NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2031264001|ref|NP_001381617|]
View 

dnaJ homolog subfamily C member 14 isoform 1 [Homo sapiens]

Protein Classification

DnaJ and Jiv90 domain-containing protein( domain architecture ID 10446388)

DnaJ and Jiv90 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 532-620 3.06e-46

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


:

Pssm-ID: 464360  Cd Length: 92  Bit Score: 159.05  E-value: 3.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 532 MNTMMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQR---VGI 608
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLWRYYACMDGKVYDITEWAICQGdslMHC 80

                          90
                  ....*....|..
gi 2031264001 609 SPDTHRVPYHIS 620
Cdd:pfam14901  81 RPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 443-504 1.55e-22

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: 91.38  E-value: 1.55e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2031264001 443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 532-620 3.06e-46

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


Pssm-ID: 464360  Cd Length: 92  Bit Score: 159.05  E-value: 3.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 532 MNTMMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQR---VGI 608
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLWRYYACMDGKVYDITEWAICQGdslMHC 80

                          90
                  ....*....|..
gi 2031264001 609 SPDTHRVPYHIS 620
Cdd:pfam14901  81 RPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 443-504 1.55e-22

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: 91.38  E-value: 1.55e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2031264001 443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 443-515 8.55e-20

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: 86.29  E-value: 8.55e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2031264001 443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNAEKRKEYEMKRMAENELSR 515
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLA 74
DnaJ smart00271
DnaJ molecular chaperone homology domain;
443-499 2.38e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 76.50  E-value: 2.38e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2031264001  443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKN--HHPRAEEAFKVLRAAWDIVSNAEK 499
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNpgDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 443-496 8.15e-17

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: 74.89  E-value: 8.15e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2031264001 443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSN 496
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNpDDPEAEEKFKEINEAYEVLSD 55
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 447-503 3.66e-15

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: 77.64  E-value: 3.66e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2031264001 447 VLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEY 503
Cdd:TIGR02349   5 ILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQY 61
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 445-504 6.12e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 74.11  E-value: 6.12e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14298    8 YEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYD 67
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 532-620 3.06e-46

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


Pssm-ID: 464360  Cd Length: 92  Bit Score: 159.05  E-value: 3.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 532 MNTMMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQR---VGI 608
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLWRYYACMDGKVYDITEWAICQGdslMHC 80

                          90
                  ....*....|..
gi 2031264001 609 SPDTHRVPYHIS 620
Cdd:pfam14901  81 RPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 443-504 1.55e-22

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: 91.38  E-value: 1.55e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2031264001 443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 443-515 8.55e-20

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: 86.29  E-value: 8.55e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2031264001 443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNAEKRKEYEMKRMAENELSR 515
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLA 74
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 443-502 1.03e-19

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 83.13  E-value: 1.03e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031264001 443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNAEKRKE 502
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNkGDPKAEERFKEINEAYELLSDAEKRAR 61
DnaJ smart00271
DnaJ molecular chaperone homology domain;
443-499 2.38e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 76.50  E-value: 2.38e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2031264001  443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKN--HHPRAEEAFKVLRAAWDIVSNAEK 499
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNpgDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 443-496 8.15e-17

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: 74.89  E-value: 8.15e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2031264001 443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSN 496
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNpDDPEAEEKFKEINEAYEVLSD 55
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 447-503 3.66e-15

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: 77.64  E-value: 3.66e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2031264001 447 VLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEY 503
Cdd:TIGR02349   5 ILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQY 61
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
440-503 1.57e-14

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 69.36  E-value: 1.57e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2031264001 440 DELNPFHVLGVEATASDVELKKAYRQLAVMVHPDKN--HHPRAEEAFKVLRAAWDIVSNAEKRKEY 503
Cdd:COG2214     3 DLKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGgeLKALAEELFQRLNEAYEVLSDPERRAEY 68
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 445-504 6.12e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 74.11  E-value: 6.12e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14298    8 YEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 447-503 1.61e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 72.48  E-value: 1.61e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2031264001 447 VLGVEATASDVELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNAEKRKEY 503
Cdd:PRK10767    9 VLGVSRNASEDEIKKAYRKLAMKYHPDRNPgDKEAEEKFKEIKEAYEVLSDPQKRAAY 66
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 445-518 2.69e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 72.16  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE------MKRMAENELSRSVN 518
Cdd:PRK14283    8 YEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDqfghagMDGFSQEDIFNNIN 87
PRK14295 PRK14295
molecular chaperone DnaJ;
445-507 4.25e-13

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 71.42  E-value: 4.25e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNAEKRKEYEMKR 507
Cdd:PRK14295   12 YKVLGVPKDATEAEIKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYDEAR 75
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 445-504 5.50e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 71.27  E-value: 5.50e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14276    7 YDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYD 66
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 445-505 1.11e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 70.18  E-value: 1.11e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYEM 505
Cdd:PRK14291    6 YEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQ 66
PRK14289 PRK14289
molecular chaperone DnaJ;
445-504 1.13e-12

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 70.25  E-value: 1.13e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPR-AEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14289    8 YEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKeAEEKFKEAAEAYDVLSDPDKRSRYD 68
PRK14279 PRK14279
molecular chaperone DnaJ;
448-508 1.44e-12

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 69.76  E-value: 1.44e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2031264001 448 LGVEATASDVELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNAEKRKEY-EMKRM 508
Cdd:PRK14279   15 LGVSSDASAEEIKKAYRKLARELHPDANpGDPAAEERFKAVSEAHDVLSDPAKRKEYdETRRL 77
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 445-504 6.74e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 67.91  E-value: 6.74e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14281    6 YEVLGVSRSADKDEIKKAYRKLALKYHPDKNpDNKEAEEHFKEVNEAYEVLSNDDKRRRYD 66
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 447-505 9.93e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 67.38  E-value: 9.93e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2031264001 447 VLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYEM 505
Cdd:PRK14278    8 LLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVDL 66
PRK14297 PRK14297
molecular chaperone DnaJ;
445-504 1.24e-11

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 67.12  E-value: 1.24e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14297    7 YEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKgNKEAEEKFKEINEAYQVLSDPQKKAQYD 67
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 445-504 5.00e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 65.15  E-value: 5.00e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14301    7 YEVLGVSRDASEDEIKKAYRKLALQYHPDRNpDNPEAEQKFKEAAEAYEVLRDAEKRARYD 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 445-504 5.32e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 65.21  E-value: 5.32e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKN-HHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14277    8 YEILGVDRNATEEEIKKAYRRLAKKYHPDLNpGDKEAEQKFKEINEAYEILSDPQKRAQYD 68
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 445-504 1.05e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 64.14  E-value: 1.05e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14292    5 YELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 445-504 1.37e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 63.81  E-value: 1.37e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14296    7 YEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYD 66
PRK14280 PRK14280
molecular chaperone DnaJ;
445-504 1.38e-10

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 63.59  E-value: 1.38e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14280    7 YEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYD 66
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 445-504 1.80e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 62.65  E-value: 1.80e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14299    7 YAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYD 66
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 445-504 2.64e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 62.70  E-value: 2.64e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14286    7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKgNKESEEKFKEATEAYEILRDPKKRQAYD 67
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 445-536 3.28e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 62.55  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNAEKRKEYEmkRMAENELSRSVNEFLSK 523
Cdd:PRK14284    4 YTILGVSKTASPEEIKKAYRKLAVKYHPDKNPgDAEAEKRFKEVSEAYEVLSDAQKRESYD--RYGKDGPFAGAGGFGGA 81

                          90
                  ....*....|...
gi 2031264001 524 LQDDLKEAMNTMM 536
Cdd:PRK14284   82 GMGNMEDALRTFM 94
PRK10266 PRK10266
curved DNA-binding protein;
445-512 3.59e-10

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 61.76  E-value: 3.59e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYEMKRMAENE 512
Cdd:PRK10266    7 YAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQLWQHRND 74
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 445-504 5.72e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 61.56  E-value: 5.72e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14287    7 YEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYD 66
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 445-504 8.85e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 61.18  E-value: 8.85e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14300    6 YQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYD 65
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 445-504 1.89e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 60.16  E-value: 1.89e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPR-AEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14294    7 YEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKeAEELFKEAAEAYEVLSDPKKRGIYD 67
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 445-504 2.59e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 59.56  E-value: 2.59e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKN--HHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14290    6 YKILGVDRNASQEDIKKAFRELAKKWHPDLHpgNKAEAEEKFKEISEAYEVLSDPQKRRQYD 67
PRK14293 PRK14293
molecular chaperone DnaJ;
445-504 2.83e-09

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 59.62  E-value: 2.83e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14293    6 YEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYD 65
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
443-497 3.01e-09

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 54.03  E-value: 3.01e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2031264001 443 NPFHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKV-------LRAAWDIVSNA 497
Cdd:COG1076     5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRLAAGLPEEEQRLalqkaaaINEAYETLKDP 66
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 445-504 7.10e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 58.27  E-value: 7.10e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPR--AEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14282    7 YEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRkeAEQKFKEIQEAYEVLSDPQKRAMYD 68
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 445-504 9.11e-09

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 58.29  E-value: 9.11e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPraeEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PTZ00037   31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDP---EKFKEISRAYEVLSDPEKRKIYD 87
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 445-504 1.06e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 54.61  E-value: 1.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDKNH-HPRAEEAFKVLRAAWDIVSNAEKRKEYE 504
Cdd:PRK14285    6 YEILGLSKGASKDEIKKAYRKIAIKYHPDKNKgNKEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14288 PRK14288
molecular chaperone DnaJ;
441-526 2.55e-06

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 50.07  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2031264001 441 ELNPFHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPR-AEEAFKVLRAAWDIVSNAEKRKEYE-MKRMAENELSRSVN 518
Cdd:PRK14288    2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKeAEEKFKLINEAYGVLSDEKKRALYDrYGKKGLNQAGASQS 81


                  ....*...
gi 2031264001 519 EFLSKLQD 526
Cdd:PRK14288   82 DFSDFFED 89
djlA PRK09430
co-chaperone DjlA;
445-474 8.23e-05

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 44.80  E-value: 8.23e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2031264001 445 FHVLGVEATASDVELKKAYRQLAVMVHPDK 474
Cdd:PRK09430  203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
 
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