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Conserved domains on  [gi|2165432866|ref|WP_231876638|]
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MULTISPECIES: DNA-J related domain-containing protein [unclassified Oleiphilus]

Protein Classification

DNA-J related domain-containing protein( domain architecture ID 19385448)

DNA-J related domain-containing protein consists of an N-terminal DNA-J related domain and C-terminal J domain (also known as DnaJ domain); 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:  10542335|9585179|15170475|9644977|35729039|8016869
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DNAJ_related super family cl13736
DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino ...
 5-112 2.79e-28

DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino acids in length. The family is found in association with pfam00226. There is a conserved YYLD sequence motif. Mostof the sequences in this family are annotated as DNA-J related proteins but there is little publication to back this up.


The actual alignment was detected with superfamily member pfam12339:

Pssm-ID: 432489  Cd Length: 120  Bit Score: 101.53  E-value: 2.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165432866   5 WREYDLIKYLKDSNDLELPNMELNQALSLFKTHFLIRHALYSLKSKWAKNKSAHLEIGIINIQKFPYITH-NETSVSNSD 83
Cdd:pfam12339  12 IKEHTLIKELKERPYGLFPPLDLSPPLDLFRTHFLLFHALYRLQERLWPEGWGQLQIHALDIRLLPPAPTsADAALDEAD 91

                          90       100
                  ....*....|....*....|....*....
gi 2165432866  84 LLGTYYLDHDNYFDMTKEEISLLLNGFWQ 112
Cdd:pfam12339  92 PLREYYLDWSNYEDTDEADVERLLDSFWT 120
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 124-170 1.53e-10

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: 56.25  E-value: 1.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKGGD----EQKFKELSKAKDEL 170
Cdd:COG0484     3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGdpeaEEKFKEINEAYEVL 53
 
Name Accession Description Interval E-value
DNAJ_related pfam12339
DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino ...
 5-112 2.79e-28

DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino acids in length. The family is found in association with pfam00226. There is a conserved YYLD sequence motif. Mostof the sequences in this family are annotated as DNA-J related proteins but there is little publication to back this up.


Pssm-ID: 432489  Cd Length: 120  Bit Score: 101.53  E-value: 2.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165432866   5 WREYDLIKYLKDSNDLELPNMELNQALSLFKTHFLIRHALYSLKSKWAKNKSAHLEIGIINIQKFPYITH-NETSVSNSD 83
Cdd:pfam12339  12 IKEHTLIKELKERPYGLFPPLDLSPPLDLFRTHFLLFHALYRLQERLWPEGWGQLQIHALDIRLLPPAPTsADAALDEAD 91

                          90       100
                  ....*....|....*....|....*....
gi 2165432866  84 LLGTYYLDHDNYFDMTKEEISLLLNGFWQ 112
Cdd:pfam12339  92 PLREYYLDWSNYEDTDEADVERLLDSFWT 120
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 124-170 1.53e-10

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: 56.25  E-value: 1.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKGGD----EQKFKELSKAKDEL 170
Cdd:COG0484     3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGdpeaEEKFKEINEAYEVL 53
PRK14297 PRK14297
molecular chaperone DnaJ;
120-170 1.21e-09

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 55.94  E-value: 1.21e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2165432866 120 SEEAYQALGLEIGASYADIKRAFKKKAQTMHPDKG-GD---EQKFKELSKAKDEL 170
Cdd:PRK14297    3 SKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNkGNkeaEEKFKEINEAYQVL 57
DnaJ smart00271
DnaJ molecular chaperone homology domain;
121-170 1.26e-09

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 51.85  E-value: 1.26e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2165432866  121 EEAYQALGLEIGASYADIKRAFKKKAQTMHPDKGGD-----EQKFKELSKAKDEL 170
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGdkeeaEEKFKEINEAYEVL 55
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 122-170 3.70e-09

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: 50.24  E-value: 3.70e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2165432866 122 EAYQALGLEIGASYADIKRAFKKKAQTMHPDKGGD----EQKFKELSKAKDEL 170
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdpeaEEKFKEINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 124-170 7.83e-09

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: 49.78  E-value: 7.83e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKG----GDEQKFKELSKAKDEL 170
Cdd:pfam00226   3 YEILGVSPDASDEEIKKAYRKLALKYHPDKNpgdpEAEEKFKEINEAYEVL 53
 
Name Accession Description Interval E-value
DNAJ_related pfam12339
DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino ...
 5-112 2.79e-28

DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino acids in length. The family is found in association with pfam00226. There is a conserved YYLD sequence motif. Mostof the sequences in this family are annotated as DNA-J related proteins but there is little publication to back this up.


Pssm-ID: 432489  Cd Length: 120  Bit Score: 101.53  E-value: 2.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165432866   5 WREYDLIKYLKDSNDLELPNMELNQALSLFKTHFLIRHALYSLKSKWAKNKSAHLEIGIINIQKFPYITH-NETSVSNSD 83
Cdd:pfam12339  12 IKEHTLIKELKERPYGLFPPLDLSPPLDLFRTHFLLFHALYRLQERLWPEGWGQLQIHALDIRLLPPAPTsADAALDEAD 91

                          90       100
                  ....*....|....*....|....*....
gi 2165432866  84 LLGTYYLDHDNYFDMTKEEISLLLNGFWQ 112
Cdd:pfam12339  92 PLREYYLDWSNYEDTDEADVERLLDSFWT 120
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 124-170 1.53e-10

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: 56.25  E-value: 1.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKGGD----EQKFKELSKAKDEL 170
Cdd:COG0484     3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGdpeaEEKFKEINEAYEVL 53
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
121-172 1.75e-10

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 54.72  E-value: 1.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2165432866 121 EEAYQALGLEIGASYADIKRAFKKKAQTMHPDKGG-----DEQKFKELSKAKDELLK 172
Cdd:COG2214     5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGelkalAEELFQRLNEAYEVLSD 61
PRK14297 PRK14297
molecular chaperone DnaJ;
120-170 1.21e-09

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 55.94  E-value: 1.21e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2165432866 120 SEEAYQALGLEIGASYADIKRAFKKKAQTMHPDKG-GD---EQKFKELSKAKDEL 170
Cdd:PRK14297    3 SKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNkGNkeaEEKFKEINEAYQVL 57
DnaJ smart00271
DnaJ molecular chaperone homology domain;
121-170 1.26e-09

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 51.85  E-value: 1.26e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2165432866  121 EEAYQALGLEIGASYADIKRAFKKKAQTMHPDKGGD-----EQKFKELSKAKDEL 170
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGdkeeaEEKFKEINEAYEVL 55
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 113-166 1.32e-09

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 55.98  E-value: 1.32e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2165432866 113 RFNNPDQSEEAYQALGLEIGASYADIKRAFKKKAQTMHPDKGGDEQKFKELSKA 166
Cdd:PTZ00037   20 RRKREVDNEKLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEKFKEISRA 73
PHA03102 PHA03102
Small T antigen; Reviewed
 120-170 1.67e-09

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 53.52  E-value: 1.67e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2165432866 120 SEEAYQALGLEIGA--SYADIKRAFKKKAQTMHPDKGGDEQKFKEL----SKAKDEL 170
Cdd:PHA03102    4 SKELMDLLGLPRSAwgNLPLMRKAYLRKCLEFHPDKGGDEEKMKELntlyKKFRESV 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 122-170 3.70e-09

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: 50.24  E-value: 3.70e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2165432866 122 EAYQALGLEIGASYADIKRAFKKKAQTMHPDKGGD----EQKFKELSKAKDEL 170
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdpeaEEKFKEINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 124-170 7.83e-09

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: 49.78  E-value: 7.83e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKG----GDEQKFKELSKAKDEL 170
Cdd:pfam00226   3 YEILGVSPDASDEEIKKAYRKLALKYHPDKNpgdpEAEEKFKEINEAYEVL 53
PHA02624 PHA02624
large T antigen; Provisional
 118-170 1.20e-08

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 53.45  E-value: 1.20e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2165432866 118 DQSEEAYQALGLEIGA--SYADIKRAFKKKAQTMHPDKGGDEQKFKELSKAKDEL 170
Cdd:PHA02624    8 EESKELMDLLGLPMAAwgNLPLMRKAYLRKCKEYHPDKGGDEEKMKRLNSLYKKL 62
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 124-173 8.14e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 50.82  E-value: 8.14e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKGGDEQ---KFKELSKAKDELL---KR 173
Cdd:PRK14278    6 YGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEaqeKFKEISVAYEVLSdpeKR 61
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 124-166 1.10e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 50.23  E-value: 1.10e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKGGD---EQKFKELSKA 166
Cdd:PRK14298    8 YEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEpdaEEKFKEISEA 53
PRK14280 PRK14280
molecular chaperone DnaJ;
124-166 2.92e-07

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 48.95  E-value: 2.92e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPD---KGGDEQKFKELSKA 166
Cdd:PRK14280    7 YEVLGVSKSASKDEIKKAYRKLSKKYHPDinkEEGADEKFKEISEA 52
PRK14295 PRK14295
molecular chaperone DnaJ;
124-170 3.81e-07

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 48.69  E-value: 3.81e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPD--KG--GDEQKFKELSKAKDEL 170
Cdd:PRK14295   12 YKVLGVPKDATEAEIKKAYRKLAREYHPDanKGdaKAEERFKEISEAYDVL 62
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 120-170 4.53e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 48.47  E-value: 4.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2165432866 120 SEEAYQALGLEIGASYADIKRAFKKKAQTMHPDK---GGDEQKFKELSKAKDEL 170
Cdd:PRK14300    2 SQDYYQILGVSKTASQADLKKAYLKLAKQYHPDTtdaKDAEKKFKEINAAYDVL 55
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 119-166 4.53e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 48.64  E-value: 4.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2165432866 119 QSEEAYQALGLEIGASYADIKRAFKKKAQTMHPDKG-GD---EQKFKELSKA 166
Cdd:PRK14277    3 AKKDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNpGDkeaEQKFKEINEA 54
PRK14289 PRK14289
molecular chaperone DnaJ;
124-170 4.61e-07

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 48.67  E-value: 4.61e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKG-GD---EQKFKELSKAKDEL 170
Cdd:PRK14289    8 YEVLGVSKTATVDEIKKAYRKKAIQYHPDKNpGDkeaEEKFKEAAEAYDVL 58
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 121-170 7.45e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 47.78  E-value: 7.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2165432866 121 EEAYQALGLEIGASYADIKRAFKKKAQTMHPD---KGGDEQKFKELSKAKDEL 170
Cdd:PRK14276    4 TEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDinkEPGAEEKYKEVQEAYETL 56
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 124-166 8.34e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 47.90  E-value: 8.34e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPD---KGGDEQKFKELSKA 166
Cdd:PRK14283    8 YEVLGVDRNADKKEIKKAYRKLARKYHPDvseEEGAEEKFKEISEA 53
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 124-170 1.01e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 47.43  E-value: 1.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKGGD----EQKFKELSKAKDEL 170
Cdd:PRK14301    7 YEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDnpeaEQKFKEAAEAYEVL 57
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 124-166 2.53e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 46.09  E-value: 2.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPD---KGGDEQKFKELSKA 166
Cdd:PRK14299    7 YAILGVPKNASQDEIKKAFKKLARKYHPDvnkSPGAEEKFKEINEA 52
PRK14293 PRK14293
molecular chaperone DnaJ;
124-166 3.53e-06

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 45.75  E-value: 3.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPD---KGGDEQKFKELSKA 166
Cdd:PRK14293    6 YEILGVSRDADKDELKRAYRRLARKYHPDvnkEPGAEDRFKEINRA 51
PRK14279 PRK14279
molecular chaperone DnaJ;
124-170 4.89e-06

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 45.49  E-value: 4.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKG-GD---EQKFKELSKAKDEL 170
Cdd:PRK14279   12 YKELGVSSDASAEEIKKAYRKLARELHPDANpGDpaaEERFKAVSEAHDVL 62
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 120-170 9.98e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 44.54  E-value: 9.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2165432866 120 SEEAYQALGLEIGASYADIKRAFKKKAQTMHPD-----KGGDEQKFKELSKAKDEL 170
Cdd:PRK14290    2 AKDYYKILGVDRNASQEDIKKAFRELAKKWHPDlhpgnKAEAEEKFKEISEAYEVL 57
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
119-167 1.80e-05

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 40.94  E-value: 1.80e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 119 QSEEAYQALGLEIGASYADIKRAFKKKAQTMHPDK--GGDEQKFKELSKAK 167
Cdd:COG1076     2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaAGLPEEEQRLALQK 52
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 119-170 7.81e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 42.09  E-value: 7.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2165432866 119 QSEEAYQALGLEIGASYADIKRAFKKKAQTMHPD-----KGGDEQKFKELSKAKDEL 170
Cdd:PRK14282    2 EKKDYYEILGVSRNATQEEIKRAYKRLVKEWHPDrhpenRKEAEQKFKEIQEAYEVL 58
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 124-166 1.23e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 41.29  E-value: 1.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPD---KGGDEQKFKELSKA 166
Cdd:PRK14291    6 YEILGVSRNATQEEIKKAYRRLARKYHPDfnkNPEAEEKFKEINEA 51
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 124-166 1.59e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 40.90  E-value: 1.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKG-GD---EQKFKELSKA 166
Cdd:PRK14294    7 YEILGVTRDASEEEIKKSYRKLAMKYHPDRNpGDkeaEELFKEAAEA 53
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 124-170 3.22e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 39.97  E-value: 3.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2165432866 124 YQALGLEIGASYADIKRAFKKKAQTMHPDKGGDEQK----FKELSKAKDEL 170
Cdd:PRK14285    6 YEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEaesiFKEATEAYEVL 56
djlA PRK09430
co-chaperone DjlA;
108-153 4.26e-04

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 39.41  E-value: 4.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2165432866 108 NGFWQRFNNPDQSEEAYQALGLEIGASYADIKRAFKKKAQTMHPDK 153
Cdd:PRK09430  187 GGGYQQAQRGPTLEDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK 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.
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