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Conserved domains on  [gi|6321724|ref|NP_011801|]
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zuotin [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 50-433 9.05e-169

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


:

Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 478.37  E-value: 9.05e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724   50 SEFERIEAEKNVKtvdeSNVDPDELLFDTELADEDLLTHDARDWKTADLYAAMGLSKLRFRATESQIIKAHRKQVVKYHP 129
Cdd:COG5269   1 MPNWIIKFEKPVG----ELARIHSEYFKGRNVLNLYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724  130 DKQsAAGGSLDQDGFFKIIQKAFETLTDSNKRAQYDSCDFVADVPPPKKGTDYDFYEAWGPVFEAEARFSKKTPIPSLGN 209
Cdd:COG5269  77 DKT-AAGGNKGCDEFFKLIQKAREVLGDRKLRLQYDSNDFDADVPPPRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724  210 KDSSKKEVEQFYAFWHRFDSWRTFEFLDEDVPDDSSNRDHKRYIERKNKAARDKKKTADNARLVKLVERAVSEDPRIKMF 289
Cdd:COG5269 156 SDSSLKEVEEFYEFWSNFDSWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSF 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724  290 KEEEKKEKERRKWEREAGARAEAEAKAKAEAEAKAKAESEAKANASAKADKKKAKEAAKAAKKKNKRAIRNSAKEADYFG 369
Cdd:COG5269 236 KEQEKEMKKIRKWEREAGARLKALAALKGKAEAKNKAEIEAEALASATAVKKKAKEVMKKALKMEKKAIKNAAKDADYFG 315

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321724  370 DADKATTIDEQVGLIVDSLNDEELVSTADKIKANAAGAKEVLKESAKTIVDSGKLPSSLLSYFV 433
Cdd:COG5269 316 DADKAEHIDEDVDLIMDKLGDEELGQLAADIKAEAAGAAAVFDEFAKMFIDRGKLPSADLSFFA 379
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 14-50 3.32e-10

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: 54.82  E-value: 3.32e-10
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6321724   14 EVNSSATKTPFVRRPVEPVGKFFLQHAQRTLRNHTWS 50
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRTFS 38
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 50-433 9.05e-169

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 478.37  E-value: 9.05e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724   50 SEFERIEAEKNVKtvdeSNVDPDELLFDTELADEDLLTHDARDWKTADLYAAMGLSKLRFRATESQIIKAHRKQVVKYHP 129
Cdd:COG5269   1 MPNWIIKFEKPVG----ELARIHSEYFKGRNVLNLYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724  130 DKQsAAGGSLDQDGFFKIIQKAFETLTDSNKRAQYDSCDFVADVPPPKKGTDYDFYEAWGPVFEAEARFSKKTPIPSLGN 209
Cdd:COG5269  77 DKT-AAGGNKGCDEFFKLIQKAREVLGDRKLRLQYDSNDFDADVPPPRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724  210 KDSSKKEVEQFYAFWHRFDSWRTFEFLDEDVPDDSSNRDHKRYIERKNKAARDKKKTADNARLVKLVERAVSEDPRIKMF 289
Cdd:COG5269 156 SDSSLKEVEEFYEFWSNFDSWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSF 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724  290 KEEEKKEKERRKWEREAGARAEAEAKAKAEAEAKAKAESEAKANASAKADKKKAKEAAKAAKKKNKRAIRNSAKEADYFG 369
Cdd:COG5269 236 KEQEKEMKKIRKWEREAGARLKALAALKGKAEAKNKAEIEAEALASATAVKKKAKEVMKKALKMEKKAIKNAAKDADYFG 315

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321724  370 DADKATTIDEQVGLIVDSLNDEELVSTADKIKANAAGAKEVLKESAKTIVDSGKLPSSLLSYFV 433
Cdd:COG5269 316 DADKAEHIDEDVDLIMDKLGDEELGQLAADIKAEAAGAAAVFDEFAKMFIDRGKLPSADLSFFA 379
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 97-165 1.61e-15

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: 1.61e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724     97 DLYAAMGLSKLrfrATESQIIKAHRKQVVKYHPDKqsaAGGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:pfam00226   1 DYYEILGVSPD---ASDEEIKKAYRKLALKYHPDK---NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14280 PRK14280
molecular chaperone DnaJ;
97-165 1.28e-11

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 65.90  E-value: 1.28e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGsldqDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14280   5 DYYEVLGVSK---SASKDEIKKAYRKLSKKYHPDINKEEGA----DEKFKEISEAYEVLSDDQKRAQYD 66
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 97-157 1.05e-10

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: 56.78  E-value: 1.05e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321724   97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGSLDQdgfFKIIQKAFETLTD 157
Cdd:cd06257   1 DYYDILGVPP---DASDEEIKKAYRKLALKYHPDKNPDDPEAEEK---FKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
97-160 1.51e-10

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 56.47  E-value: 1.51e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321724      97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKqsAAGGSLDQDGFFKIIQKAFETLTDSNK 160
Cdd:smart00271   2 DYYEILGVPR---DASLDEIKKAYRKLALKYHPDK--NPGDKEEAEEKFKEINEAYEVLSDPEK 60
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 14-50 3.32e-10

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: 54.82  E-value: 3.32e-10
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6321724   14 EVNSSATKTPFVRRPVEPVGKFFLQHAQRTLRNHTWS 50
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRTFS 38
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 50-433 9.05e-169

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 478.37  E-value: 9.05e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724   50 SEFERIEAEKNVKtvdeSNVDPDELLFDTELADEDLLTHDARDWKTADLYAAMGLSKLRFRATESQIIKAHRKQVVKYHP 129
Cdd:COG5269   1 MPNWIIKFEKPVG----ELARIHSEYFKGRNVLNLYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724  130 DKQsAAGGSLDQDGFFKIIQKAFETLTDSNKRAQYDSCDFVADVPPPKKGTDYDFYEAWGPVFEAEARFSKKTPIPSLGN 209
Cdd:COG5269  77 DKT-AAGGNKGCDEFFKLIQKAREVLGDRKLRLQYDSNDFDADVPPPRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGP 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724  210 KDSSKKEVEQFYAFWHRFDSWRTFEFLDEDVPDDSSNRDHKRYIERKNKAARDKKKTADNARLVKLVERAVSEDPRIKMF 289
Cdd:COG5269 156 SDSSLKEVEEFYEFWSNFDSWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSF 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724  290 KEEEKKEKERRKWEREAGARAEAEAKAKAEAEAKAKAESEAKANASAKADKKKAKEAAKAAKKKNKRAIRNSAKEADYFG 369
Cdd:COG5269 236 KEQEKEMKKIRKWEREAGARLKALAALKGKAEAKNKAEIEAEALASATAVKKKAKEVMKKALKMEKKAIKNAAKDADYFG 315

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321724  370 DADKATTIDEQVGLIVDSLNDEELVSTADKIKANAAGAKEVLKESAKTIVDSGKLPSSLLSYFV 433
Cdd:COG5269 316 DADKAEHIDEDVDLIMDKLGDEELGQLAADIKAEAAGAAAVFDEFAKMFIDRGKLPSADLSFFA 379
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 97-165 1.61e-15

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: 1.61e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724     97 DLYAAMGLSKLrfrATESQIIKAHRKQVVKYHPDKqsaAGGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:pfam00226   1 DYYEILGVSPD---ASDEEIKKAYRKLALKYHPDK---NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14280 PRK14280
molecular chaperone DnaJ;
97-165 1.28e-11

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 65.90  E-value: 1.28e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGsldqDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14280   5 DYYEVLGVSK---SASKDEIKKAYRKLSKKYHPDINKEEGA----DEKFKEISEAYEVLSDDQKRAQYD 66
RAC_head pfam16717
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
 352-425 1.58e-11

Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.


Pssm-ID: 435537  Cd Length: 87  Bit Score: 59.97  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724    352 KKNKRAIRNSAKEADYF--GDADKATTID---EQVGLIVDSLNDEELVSTADKIKA--NAAGAKEVLKESAKTIVDSGKL 424
Cdd:pfam16717   7 KKNKRVLRGSVKDANYFadGEAEKAAVIDgvlADVDLLCEKLDDEELAELAEKLEGakDAEAVKAVFEEEVKELVDAGKL 86


                  .
gi 6321724    425 P 425
Cdd:pfam16717  87 K 87
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 97-165 2.54e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 64.72  E-value: 2.54e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGsldqDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14276   5 EYYDRLGVSK---DASQDEIKKAYRKLSKKYHPDINKEPGA----EEKYKEVQEAYETLSDPQKRAAYD 66
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 97-165 3.04e-11

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: 60.87  E-value: 3.04e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724   97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGSLDQdgfFKIIQKAFETLTDSNKRAQYD 165
Cdd:COG0484   1 DYYEILGVSR---DASAEEIKKAYRKLAKKYHPDRNPGDPEAEEK---FKEINEAYEVLSDPEKRAAYD 63
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 97-193 5.80e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 63.66  E-value: 5.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGSLDQDgfFKIIQKAFETLTDSNKRAQYDSCDFVADVPPp 176
Cdd:PRK14282   5 DYYEILGVSR---NATQEEIKRAYKRLVKEWHPDRHPENRKEAEQK--FKEIQEAYEVLSDPQKRAMYDRFGYVGEQPP- 78

                         90
                 ....*....|....*..
gi 6321724   177 kkgtdYDFYEAWGPVFE 193
Cdd:PRK14282  79 -----YQETESGGGFFE 90
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 97-165 8.71e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 63.24  E-value: 8.71e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSaagGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK10767   5 DYYEVLGVSR---NASEDEIKKAYRKLAMKYHPDRNP---GDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 97-157 1.05e-10

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: 56.78  E-value: 1.05e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321724   97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGSLDQdgfFKIIQKAFETLTD 157
Cdd:cd06257   1 DYYDILGVPP---DASDEEIKKAYRKLALKYHPDKNPDDPEAEEK---FKEINEAYEVLSD 55
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 95-165 1.07e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 62.94  E-value: 1.07e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321724    95 TADLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGsldqDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14298   4 TRDYYEILGLSK---DASVEDIKKAYRKLAMKYHPDKNKEPDA----EEKFKEISEAYAVLSDAEKRAQYD 67
DnaJ smart00271
DnaJ molecular chaperone homology domain;
97-160 1.51e-10

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 56.47  E-value: 1.51e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321724      97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKqsAAGGSLDQDGFFKIIQKAFETLTDSNK 160
Cdd:smart00271   2 DYYEILGVPR---DASLDEIKKAYRKLALKYHPDK--NPGDKEEAEEKFKEINEAYEVLSDPEK 60
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 14-50 3.32e-10

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: 54.82  E-value: 3.32e-10
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6321724   14 EVNSSATKTPFVRRPVEPVGKFFLQHAQRTLRNHTWS 50
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRTFS 38
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 97-165 3.81e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 61.16  E-value: 3.81e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSaagGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14285   4 DYYEILGLSK---GASKDEIKKAYRKIAIKYHPDKNK---GNKEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14297 PRK14297
molecular chaperone DnaJ;
97-169 8.37e-10

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 60.18  E-value: 8.37e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSaagGSLDQDGFFKIIQKAFETLTDSNKRAQYD---SCDF 169
Cdd:PRK14297   5 DYYEVLGLEK---GASDDEIKKAFRKLAIKYHPDKNK---GNKEAEEKFKEINEAYQVLSDPQKKAQYDqfgTADF 74
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 96-165 1.26e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 59.86  E-value: 1.26e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724    96 ADLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSaagGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14284   1 MDYYTILGVSK---TASPEEIKKAYRKLAVKYHPDKNP---GDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 97-165 1.66e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 59.43  E-value: 1.66e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDkqsAAGGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14277   6 DYYEILGVDR---NATEEEIKKAYRRLAKKYHPD---LNPGDKEAEQKFKEINEAYEILSDPQKRAQYD 68
PRK14289 PRK14289
molecular chaperone DnaJ;
97-165 2.73e-09

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 58.69  E-value: 2.73e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSaagGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14289   6 DYYEVLGVSK---TATVDEIKKAYRKKAIQYHPDKNP---GDKEAEEKFKEAAEAYDVLSDPDKRSRYD 68
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 76-165 2.88e-09

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 58.68  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724    76 FDTELADEDLLTHDARDWKTADLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKqsaaGGslDQDGfFKIIQKAFETL 155
Cdd:PTZ00037   8 FDGMPGGGFDGGRRKREVDNEKLYEVLNLSK---DCTTSEIKKAYRKLAIKHHPDK----GG--DPEK-FKEISRAYEVL 77

                         90
                 ....*....|
gi 6321724   156 TDSNKRAQYD 165
Cdd:PTZ00037  78 SDPEKRKIYD 87
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 97-165 2.89e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 55.58  E-value: 2.89e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSaagGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14281   4 DYYEVLGVSR---SADKDEIKKAYRKLALKYHPDKNP---DNKEAEEHFKEVNEAYEVLSNDDKRRRYD 66
PRK14295 PRK14295
molecular chaperone DnaJ;
90-165 4.65e-08

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 54.85  E-value: 4.65e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321724    90 ARDWKTADLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGSLDQdgfFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14295   3 TKDYIEKDYYKVLGVPK---DATEAEIKKAYRKLAREYHPDANKGDAKAEER---FKEISEAYDVLSDEKKRKEYD 72
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
96-165 9.72e-08

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 49.33  E-value: 9.72e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321724   96 ADLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKqsaaGGSLDQDG--FFKIIQKAFETLTDSNKRAQYD 165
Cdd:COG2214   5 KDHYAVLGVPP---DASLEEIRQAYRRLAKLLHPDR----GGELKALAeeLFQRLNEAYEVLSDPERRAEYD 69
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 96-165 6.79e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 51.04  E-value: 6.79e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724    96 ADLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGSLDqdgfFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14292   2 MDYYELLGVSR---TASADEIKSAYRKLALKYHPDRNKEKGAAEK----FAQINEAYAVLSDAEKRAHYD 64
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 99-165 1.03e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 50.37  E-value: 1.03e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321724    99 YAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSaagGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14286   7 YDILGVSK---SANDEEIKSAYRKLAIKYHPDKNK---GNKESEEKFKEATEAYEILRDPKKRQAYD 67
PRK14293 PRK14293
molecular chaperone DnaJ;
96-165 1.04e-06

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 50.37  E-value: 1.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724    96 ADLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGSlDQdgfFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14293   3 ADYYEILGVSR---DADKDELKRAYRRLARKYHPDVNKEPGAE-DR---FKEINRAYEVLSDPETRARYD 65
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 97-165 1.25e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 50.13  E-value: 1.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSaagGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14301   5 DYYEVLGVSR---DASEDEIKKAYRKLALQYHPDRNP---DNPEAEQKFKEAAEAYEVLRDAEKRARYD 67
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 95-165 1.94e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 49.63  E-value: 1.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321724    95 TADLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAggslDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14300   2 SQDYYQILGVSK---TASQADLKKAYLKLAKQYHPDTTDAK----DAEKKFKEINAAYDVLKDEQKRAAYD 65
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 97-165 2.39e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 49.38  E-value: 2.39e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSaagGSLDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14294   5 DYYEILGVTR---DASEEEIKKSYRKLAMKYHPDRNP---GDKEAEELFKEAAEAYEVLSDPKKRGIYD 67
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 97-165 2.95e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 49.05  E-value: 2.95e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGSLDqdgfFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14283   6 DYYEVLGVDR---NADKKEIKKAYRKLARKYHPDVSEEEGAEEK----FKEISEAYAVLSDDEKRQRYD 67
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 97-171 4.06e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 48.77  E-value: 4.06e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSaaGGSLDQDGFFKIIQKAFETLTDSNKRAQYD---SCDFVA 171
Cdd:PRK14290   4 DYYKILGVDR---NASQEDIKKAFRELAKKWHPDLHP--GNKAEAEEKFKEISEAYEVLSDPQKRRQYDqtgTVDFGA 76
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 94-165 4.23e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 48.40  E-value: 4.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321724    94 KTADLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPDKQSAAGGsldqDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14296   2 KKKDYYEVLGVSK---TASEQEIRQAYRKLAKQYHPDLNKSPDA----HDKMVEINEAADVLLDKDKRKQYD 66
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 97-165 4.37e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 48.61  E-value: 4.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321724    97 DLYAAMGLSKlrfRATESQIIKAHRKQVVKYHPD--KQSAAggsldqDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK14291   4 DYYEILGVSR---NATQEEIKKAYRRLARKYHPDfnKNPEA------EEKFKEINEAYQVLSDPEKRKLYD 65
PRK10266 PRK10266
curved DNA-binding protein;
97-165 3.34e-05

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 45.58  E-value: 3.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724    97 DLYAAMGLSKlrfrATESQIIK-AHRKQVVKYHPDKQSAAggslDQDGFFKIIQKAFETLTDSNKRAQYD 165
Cdd:PRK10266   5 DYYAIMGVKP----TDDLKTIKtAYRRLARKYHPDVSKEP----DAEARFKEVAEAWEVLSDEQRRAEYD 66
PRK14288 PRK14288
molecular chaperone DnaJ;
111-201 9.32e-05

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 44.29  E-value: 9.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321724   111 ATESQIIKAHRKQVVKYHPDKQSaagGSLDQDGFFKIIQKAFETLTDSNKRAQYDSCDFVADVPPPKKGTDY-DFYEAWG 189
Cdd:PRK14288  15 SNQETIKKSYRKLALKYHPDRNA---GDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGASQSDFsDFFEDLG 91

                         90
                 ....*....|..
gi 6321724   190 PVFEAEARFSKK 201
Cdd:PRK14288  92 SFFEDAFGFGAR 103
 
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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