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Conserved domains on  [gi|56687498|ref|NP_056106|]
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dnaJ homolog subfamily C member 16 isoform 1 precursor [Homo sapiens]

Protein Classification

antitermination protein( domain architecture ID 13534556)

antitermination protein positively regulates expression of some phage genes

Graphical summary

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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 ...
 136-245 7.97e-62

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: 202.99  E-value: 7.97e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498 136 DSIDEKYLLHFSHYVNEVVPDSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEELGVGIGVVHAGYERRLAHHLGAHST 215
Cdd:cd02963   1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 56687498 216 PSILGIINGKISFFHNAVV-RENLRQFVESL 245
Cdd:cd02963  81 PAIVGIINGQVTFYHDSSFtKQHVVDFVRKL 111
DnaJ_bact super family cl37091
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 29-142 2.23e-35

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: 137.73  E-value: 2.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498    29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGENqgyqkQQQQR 108
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFN-----GGGGG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 56687498   109 EYRFRHFHENFYFD------ESFFHFPFNSERRDSIDEKY 142
Cdd:TIGR02349  76 GGGGFNGFDIGFFGdfgdifGDFFGGGGGSGRRRRSGPRR 115
 
Name Accession Description Interval E-value
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 136-245 7.97e-62

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: 202.99  E-value: 7.97e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498 136 DSIDEKYLLHFSHYVNEVVPDSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEELGVGIGVVHAGYERRLAHHLGAHST 215
Cdd:cd02963   1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 56687498 216 PSILGIINGKISFFHNAVV-RENLRQFVESL 245
Cdd:cd02963  81 PAIVGIINGQVTFYHDSSFtKQHVVDFVRKL 111
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 29-142 2.23e-35

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: 137.73  E-value: 2.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498    29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGENqgyqkQQQQR 108
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFN-----GGGGG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 56687498   109 EYRFRHFHENFYFD------ESFFHFPFNSERRDSIDEKY 142
Cdd:TIGR02349  76 GGGGFNGFDIGFFGdfgdifGDFFGGGGGSGRRRRSGPRR 115
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 29-114 2.25e-32

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: 122.12  E-value: 2.25e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGENQGYQKQQQQ 107
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80


                ....*..
gi 56687498 108 REYRFRH 114
Cdd:COG0484  81 AAAEAAA 87
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 29-90 2.29e-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: 2.29e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56687498    29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKN-KDPGAEDKFIQISKAYEILSNEEKRSNYD 90
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 29-96 1.64e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 121.02  E-value: 1.64e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAG 96
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPgDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAA 73
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
29-170 3.90e-25

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 109.14  E-value: 3.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGENQGYQKQQQQR 108
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGEGGFGFDAF 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56687498  109 EYrFRHFHENFYFDESFFHFPFNSERRDSIDEKYLLHFSHyvNEVVPDSfkkpyLIKITSDW 170
Cdd:NF037946  86 DV-FSSFFETINKSGAFLDDSVDESVSADDDLDRLFDDSK--EPSFTSG-----LDEIVQFW 139
DnaJ smart00271
DnaJ molecular chaperone homology domain;
29-85 1.67e-23

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 94.22  E-value: 1.67e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 56687498     29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD--PGAEDKFIQISKAYEILSNEEK 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 3.54e-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: 92.99  E-value: 3.54e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 56687498  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDKFIQISKAYEILSN 82
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 159-246 2.67e-05

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 43.65  E-value: 2.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498 159 KKPYLIKITSDWCFSCIHIEPVWKEVIQELEElGVGIGVVHAGYERRLAHHLGAHSTPSILGIINGKISF-FHNAVVREN 237
Cdd:COG3118  18 DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGG-KVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDrFVGALPKEQ 96


                ....*....
gi 56687498 238 LRQFVESLL 246
Cdd:COG3118  97 LREFLDKVL 105
 
Name Accession Description Interval E-value
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 136-245 7.97e-62

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: 202.99  E-value: 7.97e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498 136 DSIDEKYLLHFSHYVNEVVPDSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEELGVGIGVVHAGYERRLAHHLGAHST 215
Cdd:cd02963   1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 56687498 216 PSILGIINGKISFFHNAVV-RENLRQFVESL 245
Cdd:cd02963  81 PAIVGIINGQVTFYHDSSFtKQHVVDFVRKL 111
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 29-142 2.23e-35

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: 137.73  E-value: 2.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498    29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGENqgyqkQQQQR 108
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFN-----GGGGG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 56687498   109 EYRFRHFHENFYFD------ESFFHFPFNSERRDSIDEKY 142
Cdd:TIGR02349  76 GGGGFNGFDIGFFGdfgdifGDFFGGGGGSGRRRRSGPRR 115
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 29-114 2.25e-32

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: 122.12  E-value: 2.25e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGENQGYQKQQQQ 107
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80


                ....*..
gi 56687498 108 REYRFRH 114
Cdd:COG0484  81 AAAEAAA 87
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 29-90 2.29e-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: 2.29e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56687498    29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKN-KDPGAEDKFIQISKAYEILSNEEKRSNYD 90
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 29-96 1.64e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 121.02  E-value: 1.64e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAG 96
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPgDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAA 73
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 29-98 1.07e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 118.65  E-value: 1.07e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGEN 98
Cdd:PRK14276   5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGAN 74
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 29-137 3.70e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 117.18  E-value: 3.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAG----------EN 98
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAfsgsgqqqqgQE 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 56687498   99 QGYQKQQQQREYRFRHFHENFYFDESFFHFPFNSERRDS 137
Cdd:PRK14291  84 GFSDFGGGNIEDILEDVFDIFGFGDIFGRRRATRERRKT 122
PRK14293 PRK14293
molecular chaperone DnaJ;
29-96 3.78e-28

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 117.01  E-value: 3.78e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAG 96
Cdd:PRK14293   4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQFGEAG 71
PRK14280 PRK14280
molecular chaperone DnaJ;
29-98 1.07e-27

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 115.59  E-value: 1.07e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGEN 98
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPN 74
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 29-126 2.11e-27

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 114.95  E-value: 2.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGENQGYQKQQQQR 108
Cdd:PRK14298   6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSAEDIFR 85

                         90
                 ....*....|....*...
gi 56687498  109 EYRFRHFHENFyfdESFF 126
Cdd:PRK14298  86 GADFGGFGDIF---EMFF 100
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 29-86 3.38e-27

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 104.70  E-value: 3.38e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 56687498  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKR 86
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKgDPKAEERFKEINEAYELLSDAEKR 59
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
29-170 3.90e-25

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 109.14  E-value: 3.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGENQGYQKQQQQR 108
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGEGGFGFDAF 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56687498  109 EYrFRHFHENFYFDESFFHFPFNSERRDSIDEKYLLHFSHyvNEVVPDSfkkpyLIKITSDW 170
Cdd:NF037946  86 DV-FSSFFETINKSGAFLDDSVDESVSADDDLDRLFDDSK--EPSFTSG-----LDEIVQFW 139
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 29-96 7.01e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 107.60  E-value: 7.01e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAG 96
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAG 73
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 29-95 1.36e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 104.64  E-value: 1.36e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDA 95
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTT 71
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 29-96 1.38e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 103.73  E-value: 1.38e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDKFIQISKAYEILSNEEKRSNYDQYGDAG 96
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDnKEAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAG 72
PRK14295 PRK14295
molecular chaperone DnaJ;
23-96 1.44e-23

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 103.78  E-value: 1.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   23 LSALDF---DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQ----YGD 94
Cdd:PRK14295   1 MSTKDYiekDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYDEarslFGN 80


                 ..
gi 56687498   95 AG 96
Cdd:PRK14295  81 GG 82
DnaJ smart00271
DnaJ molecular chaperone homology domain;
29-85 1.67e-23

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 94.22  E-value: 1.67e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 56687498     29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD--PGAEDKFIQISKAYEILSNEEK 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 3.54e-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: 92.99  E-value: 3.54e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 56687498  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDKFIQISKAYEILSN 82
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 29-95 5.30e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 101.50  E-value: 5.30e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDA 95
Cdd:PRK14292   3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDRFGTA 69
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 29-98 1.93e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 100.13  E-value: 1.93e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGEN 98
Cdd:PRK14278   4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVDLGGDPLES 73
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 29-96 2.01e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 100.26  E-value: 2.01e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNkdPG---AEDKFIQISKAYEILSNEEKRSNYDQYGDAG 96
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLN--PGdkeAEQKFKEINEAYEILSDPQKRAQYDQFGHAA 74
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 29-128 2.03e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 99.82  E-value: 2.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGENQGYQkqqqq 107
Cdd:PRK14301   5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDnPEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVNGNGG----- 79

                         90       100
                 ....*....|....*....|.
gi 56687498  108 reyrFRHFHENfyfDESFFHF 128
Cdd:PRK14301  80 ----FGGFSSA---EDIFSHF 93
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
29-91 1.83e-21

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 89.39  E-value: 1.83e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56687498  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPG--AEDKFIQISKAYEILSNEEKRSNYDQ 91
Cdd:COG2214   6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalAEELFQRLNEAYEVLSDPERRAEYDR 70
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 29-142 2.25e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 96.79  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD--PGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGE---NQGYQK 103
Cdd:PRK14282   5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPEnrKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGEqppYQETES 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 56687498  104 QQQQREYRFRHFhENFyFDESFFHFPFNSERRDSIDEKY 142
Cdd:PRK14282  85 GGGFFEDIFKDF-ENI-FNRDIFDIFFGERRTQEEQREY 121
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 29-135 2.36e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 93.68  E-value: 2.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNkdPG---AEDKFIQISKAYEILSNEEKRSNYDQYGDAGENQGYQKQQ 105
Cdd:PRK14294   5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRN--PGdkeAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGTGFSGF 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 56687498  106 QQREYRFRHFHENFyfdESFFHFPFNSERR 135
Cdd:PRK14294  83 SGFDDIFSSFGDIF---EDFFGFGGGRRGR 109
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 29-98 3.79e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 93.15  E-value: 3.79e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGEN 98
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTDPN 74
PRK14289 PRK14289
molecular chaperone DnaJ;
29-96 4.78e-20

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 92.97  E-value: 4.78e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAG 96
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPgDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAG 74
PRK14279 PRK14279
molecular chaperone DnaJ;
29-91 6.51e-20

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 92.87  E-value: 6.51e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQ 91
Cdd:PRK14279  10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPgDPAAEERFKAVSEAHDVLSDPAKRKEYDE 73
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 29-95 6.88e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 92.32  E-value: 6.88e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDA 95
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHA 71
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 29-96 6.90e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 92.60  E-value: 6.90e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAG 96
Cdd:PRK14284   2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPgDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKDG 70
PRK14297 PRK14297
molecular chaperone DnaJ;
29-98 9.71e-20

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 92.15  E-value: 9.71e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGEN 98
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKgNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFN 75
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 29-98 2.72e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 90.46  E-value: 2.72e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYG-DAGEN 98
Cdd:PRK14300   4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGhDAFQN 74
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 29-93 1.31e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 88.45  E-value: 1.31e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD--PGAEDKFIQISKAYEILSNEEKRSNYDQYG 93
Cdd:PRK14290   4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGnkAEAEEKFKEISEAYEVLSDPQKRRQYDQTG 70
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 31-96 1.36e-18

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 89.11  E-value: 1.36e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56687498   31 YRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPgaeDKFIQISKAYEILSNEEKRSNYDQYGDAG 96
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDP---EKFKEISRAYEVLSDPEKRKIYDEYGEEG 93
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 31-98 2.89e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 87.35  E-value: 2.89e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56687498   31 YRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGEN 98
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKgNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVN 75
PRK10266 PRK10266
curved DNA-binding protein;
29-91 1.14e-16

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 81.41  E-value: 1.14e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQ 91
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQ 67
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 29-93 6.95e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 76.95  E-value: 6.95e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDKFIQISKAYEILSNEEKRSNYDQYG 93
Cdd:PRK14285   4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGnKEAESIFKEATEAYEVLIDDNKRAQYDRFG 69
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
29-83 2.64e-13

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 65.59  E-value: 2.64e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56687498  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDK--NKDPG-----AEDKFIQISKAYEILSNE 83
Cdd:COG1076   5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRlaAGLPEeeqrlALQKAAAINEAYETLKDP 66
PRK14288 PRK14288
molecular chaperone DnaJ;
26-143 8.22e-13

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 70.87  E-value: 8.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   26 LDFDPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAGENQGYQKq 104
Cdd:PRK14288   1 MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAgDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGAS- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 56687498  105 qqqrEYRFRHFHENF--YFDESFFHFPFNSER-RDSIDEKYL 143
Cdd:PRK14288  80 ----QSDFSDFFEDLgsFFEDAFGFGARGSKRqKSSIAPDYL 117
djlA PRK09430
co-chaperone DjlA;
29-80 6.78e-09

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 57.51  E-value: 6.78e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498   29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPG--------AEDKFIQISKAYEIL 80
Cdd:PRK09430 201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKLVAKGlppemmemAKEKAQEIQAAYELI 260
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 31-96 3.69e-07

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 54.02  E-value: 3.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56687498    31 YRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRSNYDQYGDAG 96
Cdd:PTZ00341  576 YDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKFGYDG 641
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 29-90 9.62e-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: 9.62e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56687498  29 DPYRVLGVSRTASQAD---IKKAYKKLAREWHPDKNKDPGAEDK---FIQISKAYEILSNEEKRSNYD 90
Cdd:COG5269  44 DLYALLGLSKYRTKAIppqILKAHKKKVYKYHPDKTAAGGNKGCdefFKLIQKAREVLGDRKLRLQYD 111
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 159-246 2.67e-05

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 43.65  E-value: 2.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498 159 KKPYLIKITSDWCFSCIHIEPVWKEVIQELEElGVGIGVVHAGYERRLAHHLGAHSTPSILGIINGKISF-FHNAVVREN 237
Cdd:COG3118  18 DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGG-KVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDrFVGALPKEQ 96


                ....*....
gi 56687498 238 LRQFVESLL 246
Cdd:COG3118  97 LREFLDKVL 105
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 160-243 1.03e-04

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: 41.77  E-value: 1.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498 160 KPYLIKITSDWCFSCIHIEPVWKEVIQELEElgVGIGVVHAGYERRLAHHLGAHSTPSILGIINGKISF-FHNAVVRENL 238
Cdd:cd02947  11 KPVVVDFWAPWCGPCKAIAPVLEELAEEYPK--VKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDrVVGADPKEEL 88


                ....*
gi 56687498 239 RQFVE 243
Cdd:cd02947  89 EEFLE 93
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 162-243 4.14e-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: 40.44  E-value: 4.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498 162 YLIKITSDWCFSCIHIEPVWKEVIQELEELGVGIGVVHAGYERRLAHHLGAHSTPSILGIINGKISFFHNAVVRENLRQF 241
Cdd:cd02994  19 WMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKDGVFRRYQGPRDKEDLISF 98


                ..
gi 56687498 242 VE 243
Cdd:cd02994  99 IE 100
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 151-246 5.15e-04

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 40.83  E-value: 5.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498 151 NEVVPDSFK-KPYLIKITSDWCFSCIHIEPVWKEVIQELEELGVgIGV---------------------VHAGYERRLAH 208
Cdd:COG0526  19 KPLSLADLKgKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVF-VGVdvdenpeavkaflkelglpypVLLDPDGELAK 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 56687498 209 HLGAHSTPSILgII--NGKISFFHN-AVVRENLRQFVESLL 246
Cdd:COG0526  98 AYGVRGIPTTV-LIdkDGKIVARHVgPLSPEELEEALEKLL 137
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 156-231 9.88e-03

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 36.28  E-value: 9.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56687498 156 DSFKKP-----YLIKITSDWCFSCIHIEPVWKEVIQELEELG--VGIGVVHAGYERRLAHHLGAHSTPSILgIINGKISF 228
Cdd:cd03000   7 DSFKDVrkediWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGspVRVGKLDATAYSSIASEFGVRGYPTIK-LLKGDLAY 85


                ...
gi 56687498 229 FHN 231
Cdd:cd03000  86 NYR 88
 
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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