NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6321420|ref|NP_011497|]
View 

J-type chaperone JAC1 [Saccharomyces cerevisiae S288C]

Protein Classification

co-chaperone HscB; Fe-S protein assembly co-chaperone HscB( domain architecture ID 11489531)

co-chaperone HscB is involved in the maturation of iron-sulfur cluster-containing proteins| Fe-S protein assembly co-chaperone HscB acts as a co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 29-179 4.96e-60

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


:

Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 183.93  E-value: 4.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420     29 WTIDQSRLRKEYRQLQAQHHPDMAQ------QGSEQSSTLNQAYHTLKDPLRRSQYMLKLLrNIDLTQEQTSnEVTTSDP 102
Cdd:TIGR00714   1 WQLDQSRLRKRYRQLQAQYHPDASGmaqeqlAASQQSTTLNQAYHTLKDPLRRAEYMLKLL-NIDLTQEQTS-ERDTAFP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321420    103 QLLLKVLDIHDELSQMDDEAGVKLLEKQNKERIQDIEAQLGQCYNDKDYAAAVKLTVELKYWYNLAKAFKDWAPGKQ 179
Cdd:TIGR00714  79 MELLKVRDELDEIEQMDDEAGLELLEKQNKEMIQDIEAQLGQCLNDQDWAAAVKYTVKLKYWYKLASAFEDWEEGKQ 155
 
Name Accession Description Interval E-value
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 29-179 4.96e-60

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 183.93  E-value: 4.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420     29 WTIDQSRLRKEYRQLQAQHHPDMAQ------QGSEQSSTLNQAYHTLKDPLRRSQYMLKLLrNIDLTQEQTSnEVTTSDP 102
Cdd:TIGR00714   1 WQLDQSRLRKRYRQLQAQYHPDASGmaqeqlAASQQSTTLNQAYHTLKDPLRRAEYMLKLL-NIDLTQEQTS-ERDTAFP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321420    103 QLLLKVLDIHDELSQMDDEAGVKLLEKQNKERIQDIEAQLGQCYNDKDYAAAVKLTVELKYWYNLAKAFKDWAPGKQ 179
Cdd:TIGR00714  79 MELLKVRDELDEIEQMDDEAGLELLEKQNKEMIQDIEAQLGQCLNDQDWAAAVKYTVKLKYWYKLASAFEDWEEGKQ 155
hscB PRK05014
co-chaperone HscB; Provisional
 14-167 7.99e-17

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 73.79  E-value: 7.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420    14 FYELFpktfpkKLPI-WTIDQSRLRKEYRQLQAQHHPDMAQQGSEQ--------SSTLNQAYHTLKDPLRRSQYMLKlLR 84
Cdd:PRK05014   3 YFTLF------GLPArYDIDTQLLASRYQELQRQFHPDKFANASERerllavqqAATINDAYQTLKHPLKRAEYLLS-LH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420    85 NIDLTQEQTsnevTTSDPQLLLKVLDIHDEL----SQMDDEAGVKLLEKQNKERIQDIEAQLGQCYNDKDYAAAVKLTVE 160
Cdd:PRK05014  76 GFDLAHEQH----TVRDTAFLMEQMELREELedieQSKDPEAALESFIKRVKKMFKTRLQQMVEQLDNEAWDAAADTVRK 151


                 ....*..
gi 6321420   161 LKYWYNL 167
Cdd:PRK05014 152 LKFLDKL 158
HSCB_C pfam07743
HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization ...
 101-172 1.99e-14

HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization domain and is found on co-chaperone proteins.


Pssm-ID: 462252  Cd Length: 75  Bit Score: 64.85  E-value: 1.99e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321420    101 DPQLLLKVLDIHDELS--QMDDEAGVKLLEKQNKERIQDIEAQLGQCYNDKDYAAAVKLTVELKYWYNLAKAFK 172
Cdd:pfam07743   2 DPEFLMEQMEWREELEeaEARDEEELEELKAENKERIKELEAELEEAFDEQDLEAAADLVRRLRYLEKIQEEIK 75
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
30-72 4.02e-09

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 50.95  E-value: 4.02e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6321420   30 TIDQSRLRKEYRQLQAQHHPD-MAQQGSE--------QSSTLNQAYHTLKDP 72
Cdd:COG1076  15 DADDAELKRAYRKLQREHHPDrLAAGLPEeeqrlalqKAAAINEAYETLKDP 66
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 29-71 1.11e-06

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: 43.69  E-value: 1.11e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 6321420   29 WTIDQSRLRKEYRQLQAQHHPDMAQ---QGSEQSSTLNQAYHTLKD 71
Cdd:cd06257  10 PDASDEEIKKAYRKLALKYHPDKNPddpEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
30-74 3.92e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 42.61  E-value: 3.92e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6321420      30 TIDQSRLRKEYRQLQAQHHPDMAQQGS----EQSSTLNQAYHTLKDPLR 74
Cdd:smart00271  12 DASLDEIKKAYRKLALKYHPDKNPGDKeeaeEKFKEINEAYEVLSDPEK 60
 
Name Accession Description Interval E-value
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 29-179 4.96e-60

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 183.93  E-value: 4.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420     29 WTIDQSRLRKEYRQLQAQHHPDMAQ------QGSEQSSTLNQAYHTLKDPLRRSQYMLKLLrNIDLTQEQTSnEVTTSDP 102
Cdd:TIGR00714   1 WQLDQSRLRKRYRQLQAQYHPDASGmaqeqlAASQQSTTLNQAYHTLKDPLRRAEYMLKLL-NIDLTQEQTS-ERDTAFP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321420    103 QLLLKVLDIHDELSQMDDEAGVKLLEKQNKERIQDIEAQLGQCYNDKDYAAAVKLTVELKYWYNLAKAFKDWAPGKQ 179
Cdd:TIGR00714  79 MELLKVRDELDEIEQMDDEAGLELLEKQNKEMIQDIEAQLGQCLNDQDWAAAVKYTVKLKYWYKLASAFEDWEEGKQ 155
hscB PRK05014
co-chaperone HscB; Provisional
 14-167 7.99e-17

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 73.79  E-value: 7.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420    14 FYELFpktfpkKLPI-WTIDQSRLRKEYRQLQAQHHPDMAQQGSEQ--------SSTLNQAYHTLKDPLRRSQYMLKlLR 84
Cdd:PRK05014   3 YFTLF------GLPArYDIDTQLLASRYQELQRQFHPDKFANASERerllavqqAATINDAYQTLKHPLKRAEYLLS-LH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420    85 NIDLTQEQTsnevTTSDPQLLLKVLDIHDEL----SQMDDEAGVKLLEKQNKERIQDIEAQLGQCYNDKDYAAAVKLTVE 160
Cdd:PRK05014  76 GFDLAHEQH----TVRDTAFLMEQMELREELedieQSKDPEAALESFIKRVKKMFKTRLQQMVEQLDNEAWDAAADTVRK 151


                 ....*..
gi 6321420   161 LKYWYNL 167
Cdd:PRK05014 152 LKFLDKL 158
hscB PRK01356
co-chaperone HscB; Provisional
 28-167 4.75e-15

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 69.14  E-value: 4.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420    28 IWTIDQSRLRKEYRQLQAQHHPDMAQQGSEQ------SSTLNQAYHTLKDPLRRSQYMLkLLRNIDLTQEQTSNEVTtsd 101
Cdd:PRK01356  13 EYNIDLKILEKQYFAMQVKYHPDKAKTLQEKeqnliiASELNNAYSTLKDALKRAEYML-LLQNINLNDEKTRSLLS--- 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321420   102 pqlLLKVLDIHDELSQMDDEAGVKLLEK-QNKERI--QDIEAQLGQCYNDKDYAAAVKLTVELKYWYNL 167
Cdd:PRK01356  89 ---PLELSIFWDEMERIENTILFSDLEKiKNKYELmyKNEIDSLKQAFEEQNLSDATIKTSKLKYIGTL 154
hscB PRK00294
co-chaperone HscB; Provisional
 27-148 1.27e-14

co-chaperone HscB; Provisional


Pssm-ID: 166894 [Multi-domain]  Cd Length: 173  Bit Score: 67.96  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420    27 PIWTIDQSRLRKEYRQLQAQHHPDMAQQGSE--------QSSTLNQAYHTLKDPLRRSQYMLKllrnidLTQEQTSNEVT 98
Cdd:PRK00294  14 PSFRLDLDQLATRYRELAREVHPDRFADAPEreqrlaleRSASLNEAYQTLKSPPRRARYLLA------LSGHEVPLEVT 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6321420    99 TSDPQLLLKVLDIHDELSQMDDEA---GVKLLEKQNKERIQDIEAQLGQCYND 148
Cdd:PRK00294  88 VHDPEFLLQQMQLREELEELQDEAdlaGVATFKRRLKAAQDELNESFAACWDD 140
HSCB_C pfam07743
HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization ...
 101-172 1.99e-14

HSCB C-terminal oligomerization domain; This domain is the HSCB C-terminal oligomerization domain and is found on co-chaperone proteins.


Pssm-ID: 462252  Cd Length: 75  Bit Score: 64.85  E-value: 1.99e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321420    101 DPQLLLKVLDIHDELS--QMDDEAGVKLLEKQNKERIQDIEAQLGQCYNDKDYAAAVKLTVELKYWYNLAKAFK 172
Cdd:pfam07743   2 DPEFLMEQMEWREELEeaEARDEEELEELKAENKERIKELEAELEEAFDEQDLEAAADLVRRLRYLEKIQEEIK 75
hscB PRK03578
Fe-S protein assembly co-chaperone HscB;
10-154 4.38e-12

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 235133 [Multi-domain]  Cd Length: 176  Bit Score: 61.19  E-value: 4.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420    10 FTSTFYELF--PKTFpkklpiwTIDQSRLRKEYRQLQAQHHPDMAQQGSE-------QSST-LNQAYHTLKDPLRRSQYM 79
Cdd:PRK03578   4 LKDDHFSLFglPARF-------ALDEAALDAAYRTVQAQVHPDRFAAAGDaekrvamQWATrANEAYQTLRDPLKRARYL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420    80 LKlLRNIDLTQEqtSNevTTSDPQLLL------------KVLDIHDELSQMDDEagvklLEKQNKERIQDIEAQLGQcyn 147
Cdd:PRK03578  77 LH-LRGVDVQAE--NN--TAMPPAFLMqqmewreaiedaRAARDVDALDALLAE-----LRDERRERYAELGALLDS--- 143


                 ....*..
gi 6321420   148 DKDYAAA 154
Cdd:PRK03578 144 RGDDQAA 150
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
30-72 4.02e-09

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 50.95  E-value: 4.02e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6321420   30 TIDQSRLRKEYRQLQAQHHPD-MAQQGSE--------QSSTLNQAYHTLKDP 72
Cdd:COG1076  15 DADDAELKRAYRKLQREHHPDrLAAGLPEeeqrlalqKAAAINEAYETLKDP 66
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
32-95 5.35e-08

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 48.56  E-value: 5.35e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321420   32 DQSRLRKEYRQLQAQHHPD----MAQQGSEQSSTLNQAYHTLKDPLRRSQYMLKLLRNIDLTQEQTSN 95
Cdd:COG2214  18 SLEEIRQAYRRLAKLLHPDrggeLKALAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKGSASQPSA 85
hscB PRK01773
Fe-S protein assembly co-chaperone HscB;
26-167 5.59e-08

Fe-S protein assembly co-chaperone HscB;


Pssm-ID: 179335 [Multi-domain]  Cd Length: 173  Bit Score: 50.13  E-value: 5.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321420    26 LPI-WTIDQSRLRKEYRQLQAQHHPDMAQQGSEQ--------SSTLNQAYHTLKDPLRRSQYMLKLLRNIDLTQEQTSNe 96
Cdd:PRK01773  10 LPVdFQLDNALLSERYLALQKSLHPDNFANSSAQeqrlamqkSAEVNDALQILKDPILRAEAIIALNTGEQQNLEEKST- 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321420    97 vttSDPQLLLKVLDIHDELSQMD---DEAGVKLLEKQNKERIQDIEAQLGQCYNDKDYAAAVKLTVELKYWYNL 167
Cdd:PRK01773  89 ---QDMAFLMQQMEWREQLEEIEqqqDEDALTAFSKEIKQEQQAILTELSTALNSQQWQQASQINDRLRFIKKL 159
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 29-71 1.11e-06

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: 43.69  E-value: 1.11e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 6321420   29 WTIDQSRLRKEYRQLQAQHHPDMAQ---QGSEQSSTLNQAYHTLKD 71
Cdd:cd06257  10 PDASDEEIKKAYRKLALKYHPDKNPddpEAEEKFKEINEAYEVLSD 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 30-103 3.36e-06

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: 44.69  E-value: 3.36e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321420   30 TIDQSRLRKEYRQLQAQHHPDM---AQQGSEQSSTLNQAYHTLKDPLRRSQYMLKLLRNIDLTQEQTSNEVTTSDPQ 103
Cdd:COG0484  11 DASAEEIKKAYRKLAKKYHPDRnpgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAESAAAEAAA 87
DnaJ smart00271
DnaJ molecular chaperone homology domain;
30-74 3.92e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 42.61  E-value: 3.92e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 6321420      30 TIDQSRLRKEYRQLQAQHHPDMAQQGS----EQSSTLNQAYHTLKDPLR 74
Cdd:smart00271  12 DASLDEIKKAYRKLALKYHPDKNPGDKeeaeEKFKEINEAYEVLSDPEK 60
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 32-78 6.71e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 45.08  E-value: 6.71e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 6321420    32 DQSRLRKEYRQLQAQHHPDMAQQ-GSEQS-STLNQAYHTLKDPLRRSQY 78
Cdd:PRK14276  17 SQDEIKKAYRKLSKKYHPDINKEpGAEEKyKEVQEAYETLSDPQKRAAY 65
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 32-78 2.05e-05

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: 40.53  E-value: 2.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 6321420     32 DQSRLRKEYRQLQAQHHPDMAQ---QGSEQSSTLNQAYHTLKDPLRRSQY 78
Cdd:pfam00226  13 SDEEIKKAYRKLALKYHPDKNPgdpEAEEKFKEINEAYEVLSDPEKRAIY 62
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 30-78 1.04e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 41.92  E-value: 1.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6321420    30 TIDQSRLRKEYRQLQAQHHPDMAQQGSEQS--STLNQAYHTLKDPLRRSQY 78
Cdd:PRK14300  14 TASQADLKKAYLKLAKQYHPDTTDAKDAEKkfKEINAAYDVLKDEQKRAAY 64
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 33-78 2.15e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 40.91  E-value: 2.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 6321420    33 QSRLRKEYRQLQAQHHPDMAQ--QGSEQSSTLNQAYHTLKDPLRRSQY 78
Cdd:PRK14291  17 QEEIKKAYRRLARKYHPDFNKnpEAEEKFKEINEAYQVLSDPEKRKLY 64
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 33-78 2.35e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 40.60  E-value: 2.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 6321420    33 QSRLRKEYRQLQAQHHPDMAQQ--GSEQSSTLNQAYHTLKDPLRRSQY 78
Cdd:PRK14298  19 VEDIKKAYRKLAMKYHPDKNKEpdAEEKFKEISEAYAVLSDAEKRAQY 66
PRK14280 PRK14280
molecular chaperone DnaJ;
36-78 6.71e-04

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 39.32  E-value: 6.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 6321420    36 LRKEYRQLQAQHHPDMAQQ--GSEQSSTLNQAYHTLKDPLRRSQY 78
Cdd:PRK14280  21 IKKAYRKLSKKYHPDINKEegADEKFKEISEAYEVLSDDQKRAQY 65
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 33-78 6.73e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 39.15  E-value: 6.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 6321420    33 QSRLRKEYRQLQAQHHPDMAQQ--GSEQSSTLNQAYHTLKDPLRRSQY 78
Cdd:PRK14299  18 QDEIKKAFKKLARKYHPDVNKSpgAEEKFKEINEAYTVLSDPEKRRIY 65
PRK14293 PRK14293
molecular chaperone DnaJ;
32-78 7.61e-04

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 39.20  E-value: 7.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 6321420    32 DQSRLRKEYRQLQAQHHPDMAQQ-GSEQS-STLNQAYHTLKDPLRRSQY 78
Cdd:PRK14293  16 DKDELKRAYRRLARKYHPDVNKEpGAEDRfKEINRAYEVLSDPETRARY 64
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 33-78 8.03e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 39.14  E-value: 8.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 6321420    33 QSRLRKEYRQLQAQHHPDM----AQQGSEQSSTLNQAYHTLKDPLRRSQY 78
Cdd:PRK14290  17 QEDIKKAFRELAKKWHPDLhpgnKAEAEEKFKEISEAYEVLSDPQKRRQY 66
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 30-78 9.29e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 39.10  E-value: 9.29e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6321420    30 TIDQSRLRKEYRQLQAQHHPDMAQQ--GSEQSSTLNQAYHTLKDPLRRSQY 78
Cdd:PRK14292  13 TASADEIKSAYRKLALKYHPDRNKEkgAAEKFAQINEAYAVLSDAEKRAHY 63
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 30-78 1.18e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 38.65  E-value: 1.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6321420    30 TIDQSRLRKEYRQLQAQHHPDMAQQ--GSEQSSTLNQAYHTLKDPLRRSQY 78
Cdd:PRK14283  16 NADKKEIKKAYRKLARKYHPDVSEEegAEEKFKEISEAYAVLSDDEKRQRY 66
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 36-78 1.22e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 38.45  E-value: 1.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 6321420    36 LRKEYRQLQAQHHPDM--AQQGSEQSSTLNQAYHTLKDPLRRSQY 78
Cdd:PRK14287  21 VKKAYRKLARKYHPDVnkAPDAEDKFKEVKEAYDTLSDPQKKAHY 65
PRK14295 PRK14295
molecular chaperone DnaJ;
36-78 1.90e-03

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 37.91  E-value: 1.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 6321420    36 LRKEYRQLQAQHHPDmAQQGSEQSST----LNQAYHTLKDPLRRSQY 78
Cdd:PRK14295  26 IKKAYRKLAREYHPD-ANKGDAKAEErfkeISEAYDVLSDEKKRKEY 71
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 34-78 3.36e-03

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 37.49  E-value: 3.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 6321420    34 SRLRKEYRQLQAQHHPDMAQQgSEQSSTLNQAYHTLKDPLRRSQY 78
Cdd:PTZ00037  43 SEIKKAYRKLAIKHHPDKGGD-PEKFKEISRAYEVLSDPEKRKIY 86
PRK10266 PRK10266
curved DNA-binding protein;
30-85 8.97e-03

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 35.95  E-value: 8.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6321420    30 TIDQSRLRKEYRQLQAQHHPDMAQQ--GSEQSSTLNQAYHTLKDPLRRSQY-MLKLLRN 85
Cdd:PRK10266  15 TDDLKTIKTAYRRLARKYHPDVSKEpdAEARFKEVAEAWEVLSDEQRRAEYdQLWQHRN 73
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH