NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958777623|ref|XP_038966359|]
View 

dnaJ homolog subfamily C member 16 isoform X1 [Rattus norvegicus]

Protein Classification

DnaJ homolog subfamily C member 16( domain architecture ID 13534556)

DnaJ homolog subfamily C member 16 (DNAJC16) plays an important role in regulating the size of autophagosomes during the formation process

CATH:  1.10.287.110|3.40.30.10
Gene Ontology:  GO:0016243
PubMed:  9585179|15170475|9099998|10049365|15558583|35729039|9644977|8016869|10542335|12074972|30367780
SCOP:  4000605|3000031

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 ...
 133-242 1.17e-61

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: 200.68  E-value: 1.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623 133 DSIDEKYLLHFSHYVNEVVPDSFKKPYLIKITSDWCFSCIHIEPIWKEVVQELEGLGVGIGVVHAGYERRLAHHLGAHST 212
Cdd:cd02963     1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958777623 213 PSILGIINGKISFFHNAVVH-ENLRQFVESL 242
Cdd:cd02963    81 PAIVGIINGQVTFYHDSSFTkQHVVDFVRKL 111
DnaJ_bact super family cl37091
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 29-139 5.20e-36

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


The actual alignment was detected with superfamily member TIGR02349:

Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 138.89  E-value: 5.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGyqQQREYR 108
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGG--GGGGGG 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958777623 109 FRHFHENFYFD------ESFFHFPFNSERRDSIDEKY 139
Cdd:TIGR02349  79 GFNGFDIGFFGdfgdifGDFFGGGGGSGRRRRSGPRR 115
 
Name Accession Description Interval E-value
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 133-242 1.17e-61

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: 200.68  E-value: 1.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623 133 DSIDEKYLLHFSHYVNEVVPDSFKKPYLIKITSDWCFSCIHIEPIWKEVVQELEGLGVGIGVVHAGYERRLAHHLGAHST 212
Cdd:cd02963     1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958777623 213 PSILGIINGKISFFHNAVVH-ENLRQFVESL 242
Cdd:cd02963    81 PAIVGIINGQVTFYHDSSFTkQHVVDFVRKL 111
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 29-139 5.20e-36

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 138.89  E-value: 5.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGyqQQREYR 108
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGG--GGGGGG 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958777623 109 FRHFHENFYFD------ESFFHFPFNSERRDSIDEKY 139
Cdd:TIGR02349  79 GFNGFDIGFFGdfgdifGDFFGGGGGSGRRRRSGPRR 115
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 29-108 1.80e-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: 1.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQQQREY 107
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80


                  .
gi 1958777623 108 R 108
Cdd:COG0484    81 A 81
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 29-90 1.23e-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: 116.80  E-value: 1.23e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKN-KDPGAEDKFIQISKAYEILSNEEKRTNYD 90
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 29-134 2.58e-30

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 122.96  E-value: 2.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAG-ENQGYQQQREY 107
Cdd:PRK14291    4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAfSGSGQQQQGQE 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958777623 108 RF------------RHFHENFYFDESFFHFPFNSERRDS 134
Cdd:PRK14291   84 GFsdfgggniedilEDVFDIFGFGDIFGRRRATRERRKT 122
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
29-167 4.36e-25

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 108.75  E-value: 4.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQ--GYQQQRE 106
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGegGFGFDAF 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958777623 107 YRFRHFHENFYFDESFFHFPFNSERRDSIDEKYLLHFSHyvNEVVPDSfkkpyLIKITSDW 167
Cdd:NF037946   86 DVFSSFFETINKSGAFLDDSVDESVSADDDLDRLFDDSK--EPSFTSG-----LDEIVQFW 139
DnaJ smart00271
DnaJ molecular chaperone homology domain;
29-85 7.53e-24

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 94.99  E-value: 7.53e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777623   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 1.87e-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: 1.87e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDKFIQISKAYEILSN 82
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 156-243 2.18e-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: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623 156 KKPYLIKITSDWCFSCIHIEPIWKEVVQELEGlGVGIGVVHAGYERRLAHHLGAHSTPSILGIINGKISFFHNAVVHEN- 234
Cdd:COG3118    18 DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGG-KVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKEq 96


                  ....*....
gi 1958777623 235 LRQFVESLL 243
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 ...
 133-242 1.17e-61

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: 200.68  E-value: 1.17e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623 133 DSIDEKYLLHFSHYVNEVVPDSFKKPYLIKITSDWCFSCIHIEPIWKEVVQELEGLGVGIGVVHAGYERRLAHHLGAHST 212
Cdd:cd02963     1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958777623 213 PSILGIINGKISFFHNAVVH-ENLRQFVESL 242
Cdd:cd02963    81 PAIVGIINGQVTFYHDSSFTkQHVVDFVRKL 111
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 29-139 5.20e-36

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 138.89  E-value: 5.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGyqQQREYR 108
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGG--GGGGGG 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958777623 109 FRHFHENFYFD------ESFFHFPFNSERRDSIDEKY 139
Cdd:TIGR02349  79 GFNGFDIGFFGdfgdifGDFFGGGGGSGRRRRSGPRR 115
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 29-108 1.80e-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: 1.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQQQREY 107
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80


                  .
gi 1958777623 108 R 108
Cdd:COG0484    81 A 81
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 29-90 1.23e-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: 116.80  E-value: 1.23e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKN-KDPGAEDKFIQISKAYEILSNEEKRTNYD 90
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 29-134 2.58e-30

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 122.96  E-value: 2.58e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAG-ENQGYQQQREY 107
Cdd:PRK14291    4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAfSGSGQQQQGQE 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958777623 108 RF------------RHFHENFYFDESFFHFPFNSERRDS 134
Cdd:PRK14291   84 GFsdfgggniedilEDVFDIFGFGDIFGRRRATRERRKT 122
PRK14280 PRK14280
molecular chaperone DnaJ;
29-133 3.09e-29

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 119.83  E-value: 3.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQQQReYR 108
Cdd:PRK14280    5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGGGG-FG 83

                          90       100
                  ....*....|....*....|....*..
gi 1958777623 109 FRHFHENFYFDESFFHFpFN--SERRD 133
Cdd:PRK14280   84 GGDFGGGFGFEDIFSSF-FGggGRRRD 109
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 29-100 5.75e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 119.09  E-value: 5.75e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQG 100
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPgDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEQG 77
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 29-101 7.97e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 118.65  E-value: 7.97e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGY 101
Cdd:PRK14276    5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGF 77
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 29-123 4.24e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 116.49  E-value: 4.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQQQREYR 108
Cdd:PRK14298    6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSAEDIFR 85

                          90
                  ....*....|....*...
gi 1958777623 109 ---FRHFHENFyfdESFF 123
Cdd:PRK14298   86 gadFGGFGDIF---EMFF 100
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 29-86 1.52e-27

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 105.47  E-value: 1.52e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKR 86
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKgDPKAEERFKEINEAYELLSDAEKR 59
PRK14293 PRK14293
molecular chaperone DnaJ;
29-96 5.42e-27

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 113.16  E-value: 5.42e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAG 96
Cdd:PRK14293    4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQFGEAG 71
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 29-132 5.92e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 110.30  E-value: 5.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENqGYQQQREYR 108
Cdd:PRK14283    6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGMD-GFSQEDIFN 84

                          90       100
                  ....*....|....*....|....*....
gi 1958777623 109 FRHFHE-----NFYFDESFFHFPFNSERR 132
Cdd:PRK14283   85 NINFEDifqgfGFGIGNIFDMFGFGGGSR 113
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 29-102 6.26e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 108.10  E-value: 6.26e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQ 102
Cdd:PRK14299    5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQ 78
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
29-167 4.36e-25

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 108.75  E-value: 4.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQ--GYQQQRE 106
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHDGVDGegGFGFDAF 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958777623 107 YRFRHFHENFYFDESFFHFPFNSERRDSIDEKYLLHFSHyvNEVVPDSfkkpyLIKITSDW 167
Cdd:NF037946   86 DVFSSFFETINKSGAFLDDSVDESVSADDDLDRLFDDSK--EPSFTSG-----LDEIVQFW 139
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 29-132 5.92e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 107.58  E-value: 5.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNkdPG---AEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQQQR 105
Cdd:PRK14277    6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLN--PGdkeAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFDPGGFGQG 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958777623 106 EYRFRHFHENFY-FD--------ESFFHFPFNSERR 132
Cdd:PRK14277   84 GFGQGGFGGGGFdFDfggfgdifEDIFGDFFGTGRR 119
DnaJ smart00271
DnaJ molecular chaperone homology domain;
29-85 7.53e-24

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 94.99  E-value: 7.53e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777623   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 1.87e-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: 1.87e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDKFIQISKAYEILSN 82
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
PRK14295 PRK14295
molecular chaperone DnaJ;
23-90 1.95e-23

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 103.00  E-value: 1.95e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958777623  23 LSALDF---DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRTNYD 90
Cdd:PRK14295    1 MSTKDYiekDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYD 72
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 29-139 4.57e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 101.41  E-value: 4.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD--PGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQQQR- 105
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPEnrKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPPYQETEs 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958777623 106 -----EYRFRHFhENFyFDESFFHFPFNSERRDSIDEKY 139
Cdd:PRK14282   85 gggffEDIFKDF-ENI-FNRDIFDIFFGERRTQEEQREY 121
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 29-100 7.42e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 100.90  E-value: 7.42e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQG 100
Cdd:PRK14278    4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVDLGGDPLESAG 75
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 29-95 8.81e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 100.73  E-value: 8.81e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDA 95
Cdd:PRK14292    3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDRFGTA 69
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 29-96 9.69e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 101.04  E-value: 9.69e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDKFIQISKAYEILSNEEKRTNYDHYGDAG 96
Cdd:PRK14281    4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDnKEAEEHFKEVNEAYEVLSNDDKRRRYDQFGHAG 72
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 29-132 2.39e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 99.43  E-value: 2.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGEN-----QGYQ 102
Cdd:PRK14301    5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDnPEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVNgnggfGGFS 84

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958777623 103 QQrEYRFRHFHENFyfdESFFHFPFNSERR 132
Cdd:PRK14301   85 SA-EDIFSHFSDIF---GDLFGFSGGGSRR 110
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 29-132 5.79e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 98.30  E-value: 5.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNkdPG---AEDKFIQISKAYEILSNEEKRTNYDHYGDAG-ENQGYQqq 104
Cdd:PRK14294    5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRN--PGdkeAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGlSGTGFS-- 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958777623 105 reyRFRHFHENF--YFD--ESFFHFPFNSERR 132
Cdd:PRK14294   81 ---GFSGFDDIFssFGDifEDFFGFGGGRRGR 109
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
29-90 2.64e-21

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 88.62  E-value: 2.64e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPG--AEDKFIQISKAYEILSNEEKRTNYD 90
Cdd:COG2214     6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 29-101 3.10e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 95.85  E-value: 3.10e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGY 101
Cdd:PRK14287    5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTDPNQGF 77
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 29-138 5.91e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 92.38  E-value: 5.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYG-DAGENqgyQQQREY 107
Cdd:PRK14300    4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGhDAFQN---QQSRGG 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958777623 108 RFRH--FHE--NFYFDESFFHFPFNSERRDSIDEK 138
Cdd:PRK14300   81 GGNHggFHPdiNDIFGDFFSDFMGGSRRSRPTSSK 115
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 29-100 6.51e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 92.21  E-value: 6.51e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQG 100
Cdd:PRK14284    2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPgDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKDGPFAG 74
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 29-122 9.85e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 91.53  E-value: 9.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD--PGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQQQRE 106
Cdd:PRK14290    4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGnkAEAEEKFKEISEAYEVLSDPQKRRQYDQTGTVDFGAGGSNFNW 83

                          90
                  ....*....|....*..
gi 1958777623 107 YRFRHFHE-NFYFDESF 122
Cdd:PRK14290   84 DNFTHFSDiNDIFNQIF 100
PRK14279 PRK14279
molecular chaperone DnaJ;
29-90 1.12e-19

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 91.72  E-value: 1.12e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRTNYD 90
Cdd:PRK14279   10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPgDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 31-102 3.42e-19

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 90.65  E-value: 3.42e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958777623  31 YRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPgaeDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQ 102
Cdd:PTZ00037   31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDP---EKFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQ 99
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 29-95 4.46e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 89.62  E-value: 4.46e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDA 95
Cdd:PRK14296    5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHA 71
PRK14289 PRK14289
molecular chaperone DnaJ;
29-96 7.23e-19

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 89.12  E-value: 7.23e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAG 96
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPgDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAG 74
PRK14297 PRK14297
molecular chaperone DnaJ;
29-132 8.22e-19

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 88.69  E-value: 8.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGEN-------QG 100
Cdd:PRK14297    5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKgNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNgaggfgsGG 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958777623 101 YQQQREYRFRHFHENFyfdESFFHFPFNSERR 132
Cdd:PRK14297   85 FGGFDFSDMGGFGDIF---DSFFGGGFGSSSR 113
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 31-100 3.76e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 86.58  E-value: 3.76e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958777623  31 YRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQG 100
Cdd:PRK14286    7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKgNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAG 77
PRK10266 PRK10266
curved DNA-binding protein;
29-123 1.95e-17

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 83.72  E-value: 1.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYD----HYGDAGENQGYQQQ 104
Cdd:PRK10266    5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDqlwqHRNDPQFNRQFQHG 84

                          90       100
                  ....*....|....*....|.
gi 1958777623 105 --REYRFRHFHENFyfdESFF 123
Cdd:PRK10266   85 dgQSFNAEDFDDIF---SSIF 102
PRK14288 PRK14288
molecular chaperone DnaJ;
26-140 6.53e-15

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 77.04  E-value: 6.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  26 LDFDPYRVLGVSRTASQADIKKAYKKLAREWHPDKNK-DPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQGYQQQ 104
Cdd:PRK14288    1 MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAgDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGASQ 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958777623 105 REyrFRHFHENF--YFDESFFHFPFNSER-RDSIDEKYL 140
Cdd:PRK14288   81 SD--FSDFFEDLgsFFEDAFGFGARGSKRqKSSIAPDYL 117
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 29-93 1.16e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 76.18  E-value: 1.16e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKD-PGAEDKFIQISKAYEILSNEEKRTNYDHYG 93
Cdd:PRK14285    4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGnKEAESIFKEATEAYEVLIDDNKRAQYDRFG 69
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
29-83 2.22e-13

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 65.59  E-value: 2.22e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDK--NKDPG-----AEDKFIQISKAYEILSNE 83
Cdd:COG1076     5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRlaAGLPEeeqrlALQKAAAINEAYETLKDP 66
djlA PRK09430
co-chaperone DjlA;
29-80 7.04e-09

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 57.13  E-value: 7.04e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623  29 DPYRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPG--------AEDKFIQISKAYEIL 80
Cdd:PRK09430  201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKLVAKGlppemmemAKEKAQEIQAAYELI 260
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 31-99 6.00e-07

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 52.87  E-value: 6.00e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777623   31 YRVLGVSRTASQADIKKAYKKLAREWHPDKNKDPGAEDKFIQISKAYEILSNEEKRTNYDHYGDAGENQ 99
Cdd:PTZ00341   576 YDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKFGYDGIKG 644
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 29-90 6.35e-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: 48.88  E-value: 6.35e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958777623  29 DPYRVLGVSRTASQAD---IKKAYKKLAREWHPDKNKDPGAEDK---FIQISKAYEILSNEEKRTNYD 90
Cdd:COG5269    44 DLYALLGLSKYRTKAIppqILKAHKKKVYKYHPDKTAAGGNKGCdefFKLIQKAREVLGDRKLRLQYD 111
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 156-243 2.18e-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: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623 156 KKPYLIKITSDWCFSCIHIEPIWKEVVQELEGlGVGIGVVHAGYERRLAHHLGAHSTPSILGIINGKISFFHNAVVHEN- 234
Cdd:COG3118    18 DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGG-KVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKEq 96


                  ....*....
gi 1958777623 235 LRQFVESLL 243
Cdd:COG3118    97 LREFLDKVL 105
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 148-243 2.60e-05

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 44.30  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623 148 NEVVPDSFK-KPYLIKITSDWCFSCIHIEPIWKEVVQELEGLGVgIGV---------------------VHAGYERRLAH 205
Cdd:COG0526    19 KPLSLADLKgKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVF-VGVdvdenpeavkaflkelglpypVLLDPDGELAK 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958777623 206 HLGAHSTPSILgII--NGKISFFHN-AVVHENLRQFVESLL 243
Cdd:COG0526    98 AYGVRGIPTTV-LIdkDGKIVARHVgPLSPEELEEALEKLL 137
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 159-240 2.71e-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: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623 159 YLIKITSDWCFSCIHIEPIWKEVVQELEGLGVGIGVVHAGYERRLAHHLGAHSTPSILGIINGKISFFHNAVVHENLRQF 238
Cdd:cd02994    19 WMIEFYAPWCPACQQLQPEWEEFADWSDDLGINVAKVDVTQEPGLSGRFFVTALPTIYHAKDGVFRRYQGPRDKEDLISF 98


                  ..
gi 1958777623 239 VE 240
Cdd:cd02994    99 IE 100
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 157-240 3.92e-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: 39.85  E-value: 3.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623 157 KPYLIKITSDWCFSCIHIEPIWKEVVQELEglGVGIGVVHAGYERRLAHHLGAHSTPSILGIINGKISF-FHNAVVHENL 235
Cdd:cd02947    11 KPVVVDFWAPWCGPCKAIAPVLEELAEEYP--KVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDrVVGADPKEEL 88


                  ....*
gi 1958777623 236 RQFVE 240
Cdd:cd02947    89 EEFLE 93
PHA03102 PHA03102
Small T antigen; Reviewed
 34-64 8.20e-03

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 37.34  E-value: 8.20e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958777623  34 LGVSRTA--SQADIKKAYKKLAREWHPDKNKDP 64
Cdd:PHA03102   11 LGLPRSAwgNLPLMRKAYLRKCLEFHPDKGGDE 43
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 153-228 8.48e-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: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777623 153 DSFKKP-----YLIKITSDWCFSCIHIEPIWKEVVQELEGLG--VGIGVVHAGYERRLAHHLGAHSTPSILgIINGKISF 225
Cdd:cd03000     7 DSFKDVrkediWLVDFYAPWCGHCKKLEPVWNEVGAELKSSGspVRVGKLDATAYSSIASEFGVRGYPTIK-LLKGDLAY 85


                  ...
gi 1958777623 226 FHN 228
Cdd:cd03000    86 NYR 88
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 149-216 8.81e-03

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 36.05  E-value: 8.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958777623 149 EVVPDSFK------KPYLIKITSDWCFSCIHIEPIWKEVVQELEG-LGVGIGVVHAGYERRLAHHLGAHSTPSIL 216
Cdd:cd02961     2 ELTDDNFDelvkdsKDVLVEFYAPWCGHCKALAPEYEKLAKELKGdGKVVVAKVDCTANNDLCSEYGVRGYPTIK 76
 
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