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Conserved domains on  [gi|41152151|ref|NP_957055|]
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mitochondrial import inner membrane translocase subunit TIM14 [Danio rerio]

Protein Classification

J domain-containing protein( domain architecture ID 84)

J domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ super family cl02542
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 5-109 1.03e-26

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.


The actual alignment was detected with superfamily member PTZ00100:

Pssm-ID: 413365  Cd Length: 116  Bit Score: 95.30  E-value: 1.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152151    5 MVAVGLTLAAAGFTGRYAVRAMKHMEPQVKQALEASKSAFGSGYYRG---GFDPKMNRREASLILGVSPTANKTKIREAH 81
Cdd:PTZ00100   7 ALTFGGGVLAVRYGYRYLKNQKIFGSNNMSFPLSGFNPSLGSLFLKNdlkGFENPMSKSEAYKILNISPTASKERIREAH 86

                         90       100
                 ....*....|....*....|....*...
gi 41152151   82 RKLMILNHPDRGGSPYLAAKINEAKDLL 109
Cdd:PTZ00100  87 KQLMLRNHPDNGGSTYIASKVNEAKDLL 114
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 5-109 1.03e-26

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 95.30  E-value: 1.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152151    5 MVAVGLTLAAAGFTGRYAVRAMKHMEPQVKQALEASKSAFGSGYYRG---GFDPKMNRREASLILGVSPTANKTKIREAH 81
Cdd:PTZ00100   7 ALTFGGGVLAVRYGYRYLKNQKIFGSNNMSFPLSGFNPSLGSLFLKNdlkGFENPMSKSEAYKILNISPTASKERIREAH 86

                         90       100
                 ....*....|....*....|....*...
gi 41152151   82 RKLMILNHPDRGGSPYLAAKINEAKDLL 109
Cdd:PTZ00100  87 KQLMLRNHPDNGGSTYIASKVNEAKDLL 114
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
65-109 1.33e-10

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 53.57  E-value: 1.33e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41152151  65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSP-----YLAAKINEAKDLL 109
Cdd:COG2214  10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkalaeELFQRLNEAYEVL 59
DnaJ smart00271
DnaJ molecular chaperone homology domain;
65-109 2.67e-10

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 51.85  E-value: 2.67e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 41152151     65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAA-----KINEAKDLL 109
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVL 55
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 65-110 5.46e-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: 51.01  E-value: 5.46e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41152151  65 ILGVSPTANKTKIREAHRKLMILNHPDRG----GSPYLAAKINEAKDLLD 110
Cdd:cd06257   5 ILGVPPDASDEEIKKAYRKLALKYHPDKNpddpEAEEKFKEINEAYEVLS 54
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 65-109 1.75e-07

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: 44.77  E-value: 1.75e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 41152151    65 ILGVSPTANKTKIREAHRKLMILNHPDR-GGSPYLAAK---INEAKDLL 109
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKfkeINEAYEVL 53
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 5-109 1.03e-26

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 95.30  E-value: 1.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152151    5 MVAVGLTLAAAGFTGRYAVRAMKHMEPQVKQALEASKSAFGSGYYRG---GFDPKMNRREASLILGVSPTANKTKIREAH 81
Cdd:PTZ00100   7 ALTFGGGVLAVRYGYRYLKNQKIFGSNNMSFPLSGFNPSLGSLFLKNdlkGFENPMSKSEAYKILNISPTASKERIREAH 86

                         90       100
                 ....*....|....*....|....*...
gi 41152151   82 RKLMILNHPDRGGSPYLAAKINEAKDLL 109
Cdd:PTZ00100  87 KQLMLRNHPDNGGSTYIASKVNEAKDLL 114
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
65-109 1.33e-10

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 53.57  E-value: 1.33e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41152151  65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSP-----YLAAKINEAKDLL 109
Cdd:COG2214  10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkalaeELFQRLNEAYEVL 59
DnaJ smart00271
DnaJ molecular chaperone homology domain;
65-109 2.67e-10

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 51.85  E-value: 2.67e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 41152151     65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAA-----KINEAKDLL 109
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVL 55
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 65-110 5.46e-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: 51.01  E-value: 5.46e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41152151  65 ILGVSPTANKTKIREAHRKLMILNHPDRG----GSPYLAAKINEAKDLLD 110
Cdd:cd06257   5 ILGVPPDASDEEIKKAYRKLALKYHPDKNpddpEAEEKFKEINEAYEVLS 54
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 65-109 1.75e-07

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: 44.77  E-value: 1.75e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 41152151    65 ILGVSPTANKTKIREAHRKLMILNHPDR-GGSPYLAAK---INEAKDLL 109
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKfkeINEAYEVL 53
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 65-109 2.13e-07

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: 46.23  E-value: 2.13e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 41152151  65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAA----KINEAKDLL 109
Cdd:COG0484   5 ILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEekfkEINEAYEVL 53
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 57-115 6.33e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 46.09  E-value: 6.33e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152151   57 MNRREASLILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAK---INEAKD-LLDGQAKK 115
Cdd:PRK14296   1 MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKmveINEAADvLLDKDKRK 63
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 51-115 2.09e-06

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 44.81  E-value: 2.09e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152151   51 GGFDPKMNRREAS-----LILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAKINEAKDLLDGQAKK 115
Cdd:PTZ00037  14 GGFDGGRRKREVDneklyEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEKFKEISRAYEVLSDPEKR 83
djlA PRK09430
co-chaperone DjlA;
36-101 6.08e-06

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 43.26  E-value: 6.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41152151   36 ALEASKSAFGSGYYRGGFDPKMNRRE---ASLILGVSPTANKTKIREAHRKLMILNHPDRggspyLAAK 101
Cdd:PRK09430 173 RMMQAGFRFQQQQGGGGYQQAQRGPTledAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK-----LVAK 236
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
57-109 1.46e-05

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 39.78  E-value: 1.46e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152151  57 MNRREASLILGVSPTANKTKIREAHRKLMILNHPDR---GGSPY-------LAAKINEAKDLL 109
Cdd:COG1076   1 MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaGLPEEeqrlalqKAAAINEAYETL 63
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 65-109 2.97e-05

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 38.83  E-value: 2.97e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 41152151  65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAA----KINEAKDLL 109
Cdd:COG5407   5 VLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEerfkEINEAYELL 53
PRK14279 PRK14279
molecular chaperone DnaJ;
66-115 6.22e-05

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 40.49  E-value: 6.22e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152151   66 LGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAA----KINEAKDLLDGQAKK 115
Cdd:PRK14279  15 LGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEerfkAVSEAHDVLSDPAKR 68
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 65-115 7.45e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 40.26  E-value: 7.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152151   65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLA---AKINEAKDLLDGQAKK 115
Cdd:PRK14292   7 LLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAekfAQINEAYAVLSDAEKR 60
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 65-112 9.67e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 39.74  E-value: 9.67e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152151   65 ILGVSPTANKTKIREAHRKLMILNHPDR-GGSPYLAAK---INEAKDLL-DGQ 112
Cdd:PRK10767   9 VLGVSRNASEDEIKKAYRKLAMKYHPDRnPGDKEAEEKfkeIKEAYEVLsDPQ 61
PRK14280 PRK14280
molecular chaperone DnaJ;
57-115 1.47e-04

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 39.32  E-value: 1.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41152151   57 MNRREASLILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAK---INEAKDLLDGQAKK 115
Cdd:PRK14280   1 MAKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKfkeISEAYEVLSDDQKR 62
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 65-115 1.98e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 39.06  E-value: 1.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152151   65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAK---INEAKDLLDGQAKK 115
Cdd:PRK14298  10 ILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKfkeISEAYAVLSDAEKR 63
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 57-107 2.29e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 38.82  E-value: 2.29e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 41152151   57 MNRREASLILGVSPTANKTKIREAHRKLMILNHPDRG-GSPYLAAKINEAKD 107
Cdd:PRK14286   1 MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNkGNKESEEKFKEATE 52
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 59-115 2.78e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 38.64  E-value: 2.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152151   59 RREASLILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLA----AKINEAKDLLDGQAKK 115
Cdd:PRK14281   2 KRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAeehfKEVNEAYEVLSNDDKR 62
PRK14295 PRK14295
molecular chaperone DnaJ;
65-115 3.05e-04

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 38.68  E-value: 3.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152151   65 ILGVSPTANKTKIREAHRKLMILNHPD-RGGSPYLAAK---INEAKDLLDGQAKK 115
Cdd:PRK14295  14 VLGVPKDATEAEIKKAYRKLAREYHPDaNKGDAKAEERfkeISEAYDVLSDEKKR 68
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 57-110 3.30e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 38.57  E-value: 3.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152151   57 MNRREASLILGVSPTANKTKIREAHRKLMILNHPDRG-GSPYLAAKINEAKDLLD 110
Cdd:PRK14301   1 MSQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNpDNPEAEQKFKEAAEAYE 55
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 57-115 6.19e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 37.76  E-value: 6.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41152151   57 MNRREASLILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAK---INEAKDLLDGQAKK 115
Cdd:PRK14276   1 MNNTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKykeVQEAYETLSDPQKR 62
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 57-115 6.20e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 37.50  E-value: 6.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41152151   57 MNRREASLILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAK---INEAKDLLDGQAKK 115
Cdd:PRK14283   2 AEKRDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKfkeISEAYAVLSDDEKR 63
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 57-110 8.01e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 37.30  E-value: 8.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152151   57 MNRREASLILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAKINEAKDLLD 110
Cdd:PRK14287   1 MSKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYD 54
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 59-115 8.24e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 37.28  E-value: 8.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152151   59 RREASLILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAKI----NEAKDLLDGQAKK 115
Cdd:PRK14285   2 KRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIfkeaTEAYEVLIDDNKR 62
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 65-115 1.51e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 36.67  E-value: 1.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152151   65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAK---INEAKDLLDGQAKK 115
Cdd:PRK14291   8 ILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKfkeINEAYQVLSDPEKR 61
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 57-92 2.07e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 36.28  E-value: 2.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 41152151   57 MNRREASLILGVSPTANKTKIREAHRKLMILNHPDR 92
Cdd:PRK14294   1 MVKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDR 36
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 65-115 2.97e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 35.76  E-value: 2.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41152151   65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAK---INEAKDLLDGQAKK 115
Cdd:PRK14300   8 ILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKfkeINAAYDVLKDEQKR 61
PRK14297 PRK14297
molecular chaperone DnaJ;
57-115 3.09e-03

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 35.53  E-value: 3.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152151   57 MNRREASLILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLA----AKINEAKDLLDGQAKK 115
Cdd:PRK14297   1 MASKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAeekfKEINEAYQVLSDPQKK 63
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 65-115 3.57e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 35.59  E-value: 3.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 41152151   65 ILGVSPTANKTKIREAHRKLMILNHPDRGGSPYLAAK----INEAKDLLDGQAKK 115
Cdd:PRK14284   6 ILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKrfkeVSEAYEVLSDAQKR 60
PHA02624 PHA02624
large T antigen; Provisional
 54-109 8.86e-03

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 34.57  E-value: 8.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152151   54 DPKMNRRE-ASLI--LGVSPTA--NKTKIREAHRKLMILNHPDRGGSPYLAAKINEAKDLL 109
Cdd:PHA02624   2 DKTLSREEsKELMdlLGLPMAAwgNLPLMRKAYLRKCKEYHPDKGGDEEKMKRLNSLYKKL 62
 
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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