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Conserved domains on  [gi|18677018|dbj|BAB85076|]
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unnamed protein product [Homo sapiens]

Protein Classification

J domain-containing protein( domain architecture ID 13425018)

J domain-containing protein similar to molecular chaperone DnaJ; DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 15-79 1.17e-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: 74.82  E-value: 1.17e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18677018    15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvgEGDKEDATRRFQILGKVYSVLSDREQRAVYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDK--NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
ZUO1 super family cl34965
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 11-229 4.59e-06

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: 46.95  E-value: 4.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018  11 FGTADLYRVLGV---RREASDGEVRRGYHKVSLQVHPDRVGEGDKEDATRRFQILGKVYSVLSDREQRAVYDeqgTVDED 87
Cdd:COG5269  40 WKKVDLYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEFFKLIQKAREVLGDRKLRLQYD---SNDFD 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018  88 S----PVLTQDRDWEAYWRLLFKKISLEDIQAFEKTYKGSEEELADIKQAY---LDFKG---------DMDQIMESVLCV 151
Cdd:COG5269 117 AdvppPRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYefwSNFDSwrtfepldeDYPDDMEERDRK 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018 152 QYTEEP--------------RIRNIIQQAIdaGEVPSYNAFVKESKQKMNARK---------RRAQEEAKEAEMSRKELG 208
Cdd:COG5269 197 RYSEAKnrekraklknqdnaRLKRLVQIAK--KRDPRIKSFKEQEKEMKKIRKwereagarlKALAALKGKAEAKNKAEI 274

                       250       260
                ....*....|....*....|.
gi 18677018 209 LDEGVDSLKAAIQSRQKDRQK 229
Cdd:COG5269 275 EAEALASATAVKKKAKEVMKK 295
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 15-79 1.17e-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: 74.82  E-value: 1.17e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18677018    15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvgEGDKEDATRRFQILGKVYSVLSDREQRAVYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDK--NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 13-94 2.38e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 71.80  E-value: 2.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018   13 TADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDatrRFQILGKVYSVLSDREQRAVYDEQGTVDEDSPVLT 92
Cdd:PRK14298   4 TRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEE---KFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSA 80


                 ..
gi 18677018   93 QD 94
Cdd:PRK14298  81 ED 82
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 15-71 3.33e-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: 65.26  E-value: 3.33e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18677018  15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVgeGDKEDATRRFQILGKVYSVLSD 71
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKN--PDDPEAEEKFKEINEAYEVLSD 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 15-137 6.48e-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: 67.03  E-value: 6.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018  15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvgEGDKEDATRRFQILGKVYSVLSDREQRAVYDEQGTVDEDSPvlTQD 94
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDR--NPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLL--ATE 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 18677018  95 RDWEAYWRLLFKKISLEDIQAFEKTYKGSEEELADIKQAYLDF 137
Cdd:COG0484  77 LAESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLL 119
DnaJ smart00271
DnaJ molecular chaperone homology domain;
15-74 7.34e-14

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 64.56  E-value: 7.34e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018     15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGeGDKEDATRRFQILGKVYSVLSDREQ 74
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNP-GDKEEAEEKFKEINEAYEVLSDPEK 60
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 11-229 4.59e-06

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 46.95  E-value: 4.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018  11 FGTADLYRVLGV---RREASDGEVRRGYHKVSLQVHPDRVGEGDKEDATRRFQILGKVYSVLSDREQRAVYDeqgTVDED 87
Cdd:COG5269  40 WKKVDLYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEFFKLIQKAREVLGDRKLRLQYD---SNDFD 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018  88 S----PVLTQDRDWEAYWRLLFKKISLEDIQAFEKTYKGSEEELADIKQAY---LDFKG---------DMDQIMESVLCV 151
Cdd:COG5269 117 AdvppPRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYefwSNFDSwrtfepldeDYPDDMEERDRK 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018 152 QYTEEP--------------RIRNIIQQAIdaGEVPSYNAFVKESKQKMNARK---------RRAQEEAKEAEMSRKELG 208
Cdd:COG5269 197 RYSEAKnrekraklknqdnaRLKRLVQIAK--KRDPRIKSFKEQEKEMKKIRKwereagarlKALAALKGKAEAKNKAEI 274

                       250       260
                ....*....|....*....|.
gi 18677018 209 LDEGVDSLKAAIQSRQKDRQK 229
Cdd:COG5269 275 EAEALASATAVKKKAKEVMKK 295
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 15-79 1.17e-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: 74.82  E-value: 1.17e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18677018    15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvgEGDKEDATRRFQILGKVYSVLSDREQRAVYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDK--NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 13-94 2.38e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 71.80  E-value: 2.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018   13 TADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDatrRFQILGKVYSVLSDREQRAVYDEQGTVDEDSPVLT 92
Cdd:PRK14298   4 TRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEE---KFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQYSA 80


                 ..
gi 18677018   93 QD 94
Cdd:PRK14298  81 ED 82
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 15-71 3.33e-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: 65.26  E-value: 3.33e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18677018  15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVgeGDKEDATRRFQILGKVYSVLSD 71
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKN--PDDPEAEEKFKEINEAYEVLSD 55
PRK14297 PRK14297
molecular chaperone DnaJ;
15-85 4.02e-14

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 70.97  E-value: 4.02e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvGEGDKEdATRRFQILGKVYSVLSDREQRAVYDEQGTVD 85
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDK-NKGNKE-AEEKFKEINEAYQVLSDPQKKAQYDQFGTAD 73
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 15-137 6.48e-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: 67.03  E-value: 6.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018  15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvgEGDKEDATRRFQILGKVYSVLSDREQRAVYDEQGTVDEDSPvlTQD 94
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDR--NPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLL--ATE 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 18677018  95 RDWEAYWRLLFKKISLEDIQAFEKTYKGSEEELADIKQAYLDF 137
Cdd:COG0484  77 LAESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLL 119
DnaJ smart00271
DnaJ molecular chaperone homology domain;
15-74 7.34e-14

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 64.56  E-value: 7.34e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018     15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGeGDKEDATRRFQILGKVYSVLSDREQ 74
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNP-GDKEEAEEKFKEINEAYEVLSDPEK 60
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 15-82 8.20e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 70.16  E-value: 8.20e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvgEGDKEDATRRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14301   5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDR--NPDNPEAEQKFKEAAEAYEVLRDAEKRARYDRFG 70
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
14-81 8.34e-14

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 65.12  E-value: 8.34e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18677018  14 ADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEgDKEDATRRFQILGKVYSVLSDREQRAVYDEQ 81
Cdd:COG2214   5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGE-LKALAEELFQRLNEAYEVLSDPERRAEYDRE 71
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 15-89 2.60e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 68.67  E-value: 2.60e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEgDKEDATRRFQILGKVYSVLSDREQRAVYDEQGTVDEDSP 89
Cdd:PRK14282   5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPE-NRKEAEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGEQPP 78
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 15-82 6.47e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 67.48  E-value: 6.47e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGeGDKEdATRRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNP-GDKE-AEEKFKEIKEAYEVLSDPQKRAAYDQYG 70
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 15-82 7.31e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 67.52  E-value: 7.31e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDrVGEGDKEdATRRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPD-LNPGDKE-AEQKFKEINEAYEILSDPQKRAQYDQFG 71
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 14-90 1.81e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 66.45  E-value: 1.81e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18677018   14 ADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEgdkEDATRRFQILGKVYSVLSDREQRAVYDEQGTVDEDSPV 90
Cdd:PRK14292   2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKE---KGAAEKFAQINEAYAVLSDAEKRAHYDRFGTAPGAGMP 75
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 15-82 2.20e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 65.94  E-value: 2.20e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvGEGDKEdATRRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14294   5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDR-NPGDKE-AEELFKEAAEAYEVLSDPKKRGIYDQYG 70
PRK14289 PRK14289
molecular chaperone DnaJ;
15-82 2.45e-12

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 66.01  E-value: 2.45e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvGEGDKEdATRRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDK-NPGDKE-AEEKFKEAAEAYDVLSDPDKRSRYDQFG 71
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 15-85 2.54e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 65.72  E-value: 2.54e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDrVGEGDKEDATRRFQILGKVYSVLSDREQRAVYDEQGTVD 85
Cdd:PRK14290   4 DYYKILGVDRNASQEDIKKAFRELAKKWHPD-LHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYDQTGTVD 73
PRK14280 PRK14280
molecular chaperone DnaJ;
15-85 4.78e-12

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 65.13  E-value: 4.78e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEgdkEDATRRFQILGKVYSVLSDREQRAVYDEQGTVD 85
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKE---EGADEKFKEISEAYEVLSDDQKRAQYDQFGHAG 72
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 15-113 5.06e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 64.85  E-value: 5.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDrvgEGDKEDATRRFQILGKVYSVLSDREQRAVYDEQGTVDEDSpvLTQD 94
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPD---VSEEEGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGMDG--FSQE 80

                         90
                 ....*....|....*....
gi 18677018   95 RdweaywrlLFKKISLEDI 113
Cdd:PRK14283  81 D--------IFNNINFEDI 91
PRK14293 PRK14293
molecular chaperone DnaJ;
14-82 5.55e-12

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 64.63  E-value: 5.55e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18677018   14 ADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDatrRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14293   3 ADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAED---RFKEINRAYEVLSDPETRARYDQFG 68
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 13-82 1.33e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 63.88  E-value: 1.33e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018   13 TADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEdatRRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14300   2 SQDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAE---KKFKEINAAYDVLKDEQKRAAYDRFG 68
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 15-85 2.23e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 63.18  E-value: 2.23e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDatrRFQILGKVYSVLSDREQRAVYDEQGTVD 85
Cdd:PRK14276   5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEE---KYKEVQEAYETLSDPQKRAAYDQYGAAG 72
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 15-79 2.48e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 62.76  E-value: 2.48e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDrvgEGDKEDATRRFQILGKVYSVLSDREQRAVYD 79
Cdd:PRK14278   4 DYYGLLGVSRNASDAEIKRAYRKLARELHPD---VNPDEEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14295 PRK14295
molecular chaperone DnaJ;
15-80 3.71e-11

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 62.56  E-value: 3.71e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDrVGEGDKEdATRRFQILGKVYSVLSDREQRAVYDE 80
Cdd:PRK14295  10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPD-ANKGDAK-AEERFKEISEAYDVLSDEKKRKEYDE 73
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 14-82 4.73e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 62.17  E-value: 4.73e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18677018   14 ADLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvGEGDKEdATRRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14284   1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDK-NPGDAE-AEKRFKEVSEAYEVLSDAQKRESYDRYG 67
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 15-82 1.21e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 60.98  E-value: 1.21e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvgEGDKEDATRRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDK--NPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQFG 69
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 17-82 5.22e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 58.85  E-value: 5.22e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18677018   17 YRVLGVRREASDGEVRRGYHKVSLQVHPDRvGEGDKEdATRRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDK-NKGNKE-SEEKFKEATEAYEILRDPKKRQAYDQFG 70
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 15-83 5.96e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 58.41  E-value: 5.96e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDatrRFQILGKVYSVLSDREQRAVYDEQGT 83
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEE---KFKEINEAYTVLSDPEKRRIYDTYGT 70
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 16-82 6.45e-10

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 58.68  E-value: 6.45e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18677018   16 LYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKedatrrFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PTZ00037  30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEK------FKEISRAYEVLSDPEKRKIYDEYG 90
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 15-76 7.54e-10

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 53.46  E-value: 7.54e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18677018  15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvGEGDKeDATRRFQILGKVYSVLSDREQRA 76
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDR-NKGDP-KAEERFKEINEAYELLSDAEKRA 60
PRK14279 PRK14279
molecular chaperone DnaJ;
15-80 9.89e-10

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 58.21  E-value: 9.89e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvGEGDKEdATRRFQILGKVYSVLSDREQRAVYDE 80
Cdd:PRK14279  10 DFYKELGVSSDASAEEIKKAYRKLARELHPDA-NPGDPA-AEERFKAVSEAHDVLSDPAKRKEYDE 73
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 15-113 3.48e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 56.70  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRvgeGDKEDATRRFQILGKVYSVLSDREQRAVYDEQGTvDEDSPVLTQD 94
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDF---NKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGH-AAFSGSGQQQ 79

                         90
                 ....*....|....*....
gi 18677018   95 RDWEAYWRLLFkkISLEDI 113
Cdd:PRK14291  80 QGQEGFSDFGG--GNIEDI 96
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 15-85 4.02e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 56.17  E-value: 4.02e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDatrRFQILGKVYSVLSDREQRAVYDEQGTVD 85
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAED---KFKEVKEAYDTLSDPQKKAHYDQFGHTD 72
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 15-82 5.92e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 52.64  E-value: 5.92e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDatrRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHD---KMVEINEAADVLLDKDKRKQYDQFG 69
PRK14288 PRK14288
molecular chaperone DnaJ;
17-82 7.36e-08

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 52.38  E-value: 7.36e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18677018   17 YRVLGVRREASDGEVRRGYHKVSLQVHPDRvGEGDKEdATRRFQILGKVYSVLSDREQRAVYDEQG 82
Cdd:PRK14288   6 YEILEVEKHSNQETIKKSYRKLALKYHPDR-NAGDKE-AEEKFKLINEAYGVLSDEKKRALYDRYG 69
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
11-72 9.18e-08

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 48.25  E-value: 9.18e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18677018  11 FGTADLYRVLGVRREASDGEVRRGYHKVSLQVHPDR----VGEGDKEDATRRFQILGKVYSVLSDR 72
Cdd:COG1076   1 MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaagLPEEEQRLALQKAAAINEAYETLKDP 66
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 11-229 4.59e-06

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 46.95  E-value: 4.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018  11 FGTADLYRVLGV---RREASDGEVRRGYHKVSLQVHPDRVGEGDKEDATRRFQILGKVYSVLSDREQRAVYDeqgTVDED 87
Cdd:COG5269  40 WKKVDLYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEFFKLIQKAREVLGDRKLRLQYD---SNDFD 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018  88 S----PVLTQDRDWEAYWRLLFKKISLEDIQAFEKTYKGSEEELADIKQAY---LDFKG---------DMDQIMESVLCV 151
Cdd:COG5269 117 AdvppPRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYefwSNFDSwrtfepldeDYPDDMEERDRK 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677018 152 QYTEEP--------------RIRNIIQQAIdaGEVPSYNAFVKESKQKMNARK---------RRAQEEAKEAEMSRKELG 208
Cdd:COG5269 197 RYSEAKnrekraklknqdnaRLKRLVQIAK--KRDPRIKSFKEQEKEMKKIRKwereagarlKALAALKGKAEAKNKAEI 274

                       250       260
                ....*....|....*....|.
gi 18677018 209 LDEGVDSLKAAIQSRQKDRQK 229
Cdd:COG5269 275 EAEALASATAVKKKAKEVMKK 295
PRK10266 PRK10266
curved DNA-binding protein;
15-80 4.85e-06

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 46.74  E-value: 4.85e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18677018   15 DLYRVLGVRREASDGEVRRGYHKVSLQVHPDRVGEGDKEDatrRFQILGKVYSVLSDREQRAVYDE 80
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEA---RFKEVAEAWEVLSDEQRRAEYDQ 67
djlA PRK09430
co-chaperone DjlA;
14-66 9.18e-04

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 39.80  E-value: 9.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18677018   14 ADLYRVLGVRREASDGEVRRGYHKVSLQVHPDR-VGEGDKED----ATRRFQILGKVY 66
Cdd:PRK09430 200 EDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDKlVAKGLPPEmmemAKEKAQEIQAAY 257
 
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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