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Conserved domains on  [gi|1063710315|ref|NP_001319504|]
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DNAJ heat shock N-terminal domain-containing protein [Arabidopsis thaliana]

Protein Classification

J domain-containing protein( domain architecture ID 1003637)

J domain-containing protein with protein disulfide isomerase (PDI) domain(s), similar to human DnaJ homolog subfamily C member 10 (also called ER-resident protein ERdj5) that is involved in the correct folding of proteins and degradation of misfolded proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
27-88 1.22e-30

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: 113.72  E-value: 1.22e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKN-KDKGAQEKFAEINNAYEILSDEEKRKNYD 88
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14289 super family cl36358
molecular chaperone DnaJ;
27-204 1.90e-23

molecular chaperone DnaJ;


The actual alignment was detected with superfamily member PRK14289:

Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 102.60  E-value: 1.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYG-----DEKGQPGFD 100
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPgDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGhagvgGAAGGGGFS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315 101 SGfpggnggysysssgggfnfggpggwqnmgggggsksfsfsfggpsessfGFGMDDIFSMFS---GGSSKGKEQFGGFG 177
Cdd:PRK14289   86 GE-------------------------------------------------GMSMEDIFSMFGdifGGHGGGFGGFGGFG 116
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063710315 178 SSSNAESKSKSSTV-----AAIKTINSQVYKK 204
Cdd:PRK14289  117 GGGSQQRVFRGSDLrvkvkLNLKEISTGVEKK 148
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
435-558 5.32e-03

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd02983:

Pssm-ID: 469754  Cd Length: 130  Bit Score: 37.33  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315 435 EKIPLLSRPNFDSICGENtPVCIIGAFRS-----SNGKEKLQSIMSKVSQKSlsrrqasttgSQDTVSYSLLDATKQSAF 509
Cdd:cd02983     3 EIIELTSEDVFEETCEEK-QLCIIAFLPHildcqASCRNKYLEILKSVAEKF----------KKKPWGWLWTEAGAQLDL 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1063710315 510 LSSLDKSEFKTSSdklLIAYKPRRGKFATFKGDMTIEEVEKFVAAVLNG 558
Cdd:cd02983    72 EEALNIGGFGYPA---MVAINFRKMKFATLKGSFSEDGINEFLRELSYG 117
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
27-88 1.22e-30

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: 113.72  E-value: 1.22e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKN-KDKGAQEKFAEINNAYEILSDEEKRKNYD 88
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
27-180 6.20e-30

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: 120.78  E-value: 6.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYG---DEKGQPGFDSGF 103
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGhagFNGGGGGGGGGF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710315 104 pggnggysysssgggfnfggpggwqnmgggggsksfsfsfgGPSESSFGFGMDDIFSMFsggsskgkeqFGGFGSSS 180
Cdd:TIGR02349  81 -----------------------------------------NGFDIGFFGDFGDIFGDF----------FGGGGGSG 106
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
27-94 5.27e-29

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: 112.10  E-value: 5.27e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYGDEK 94
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAA 69
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
27-100 7.90e-27

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 113.38  E-value: 7.90e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYG--DEKGQPGFD 100
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGhdGVDGEGGFG 81
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
27-103 1.06e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 112.10  E-value: 1.06e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGDEKGQPGFDSGF 103
Cdd:PRK14276    5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFGGGA 81
PRK14289 PRK14289
molecular chaperone DnaJ;
27-204 1.90e-23

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 102.60  E-value: 1.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYG-----DEKGQPGFD 100
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPgDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGhagvgGAAGGGGFS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315 101 SGfpggnggysysssgggfnfggpggwqnmgggggsksfsfsfggpsessfGFGMDDIFSMFS---GGSSKGKEQFGGFG 177
Cdd:PRK14289   86 GE-------------------------------------------------GMSMEDIFSMFGdifGGHGGGFGGFGGFG 116
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063710315 178 SSSNAESKSKSSTV-----AAIKTINSQVYKK 204
Cdd:PRK14289  117 GGGSQQRVFRGSDLrvkvkLNLKEISTGVEKK 148
DnaJ smart00271
DnaJ molecular chaperone homology domain;
26-83 1.06e-22

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 91.53  E-value: 1.06e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315   26 VDPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKD--KGAQEKFAEINNAYEILSDEEK 83
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGdkEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
27-80 1.28e-22

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: 91.07  E-value: 1.28e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKD-KGAQEKFAEINNAYEILSD 80
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
P5_C cd02983
P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI) ...
435-558 5.32e-03

P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI)-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI.


Pssm-ID: 239281  Cd Length: 130  Bit Score: 37.33  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315 435 EKIPLLSRPNFDSICGENtPVCIIGAFRS-----SNGKEKLQSIMSKVSQKSlsrrqasttgSQDTVSYSLLDATKQSAF 509
Cdd:cd02983     3 EIIELTSEDVFEETCEEK-QLCIIAFLPHildcqASCRNKYLEILKSVAEKF----------KKKPWGWLWTEAGAQLDL 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1063710315 510 LSSLDKSEFKTSSdklLIAYKPRRGKFATFKGDMTIEEVEKFVAAVLNG 558
Cdd:cd02983    72 EEALNIGGFGYPA---MVAINFRKMKFATLKGSFSEDGINEFLRELSYG 117
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
27-88 1.22e-30

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: 113.72  E-value: 1.22e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKN-KDKGAQEKFAEINNAYEILSDEEKRKNYD 88
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
27-180 6.20e-30

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: 120.78  E-value: 6.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYG---DEKGQPGFDSGF 103
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQFGhagFNGGGGGGGGGF 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710315 104 pggnggysysssgggfnfggpggwqnmgggggsksfsfsfgGPSESSFGFGMDDIFSMFsggsskgkeqFGGFGSSS 180
Cdd:TIGR02349  81 -----------------------------------------NGFDIGFFGDFGDIFGDF----------FGGGGGSG 106
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
27-94 5.27e-29

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: 112.10  E-value: 5.27e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYGDEK 94
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAA 69
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
27-100 7.90e-27

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 113.38  E-value: 7.90e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYG--DEKGQPGFD 100
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYDKYGhdGVDGEGGFG 81
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
27-103 1.06e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 112.10  E-value: 1.06e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGDEKGQPGFDSGF 103
Cdd:PRK14276    5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFGGGA 81
PRK14280 PRK14280
molecular chaperone DnaJ;
27-168 2.73e-26

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 110.58  E-value: 2.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGDEKGQPGFDSGFpgg 106
Cdd:PRK14280    5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGGGG--- 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063710315 107 nggysysssgggfnfggpggwqnmgggggsksfsfsfGGPSESSFGFGMDDIFSMFSGGSSK 168
Cdd:PRK14280   82 -------------------------------------FGGGDFGGGFGFEDIFSSFFGGGGR 106
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
27-102 9.67e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 109.08  E-value: 9.67e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYGDEkgqpGFDSG 102
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPgDKEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHA----AFEQG 77
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
27-104 4.40e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 105.41  E-value: 4.40e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGDEKGQPGFDSGFP 104
Cdd:PRK14299    5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQGPPP 82
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
27-85 4.99e-25

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 98.15  E-value: 4.99e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRK 85
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKgDPKAEERFKEINEAYELLSDAEKRA 60
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
27-93 7.83e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 103.70  E-value: 7.83e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGDE 93
Cdd:PRK14291    4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGHA 70
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
27-91 1.48e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 102.62  E-value: 1.48e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYG 91
Cdd:PRK14298    6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFG 70
PRK14289 PRK14289
molecular chaperone DnaJ;
27-204 1.90e-23

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 102.60  E-value: 1.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYG-----DEKGQPGFD 100
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPgDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGhagvgGAAGGGGFS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315 101 SGfpggnggysysssgggfnfggpggwqnmgggggsksfsfsfggpsessfGFGMDDIFSMFS---GGSSKGKEQFGGFG 177
Cdd:PRK14289   86 GE-------------------------------------------------GMSMEDIFSMFGdifGGHGGGFGGFGGFG 116
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063710315 178 SSSNAESKSKSSTV-----AAIKTINSQVYKK 204
Cdd:PRK14289  117 GGGSQQRVFRGSDLrvkvkLNLKEISTGVEKK 148
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
27-103 7.58e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 100.51  E-value: 7.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGDEKGQP-----GFDS 101
Cdd:PRK14278    4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVDLGGDPLESAgggggGFGG 83

                  ..
gi 1063710315 102 GF 103
Cdd:PRK14278   84 GF 85
DnaJ smart00271
DnaJ molecular chaperone homology domain;
26-83 1.06e-22

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 91.53  E-value: 1.06e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315   26 VDPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKD--KGAQEKFAEINNAYEILSDEEK 83
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGdkEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
27-80 1.28e-22

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: 91.07  E-value: 1.28e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKD-KGAQEKFAEINNAYEILSD 80
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
PRK14293 PRK14293
molecular chaperone DnaJ;
27-104 2.02e-22

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 99.29  E-value: 2.02e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGdEKGQPGfDSGFP 104
Cdd:PRK14293    4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQFG-EAGVSG-AAGFP 79
PRK14297 PRK14297
molecular chaperone DnaJ;
27-102 5.06e-22

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 98.32  E-value: 5.06e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYG--DEKGQPGFDSG 102
Cdd:PRK14297    5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKgNKEAEEKFKEINEAYQVLSDPQKKAQYDQFGtaDFNGAGGFGSG 83
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
26-100 1.30e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 96.88  E-value: 1.30e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710315  26 VDPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYG--DEKGQPGFD 100
Cdd:PRK14292    2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDRFGtaPGAGMPGGD 78
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
23-175 9.84e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 94.12  E-value: 9.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  23 AKSVDPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYgdekGQPGFDsG 102
Cdd:PRK14283    2 AEKRDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQF----GHAGMD-G 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063710315 103 FPGGNGGYSYSSSGGGfnfggpggwqnmgggggsksfsfsfggpseSSFGFGMDDIFSMFS-GGSSKGKEQFGG 175
Cdd:PRK14283   77 FSQEDIFNNINFEDIF------------------------------QGFGFGIGNIFDMFGfGGGSRHGPQRGA 120
PRK14295 PRK14295
molecular chaperone DnaJ;
27-104 1.01e-20

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 94.53  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYD----LYGDEKGQPGFDS 101
Cdd:PRK14295   10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYDearsLFGNGGFRPGPGG 89

                  ...
gi 1063710315 102 GFP 104
Cdd:PRK14295   90 GGG 92
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
27-102 1.76e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 93.71  E-value: 1.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYGDE------KGQPGF 99
Cdd:PRK14277    6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPgDKEAEQKFKEINEAYEILSDPQKRAQYDQFGHAafdpggFGQGGF 85

                  ...
gi 1063710315 100 DSG 102
Cdd:PRK14277   86 GQG 88
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
27-102 4.01e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 92.56  E-value: 4.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKD-KGAQEKFAEINNAYEILSDEEKRKNYDLYGD--------EKGQP 97
Cdd:PRK14281    4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDnKEAEEHFKEVNEAYEVLSNDDKRRRYDQFGHagvgssaaSGGGP 83

                  ....*
gi 1063710315  98 GFDSG 102
Cdd:PRK14281   84 GYGGG 88
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
29-104 6.53e-19

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 89.11  E-value: 6.53e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063710315  29 YKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDkgaQEKFAEINNAYEILSDEEKRKNYDLYGDEkgqpGFDSGFP 104
Cdd:PTZ00037   31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD---PEKFKEISRAYEVLSDPEKRKIYDEYGEE----GLEGGEQ 99
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
27-103 1.08e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 87.90  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYGDE-------KGQPG 98
Cdd:PRK14294    5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPgDKEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEglsgtgfSGFSG 84

                  ....*
gi 1063710315  99 FDSGF 103
Cdd:PRK14294   85 FDDIF 89
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
27-99 1.12e-18

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 80.92  E-value: 1.12e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKG--AQEKFAEINNAYEILSDEEKRKNYDLYGDEKGQPGF 99
Cdd:COG2214     6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKGSA 80
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
27-99 6.26e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 86.05  E-value: 6.26e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYGDE---KGQPGF 99
Cdd:PRK14284    2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPgDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKDgpfAGAGGF 78
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
27-103 7.57e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 85.56  E-value: 7.57e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKG-AQEKFAEINNAYEILSDEEKRKNYDLYGDEK-GQPGFDSGF 103
Cdd:PRK14301    5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPeAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGvNGNGGFGGF 83
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
24-103 1.50e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 84.61  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  24 KSVDPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGDE--KGQPGFDS 101
Cdd:PRK14296    2 KKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQFGHAafDGSSGFSS 81

                  ..
gi 1063710315 102 GF 103
Cdd:PRK14296   82 NF 83
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
29-102 2.17e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 84.27  E-value: 2.17e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063710315  29 YKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYGD---EKGQPGFDSG 102
Cdd:PRK14286    7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKgNKESEEKFKEATEAYEILRDPKKRQAYDQFGKagvNAGAGGFGQG 84
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
25-103 3.10e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 83.53  E-value: 3.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  25 SVDPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGDE-------KGQP 97
Cdd:PRK14300    2 SQDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRFGHDafqnqqsRGGG 81

                  ....*.
gi 1063710315  98 GFDSGF 103
Cdd:PRK14300   82 GNHGGF 87
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
27-91 2.44e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 80.99  E-value: 2.44e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKD--KGAQEKFAEINNAYEILSDEEKRKNYDLYG 91
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPEnrKEAEQKFKEIQEAYEVLSDPQKRAMYDRFG 71
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
27-102 9.10e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 79.20  E-value: 9.10e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKD--KGAQEKFAEINNAYEILSDEEKRKNYdlygDEKGQPGFDSG 102
Cdd:PRK14290    4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGnkAEAEEKFKEISEAYEVLSDPQKRRQY----DQTGTVDFGAG 77
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
27-103 1.26e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 78.49  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKD-KGAQEKFAEINNAYEILSDEEKRKNYDLYGDEK-----GQPGFD 100
Cdd:PRK14285    4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGnKEAESIFKEATEAYEVLIDDNKRAQYDRFGHTAfegggGFEGFS 83

                  ...
gi 1063710315 101 SGF 103
Cdd:PRK14285   84 GGF 86
PRK14279 PRK14279
molecular chaperone DnaJ;
27-88 3.02e-15

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 77.85  E-value: 3.02e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYD 88
Cdd:PRK14279   10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPgDPAAEERFKAVSEAHDVLSDPAKRKEYD 72
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
27-102 4.06e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 77.36  E-value: 4.06e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGDEKGQPGFDSG 102
Cdd:PRK14287    5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTDPNQGFGGG 80
PRK10266 PRK10266
curved DNA-binding protein;
27-103 2.82e-13

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 70.62  E-value: 2.82e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYGDEKGQPGFDSGF 103
Cdd:PRK10266    5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQLWQHRNDPQFNRQF 81
PRK14288 PRK14288
molecular chaperone DnaJ;
29-93 7.39e-12

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 67.02  E-value: 7.39e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063710315  29 YKVLGVSKDAKQREIQKAFHKQSLKYHPDKNK-DKGAQEKFAEINNAYEILSDEEKRKNYDLYGDE 93
Cdd:PRK14288    6 YEILEVEKHSNQETIKKSYRKLALKYHPDRNAgDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKK 71
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
27-81 7.02e-11

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 58.27  E-value: 7.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDK-------NKDKGAQEKFAEINNAYEILSDE 81
Cdd:COG1076     5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaglpeEEQRLALQKAAAINEAYETLKDP 66
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
29-91 6.56e-08

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 55.56  E-value: 6.56e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063710315   29 YKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKGAQEKFAEINNAYEILSDEEKRKNYDLYG 91
Cdd:PTZ00341   576 YDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKFG 638
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
24-88 5.79e-07

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 51.96  E-value: 5.79e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063710315  24 KSVDPYKVLGVSK---DAKQREIQKAFHKQSLKYHPDKNK---DKGAQEKFAEINNAYEILSDEEKRKNYD 88
Cdd:COG5269    41 KKVDLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAaggNKGCDEFFKLIQKAREVLGDRKLRLQYD 111
djlA PRK09430
co-chaperone DjlA;
27-78 1.03e-06

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 50.58  E-value: 1.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315  27 DPYKVLGVSKDAKQREIQKAFHKQSLKYHPDKNKDKG--------AQEKFAEINNAYEIL 78
Cdd:PRK09430  201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKLVAKGlppemmemAKEKAQEIQAAYELI 260
PHA03102 PHA03102
Small T antigen; Reviewed
43-102 2.11e-03

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 38.88  E-value: 2.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063710315  43 IQKAFHKQSLKYHPDKNkdkGAQEKFAEINNAYEILSDEEKRKNYDLYGD----EKGQPGFDSG 102
Cdd:PHA03102   24 MRKAYLRKCLEFHPDKG---GDEEKMKELNTLYKKFRESVKSLRDLDGEEdsssEEEDVPSGYV 84
hscB PRK01356
co-chaperone HscB; Provisional
43-89 4.00e-03

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 38.32  E-value: 4.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063710315  43 IQKAFHKQSLKYHPDKNKDKGAQEKF----AEINNAYEILSDEEKRKNYDL 89
Cdd:PRK01356   21 LEKQYFAMQVKYHPDKAKTLQEKEQNliiaSELNNAYSTLKDALKRAEYML 71
P5_C cd02983
P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI) ...
435-558 5.32e-03

P5 family, C-terminal redox inactive TRX-like domain; P5 is a protein disulfide isomerase (PDI)-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. The C-terminal domain is likely involved in substrate binding, similar to the b and b' domains of PDI.


Pssm-ID: 239281  Cd Length: 130  Bit Score: 37.33  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063710315 435 EKIPLLSRPNFDSICGENtPVCIIGAFRS-----SNGKEKLQSIMSKVSQKSlsrrqasttgSQDTVSYSLLDATKQSAF 509
Cdd:cd02983     3 EIIELTSEDVFEETCEEK-QLCIIAFLPHildcqASCRNKYLEILKSVAEKF----------KKKPWGWLWTEAGAQLDL 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1063710315 510 LSSLDKSEFKTSSdklLIAYKPRRGKFATFKGDMTIEEVEKFVAAVLNG 558
Cdd:cd02983    72 EEALNIGGFGYPA---MVAINFRKMKFATLKGSFSEDGINEFLRELSYG 117
PHA02624 PHA02624
large T antigen; Provisional
43-104 5.73e-03

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 39.58  E-value: 5.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063710315  43 IQKAFHKQSLKYHPDKNkdkGAQEKFAEINNAYEILsDEEKRKNYDLYGDEKGQPGFDSGFP 104
Cdd:PHA02624   30 MRKAYLRKCKEYHPDKG---GDEEKMKRLNSLYKKL-QEGVKSARQSFGTQDSSEIPTYGTP 87
 
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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