEATEAYEVLIDDNKRAQYDRFG 69
PRK14288 PRK14288
molecular chaperone DnaJ;
26-139 4.21e-14

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 74.73  E-value: 4.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818   26 LDFDPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQKQ 104
Cdd:PRK14288   1 MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAgDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGASQ 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 27261818  105 QrehRFRHFHENFyfdESFFHFPFNAERRDSGDEK 139
Cdd:PRK14288  81 S---DFSDFFEDL---GSFFEDAFGFGARGSKRQK 109
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
29-83 2.82e-13

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 65.59  E-value: 2.82e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27261818  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDK--NKDPG-----AEDRFIQISKAYEILSNE 83
Cdd:COG1076   5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRlaAGLPEeeqrlALQKAAAINEAYETLKDP 66
djlA PRK09430
co-chaperone DjlA;
29-60 3.80e-08

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 55.20  E-value: 3.80e-08
                         10        20        30
                 ....*....|....*....|....*....|..
gi 27261818   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDK 60
Cdd:PRK09430 201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 31-99 1.61e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 51.71  E-value: 1.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27261818    31 YRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDRFIQISKAYEILSNEEKRTNYDHYGDAGENQ 99
Cdd:PTZ00341  576 YDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKFGYDGIKG 644
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 29-90 9.80e-06

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 48.49  E-value: 9.80e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27261818  29 DPYRVLGVSRTASQAD---IKKAYKKLAREWHPDKNKDPGAEDR---FIQISKAYEILSNEEKRTNYD 90
Cdd:COG5269  44 DLYALLGLSKYRTKAIppqILKAHKKKVYKYHPDKTAAGGNKGCdefFKLIQKAREVLGDRKLRLQYD 111
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 149-244 2.13e-04

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 41.98  E-value: 2.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818 149 NEVLPESFK-RPYLIKITSDWCFSCIHIEPVWKEVVQELEGLGVgIGV---------------------VHAGYERRLAH 206
Cdd:COG0526  19 KPLSLADLKgKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVF-VGVdvdenpeavkaflkelglpypVLLDPDGELAK 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 27261818 207 HLGAHSTPSILgVIS--GKITFFHN-AVVHENLRQFVESLL 244
Cdd:COG0526  98 AYGVRGIPTTV-LIDkdGKIVARHVgPLSPEELEEALEKLL 137
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 160-241 5.52e-04

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 40.06  E-value: 5.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818 160 YLIKITSDWCFSCIHIEPVWKEVVQELEGLGVGIGVVHAGYERRLAHHLGAHSTPSILGVISGKITFFHNAVVHENLRQF 239
Cdd:cd02994  19 WMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKDGVFRRYQGPRDKEDLISF 98


                ..
gi 27261818 240 VE 241
Cdd:cd02994  99 IE 100
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 158-241 9.65e-03

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 36.00  E-value: 9.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27261818 158 RPYLIKITSDWCFSCIHIEPVWKEVVQELEglGVGIGVVHAGYERRLAHHLGAHSTPSILGVISGKITF-FHNAVVHENL 236
Cdd:cd02947  11 KPVVVDFWAPWCGPCKAIAPVLEELAEEYP--KVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDrVVGADPKEEL 88


                ....*
gi 27261818 237 RQFVE 241
Cdd:cd02947  89 EEFLE 93
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH