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Conserved domains on  [gi|21687102|ref|NP_660304|]
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mitochondrial import inner membrane translocase subunit TIM14 isoform 1 [Homo sapiens]

Protein Classification

J domain-containing protein( domain architecture ID 84)

J domain-containing protein similar to molecular chaperone DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
PubMed:  35729039|9644977|8016869|15170475
SCOP:  4000605

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 ...
 53-110 1.61e-27

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: 97.61  E-value: 1.61e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21687102   53 GFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKDLL 110
Cdd:PTZ00100  57 GFENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNGGSTYIASKVNEAKDLL 114
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 53-110 1.61e-27

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 97.61  E-value: 1.61e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21687102   53 GFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKDLL 110
Cdd:PTZ00100  57 GFENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNGGSTYIASKVNEAKDLL 114
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
66-110 1.10e-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: 1.10e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21687102  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAA-----KINEAKDLL 110
Cdd:COG2214  10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAeelfqRLNEAYEVL 59
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-111 7.04e-10

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 50.70  E-value: 7.04e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 21687102     66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAA-----KINEAKDLLE 111
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVLS 56
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-110 2.47e-09

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: 49.08  E-value: 2.47e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21687102  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIA----AKINEAKDLL 110
Cdd:cd06257   5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAeekfKEINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-110 7.65e-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: 42.85  E-value: 7.65e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 21687102    66 ILGVSPTANKGKIRDAHRRIMLLNHPDK-GGSPYIAAK---INEAKDLL 110
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKfkeINEAYEVL 53
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 53-110 1.61e-27

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 97.61  E-value: 1.61e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21687102   53 GFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKDLL 110
Cdd:PTZ00100  57 GFENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNGGSTYIASKVNEAKDLL 114
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
66-110 1.10e-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: 1.10e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 21687102  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAA-----KINEAKDLL 110
Cdd:COG2214  10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAeelfqRLNEAYEVL 59
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-111 7.04e-10

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 50.70  E-value: 7.04e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 21687102     66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAA-----KINEAKDLLE 111
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVLS 56
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-110 2.47e-09

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: 49.08  E-value: 2.47e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21687102  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIA----AKINEAKDLL 110
Cdd:cd06257   5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAeekfKEINEAYEVL 53
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-110 3.50e-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: 45.85  E-value: 3.50e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21687102  66 ILGVSPTANKGKIRDAHRRIMLLNHPDK-GGSPYIAAK---INEAKDLL 110
Cdd:COG0484   5 ILGVSRDASAEEIKKAYRKLAKKYHPDRnPGDPEAEEKfkeINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-110 7.65e-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: 42.85  E-value: 7.65e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 21687102    66 ILGVSPTANKGKIRDAHRRIMLLNHPDK-GGSPYIAAK---INEAKDLL 110
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKfkeINEAYEVL 53
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 58-116 7.07e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 43.40  E-value: 7.07e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21687102   58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAK---INEAKDLLEGQAKK 116
Cdd:PRK14296   1 MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKmveINEAADVLLDKDKR 62
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 37-116 5.58e-05

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 40.57  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21687102   37 FQSLPKSAFSGGyyrgGFEPKMTKREAA-----LILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKDLLE 111
Cdd:PTZ00037   3 FSGFPFDGMPGG----GFDGGRRKREVDneklyEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEKFKEISRAYEVLS 78


                 ....*
gi 21687102  112 GQAKK 116
Cdd:PTZ00037  79 DPEKR 83
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
58-110 1.30e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.47  E-value: 1.30e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21687102  58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDK---GGSP---YIA----AKINEAKDLL 110
Cdd:COG1076   1 MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaGLPEeeqRLAlqkaAAINEAYETL 63
PHA02624 PHA02624
large T antigen; Provisional
 58-111 2.15e-04

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 39.20  E-value: 2.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21687102   58 MTKREAALI---LGVSPTA--NKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKDLLE 111
Cdd:PHA02624   5 LSREESKELmdlLGLPMAAwgNLPLMRKAYLRKCKEYHPDKGGDEEKMKRLNSLYKKLQ 63
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 59-116 2.20e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 39.02  E-value: 2.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21687102   59 TKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIA----AKINEAKDLLEGQAKK 116
Cdd:PRK14281   1 MKRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAeehfKEVNEAYEVLSNDDKR 62
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 59-116 3.18e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 38.68  E-value: 3.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21687102   59 TKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAK---INEAKDLLEGQAKK 116
Cdd:PRK14298   3 TTRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKfkeISEAYAVLSDAEKR 63
PHA03102 PHA03102
Small T antigen; Reviewed
 67-105 3.31e-04

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 37.73  E-value: 3.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 21687102   67 LGVSPTA--NKGKIRDAHRRIMLLNHPDKGGSPYIAAKINE 105
Cdd:PHA03102  11 LGLPRSAwgNLPLMRKAYLRKCLEFHPDKGGDEEKMKELNT 51
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 66-116 4.45e-04

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 35.75  E-value: 4.45e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21687102  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKG-GSPYIAAK---INEAKDLLEGQAKK 116
Cdd:COG5407   5 VLGVAKTASADEIKKAYRKLAKKYHPDRNkGDPKAEERfkeINEAYELLSDAEKR 59
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 58-111 6.55e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 37.66  E-value: 6.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21687102   58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKG-GSPYIAAKINEAKDLLE 111
Cdd:PRK14286   1 MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNkGNKESEEKFKEATEAYE 55
djlA PRK09430
co-chaperone DjlA;
45-93 7.68e-04

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 37.10  E-value: 7.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21687102   45 FSGGYYRGGFEP---KMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDK 93
Cdd:PRK09430 181 FQQQQGGGGYQQaqrGPTLEDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 58-111 7.93e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 37.41  E-value: 7.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21687102   58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKG-GSPYIAAKINEAKDLLE 111
Cdd:PRK14301   1 MSQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNpDNPEAEQKFKEAAEAYE 55
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 66-116 9.75e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 37.18  E-value: 9.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21687102   66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIA---AKINEAKDLLEGQAKK 116
Cdd:PRK14292   7 LLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAekfAQINEAYAVLSDAEKR 60
PRK14279 PRK14279
molecular chaperone DnaJ;
58-116 1.44e-03

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 36.63  E-value: 1.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21687102   58 MTKREAA-----LILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAA----KINEAKDLLEGQAKK 116
Cdd:PRK14279   1 MAQREWVekdfyKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEerfkAVSEAHDVLSDPAKR 68
PRK14280 PRK14280
molecular chaperone DnaJ;
58-116 1.74e-03

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 36.24  E-value: 1.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21687102   58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAK---INEAKDLLEGQAKK 116
Cdd:PRK14280   1 MAKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKfkeISEAYEVLSDDQKR 62
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 58-116 1.95e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 36.34  E-value: 1.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21687102   58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAK---INEAKDLLEGQAKK 116
Cdd:PRK14283   2 AEKRDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKfkeISEAYAVLSDDEKR 63
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 60-116 2.02e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 36.12  E-value: 2.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21687102   60 KREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKI----NEAKDLLEGQAKK 116
Cdd:PRK14285   2 KRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIfkeaTEAYEVLIDDNKR 62
PRK14295 PRK14295
molecular chaperone DnaJ;
66-116 3.19e-03

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 35.59  E-value: 3.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21687102   66 ILGVSPTANKGKIRDAHRRIMLLNHPDKG-GSPYIAAK---INEAKDLLEGQAKK 116
Cdd:PRK14295  14 VLGVPKDATEAEIKKAYRKLAREYHPDANkGDAKAEERfkeISEAYDVLSDEKKR 68
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 59-116 3.81e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 35.52  E-value: 3.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21687102   59 TKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAK---INEAKDLLEGQAKK 116
Cdd:PRK14291   1 AKKDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKfkeINEAYQVLSDPEKR 61
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 58-110 5.99e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 34.73  E-value: 5.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21687102   58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDK-GGSPYIAAK---INEAKDLL 110
Cdd:PRK10767   1 MAKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRnPGDKEAEEKfkeIKEAYEVL 57
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 58-108 8.92e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 34.21  E-value: 8.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21687102   58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGGSPYIAAKINEAKD 108
Cdd:PRK14287   1 MSKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKE 51
 
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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