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Conserved domains on  [gi|334187241|ref|NP_195464|]
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Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

Protein Classification

J domain-containing protein( domain architecture ID 10914228)

J domain-containing protein similar to molecular chaperone DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
PubMed:  9585179|35729039|9644977|8016869|15170475
SCOP:  4000605

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 ...
 56-120 3.77e-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: 89.84  E-value: 3.77e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241   56 NAYDILNVSETSSIAEIKASFRRLAKETHPDLieSKKDPSNSRRFVQILAAYEILSDSEKRAHYD 120
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDK--NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ super family cl02542
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 7-86 1.74e-04

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.


The actual alignment was detected with superfamily member PTZ00100:

Pssm-ID: 413365  Cd Length: 116  Bit Score: 41.37  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187241   7 LIRRRFSRLVPvqlNYGFEPSRILFNPSQGRTRLLSGEAESNRN---EFPVE--NAYDILNVSETSSIAEIKASFRRLAK 81
Cdd:PTZ00100  15 LAVRYGYRYLK---NQKIFGSNNMSFPLSGFNPSLGSLFLKNDLkgfENPMSksEAYKILNISPTASKERIREAHKQLML 91


                 ....*
gi 334187241  82 ETHPD 86
Cdd:PTZ00100  92 RNHPD 96
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 56-120 3.77e-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: 89.84  E-value: 3.77e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241   56 NAYDILNVSETSSIAEIKASFRRLAKETHPDLieSKKDPSNSRRFVQILAAYEILSDSEKRAHYD 120
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDK--NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 56-122 1.50e-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: 87.84  E-value: 1.50e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187241  56 NAYDILNVSETSSIAEIKASFRRLAKETHPDLieSKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDR--NPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRF 65
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 58-122 3.71e-18

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: 86.12  E-value: 3.71e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241   58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDR---NKDKEAEEKFKEINEAYEVLSDPEKRAQYDQF 64
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 58-122 1.37e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 81.34  E-value: 1.37e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDliESKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPD--RNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYDQY 69
DnaJ smart00271
DnaJ molecular chaperone homology domain;
55-115 1.03e-15

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 71.50  E-value: 1.03e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187241    55 ENAYDILNVSETSSIAEIKASFRRLAKETHPDLiESKKDPSNSRRFVQILAAYEILSDSEK 115
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDK-NPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 56-112 1.43e-15

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: 70.65  E-value: 1.43e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334187241  56 NAYDILNVSETSSIAEIKASFRRLAKETHPDLieSKKDPSNSRRFVQILAAYEILSD 112
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDK--NPDDPEAEEKFKEINEAYEVLSD 55
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 7-86 1.74e-04

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 41.37  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187241   7 LIRRRFSRLVPvqlNYGFEPSRILFNPSQGRTRLLSGEAESNRN---EFPVE--NAYDILNVSETSSIAEIKASFRRLAK 81
Cdd:PTZ00100  15 LAVRYGYRYLK---NQKIFGSNNMSFPLSGFNPSLGSLFLKNDLkgfENPMSksEAYKILNISPTASKERIREAHKQLML 91


                 ....*
gi 334187241  82 ETHPD 86
Cdd:PTZ00100  92 RNHPD 96
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 56-120 3.77e-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: 89.84  E-value: 3.77e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241   56 NAYDILNVSETSSIAEIKASFRRLAKETHPDLieSKKDPSNSRRFVQILAAYEILSDSEKRAHYD 120
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDK--NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 56-122 1.50e-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: 87.84  E-value: 1.50e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187241  56 NAYDILNVSETSSIAEIKASFRRLAKETHPDLieSKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDR--NPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRF 65
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 58-122 3.71e-18

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: 86.12  E-value: 3.71e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241   58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDR---NKDKEAEEKFKEINEAYEVLSDPEKRAQYDQF 64
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
52-127 4.40e-18

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 79.38  E-value: 4.40e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187241  52 FPVENAYDILNVSETSSIAEIKASFRRLAKETHPDLIESKKDPSNsRRFVQILAAYEILSDSEKRAHYDRYLLSRR 127
Cdd:COG2214    2 PDLKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAE-ELFQRLNEAYEVLSDPERRAEYDRELGQSG 76
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 58-122 1.37e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 81.34  E-value: 1.37e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDliESKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK10767   7 YEVLGVSRNASEDEIKKAYRKLAMKYHPD--RNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYDQY 69
DnaJ smart00271
DnaJ molecular chaperone homology domain;
55-115 1.03e-15

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 71.50  E-value: 1.03e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187241    55 ENAYDILNVSETSSIAEIKASFRRLAKETHPDLiESKKDPSNSRRFVQILAAYEILSDSEK 115
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDK-NPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 56-112 1.43e-15

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: 70.65  E-value: 1.43e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334187241  56 NAYDILNVSETSSIAEIKASFRRLAKETHPDLieSKKDPSNSRRFVQILAAYEILSD 112
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDK--NPDDPEAEEKFKEINEAYEVLSD 55
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 58-122 1.81e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 78.01  E-value: 1.81e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDlieSKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14292   5 YELLGVSRTASADEIKSAYRKLALKYHPD---RNKEKGAAEKFAQINEAYAVLSDAEKRAHYDRF 66
PRK14293 PRK14293
molecular chaperone DnaJ;
58-122 6.89e-15

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 76.18  E-value: 6.89e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14293   6 YEILGVSRDADKDELKRAYRRLARKYHPDV---NKEPGAEDRFKEINRAYEVLSDPETRARYDQF 67
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 58-122 9.57e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 75.89  E-value: 9.57e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14276   7 YDRLGVSKDASQDEIKKAYRKLSKKYHPDI---NKEPGAEEKYKEVQEAYETLSDPQKRAAYDQY 68
PRK14280 PRK14280
molecular chaperone DnaJ;
58-122 3.29e-14

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 74.37  E-value: 3.29e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14280   7 YEVLGVSKSASKDEIKKAYRKLSKKYHPDI---NKEEGADEKFKEISEAYEVLSDDQKRAQYDQF 68
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 58-122 3.91e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 74.11  E-value: 3.91e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDlieSKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14298   8 YEILGLSKDASVEDIKKAYRKLAMKYHPD---KNKEPDAEEKFKEISEAYAVLSDAEKRAQYDRF 69
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 58-122 2.22e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 71.72  E-value: 2.22e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14291   6 YEILGVSRNATQEEIKKAYRRLARKYHPDF---NKNPEAEEKFKEINEAYQVLSDPEKRKLYDQF 67
PRK14295 PRK14295
molecular chaperone DnaJ;
58-120 2.86e-13

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 71.42  E-value: 2.86e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDliESKKDPSNSRRFVQILAAYEILSDSEKRAHYD 120
Cdd:PRK14295  12 YKVLGVPKDATEAEIKKAYRKLAREYHPD--ANKGDAKAEERFKEISEAYDVLSDEKKRKEYD 72
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 58-122 3.18e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 71.37  E-value: 3.18e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLieSKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14277   8 YEILGVDRNATEEEIKKAYRRLAKKYHPDL--NPGDKEAEQKFKEINEAYEILSDPQKRAQYDQF 70
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 58-122 5.43e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 69.58  E-value: 5.43e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14299   7 YAILGVPKNASQDEIKKAFKKLARKYHPDV---NKSPGAEEKFKEINEAYTVLSDPEKRRIYDTY 68
PRK10266 PRK10266
curved DNA-binding protein;
58-126 1.18e-12

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 68.69  E-value: 1.18e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYDRYLLSR 126
Cdd:PRK10266   7 YAIMGVKPTDDLKTIKTAYRRLARKYHPDV---SKEPDAEARFKEVAEAWEVLSDEQRRAEYDQLWQHR 72
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 58-122 1.60e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 69.05  E-value: 1.60e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDL-IESKKDPSnsRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14282   7 YEILGVSRNATQEEIKRAYKRLVKEWHPDRhPENRKEAE--QKFKEIQEAYEVLSDPQKRAMYDRF 70
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 58-122 1.93e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 69.10  E-value: 1.93e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDliESKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14284   4 YTILGVSKTASPEEIKKAYRKLAVKYHPD--KNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDRY 66
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 58-120 4.43e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 67.77  E-value: 4.43e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYD 120
Cdd:PRK14278   6 YGLLGVSRNASDAEIKRAYRKLARELHPDV---NPDEEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 55-122 4.49e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 67.73  E-value: 4.49e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334187241  55 ENAYDILNVSETSSIAEIKASFRRLAKETHPDLIESKkdpSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14300   3 QDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAK---DAEKKFKEINAAYDVLKDEQKRAAYDRF 67
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 58-122 2.22e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 65.62  E-value: 2.22e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLIEskkDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14283   8 YEVLGVDRNADKKEIKKAYRKLARKYHPDVSE---EEGAEEKFKEISEAYAVLSDDEKRQRYDQF 69
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 58-122 4.52e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 64.38  E-value: 4.52e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDliESKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14301   7 YEVLGVSRDASEDEIKKAYRKLALQYHPD--RNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRF 69
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 58-122 5.79e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 64.20  E-value: 5.79e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14296   7 YEVLGVSKTASEQEIRQAYRKLAKQYHPDL---NKSPDAHDKMVEINEAADVLLDKDKRKQYDQF 68
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 43-122 6.93e-11

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 64.07  E-value: 6.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187241  43 GEAESNRNEFPVENA--YDILNVSETSSIAEIKASFRRLAKETHPDlieSKKDPsnsRRFVQILAAYEILSDSEKRAHYD 120
Cdd:PTZ00037  14 GGFDGGRRKREVDNEklYEVLNLSKDCTTSEIKKAYRKLAIKHHPD---KGGDP---EKFKEISRAYEVLSDPEKRKIYD 87


                 ..
gi 334187241 121 RY 122
Cdd:PTZ00037  88 EY 89
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 58-122 1.15e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 63.49  E-value: 1.15e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLiesKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14287   7 YEVLGVDRNASVDEVKKAYRKLARKYHPDV---NKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQF 68
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 58-122 1.39e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 62.86  E-value: 1.39e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDlieskKDPSNSR---RFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14294   7 YEILGVTRDASEEEIKKSYRKLAMKYHPD-----RNPGDKEaeeLFKEAAEAYEVLSDPKKRGIYDQY 69
PRK14279 PRK14279
molecular chaperone DnaJ;
48-128 2.32e-10

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 62.44  E-value: 2.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187241  48 NRNEFPVENAYDILNVSETSSIAEIKASFRRLAKETHPDliESKKDPSNSRRFVQILAAYEILSDSEKRAHYDRyllSRR 127
Cdd:PRK14279   2 AQREWVEKDFYKELGVSSDASAEEIKKAYRKLARELHPD--ANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDE---TRR 76


                 .
gi 334187241 128 M 128
Cdd:PRK14279  77 L 77
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 58-122 2.47e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 62.31  E-value: 2.47e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDliESKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPD--KNKGNKESEEKFKEATEAYEILRDPKKRQAYDQF 69
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 58-122 2.82e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 62.13  E-value: 2.82e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDlieskKDPSNS---RRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14281   6 YEVLGVSRSADKDEIKKAYRKLALKYHPD-----KNPDNKeaeEHFKEVNEAYEVLSNDDKRRRYDQF 68
PRK14289 PRK14289
molecular chaperone DnaJ;
58-122 4.87e-10

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 61.39  E-value: 4.87e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDlieskKDPSN---SRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14289   8 YEVLGVSKTATVDEIKKAYRKKAIQYHPD-----KNPGDkeaEEKFKEAAEAYDVLSDPDKRSRYDQF 70
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 58-121 6.20e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 61.10  E-value: 6.20e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDLIESKKDPSnSRRFVQILAAYEILSDSEKRAHYDR 121
Cdd:PRK14290   6 YKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEA-EEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14297 PRK14297
molecular chaperone DnaJ;
58-122 8.23e-10

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 60.57  E-value: 8.23e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDliESKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14297   7 YEVLGLEKGASDDEIKKAFRKLAIKYHPD--KNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQF 69
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
55-112 6.73e-09

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 52.49  E-value: 6.73e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187241  55 ENAYDILNVSETSSIAEIKASFRRLAKETHPDLIESKKDPSNSR----RFVQILAAYEILSD 112
Cdd:COG1076    4 DDAFELLGLPPDADDAELKRAYRKLQREHHPDRLAAGLPEEEQRlalqKAAAINEAYETLKD 65
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 58-122 1.17e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 56.92  E-value: 1.17e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDliESKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14285   6 YEILGLSKGASKDEIKKAYRKIAIKYHPD--KNKGNKEAESIFKEATEAYEVLIDDNKRAQYDRF 68
PRK14288 PRK14288
molecular chaperone DnaJ;
58-122 3.17e-07

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 52.38  E-value: 3.17e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187241  58 YDILNVSETSSIAEIKASFRRLAKETHPDliESKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PRK14288   6 YEILEVEKHSNQETIKKSYRKLALKYHPD--RNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRY 68
djlA PRK09430
co-chaperone DjlA;
54-110 5.33e-05

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 45.19  E-value: 5.33e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187241  54 VENAYDILNVSETSSIAEIKASFRRLAKETHPDLIESKKDPSN-----SRRFVQILAAYEIL 110
Cdd:PRK09430 199 LEDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKLVAKGLPPEmmemaKEKAQEIQAAYELI 260
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 44-122 7.68e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.55  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187241   44 EAESNRN-EFPVENAYDILNVSETSSIAEIKASFRRLAKETHPdliESKKDPSNSRRFVQILAAYEILSDSEKRAHYDRY 122
Cdd:PTZ00341  561 DSEAAPTiEIPDTLFYDILGVGVNADMKEISERYFKLAENYYP---PKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKF 637
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 7-86 1.74e-04

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 41.37  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187241   7 LIRRRFSRLVPvqlNYGFEPSRILFNPSQGRTRLLSGEAESNRN---EFPVE--NAYDILNVSETSSIAEIKASFRRLAK 81
Cdd:PTZ00100  15 LAVRYGYRYLK---NQKIFGSNNMSFPLSGFNPSLGSLFLKNDLkgfENPMSksEAYKILNISPTASKERIREAHKQLML 91


                 ....*
gi 334187241  82 ETHPD 86
Cdd:PTZ00100  92 RNHPD 96
 
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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