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Conserved domains on  [gi|1811009100|ref|XP_032315654|]
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LOW QUALITY PROTEIN: dnaJ homolog subfamily B member 6-like, partial [Camelus ferus]

Protein Classification

J domain-containing protein( domain architecture ID 13623118)

J domain-containing protein similar to molecular chaperone DnaJ; 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 Hsp70. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70

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 ...
 4-66 4.28e-33

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: 116.42  E-value: 4.28e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPeKKEEAERKFKQVAEAYEVLPDANKRDIY 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNP-GDPEAEEKFKEINEAYEVLSDPEKRAIY 62
PRK14282 super family cl32986
chaperone protein DnaJ; Provisional
 4-136 9.47e-26

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK14282:

Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 105.26  E-value: 9.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSH 83
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPPYQETES 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1811009100  84 FDGPFgfgftf*npDDVFREF--FGGRDPFSfdffedpfeDFFGNQRGPRGSRNR 136
Cdd:PRK14282   85 GGGFF---------EDIFKDFenIFNRDIFD---------IFFGERRTQEEQREY 121
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 4-66 4.28e-33

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: 116.42  E-value: 4.28e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPeKKEEAERKFKQVAEAYEVLPDANKRDIY 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNP-GDPEAEEKFKEINEAYEVLSDPEKRAIY 62
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 4-107 6.90e-33

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: 124.64  E-value: 6.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKkeEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSh 83
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDK--EAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGG- 77

                          90       100
                  ....*....|....*....|....
gi 1811009100  84 FDGPFGFGFTF*NPDDVFREFFGG 107
Cdd:TIGR02349  78 GGFNGFDIGFFGDFGDIFGDFFGG 101
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 4-71 4.40e-32

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 122.56  E-value: 4.40e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYGK 71
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDK-EAEEKFKEIKEAYEVLSDPQKRAAYDQYGH 71
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 4-70 1.20e-31

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: 115.57  E-value: 1.20e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDP-EAEEKFKEINEAYEVLSDPEKRAAYDRFG 66
DnaJ smart00271
DnaJ molecular chaperone homology domain;
3-62 1.87e-29

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 106.94  E-value: 1.87e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100    3 VDYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKEEAERKFKQVAEAYEVLPDANK 62
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 4-59 1.12e-26

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: 99.54  E-value: 1.12e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPeKKEEAERKFKQVAEAYEVLPD 59
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNP-DDPEAEEKFKEINEAYEVLSD 55
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 4-136 9.47e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 105.26  E-value: 9.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSH 83
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPPYQETES 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1811009100  84 FDGPFgfgftf*npDDVFREF--FGGRDPFSfdffedpfeDFFGNQRGPRGSRNR 136
Cdd:PRK14282   85 GGGFF---------EDIFKDFenIFNRDIFD---------IFFGERRTQEEQREY 121
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
4-107 5.18e-23

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 98.74  E-value: 5.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEgldggrgggsh 83
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN--KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHD----------- 72

                          90       100
                  ....*....|....*....|....
gi 1811009100  84 fdGPFGFGFTF*NPDDVFREFFGG 107
Cdd:NF037946   73 --GVDGEGGFGFDAFDVFSSFFET 94
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 4-66 4.28e-33

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: 116.42  E-value: 4.28e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPeKKEEAERKFKQVAEAYEVLPDANKRDIY 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNP-GDPEAEEKFKEINEAYEVLSDPEKRAIY 62
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 4-107 6.90e-33

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: 124.64  E-value: 6.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKkeEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSh 83
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDK--EAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGG- 77

                          90       100
                  ....*....|....*....|....
gi 1811009100  84 FDGPFGFGFTF*NPDDVFREFFGG 107
Cdd:TIGR02349  78 GGFNGFDIGFFGDFGDIFGDFFGG 101
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 4-71 4.40e-32

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 122.56  E-value: 4.40e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYGK 71
Cdd:PRK10767    5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDK-EAEEKFKEIKEAYEVLSDPQKRAAYDQYGH 71
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 4-70 1.20e-31

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: 115.57  E-value: 1.20e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:COG0484     1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDP-EAEEKFKEINEAYEVLSDPEKRAAYDRFG 66
DnaJ smart00271
DnaJ molecular chaperone homology domain;
3-62 1.87e-29

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 106.94  E-value: 1.87e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100    3 VDYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKEEAERKFKQVAEAYEVLPDANK 62
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPEK 60
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 4-72 7.58e-27

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 108.31  E-value: 7.58e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYGKE 72
Cdd:PRK14294    5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDK-EAEELFKEAAEAYEVLSDPKKRGIYDQYGHE 72
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 4-59 1.12e-26

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: 99.54  E-value: 1.12e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPeKKEEAERKFKQVAEAYEVLPD 59
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNP-DDPEAEEKFKEINEAYEVLSD 55
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 4-107 3.30e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 106.55  E-value: 3.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSh 83
Cdd:PRK14290    4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYDQTGTVDFGAGGSNFN- 82

                          90       100
                  ....*....|....*....|....
gi 1811009100  84 fdgpFGFGFTF*NPDDVFREFFGG 107
Cdd:PRK14290   83 ----WDNFTHFSDINDIFNQIFGG 102
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 4-136 9.47e-26

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 105.26  E-value: 9.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSH 83
Cdd:PRK14282    5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPPYQETES 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1811009100  84 FDGPFgfgftf*npDDVFREF--FGGRDPFSfdffedpfeDFFGNQRGPRGSRNR 136
Cdd:PRK14282   85 GGGFF---------EDIFKDFenIFNRDIFD---------IFFGERRTQEEQREY 121
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 4-107 1.31e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 105.24  E-value: 1.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKkeEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSh 83
Cdd:PRK14291    4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNP--EAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAFSGSGQQQQ- 80

                          90       100
                  ....*....|....*....|....
gi 1811009100  84 fDGPFGFGFTF*NPDDVFREFFGG 107
Cdd:PRK14291   81 -GQEGFSDFGGGNIEDILEDVFDI 103
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 4-63 1.61e-25

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 96.61  E-value: 1.61e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKR 63
Cdd:COG5407     1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDP-KAEERFKEINEAYELLSDAEKR 59
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 4-72 2.19e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 104.54  E-value: 2.19e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKE 72
Cdd:PRK14284    2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNP-GDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGKD 69
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 4-70 5.17e-25

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 103.28  E-value: 5.17e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEkKEEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:PRK14301    5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPD-NPEAEQKFKEAAEAYEVLRDAEKRARYDRFG 70
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
4-68 5.53e-25

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 96.33  E-value: 5.53e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKEEAERKFKQVAEAYEVLPDANKRDIYGR 68
Cdd:COG2214     6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEYDR 70
PRK14280 PRK14280
molecular chaperone DnaJ;
4-110 1.87e-24

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 101.72  E-value: 1.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSH 83
Cdd:PRK14280    5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDIN--KEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGGGGF 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1811009100  84 FDGPFGFGFTF*npDDVFREFFGG----RDP 110
Cdd:PRK14280   83 GGGDFGGGFGF---EDIFSSFFGGggrrRDP 110
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 4-70 3.81e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 101.42  E-value: 3.81e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:PRK14281    4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNK-EAEEHFKEVNEAYEVLSNDDKRRRYDQFG 69
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 4-138 4.16e-24

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 101.08  E-value: 4.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKegldgGRGGGSH 83
Cdd:PRK14298    6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKN--KEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGH-----AGIDNQY 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1811009100  84 FDGPFGFGFTF*NPDDVFREFFGGrdpfsfdffedpfedffGNQRGPRGSRnRGT 138
Cdd:PRK14298   79 SAEDIFRGADFGGFGDIFEMFFGG-----------------GGRRGRMGPR-RGS 115
PRK14289 PRK14289
molecular chaperone DnaJ;
4-70 3.82e-23

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 98.36  E-value: 3.82e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:PRK14289    6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDK-EAEEKFKEAAEAYDVLSDPDKRSRYDQFG 71
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
4-107 5.18e-23

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 98.74  E-value: 5.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEgldggrgggsh 83
Cdd:NF037946    6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRN--KAPDAAEIFAEINEAYEVLSNPEKRANYDKYGHD----------- 72

                          90       100
                  ....*....|....*....|....
gi 1811009100  84 fdGPFGFGFTF*NPDDVFREFFGG 107
Cdd:NF037946   73 --GVDGEGGFGFDAFDVFSSFFET 94
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 4-70 1.26e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 96.79  E-value: 1.26e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:PRK14277    6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDK-EAEQKFKEINEAYEILSDPQKRAQYDQFG 71
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 4-110 1.64e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 96.70  E-value: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSH 83
Cdd:PRK14276    5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDIN--KEPGAEEKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFGGGAG 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1811009100  84 FDGPFGFGFTF*NPDDVFREFFGG----RDP 110
Cdd:PRK14276   83 GFGGFDGSGGFGGFEDIFSSFFGGggarRNP 113
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 4-70 9.63e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 94.51  E-value: 9.63e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEkkEEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:PRK14283    6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE--EGAEEKFKEISEAYAVLSDDEKRQRYDQFG 70
PRK14297 PRK14297
molecular chaperone DnaJ;
4-70 2.06e-21

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 93.31  E-value: 2.06e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:PRK14297    5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNK-EAEEKFKEINEAYQVLSDPQKKAQYDQFG 70
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 2-107 2.26e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 93.03  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   2 VVDYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeeAERKFKQVAEAYEVLPDANKRDIYGRYGkegldggRGGG 81
Cdd:PRK14292    1 MMDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKG--AAEKFAQINEAYAVLSDAEKRAHYDRFG-------TAPG 71

                          90       100
                  ....*....|....*....|....*.
gi 1811009100  82 SHFDGPFGFGFTF*NPDDVFREFFGG 107
Cdd:PRK14292   72 AGMPGGDPFGGMGFDPMDIFEQLFGG 97
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 4-111 2.18e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 89.23  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSH 83
Cdd:PRK14299    5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVN--KSPGAEEKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQGPPP 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1811009100  84 FDGPFGFGFTF*NPD--DVFREFFGGRDPF 111
Cdd:PRK14299   83 GPPGGGDFSGFNVGDfsDFFQQLFGGRGGF 112
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 4-137 3.74e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 89.73  E-value: 3.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEkkEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEgldggrgGGSH 83
Cdd:PRK14278    4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPD--EEAQEKFKEISVAYEVLSDPEKRRIVDLGGDP-------LESA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1811009100  84 FDGPFGFGFTF*NPDDVFREFFGGrdpfsfdffedpfedfFGNQRGPRGSRNRG 137
Cdd:PRK14278   75 GGGGGGFGGGFGGLGDVFEAFFGG----------------GAASRGPRGRVRPG 112
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 4-108 5.56e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 89.28  E-value: 5.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpEKKEEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGSH 83
Cdd:PRK14285    4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKN-KGNKEAESIFKEATEAYEVLIDDNKRAQYDRFGHTAFEGGGGFEGF 82

                          90       100
                  ....*....|....*....|....*
gi 1811009100  84 FDGPFGFGFTF*NPDDVFREFFGGR 108
Cdd:PRK14285   83 SGGFSGFSDIFEDFGDIFDSFFTGN 107
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 5-107 6.80e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 88.89  E-value: 6.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   5 YYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYGKEGLDGGRGGGShF 84
Cdd:PRK14286    6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNK-ESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGGFG-Q 83

                          90       100
                  ....*....|....*....|...
gi 1811009100  85 DGPFGFGFTF*NPDDVFREFFGG 107
Cdd:PRK14286   84 GAYTDFSDIFGDFGDIFGDFFGG 106
PRK14293 PRK14293
molecular chaperone DnaJ;
4-70 2.08e-19

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 87.74  E-value: 2.08e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:PRK14293    4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVN--KEPGAEDRFKEINRAYEVLSDPETRARYDQFG 68
PRK14279 PRK14279
molecular chaperone DnaJ;
4-66 4.67e-18

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 84.01  E-value: 4.67e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKEEAERkFKQVAEAYEVLPDANKRDIY 66
Cdd:PRK14279   10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEER-FKAVSEAHDVLSDPAKRKEY 71
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 4-70 1.27e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 82.36  E-value: 1.27e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:PRK14287    5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVN--KAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFG 69
PRK14288 PRK14288
molecular chaperone DnaJ;
3-72 2.32e-17

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 81.66  E-value: 2.32e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   3 VDYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKKeEAERKFKQVAEAYEVLPDANKRDIYGRYGKE 72
Cdd:PRK14288    3 LSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDK-EAEEKFKLINEAYGVLSDEKKRALYDRYGKK 71
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
 4-70 2.62e-17

terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ homolog and probable assembly protein of the Mycoplasma terminal organelle. The terminal organelle is involved in both cytadherence and gliding motility. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274808 [Multi-domain]  Cd Length: 871  Bit Score: 82.55  E-value: 2.62e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:TIGR03835   3 DYYEVLGIDRDADEQEIKKAFRKLAKKYHPDRN--KAPDAASIFAEINEANDVLSNPKKRANYDKYG 67
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 5-107 3.80e-17

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 81.41  E-value: 3.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   5 YYEVLGVHRHASAEDIKKAYRELALKWHPDK--NPEKkeeaerkFKQVAEAYEVLPDANKRDIYGRYGKEgldggrgggs 82
Cdd:PTZ00037   30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKggDPEK-------FKEISRAYEVLSDPEKRKIYDEYGEE---------- 92

                          90       100
                  ....*....|....*....|....*
gi 1811009100  83 hfdgPFGFGFTF*NPDDVFREFFGG 107
Cdd:PTZ00037   93 ----GLEGGEQPADASDLFDLIFGG 113
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 4-70 3.37e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 78.45  E-value: 3.37e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:PRK14296    5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLN--KSPDAHDKMVEINEAADVLLDKDKRKQYDQFG 69
PRK14295 PRK14295
molecular chaperone DnaJ;
4-66 9.19e-16

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 77.20  E-value: 9.19e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpEKKEEAERKFKQVAEAYEVLPDANKRDIY 66
Cdd:PRK14295   10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDAN-KGDAKAEERFKEISEAYDVLSDEKKRKEY 71
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 4-72 1.74e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 76.21  E-value: 1.74e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNPEKkeEAERKFKQVAEAYEVLPDANKRDIYGRYGKE 72
Cdd:PRK14300    4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAK--DAEKKFKEINAAYDVLKDEQKRAAYDRFGHD 70
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
4-65 8.62e-15

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 68.28  E-value: 8.62e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDK-----NPEKKEEAERKFKQVAEAYEVLPDANKRDI 65
Cdd:COG1076     5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaglPEEEQRLALQKAAAINEAYETLKDPRGIDL 71
PRK10266 PRK10266
curved DNA-binding protein;
4-66 1.31e-14

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 72.93  E-value: 1.31e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDKNpeKKEEAERKFKQVAEAYEVLPDANKRDIY 66
Cdd:PRK10266    5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVS--KEPDAEARFKEVAEAWEVLSDEQRRAEY 65
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 5-70 2.06e-09

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 58.64  E-value: 2.06e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811009100    5 YYEVLGVHRHASAEDIKKAYRELALKWHPDKnpEKKEEAERKFKQVAEAYEVLPDANKRDIYGRYG 70
Cdd:PTZ00341   575 FYDILGVGVNADMKEISERYFKLAENYYPPK--RSGNEGFHKFKKINEAYQILGDIDKKKMYNKFG 638
djlA PRK09430
co-chaperone DjlA;
4-57 2.15e-06

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 48.27  E-value: 2.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811009100   4 DYYEVLGVHRHASAEDIKKAYRELALKWHPDK------NPEKKEEAERKFKQVAEAYEVL 57
Cdd:PRK09430  201 DAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvakglPPEMMEMAKEKAQEIQAAYELI 260
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 3-66 4.11e-06

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 48.11  E-value: 4.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811009100   3 VDYYEVLGVHRH---ASAEDIKKAYRELALKWHPDKNPEKKEEAERK-FKQVAEAYEVLPDANKRDIY 66
Cdd:COG5269    43 VDLYALLGLSKYrtkAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEfFKLIQKAREVLGDRKLRLQY 110
PHA03102 PHA03102
Small T antigen; Reviewed
 7-42 5.24e-04

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 39.65  E-value: 5.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1811009100   7 EVLGVHRHA--SAEDIKKAYRELALKWHPDK--NPEKKEE 42
Cdd:PHA03102    9 DLLGLPRSAwgNLPLMRKAYLRKCLEFHPDKggDEEKMKE 48
hscB PRK01356
co-chaperone HscB; Provisional
 2-66 1.96e-03

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 38.32  E-value: 1.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811009100   2 VVDYYEVLGVHRHASA--EDIKKAYRELALKWHPD--KNPEKKEEAERKFKQVAEAYEVLPDANKRDIY 66
Cdd:PRK01356    1 MQNYFQLLGLPQEYNIdlKILEKQYFAMQVKYHPDkaKTLQEKEQNLIIASELNNAYSTLKDALKRAEY 69
PHA02624 PHA02624
large T antigen; Provisional
 7-39 3.33e-03

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 39.20  E-value: 3.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1811009100   7 EVLGVHRHA--SAEDIKKAYRELALKWHPDK--NPEK 39
Cdd:PHA02624   15 DLLGLPMAAwgNLPLMRKAYLRKCKEYHPDKggDEEK 51
 
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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