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Conserved domains on  [gi|42566961|ref|NP_193692|]
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Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

Protein Classification

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 ...
 66-127 1.38e-24

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: 96.77  E-value: 1.38e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961    66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNR-FTGAEGAFKLILEAWDLLSDKSQRSSYD 127
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPgDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
KLF18_N super family cl40479
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 419-543 3.30e-03

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


The actual alignment was detected with superfamily member cd21575:

Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 39.67  E-value: 3.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566961 419 TLFKEPMTTGNENSTTEEGIVKES---ETLCKEPMTTGNENSTTEEGNVKEAETFFEEPMTT--GNvkevETLFEEPMTT 493
Cdd:cd21575 157 TLYGGQMTTSSGDQTLYGGQMTTStsnQTLYGGQMTTSSGNQTLYGGQMTTPITLSGGQMTTstGD----QTLYGGQMTS 232

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 42566961 494 DNENSTPeaerlFKKPMSTGDENSTHEAQRLFKkpmttgnanSNLEAQRC 543
Cdd:cd21575 233 HQSSSLP-----YPGQLTFSSSHLIQGQHPEQK---------WNLKTQSC 268
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-127 1.38e-24

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: 96.77  E-value: 1.38e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961    66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNR-FTGAEGAFKLILEAWDLLSDKSQRSSYD 127
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPgDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-163 6.53e-22

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: 91.69  E-value: 6.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566961  66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRF-TGAEGAFKLILEAWDLLSDKSQRSSYDQKRKSNQVKQRTSGMQK 144
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGdPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80

                        90
                ....*....|....*....
gi 42566961 145 PKRSSTPKPTESDKPASSY 163
Cdd:COG0484  81 AAAEAAAAEAKEEAAEAGA 99
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-119 6.92e-20

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: 82.98  E-value: 6.92e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42566961  66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFT-GAEGAFKLILEAWDLLSD 119
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-120 2.16e-18

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 79.20  E-value: 2.16e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 42566961     66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNR--FTGAEGAFKLILEAWDLLSDK 120
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPgdKEEAEEKFKEINEAYEVLSDP 58
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 66-128 5.64e-17

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: 82.65  E-value: 5.64e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961    66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 66-128 2.76e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 80.57  E-value: 2.76e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRftG---AEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNP--GdkeAEEKFKEIKEAYEVLSDPQKRAAYDQ 68
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 419-543 3.30e-03

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 39.67  E-value: 3.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566961 419 TLFKEPMTTGNENSTTEEGIVKES---ETLCKEPMTTGNENSTTEEGNVKEAETFFEEPMTT--GNvkevETLFEEPMTT 493
Cdd:cd21575 157 TLYGGQMTTSSGDQTLYGGQMTTStsnQTLYGGQMTTSSGNQTLYGGQMTTPITLSGGQMTTstGD----QTLYGGQMTS 232

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 42566961 494 DNENSTPeaerlFKKPMSTGDENSTHEAQRLFKkpmttgnanSNLEAQRC 543
Cdd:cd21575 233 HQSSSLP-----YPGQLTFSSSHLIQGQHPEQK---------WNLKTQSC 268
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-127 1.38e-24

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: 96.77  E-value: 1.38e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961    66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNR-FTGAEGAFKLILEAWDLLSDKSQRSSYD 127
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPgDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-163 6.53e-22

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: 91.69  E-value: 6.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566961  66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRF-TGAEGAFKLILEAWDLLSDKSQRSSYDQKRKSNQVKQRTSGMQK 144
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGdPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80

                        90
                ....*....|....*....
gi 42566961 145 PKRSSTPKPTESDKPASSY 163
Cdd:COG0484  81 AAAEAAAAEAKEEAAEAGA 99
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-119 6.92e-20

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: 82.98  E-value: 6.92e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42566961  66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFT-GAEGAFKLILEAWDLLSD 119
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDpEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-120 2.16e-18

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 79.20  E-value: 2.16e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 42566961     66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNR--FTGAEGAFKLILEAWDLLSDK 120
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPgdKEEAEEKFKEINEAYEVLSDP 58
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 66-123 2.66e-17

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 76.19  E-value: 2.66e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42566961  66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRF-TGAEGAFKLILEAWDLLSDKSQR 123
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGdPKAEERFKEINEAYELLSDAEKR 59
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
64-132 3.50e-17

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 76.68  E-value: 3.50e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42566961  64 EADWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRF--TGAEGAFKLILEAWDLLSDKSQRSSYDQKRKS 132
Cdd:COG2214   4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGElkALAEELFQRLNEAYEVLSDPERRAEYDRELGQ 74
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 66-128 5.64e-17

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: 82.65  E-value: 5.64e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961    66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 66-128 2.76e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 80.57  E-value: 2.76e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRftG---AEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNP--GdkeAEEKFKEIKEAYEVLSDPQKRAAYDQ 68
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 64-128 2.02e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 78.21  E-value: 2.02e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42566961   64 EADWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14276   3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYDQ 67
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 66-128 4.07e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 77.20  E-value: 4.07e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14298   6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDR 68
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 66-128 1.27e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 75.63  E-value: 1.27e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQ 68
PRK14280 PRK14280
molecular chaperone DnaJ;
66-128 3.67e-14

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 74.37  E-value: 3.67e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYDQ 67
PRK14295 PRK14295
molecular chaperone DnaJ;
64-130 6.56e-14

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 73.73  E-value: 6.56e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42566961   64 EADWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRF-TGAEGAFKLILEAWDLLSDKSQRSSYDQKR 130
Cdd:PRK14295   8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGdAKAEERFKEISEAYDVLSDEKKRKEYDEAR 75
PRK10266 PRK10266
curved DNA-binding protein;
66-130 1.25e-13

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 71.78  E-value: 1.25e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQKR 130
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQLW 69
PRK14279 PRK14279
molecular chaperone DnaJ;
64-131 1.53e-13

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 72.46  E-value: 1.53e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42566961   64 EADWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRF-TGAEGAFKLILEAWDLLSDKSQRSSYDQKRK 131
Cdd:PRK14279   8 EKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGdPAAEERFKAVSEAHDVLSDPAKRKEYDETRR 76
PRK14293 PRK14293
molecular chaperone DnaJ;
65-128 2.80e-13

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 71.56  E-value: 2.80e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42566961   65 ADWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14293   3 ADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQ 66
PRK14297 PRK14297
molecular chaperone DnaJ;
66-128 2.97e-13

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 71.35  E-value: 2.97e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRF-TGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGnKEAEEKFKEINEAYQVLSDPQKKAQYDQ 68
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 66-128 4.47e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 70.99  E-value: 4.47e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRF-TGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGdKEAEQKFKEINEAYEILSDPQKRAQYDQ 69
PRK14289 PRK14289
molecular chaperone DnaJ;
66-128 4.75e-13

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 71.02  E-value: 4.75e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNrfTG---AEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKN--PGdkeAEEKFKEAAEAYDVLSDPDKRSRYDQ 69
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 66-128 5.75e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 70.42  E-value: 5.75e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQ 67
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 65-128 7.82e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 69.92  E-value: 7.82e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42566961   65 ADWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14292   2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDR 65
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 66-128 3.69e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 67.84  E-value: 3.69e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTG-AEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14301   5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPeAEQKFKEAAEAYEVLRDAEKRARYDR 68
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 66-128 4.30e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 67.91  E-value: 4.30e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKN-RFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNpDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQ 67
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 66-128 5.40e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 67.49  E-value: 5.40e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYDQ 66
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 65-131 6.03e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 67.56  E-value: 6.03e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42566961   65 ADWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTG-AEGAFKLILEAWDLLSDKSQRSSYDQKRK 131
Cdd:PRK14284   1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAeAEKRFKEVSEAYEVLSDAQKRESYDRYGK 68
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 64-132 1.62e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 66.17  E-value: 1.62e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566961   64 EADWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTG-AEGAFKLILEAWDLLSDKSQRSSYDQKRKS 132
Cdd:PRK14286   3 ERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKeSEEKFKEATEAYEILRDPKKRQAYDQFGKA 72
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 66-127 2.22e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 64.96  E-value: 2.22e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYD 127
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYD 66
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 66-128 3.98e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 64.97  E-value: 3.98e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYDQ 67
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 63-128 9.80e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 63.63  E-value: 9.80e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42566961   63 GEADWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNrfTG---AEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14294   2 VKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRN--PGdkeAEELFKEAAEAYEVLSDPKKRGIYDQ 68
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 66-128 3.66e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 61.87  E-value: 3.66e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKN--RFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14290   4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHpgNKAEAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 66-127 6.20e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 61.22  E-value: 6.20e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYD 127
Cdd:PRK14278   4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVD 65
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
63-119 2.03e-09

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 54.03  E-value: 2.03e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42566961  63 GEADWYRVLGVDPLADDEAVKKRYRKLALLLHPDknRFTGAEGAF---------KLILEAWDLLSD 119
Cdd:COG1076   2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPD--RLAAGLPEEeqrlalqkaAAINEAYETLKD 65
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 66-128 3.47e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 58.85  E-value: 3.47e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTG-AEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14285   4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKeAESIFKEATEAYEVLIDDNKRAQYDR 67
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 66-128 4.50e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 58.49  E-value: 4.50e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14300   4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYDR 66
PRK14288 PRK14288
molecular chaperone DnaJ;
64-134 1.84e-08

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 56.62  E-value: 1.84e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42566961   64 EADWYRVLGVDPLADDEAVKKRYRKLALLLHPDKNRFTG-AEGAFKLILEAWDLLSDKSQRSSYDQ--KRKSNQ 134
Cdd:PRK14288   2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKeAEEKFKLINEAYGVLSDEKKRALYDRygKKGLNQ 75
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 66-128 3.11e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 55.95  E-value: 3.11e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42566961   66 DWYRVLGVDPLADDEAVKKRYRKLALLLHPDKN--RFTGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PRK14282   5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHpeNRKEAEQKFKEIQEAYEVLSDPQKRAMYDR 69
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 68-128 7.53e-07

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 51.75  E-value: 7.53e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42566961   68 YRVLGVDPLADDEAVKKRYRKLALLLHPDKNrftGAEGAFKLILEAWDLLSDKSQRSSYDQ 128
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKG---GDPEKFKEISRAYEVLSDPEKRKIYDE 88
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 63-127 1.73e-05

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 47.33  E-value: 1.73e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42566961  63 GEADWYRVLGVDPL---ADDEAVKKRYRKLALLLHPDKNRFTGA---EGAFKLILEAWDLLSDKSQRSSYD 127
Cdd:COG5269  41 KKVDLYALLGLSKYrtkAIPPQILKAHKKKVYKYHPDKTAAGGNkgcDEFFKLIQKAREVLGDRKLRLQYD 111
djlA PRK09430
co-chaperone DjlA;
65-97 3.84e-05

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 45.57  E-value: 3.84e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 42566961   65 ADWYRVLGVDPLADDEAVKKRYRKLALLLHPDK 97
Cdd:PRK09430 200 EDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
KLF18_N cd21575
N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like ...
 419-543 3.30e-03

N-terminal domain of Kruppel-like factor 18; Kruppel-like factor 18 (KLF18), or Krueppel-like factor 18, is a product of a chromosomal neighbor of the KLF17 gene and is likely a product of its duplication. Phylogenetic analyses revealed that mammalian predicted KLF18 proteins and KLF17 proteins experienced elevated rates of evolution and are grouped with KLF1/KLF2/KLF4 and non-mammalian KLF17. KLF18 has been found in the human testis, though it was previously hypothesized to be a pseudogene in extant placental mammals. Mouse KLF18 expression data indicates that it may function in early embryonic development. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF18. Some KLF18 isoforms have duplicated N-terminal domains.


Pssm-ID: 410566 [Multi-domain]  Cd Length: 276  Bit Score: 39.67  E-value: 3.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42566961 419 TLFKEPMTTGNENSTTEEGIVKES---ETLCKEPMTTGNENSTTEEGNVKEAETFFEEPMTT--GNvkevETLFEEPMTT 493
Cdd:cd21575 157 TLYGGQMTTSSGDQTLYGGQMTTStsnQTLYGGQMTTSSGNQTLYGGQMTTPITLSGGQMTTstGD----QTLYGGQMTS 232

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 42566961 494 DNENSTPeaerlFKKPMSTGDENSTHEAQRLFKkpmttgnanSNLEAQRC 543
Cdd:cd21575 233 HQSSSLP-----YPGQLTFSSSHLIQGQHPEQK---------WNLKTQSC 268
 
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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