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Conserved domains on  [gi|89111951|ref|NP_859057|]
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dnaJ homolog subfamily C member 24 [Homo sapiens]

Protein Classification

diphthamide biosynthesis protein 4( domain architecture ID 10446362)

diphthamide biosynthesis protein 4 (DPH4) is a J domain-containing CSL-type zinc finger protein that is required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue

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 ...
 11-79 3.57e-17

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: 70.58  E-value: 3.57e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111951    11 DWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD------PEAEEKFKEINEAYEVLSDPEKRAIYD 63
zf-CSL pfam05207
CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which ...
 95-148 4.37e-12

CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which chelate zinc. This domain is often found associated with a pfam00226 domain. This domain is named after the conserved motif of the final cysteine.


:

Pssm-ID: 398744  Cd Length: 55  Bit Score: 57.25  E-value: 4.37e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 89111951    95 AQVYLEEMSWNEGDHSFYLSCRCGGKYSVSKDEAEEVSLIS-CDTCSLIIELLHY 148
Cdd:pfam05207   1 DEVELEDFEFDEEEESYYYPCRCGDEFEITEEDLEEGEVVVqCPSCSLWIKVIYD 55
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 11-79 3.57e-17

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: 70.58  E-value: 3.57e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111951    11 DWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD------PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 11-71 2.61e-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: 65.64  E-value: 2.61e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111951  11 DWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGN 71
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD------PEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
10-73 4.12e-15

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 65.33  E-value: 4.12e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111951     10 KDWYSILGADPSANISDLKQKYQKLILMYHPDKQStdvpaGTVEECVQKFIEIDQAWKILGNEE 73
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNP-----GDKEEAEEKFKEINEAYEVLSDPE 59
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 11-79 6.52e-15

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: 67.03  E-value: 6.52e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111951  11 DWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD------PEAEEKFKEINEAYEVLSDPEKRAAYD 63
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 9-79 3.56e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 68.30  E-value: 3.56e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111951    9 KKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14281   2 KRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDN------KEAEEHFKEVNEAYEVLSNDDKRRRYD 66
zf-CSL pfam05207
CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which ...
 95-148 4.37e-12

CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which chelate zinc. This domain is often found associated with a pfam00226 domain. This domain is named after the conserved motif of the final cysteine.


Pssm-ID: 398744  Cd Length: 55  Bit Score: 57.25  E-value: 4.37e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 89111951    95 AQVYLEEMSWNEGDHSFYLSCRCGGKYSVSKDEAEEVSLIS-CDTCSLIIELLHY 148
Cdd:pfam05207   1 DEVELEDFEFDEEEESYYYPCRCGDEFEITEEDLEEGEVVVqCPSCSLWIKVIYD 55
COG5216 COG5216
Uncharacterized conserved protein [Function unknown];
96-147 5.01e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227541  Cd Length: 67  Bit Score: 33.66  E-value: 5.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 89111951  96 QVYLEEMSWNEGDHSFYLSCRCGGKYSVSKDEAEEVSLIS-CDTCSLIIELLH 147
Cdd:COG5216   6 EIEIEDFTFSREEKTFTYPCPCGDRFEISLEDLRNGEVVArCPSCSLIVCVVY 58
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 11-79 3.57e-17

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: 70.58  E-value: 3.57e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111951    11 DWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD------PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 11-71 2.61e-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: 65.64  E-value: 2.61e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111951  11 DWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGN 71
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD------PEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
10-73 4.12e-15

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 65.33  E-value: 4.12e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111951     10 KDWYSILGADPSANISDLKQKYQKLILMYHPDKQStdvpaGTVEECVQKFIEIDQAWKILGNEE 73
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNP-----GDKEEAEEKFKEINEAYEVLSDPE 59
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 11-79 6.52e-15

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: 67.03  E-value: 6.52e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111951  11 DWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD------PEAEEKFKEINEAYEVLSDPEKRAAYD 63
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 9-79 3.56e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 68.30  E-value: 3.56e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111951    9 KKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14281   2 KRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDN------KEAEEHFKEVNEAYEVLSNDDKRRRYD 66
PRK14297 PRK14297
molecular chaperone DnaJ;
7-79 1.34e-13

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 66.35  E-value: 1.34e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDVPAgtvEEcvqKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14297   1 MASKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEA---EE---KFKEINEAYQVLSDPQKKAQYD 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 7-79 1.62e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 66.36  E-value: 1.62e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14277   2 AAKKDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGD------KEAEQKFKEINEAYEILSDPQKRAQYD 68
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
7-82 2.52e-13

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 61.66  E-value: 2.52e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 89111951   7 MPK-KDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDVPAGTveecvQKFIEIDQAWKILGNEETKREYDLQR 82
Cdd:COG2214   1 MPDlKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAE-----ELFQRLNEAYEVLSDPERRAEYDREL 72
PRK14295 PRK14295
molecular chaperone DnaJ;
2-82 3.23e-13

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 65.64  E-value: 3.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111951    2 MAVEQMPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDVPAgtvEEcvqKFIEIDQAWKILGNEETKREYDLQ 81
Cdd:PRK14295   1 MSTKDYIEKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKA---EE---RFKEISEAYDVLSDEKKRKEYDEA 74


                 .
gi 89111951   82 R 82
Cdd:PRK14295  75 R 75
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 9-79 1.26e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 63.71  E-value: 1.26e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111951    9 KKDWYSILGADPSANISDLKQKYQKLILMYHPDKqSTDVPAgtvEEcvqKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14298   4 TRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDK-NKEPDA---EE---KFKEISEAYAVLSDAEKRAQYD 67
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 7-79 4.36e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 62.15  E-value: 4.36e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTdvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14283   2 AEKRDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE-------EGAEEKFKEISEAYAVLSDDEKRQRYD 67
zf-CSL pfam05207
CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which ...
 95-148 4.37e-12

CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which chelate zinc. This domain is often found associated with a pfam00226 domain. This domain is named after the conserved motif of the final cysteine.


Pssm-ID: 398744  Cd Length: 55  Bit Score: 57.25  E-value: 4.37e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 89111951    95 AQVYLEEMSWNEGDHSFYLSCRCGGKYSVSKDEAEEVSLIS-CDTCSLIIELLHY 148
Cdd:pfam05207   1 DEVELEDFEFDEEEESYYYPCRCGDEFEITEEDLEEGEVVVqCPSCSLWIKVIYD 55
PRK10266 PRK10266
curved DNA-binding protein;
7-79 9.36e-12

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 60.99  E-value: 9.36e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDkQSTDVPAGTveecvqKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK10266   1 MELKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPD-VSKEPDAEA------RFKEVAEAWEVLSDEQRRAEYD 66
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
7-69 1.87e-11

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 56.34  E-value: 1.87e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951   7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDVPAGTVEECVQKFIEIDQAWKIL 69
Cdd:COG1076   1 MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRLAAGLPEEEQRLALQKAAAINEAYETL 63
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 7-79 7.09e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 58.65  E-value: 7.09e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtVEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14282   1 REKKDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPEN-----RKEAEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 7-91 9.72e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 58.24  E-value: 9.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYDlQRCEDD 86
Cdd:PRK14294   1 MVKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGD------KEAEELFKEAAEAYEVLSDPKKRGIYD-QYGHEG 73


                 ....*
gi 89111951   87 LRNVG 91
Cdd:PRK14294  74 LSGTG 78
PRK14289 PRK14289
molecular chaperone DnaJ;
7-79 1.33e-10

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 57.92  E-value: 1.33e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14289   2 AEKRDYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGD------KEAEEKFKEAAEAYDVLSDPDKRSRYD 68
PRK14280 PRK14280
molecular chaperone DnaJ;
7-79 1.98e-10

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 57.42  E-value: 1.98e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPD--KQstdvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14280   1 MAKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDinKE---------EGADEKFKEISEAYEVLSDDQKRAQYD 66
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 9-79 2.25e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 57.47  E-value: 2.25e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111951    9 KKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTdvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14291   2 KKDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKN-------PEAEEKFKEINEAYQVLSDPEKRKLYD 65
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 7-79 2.97e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 56.92  E-value: 2.97e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14286   1 MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGN------KESEEKFKEATEAYEILRDPKKRQAYD 67
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 11-79 3.20e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 56.77  E-value: 3.20e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111951   11 DWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDVpagtveECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14284   2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDA------EAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 7-79 4.36e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 56.10  E-value: 4.36e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTdvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14299   1 MAYKDYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKS-------PGAEEKFKEINEAYTVLSDPEKRRIYD 66
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 10-79 6.58e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 56.09  E-value: 6.58e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111951   10 KDWYSILGADPSANISDLKQKYQKLILMYHPDKQStdvpaGTVEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14290   3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHP-----GNKAEAEEKFKEISEAYEVLSDPQKRRQYD 67
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 10-79 7.74e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 55.79  E-value: 7.74e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111951   10 KDWYSILGADPSANISDLKQKYQKLILMYHPDKQStdvpAGTVEecvQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14300   3 QDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTD----AKDAE---KKFKEINAAYDVLKDEQKRAAYD 65
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 7-79 1.01e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 55.52  E-value: 1.01e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14301   1 MSQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDN------PEAEQKFKEAAEAYEVLRDAEKRARYD 67
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 9-79 1.25e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 55.00  E-value: 1.25e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111951    9 KKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14285   2 KRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGN------KEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 7-79 1.37e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 55.02  E-value: 1.37e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDkqstdvpAGTVEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14287   1 MSKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPD-------VNKAPDAEDKFKEVKEAYDTLSDPQKKAHYD 66
PRK14293 PRK14293
molecular chaperone DnaJ;
1-79 2.81e-09

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 54.23  E-value: 2.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111951    1 MMAveqmpkkDWYSILGADPSANISDLKQKYQKLILMYHPD--KQstdvpAGTvEEcvqKFIEIDQAWKILGNEETKREY 78
Cdd:PRK14293   1 MAA-------DYYEILGVSRDADKDELKRAYRRLARKYHPDvnKE-----PGA-ED---RFKEINRAYEVLSDPETRARY 64


                 .
gi 89111951   79 D 79
Cdd:PRK14293  65 D 65
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 10-80 1.51e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 51.98  E-value: 1.51e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89111951   10 KDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTdvpagtvEECVQKFIEIDQAWKILGNEETKREYDL 80
Cdd:PRK14278   3 RDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPD-------EEAQEKFKEISVAYEVLSDPEKRRIVDL 66
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 7-79 2.94e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 51.10  E-value: 2.94e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPD-KQSTDVPagtveecvQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14296   1 MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDlNKSPDAH--------DKMVEINEAADVLLDKDKRKQYD 66
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 11-79 3.27e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 51.04  E-value: 3.27e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 89111951   11 DWYSILGADPSANISDLKQKYQKLILMYHPDKQstdvPAGTVEEcvqKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14292   3 DYYELLGVSRTASADEIKSAYRKLALKYHPDRN----KEKGAAE---KFAQINEAYAVLSDAEKRAHYD 64
PRK14279 PRK14279
molecular chaperone DnaJ;
2-82 1.06e-07

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 49.73  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111951    2 MAVEQMPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDVPAGtveecvQKFIEIDQAWKILGNEETKREYDLQ 81
Cdd:PRK14279   1 MAQREWVEKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAE------ERFKAVSEAHDVLSDPAKRKEYDET 74


                 .
gi 89111951   82 R 82
Cdd:PRK14279  75 R 75
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 10-92 5.11e-07

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 47.51  E-value: 5.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89111951   10 KDWYSILGADPSANISDLKQKYQKLILMYHPDKqstdvpAGTVEecvqKFIEIDQAWKILGNEETKREYDlQRCEDDLRN 89
Cdd:PTZ00037  28 EKLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDK------GGDPE----KFKEISRAYEVLSDPEKRKIYD-EYGEEGLEG 96


                 ...
gi 89111951   90 VGP 92
Cdd:PTZ00037  97 GEQ 99
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 7-79 1.08e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 46.62  E-value: 1.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 89111951    7 MPKKDWYSILGADPSANISDLKQKYQKLILMYHPDkqsTDVPAGTVEecvqKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14276   1 MNNTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPD---INKEPGAEE----KYKEVQEAYETLSDPQKRAAYD 66
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 6-79 1.53e-06

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 46.32  E-value: 1.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111951     6 QMPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQStdvpagtVEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PTZ00341  569 EIPDTLFYDILGVGVNADMKEISERYFKLAENYYPPKRS-------GNEGFHKFKKINEAYQILGDIDKKKMYN 635
PRK14288 PRK14288
molecular chaperone DnaJ;
12-79 2.29e-06

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 45.84  E-value: 2.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 89111951   12 WYSILGADPSANISDLKQKYQKLILMYHPDKQSTDvpagtvEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:PRK14288   5 YYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGD------KEAEEKFKLINEAYGVLSDEKKRALYD 66
djlA PRK09430
co-chaperone DjlA;
10-42 8.82e-04

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 37.87  E-value: 8.82e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 89111951   10 KDWYSILGADPSANISDLKQKYQKLILMYHPDK 42
Cdd:PRK09430 200 EDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 9-79 1.22e-03

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 37.70  E-value: 1.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89111951   9 KKDWYSILGADP---SANISDLKQKYQKLILMYHPDKQStdvpAGTVEECVQKFIEIDQAWKILGNEETKREYD 79
Cdd:COG5269  42 KVDLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTA----AGGNKGCDEFFKLIQKAREVLGDRKLRLQYD 111
COG5216 COG5216
Uncharacterized conserved protein [Function unknown];
96-147 5.01e-03

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227541  Cd Length: 67  Bit Score: 33.66  E-value: 5.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 89111951  96 QVYLEEMSWNEGDHSFYLSCRCGGKYSVSKDEAEEVSLIS-CDTCSLIIELLH 147
Cdd:COG5216   6 EIEIEDFTFSREEKTFTYPCPCGDRFEISLEDLRNGEVVArCPSCSLIVCVVY 58
 
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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