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Conserved domains on  [gi|23956266|ref|NP_598842|]
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dnaJ homolog subfamily C member 9 [Mus musculus]

Protein Classification

J domain-containing protein( domain architecture ID 13425018)

J domain-containing protein similar to Homo sapiens DnaJ homolog subfamily C member 9 (DNAJC9) that acts as a dual histone chaperone and heat shock co-chaperone

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
SCOP:  4000605

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 1.41e-16

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: 71.74  E-value: 1.41e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956266    15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDqkEDATRRFQILGRVYAVLSDKEQKAVYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD--PEAEEKFKEINEAYEVLSDPEKRAIYD 63
ZUO1 super family cl34965
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
11-259 4.87e-03

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: 37.70  E-value: 4.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266  11 FGTADLYQVLGV---RREASDGEVRRGYHKVSLQVHPDRVEEDQKEDATRRFQILGRVYAVLSDKEQKAVYD---EQGTV 84
Cdd:COG5269  40 WKKVDLYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEFFKLIQKAREVLGDRKLRLQYDsndFDADV 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266  85 DEDSAGlnQDRDWDAYWRLLFKKISLEDIQAFEKTYKGSEEELNDIKQAY---LDFKG---------DMDQIMESVLCVQ 152
Cdd:COG5269 120 PPPRIY--TPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYefwSNFDSwrtfepldeDYPDDMEERDRKR 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266 153 YT--------------DEPRIRNIIQKAIesKEIPAYSAFVKESKQKMNARKRRAQEEAKEAELsrkelgleegvdnLKA 218
Cdd:COG5269 198 YSeaknrekraklknqDNARLKRLVQIAK--KRDPRIKSFKEQEKEMKKIRKWEREAGARLKAL-------------AAL 262
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23956266 219 LIQSRQKDRQKEMDSFLAQMeAKYCKPSKGGKRTALKKEKK 259
Cdd:COG5269 263 KGKAEAKNKAEIEAEALASA-TAVKKKAKEVMKKALKMEKK 302
 
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 1.41e-16

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: 71.74  E-value: 1.41e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956266    15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDqkEDATRRFQILGRVYAVLSDKEQKAVYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD--PEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14297 PRK14297
molecular chaperone DnaJ;
15-90 5.25e-14

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 70.97  E-value: 5.25e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQKedATRRFQILGRVYAVLSDKEQKAVYDEQGTVDEDSAG 90
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKE--AEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGAG 78
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
14-81 3.61e-13

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 63.58  E-value: 3.61e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956266  14 ADLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDqKEDATRRFQILGRVYAVLSDKEQKAVYDEQ 81
Cdd:COG2214   5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGEL-KALAEELFQRLNEAYEVLSDPERRAEYDRE 71
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
15-71 2.76e-12

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: 60.25  E-value: 2.76e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23956266  15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDqkEDATRRFQILGRVYAVLSD 71
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD--PEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
15-74 7.48e-12

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 59.17  E-value: 7.48e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266     15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRvEEDQKEDATRRFQILGRVYAVLSDKEQ 74
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDK-NPGDKEEAEEKFKEINEAYEVLSDPEK 60
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
11-259 4.87e-03

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 37.70  E-value: 4.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266  11 FGTADLYQVLGV---RREASDGEVRRGYHKVSLQVHPDRVEEDQKEDATRRFQILGRVYAVLSDKEQKAVYD---EQGTV 84
Cdd:COG5269  40 WKKVDLYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEFFKLIQKAREVLGDRKLRLQYDsndFDADV 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266  85 DEDSAGlnQDRDWDAYWRLLFKKISLEDIQAFEKTYKGSEEELNDIKQAY---LDFKG---------DMDQIMESVLCVQ 152
Cdd:COG5269 120 PPPRIY--TPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYefwSNFDSwrtfepldeDYPDDMEERDRKR 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266 153 YT--------------DEPRIRNIIQKAIesKEIPAYSAFVKESKQKMNARKRRAQEEAKEAELsrkelgleegvdnLKA 218
Cdd:COG5269 198 YSeaknrekraklknqDNARLKRLVQIAK--KRDPRIKSFKEQEKEMKKIRKWEREAGARLKAL-------------AAL 262
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23956266 219 LIQSRQKDRQKEMDSFLAQMeAKYCKPSKGGKRTALKKEKK 259
Cdd:COG5269 263 KGKAEAKNKAEIEAEALASA-TAVKKKAKEVMKKALKMEKK 302
 
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 1.41e-16

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: 71.74  E-value: 1.41e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956266    15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDqkEDATRRFQILGRVYAVLSDKEQKAVYD 79
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD--PEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14297 PRK14297
molecular chaperone DnaJ;
15-90 5.25e-14

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 70.97  E-value: 5.25e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQKedATRRFQILGRVYAVLSDKEQKAVYDEQGTVDEDSAG 90
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKE--AEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGAG 78
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
13-82 9.73e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 69.88  E-value: 9.73e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266   13 TADLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEdqkEDATRRFQILGRVYAVLSDKEQKAVYDEQG 82
Cdd:PRK14298   4 TRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE---PDAEEKFKEISEAYAVLSDAEKRAQYDRFG 70
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
15-86 1.08e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 69.82  E-value: 1.08e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQKEdATRRFQILGRVYAVLSDKEQKAVYDEQGTVDE 86
Cdd:PRK14282   5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKE-AEQKFKEIQEAYEVLSDPQKRAMYDRFGYVGE 75
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
15-92 1.12e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 69.77  E-value: 1.12e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQkeDATRRFQILGRVYAVLSDKEQKAVYDEQGtvdedSAGLN 92
Cdd:PRK14301   5 DYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNP--EAEQKFKEAAEAYEVLRDAEKRARYDRFG-----HAGVN 75
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
15-113 2.51e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 68.70  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEdqkEDATRRFQILGRVYAVLSDKEQKAVYDEQGTVDEDsaGLNQD 94
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE---EGAEEKFKEISEAYAVLSDDEKRQRYDQFGHAGMD--GFSQE 80
                         90
                 ....*....|....*....
gi 23956266   95 RdwdaywrlLFKKISLEDI 113
Cdd:PRK14283  81 D--------IFNNINFEDI 91
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
14-81 3.61e-13

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 63.58  E-value: 3.61e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956266  14 ADLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDqKEDATRRFQILGRVYAVLSDKEQKAVYDEQ 81
Cdd:COG2214   5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGEL-KALAEELFQRLNEAYEVLSDPERRAEYDRE 71
PRK14293 PRK14293
molecular chaperone DnaJ;
14-92 6.38e-13

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 67.71  E-value: 6.38e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956266   14 ADLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQKEDatrRFQILGRVYAVLSDKEQKAVYDEQGtvdedSAGLN 92
Cdd:PRK14293   3 ADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAED---RFKEINRAYEVLSDPETRARYDQFG-----EAGVS 73
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
15-82 7.22e-13

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: 64.34  E-value: 7.22e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956266  15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDqkEDATRRFQILGRVYAVLSDKEQKAVYDEQG 82
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD--PEAEEKFKEINEAYEVLSDPEKRAAYDRFG 66
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
14-83 1.31e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 66.84  E-value: 1.31e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266   14 ADLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEdqkEDATRRFQILGRVYAVLSDKEQKAVYDEQGT 83
Cdd:PRK14292   2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKE---KGAAEKFAQINEAYAVLSDAEKRAHYDRFGT 68
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
15-100 1.39e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 66.49  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDrVEEDQKEDATRRFQILGRVYAVLSDKEQKAVYDEQGTVDEDSAGlnQD 94
Cdd:PRK14290   4 DYYKILGVDRNASQEDIKKAFRELAKKWHPD-LHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYDQTGTVDFGAGG--SN 80

                 ....*.
gi 23956266   95 RDWDAY 100
Cdd:PRK14290  81 FNWDNF 86
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
15-71 2.76e-12

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: 60.25  E-value: 2.76e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23956266  15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDqkEDATRRFQILGRVYAVLSD 71
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD--PEAEEKFKEINEAYEVLSD 55
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
15-90 5.45e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 64.69  E-value: 5.45e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDrVEEDqkEDATRRFQILGRVYAVLSDKEQKAVYDEQGTVDEDSAG 90
Cdd:PRK14278   4 DYYGLLGVSRNASDAEIKRAYRKLARELHPD-VNPD--EEAQEKFKEISVAYEVLSDPEKRRIVDLGGDPLESAGG 76
PRK14280 PRK14280
molecular chaperone DnaJ;
15-85 7.18e-12

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 64.36  E-value: 7.18e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRveeDQKEDATRRFQILGRVYAVLSDKEQKAVYDEQGTVD 85
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDI---NKEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAG 72
DnaJ smart00271
DnaJ molecular chaperone homology domain;
15-74 7.48e-12

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 59.17  E-value: 7.48e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266     15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRvEEDQKEDATRRFQILGRVYAVLSDKEQ 74
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDK-NPGDKEEAEEKFKEINEAYEVLSDPEK 60
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
15-82 1.37e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 63.62  E-value: 1.37e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDqkEDATRRFQILGRVYAVLSDKEQKAVYDEQG 82
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD--KEAEEKFKEIKEAYEVLSDPQKRAAYDQYG 70
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
15-93 2.06e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 63.18  E-value: 2.06e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEdqkEDATRRFQILGRVYAVLSDKEQKAVYDEQGtvdedSAGLNQ 93
Cdd:PRK14276   5 EYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKE---PGAEEKYKEVQEAYETLSDPQKRAAYDQYG-----AAGANG 75
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
15-93 3.83e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 62.51  E-value: 3.83e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDrVEEDQKEdATRRFQILGRVYAVLSDKEQKAVYDEQGTVDEDSAGLNQ 93
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPD-LNPGDKE-AEQKFKEINEAYEILSDPQKRAQYDQFGHAAFDPGGFGQ 82
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
13-82 1.05e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 61.18  E-value: 1.05e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266   13 TADLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEedqKEDATRRFQILGRVYAVLSDKEQKAVYDEQG 82
Cdd:PRK14300   2 SQDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTD---AKDAEKKFKEINAAYDVLKDEQKRAAYDRFG 68
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
15-98 1.23e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 60.93  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQkeDATRRFQILGRVYAVLSDKEQKAVYDEQGTVDEDSAGLNQD 94
Cdd:PRK14294   5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDK--EAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGTGFSGF 82

                 ....
gi 23956266   95 RDWD 98
Cdd:PRK14294  83 SGFD 86
PRK14289 PRK14289
molecular chaperone DnaJ;
15-82 2.20e-10

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 60.23  E-value: 2.20e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQkeDATRRFQILGRVYAVLSDKEQKAVYDEQG 82
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDK--EAEEKFKEAAEAYDVLSDPDKRSRYDQFG 71
PRK14295 PRK14295
molecular chaperone DnaJ;
15-80 2.35e-10

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 59.86  E-value: 2.35e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQKedATRRFQILGRVYAVLSDKEQKAVYDE 80
Cdd:PRK14295  10 DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAK--AEERFKEISEAYDVLSDEKKRKEYDE 73
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
14-82 4.26e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 59.09  E-value: 4.26e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956266   14 ADLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQkeDATRRFQILGRVYAVLSDKEQKAVYDEQG 82
Cdd:PRK14284   1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDA--EAEKRFKEVSEAYEVLSDAQKRESYDRYG 67
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
15-83 5.67e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 58.41  E-value: 5.67e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQKEDatrRFQILGRVYAVLSDKEQKAVYDEQGT 83
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEE---KFKEINEAYTVLSDPEKRRIYDTYGT 70
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
15-82 1.05e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 58.28  E-value: 1.05e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQkeDATRRFQILGRVYAVLSDKEQKAVYDEQG 82
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNK--EAEEHFKEVNEAYEVLSNDDKRRRYDQFG 69
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
15-85 1.46e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 57.71  E-value: 1.46e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDrveEDQKEDATRRFQILGRVYAVLSDKEQKAVYDEQGTVD 85
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPD---VNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTD 72
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
15-113 3.50e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 56.32  E-value: 3.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRveeDQKEDATRRFQILGRVYAVLSDKEQKAVYDEQGTvDEDSAGLNQD 94
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDF---NKNPEAEEKFKEINEAYQVLSDPEKRKLYDQFGH-AAFSGSGQQQ 79
                         90
                 ....*....|....*....
gi 23956266   95 RDWDAYWRLLFkkISLEDI 113
Cdd:PRK14291  80 QGQEGFSDFGG--GNIEDI 96
PRK14279 PRK14279
molecular chaperone DnaJ;
15-80 3.80e-09

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 56.28  E-value: 3.80e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQKedATRRFQILGRVYAVLSDKEQKAVYDE 80
Cdd:PRK14279  10 DFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPA--AEERFKAVSEAHDVLSDPAKRKEYDE 73
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
15-76 1.83e-08

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 50.00  E-value: 1.83e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956266  15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQKedATRRFQILGRVYAVLSDKEQKA 76
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPK--AEERFKEINEAYELLSDAEKRA 60
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
16-82 1.96e-08

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 54.44  E-value: 1.96e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956266   16 LYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQKedatrrFQILGRVYAVLSDKEQKAVYDEQG 82
Cdd:PTZ00037  30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEK------FKEISRAYEVLSDPEKRKIYDEYG 90
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
17-92 3.01e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 53.84  E-value: 3.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956266   17 YQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQkeDATRRFQILGRVYAVLSDKEQKAVYDEQGtvdedSAGLN 92
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNK--ESEEKFKEATEAYEILRDPKKRQAYDQFG-----KAGVN 75
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
11-71 3.57e-08

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 49.41  E-value: 3.57e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956266  11 FGTADLYQVLGVRREASDGEVRRGYHKVSLQVHPDR----VEEDQKEDATRRFQILGRVYAVLSD 71
Cdd:COG1076   1 MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaagLPEEEQRLALQKAAAINEAYETLKD 65
PRK14288 PRK14288
molecular chaperone DnaJ;
17-135 1.46e-07

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 51.61  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266   17 YQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEDQkeDATRRFQILGRVYAVLSDKEQKAVYDEQGTVDEDSAGLNQDRD 96
Cdd:PRK14288   6 YEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDK--EAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGASQSDF 83
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 23956266   97 WDaywrlLFKKISLEDIQAFEKTYKGSEEELNDIKQAYL 135
Cdd:PRK14288  84 SD-----FFEDLGSFFEDAFGFGARGSKRQKSSIAPDYL 117
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
15-82 2.47e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 51.10  E-value: 2.47e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRveeDQKEDATRRFQILGRVYAVLSDKEQKAVYDEQG 82
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDL---NKSPDAHDKMVEINEAADVLLDKDKRKQYDQFG 69
PRK10266 PRK10266
curved DNA-binding protein;
15-80 2.89e-05

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 44.43  E-value: 2.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956266   15 DLYQVLGVRREASDGEVRRGYHKVSLQVHPDRVEEdqkEDATRRFQILGRVYAVLSDKEQKAVYDE 80
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKE---PDAEARFKEVAEAWEVLSDEQRRAEYDQ 67
djlA PRK09430
co-chaperone DjlA;
14-45 3.09e-03

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 38.25  E-value: 3.09e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 23956266   14 ADLYQVLGVRREASDGEVRRGYHKVSLQVHPD 45
Cdd:PRK09430 200 EDAYKVLGVSESDDDQEIKRAYRKLMSEHHPD 231
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
11-259 4.87e-03

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 37.70  E-value: 4.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266  11 FGTADLYQVLGV---RREASDGEVRRGYHKVSLQVHPDRVEEDQKEDATRRFQILGRVYAVLSDKEQKAVYD---EQGTV 84
Cdd:COG5269  40 WKKVDLYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEFFKLIQKAREVLGDRKLRLQYDsndFDADV 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266  85 DEDSAGlnQDRDWDAYWRLLFKKISLEDIQAFEKTYKGSEEELNDIKQAY---LDFKG---------DMDQIMESVLCVQ 152
Cdd:COG5269 120 PPPRIY--TPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYefwSNFDSwrtfepldeDYPDDMEERDRKR 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956266 153 YT--------------DEPRIRNIIQKAIesKEIPAYSAFVKESKQKMNARKRRAQEEAKEAELsrkelgleegvdnLKA 218
Cdd:COG5269 198 YSeaknrekraklknqDNARLKRLVQIAK--KRDPRIKSFKEQEKEMKKIRKWEREAGARLKAL-------------AAL 262
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23956266 219 LIQSRQKDRQKEMDSFLAQMeAKYCKPSKGGKRTALKKEKK 259
Cdd:COG5269 263 KGKAEAKNKAEIEAEALASA-TAVKKKAKEVMKKALKMEKK 302
 
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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