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Conserved domains on  [gi|74193946|dbj|BAE36900|]
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unnamed protein product [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZUO1 super family cl34965
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-191 1.78e-33

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


The actual alignment was detected with superfamily member COG5269:

Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 122.45  E-value: 1.78e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946  75 MLKTLDPKDWKNQDHYAVLGLGHVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269  31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 74193946 155 RAFNSVDptFDNSVPS-KSEAKDNFFQVFSPVFERNSR 191
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREAR 143
zuotin_NTD super family cl48853
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-47 5.59e-03

N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, also known as DnaJ-related protein ZUO1, J protein ZUO1, or heat shock protein 40 homolog ZUO1, is a component of the ribosome-associated complex (RAC), which is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. The RAC chaperone complex plays a role in regulating accurate translation termination and folding or maintaining nascent polypeptides in a folding-competent state. The ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain is stimulated by the RAC chaperone complex. ZUO1 acts as a J-protein for SSB1/SSB2 only when it is associated with SSZ1. The N-terminal domain (NTD) of ZUO1 is responsible for its interaction with SSZ1, and it contains a conserved LP-motif that binds to the SSZ1 C-terminal SBD (substrate binding domain) beta-lid domain in the same way as canonical Hsp70s bind to their substrates.


The actual alignment was detected with superfamily member cd23953:

Pssm-ID: 467935  Cd Length: 38  Bit Score: 33.25  E-value: 5.59e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 74193946  13 TAITHALTSASSVCQVEPVGRWFEAFVKRRNRNAS 47
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRT 36
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-191 1.78e-33

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 122.45  E-value: 1.78e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946  75 MLKTLDPKDWKNQDHYAVLGLGHVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269  31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 74193946 155 RAFNSVDptFDNSVPS-KSEAKDNFFQVFSPVFERNSR 191
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREAR 143
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 88-158 1.12e-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: 73.28  E-value: 1.12e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74193946    88 DHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:pfam00226   1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
87-153 7.33e-15

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 65.72  E-value: 7.33e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74193946     87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 153
Cdd:smart00271   1 TDYYEILGVPR---DASLDEIKKAYRKLALKYHPDKNPGD----KEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 88-150 4.25e-14

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: 63.72  E-value: 4.25e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74193946  88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 150
Cdd:cd06257   1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 87-157 7.39e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 65.55  E-value: 7.39e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:PRK10767   4 RDYYEVLG---VSRNASEDEIKKAYRKLAMKYHPDRNpgdKEAEEKFKE--------IKEAYEVLSDPQKRAAY 66
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-47 5.59e-03

N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, also known as DnaJ-related protein ZUO1, J protein ZUO1, or heat shock protein 40 homolog ZUO1, is a component of the ribosome-associated complex (RAC), which is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. The RAC chaperone complex plays a role in regulating accurate translation termination and folding or maintaining nascent polypeptides in a folding-competent state. The ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain is stimulated by the RAC chaperone complex. ZUO1 acts as a J-protein for SSB1/SSB2 only when it is associated with SSZ1. The N-terminal domain (NTD) of ZUO1 is responsible for its interaction with SSZ1, and it contains a conserved LP-motif that binds to the SSZ1 C-terminal SBD (substrate binding domain) beta-lid domain in the same way as canonical Hsp70s bind to their substrates.


Pssm-ID: 467935  Cd Length: 38  Bit Score: 33.25  E-value: 5.59e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 74193946  13 TAITHALTSASSVCQVEPVGRWFEAFVKRRNRNAS 47
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRT 36
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-191 1.78e-33

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 122.45  E-value: 1.78e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946  75 MLKTLDPKDWKNQDHYAVLGLGHVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269  31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 74193946 155 RAFNSVDptFDNSVPS-KSEAKDNFFQVFSPVFERNSR 191
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREAR 143
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 88-158 1.12e-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: 73.28  E-value: 1.12e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74193946    88 DHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:pfam00226   1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
87-153 7.33e-15

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 65.72  E-value: 7.33e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74193946     87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 153
Cdd:smart00271   1 TDYYEILGVPR---DASLDEIKKAYRKLALKYHPDKNPGD----KEEAEEKFKEINEAYEVLSDPEK 60
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 88-157 1.35e-14

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: 67.42  E-value: 1.35e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74193946  88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:COG0484   1 DYYEILG---VSRDASAEEIKKAYRKLAKKYHPDRNpgdPEAEEKFKE--------INEAYEVLSDPEKRAAY 62
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 88-150 4.25e-14

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: 63.72  E-value: 4.25e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74193946  88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 150
Cdd:cd06257   1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
87-157 1.57e-13

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 63.20  E-value: 1.57e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74193946  87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKrkaaGEPIKEGDNDYFTCITKAYEMLSDPVKRRAF 157
Cdd:COG2214   5 KDHYAVLGVPP---DASLEEIRQAYRRLAKLLHPDR----GGELKALAEELFQRLNEAYEVLSDPERRAEY 68
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 87-157 7.39e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 65.55  E-value: 7.39e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:PRK10767   4 RDYYEVLG---VSRNASEDEIKKAYRKLAMKYHPDRNpgdKEAEEKFKE--------IKEAYEVLSDPQKRAAY 66
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 87-180 6.26e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 60.19  E-value: 6.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDK----RKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDP 162
Cdd:PRK14282   4 KDYYEILG---VSRNATQEEIKRAYKRLVKEWHPDRhpenRKEAEQKFKE--------IQEAYEVLSDPQKRAMYDRFGY 72

                         90
                 ....*....|....*...
gi 74193946  163 TFDNSVPSKSEAKDNFFQ 180
Cdd:PRK14282  73 VGEQPPYQETESGGGFFE 90
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 87-158 1.10e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 59.40  E-value: 1.10e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14291   3 KDYYEILG---VSRNATQEEIKKAYRRLARKYHPDfnKNPEAEEKFKE--------INEAYQVLSDPEKRKLYD 65
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 86-158 3.11e-10

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 58.29  E-value: 3.11e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74193946   86 NQDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKrkaagepikEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PTZ00037  27 NEKLYEVLNLSK---DCTTSEIKKAYRKLAIKHHPDK---------GGDPEKFKEISRAYEVLSDPEKRKIYD 87
PRK14295 PRK14295
molecular chaperone DnaJ;
82-167 3.18e-10

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 58.32  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946   82 KDWKNQDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKaaGEPIKEgdnDYFTCITKAYEMLSDPVKRRAFNSVD 161
Cdd:PRK14295   4 KDYIEKDYYKVLG---VPKDATEAEIKKAYRKLAREYHPDANK--GDAKAE---ERFKEISEAYDVLSDEKKRKEYDEAR 75


                 ....*.
gi 74193946  162 PTFDNS 167
Cdd:PRK14295  76 SLFGNG 81
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 87-159 8.43e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 56.49  E-value: 8.43e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRRAFNS 159
Cdd:PRK14299   4 KDYYAILG---VPKNASQDEIKKAFKKLARKYHPDVNKSPGaeEKFKE--------INEAYTVLSDPEKRRIYDT 67
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 86-158 2.34e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 55.48  E-value: 2.34e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74193946   86 NQDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14276   3 NTEYYDRLG---VSKDASQDEIKKAYRKLSKKYHPDINKEPGaeEKYKE--------VQEAYETLSDPQKRAAYD 66
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 88-155 4.97e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 54.67  E-value: 4.97e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946   88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRR 155
Cdd:PRK14278   4 DYYGLLG---VSRNASDAEIKRAYRKLARELHPDvnPDEEAQEKFKE--------ISVAYEVLSDPEKRR 62
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 86-158 5.34e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 54.61  E-value: 5.34e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74193946   86 NQDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14286   3 ERSYYDILG---VSKSANDEEIKSAYRKLAIKYHPDKNKGNKES-----EEKFKEATEAYEILRDPKKRQAYD 67
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 88-158 6.35e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 54.46  E-value: 6.35e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74193946   88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEgdndyFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14284   2 DYYTILG---VSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKR-----FKEVSEAYEVLSDAQKRESYD 64
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 87-187 7.99e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 54.00  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEGdndyftciTKAYEMLSDPVKRRAFNSVDPT 163
Cdd:PRK14294   4 RDYYEILG---VTRDASEEEIKKSYRKLAMKYHPDRNpgdKEAEELFKEA--------AEAYEVLSDPKKRGIYDQYGHE 72

                         90       100
                 ....*....|....*....|....*
gi 74193946  164 -FDNSVPSKSEAKDNFFQVFSPVFE 187
Cdd:PRK14294  73 gLSGTGFSGFSGFDDIFSSFGDIFE 97
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 87-158 8.55e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 54.04  E-value: 8.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14277   5 KDYYEILG---VDRNATEEEIKKAYRRLAKKYHPDLNpgdKEAEQKFKE--------INEAYEILSDPQKRAQYD 68
PRK14297 PRK14297
molecular chaperone DnaJ;
86-162 1.05e-08

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 53.63  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946   86 NQDHYAVLGLghvRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRR---AFNS 159
Cdd:PRK14297   3 SKDYYEVLGL---EKGASDDEIKKAFRKLAIKYHPDKNkgnKEAEEKFKE--------INEAYQVLSDPQKKAqydQFGT 71


                 ...
gi 74193946  160 VDP 162
Cdd:PRK14297  72 ADF 74
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 87-158 2.48e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 52.50  E-value: 2.48e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74193946   87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14281   3 RDYYEVLGVSR---SADKDEIKKAYRKLALKYHPDKNpdnKEAEEHFKE--------VNEAYEVLSNDDKRRRYD 66
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 87-187 2.50e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 52.54  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946   87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKRKAAGEpikegdNDYFTCITKAYEMLSDPVKRRAFNSvdptFDN 166
Cdd:PRK14298   5 RDYYEILGLSK---DASVEDIKKAYRKLAMKYHPDKNKEPDA------EEKFKEISEAYAVLSDAEKRAQYDR----FGH 71

                         90       100
                 ....*....|....*....|....*.
gi 74193946  167 S-VPSKSEAKDNF----FQVFSPVFE 187
Cdd:PRK14298  72 AgIDNQYSAEDIFrgadFGGFGDIFE 97
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 88-154 3.26e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 52.20  E-value: 3.26e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74193946   88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKaagepiKEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK14292   3 DYYELLG---VSRTASADEIKSAYRKLALKYHPDRNK------EKGAAEKFAQINEAYAVLSDAEKR 60
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 87-158 3.33e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 52.24  E-value: 3.33e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPD----KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14290   3 KDYYKILG---VDRNASQEDIKKAFRELAKKWHPDlhpgNKAEAEEKFKE--------ISEAYEVLSDPQKRRQYD 67
PRK14280 PRK14280
molecular chaperone DnaJ;
87-154 5.28e-08

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 51.65  E-value: 5.28e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946   87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKR 154
Cdd:PRK14280   4 RDYYEVLGVSK---SASKDEIKKAYRKLSKKYHPDINKEEGadEKFKE--------ISEAYEVLSDDQKR 62
PRK14289 PRK14289
molecular chaperone DnaJ;
87-158 2.73e-07

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 49.44  E-value: 2.73e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14289   5 RDYYEVLG---VSKTATVDEIKKAYRKKAIQYHPDKNpgdKEAEEKFKE--------AAEAYDVLSDPDKRSRYD 68
PRK10266 PRK10266
curved DNA-binding protein;
87-191 6.98e-07

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 48.28  E-value: 6.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKaagEPIKEGDndyFTCITKAYEMLSDPVKRRAFNSV-----D 161
Cdd:PRK10266   4 KDYYAIMG---VKPTDDLKTIKTAYRRLARKYHPDVSK---EPDAEAR---FKEVAEAWEVLSDEQRRAEYDQLwqhrnD 74

                         90       100       110
                 ....*....|....*....|....*....|...
gi 74193946  162 PTFD---NSVPSKSEAKDNFFQVFSPVFERNSR 191
Cdd:PRK10266  75 PQFNrqfQHGDGQSFNAEDFDDIFSSIFGQHAR 107
PRK14293 PRK14293
molecular chaperone DnaJ;
88-154 9.64e-07

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 48.06  E-value: 9.64e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74193946   88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKaagEPikeGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK14293   4 DYYEILG---VSRDADKDELKRAYRRLARKYHPDVNK---EP---GAEDRFKEINRAYEVLSDPETR 61
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 87-187 1.77e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 47.29  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946   87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFNSvdptFDN 166
Cdd:PRK14285   3 RDYYEILGLSK---GASKDEIKKAYRKIAIKYHPDKNKGNKEA-----ESIFKEATEAYEVLIDDNKRAQYDR----FGH 70

                         90       100
                 ....*....|....*....|....
gi 74193946  167 SVPSKSEAKDNF---FQVFSPVFE 187
Cdd:PRK14285  71 TAFEGGGGFEGFsggFSGFSDIFE 94
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
87-151 2.53e-06

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 43.63  E-value: 2.53e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74193946  87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDkRKAAGEPIKEGD--NDYFTCITKAYEMLSDP 151
Cdd:COG1076   4 DDAFELLGLPP---DADDAELKRAYRKLQREHHPD-RLAAGLPEEEQRlaLQKAAAINEAYETLKDP 66
PRK14288 PRK14288
molecular chaperone DnaJ;
89-187 4.39e-03

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 36.98  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74193946   89 HYAVLglgHVRYTATQRQIKAAHKAMVLKHHPDKRkaAGEpiKEGDnDYFTCITKAYEMLSDPVKRRAFNSVDPTFDNSV 168
Cdd:PRK14288   5 YYEIL---EVEKHSNQETIKKSYRKLALKYHPDRN--AGD--KEAE-EKFKLINEAYGVLSDEKKRALYDRYGKKGLNQA 76

                         90
                 ....*....|....*....
gi 74193946  169 PSKSEAKDNFFQVFSPVFE 187
Cdd:PRK14288  77 GASQSDFSDFFEDLGSFFE 95
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-47 5.59e-03

N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, also known as DnaJ-related protein ZUO1, J protein ZUO1, or heat shock protein 40 homolog ZUO1, is a component of the ribosome-associated complex (RAC), which is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. The RAC chaperone complex plays a role in regulating accurate translation termination and folding or maintaining nascent polypeptides in a folding-competent state. The ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain is stimulated by the RAC chaperone complex. ZUO1 acts as a J-protein for SSB1/SSB2 only when it is associated with SSZ1. The N-terminal domain (NTD) of ZUO1 is responsible for its interaction with SSZ1, and it contains a conserved LP-motif that binds to the SSZ1 C-terminal SBD (substrate binding domain) beta-lid domain in the same way as canonical Hsp70s bind to their substrates.


Pssm-ID: 467935  Cd Length: 38  Bit Score: 33.25  E-value: 5.59e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 74193946  13 TAITHALTSASSVCQVEPVGRWFEAFVKRRNRNAS 47
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRT 36
hscB PRK01356
co-chaperone HscB; Provisional
 87-154 6.44e-03

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 35.62  E-value: 6.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74193946   87 QDHYAVLGLGHVrYTATQRQIKAAHKAMVLKHHPDKRKAAGEpiKEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK01356   2 QNYFQLLGLPQE-YNIDLKILEKQYFAMQVKYHPDKAKTLQE--KEQNLIIASELNNAYSTLKDALKR 66
djlA PRK09430
co-chaperone DjlA;
87-148 6.91e-03

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 36.33  E-value: 6.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74193946   87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEP------IKEGDNDyftcITKAYEML 148
Cdd:PRK09430 200 EDAYKVLG---VSESDDDQEIKRAYRKLMSEHHPDKLVAKGLPpemmemAKEKAQE----IQAAYELI 260
 
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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