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Conserved domains on  [gi|386770961|ref|NP_001246717|]
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uncharacterized protein Dmel_CG7394, isoform C [Drosophila melanogaster]

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 ...
 5-116 1.26e-25

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: 92.61  E-value: 1.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770961   5 VILAGLSVAAVgfagKHLMRRMPQMTTKFNEALKNLPKYDAESMAA--SKYYKGGFDPKMNKREASLILGVSPSASKIKI 82
Cdd:PTZ00100   7 ALTFGGGVLAV----RYGYRYLKNQKIFGSNNMSFPLSGFNPSLGSlfLKNDLKGFENPMSKSEAYKILNISPTASKERI 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 386770961  83 KDAHKKIMLLNHPDRGGSPYLAAKINEAKDFLDK 116
Cdd:PTZ00100  83 REAHKQLMLRNHPDNGGSTYIASKVNEAKDLLLK 116
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 5-116 1.26e-25

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 92.61  E-value: 1.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770961   5 VILAGLSVAAVgfagKHLMRRMPQMTTKFNEALKNLPKYDAESMAA--SKYYKGGFDPKMNKREASLILGVSPSASKIKI 82
Cdd:PTZ00100   7 ALTFGGGVLAV----RYGYRYLKNQKIFGSNNMSFPLSGFNPSLGSlfLKNDLKGFENPMSKSEAYKILNISPTASKERI 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 386770961  83 KDAHKKIMLLNHPDRGGSPYLAAKINEAKDFLDK 116
Cdd:PTZ00100  83 REAHKQLMLRNHPDNGGSTYIASKVNEAKDLLLK 116
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
70-114 1.55e-11

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 55.88  E-value: 1.55e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 386770961  70 ILGVSPSASKIKIKDAHKKIMLLNHPDRGGSP-----YLAAKINEAKDFL 114
Cdd:COG2214   10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkalaeELFQRLNEAYEVL 59
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 70-115 4.29e-08

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: 46.00  E-value: 4.29e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 386770961  70 ILGVSPSASKIKIKDAHKKIMLLNHPDRG----GSPYLAAKINEAKDFLD 115
Cdd:cd06257    5 ILGVPPDASDEEIKKAYRKLALKYHPDKNpddpEAEEKFKEINEAYEVLS 54
DnaJ smart00271
DnaJ molecular chaperone homology domain;
70-114 6.22e-08

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 45.69  E-value: 6.22e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 386770961    70 ILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAA-----KINEAKDFL 114
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVL 55
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 70-118 6.82e-06

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: 40.53  E-value: 6.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386770961   70 ILGVSPSASKIKIKDAHKKIMLLNHPDR-GGSPYLAAK---INEAKDFL-DKAK 118
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKfkeINEAYEVLsDPEK 58
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 5-116 1.26e-25

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 92.61  E-value: 1.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770961   5 VILAGLSVAAVgfagKHLMRRMPQMTTKFNEALKNLPKYDAESMAA--SKYYKGGFDPKMNKREASLILGVSPSASKIKI 82
Cdd:PTZ00100   7 ALTFGGGVLAV----RYGYRYLKNQKIFGSNNMSFPLSGFNPSLGSlfLKNDLKGFENPMSKSEAYKILNISPTASKERI 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 386770961  83 KDAHKKIMLLNHPDRGGSPYLAAKINEAKDFLDK 116
Cdd:PTZ00100  83 REAHKQLMLRNHPDNGGSTYIASKVNEAKDLLLK 116
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
70-114 1.55e-11

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 55.88  E-value: 1.55e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 386770961  70 ILGVSPSASKIKIKDAHKKIMLLNHPDRGGSP-----YLAAKINEAKDFL 114
Cdd:COG2214   10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkalaeELFQRLNEAYEVL 59
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 70-115 4.29e-08

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: 46.00  E-value: 4.29e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 386770961  70 ILGVSPSASKIKIKDAHKKIMLLNHPDRG----GSPYLAAKINEAKDFLD 115
Cdd:cd06257    5 ILGVPPDASDEEIKKAYRKLALKYHPDKNpddpEAEEKFKEINEAYEVLS 54
DnaJ smart00271
DnaJ molecular chaperone homology domain;
70-114 6.22e-08

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 45.69  E-value: 6.22e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 386770961    70 ILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAA-----KINEAKDFL 114
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVL 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 70-114 3.00e-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: 3.00e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 386770961  70 ILGVSPSASKIKIKDAHKKIMLLNHPDR-GGSPYLAAK---INEAKDFL 114
Cdd:COG0484    5 ILGVSRDASAEEIKKAYRKLAKKYHPDRnPGDPEAEEKfkeINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 70-118 6.82e-06

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: 40.53  E-value: 6.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386770961   70 ILGVSPSASKIKIKDAHKKIMLLNHPDR-GGSPYLAAK---INEAKDFL-DKAK 118
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKfkeINEAYEVLsDPEK 58
PRK14280 PRK14280
molecular chaperone DnaJ;
62-118 9.66e-06

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 42.79  E-value: 9.66e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDrggspylaakINEAKDFLDKAK 118
Cdd:PRK14280   1 MAKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPD----------INKEEGADEKFK 47
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 62-110 1.12e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 42.81  E-value: 1.12e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDRG-GSPYLAAKINEA 110
Cdd:PRK14301   1 MSQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNpDNPEAEQKFKEA 50
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 70-118 3.42e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 41.41  E-value: 3.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 386770961  70 ILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLA---AKINEAKDFLDKAK 118
Cdd:PRK14292   7 LLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAekfAQINEAYAVLSDAE 58
PRK14279 PRK14279
molecular chaperone DnaJ;
71-118 9.47e-05

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 40.10  E-value: 9.47e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 386770961  71 LGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAA----KINEAKDFL-DKAK 118
Cdd:PRK14279  15 LGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEerfkAVSEAHDVLsDPAK 67
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 56-114 1.32e-04

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 39.80  E-value: 1.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386770961  56 GGFDPKMNKREAS-----LILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAAKINEAKDFL 114
Cdd:PTZ00037  14 GGFDGGRRKREVDneklyEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEKFKEISRAYEVL 77
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 62-118 1.59e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 39.54  E-value: 1.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAAK---INEAKD-FLDKAK 118
Cdd:PRK14296   1 MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKmveINEAADvLLDKDK 61
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 62-118 3.25e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 38.59  E-value: 3.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDR-GGSPYLAAK---INEAKDFL-DKAK 118
Cdd:PRK10767   1 MAKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRnPGDKEAEEKfkeIKEAYEVLsDPQK 62
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 64-109 3.36e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 38.68  E-value: 3.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 386770961  64 KREASLILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAAKINE 109
Cdd:PRK14298   4 TRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKE 49
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 64-97 3.59e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 38.64  E-value: 3.59e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 386770961  64 KREASLILGVSPSASKIKIKDAHKKIMLLNHPDR 97
Cdd:PRK14281   2 KRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDK 35
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 62-115 4.72e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 38.07  E-value: 4.72e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAAKINEAKDFLD 115
Cdd:PRK14287   1 MSKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYD 54
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 62-97 4.73e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 38.21  E-value: 4.73e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDR 97
Cdd:PRK14294   1 MVKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDR 36
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
62-118 6.01e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 35.93  E-value: 6.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDR---GGSPY-------LAAKINEAKDFLDKAK 118
Cdd:COG1076    1 MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaGLPEEeqrlalqKAAAINEAYETLKDPR 67
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 62-118 6.03e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 37.76  E-value: 6.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAAK---INEAKDFL-DKAK 118
Cdd:PRK14276   1 MNNTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKykeVQEAYETLsDPQK 61
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 62-110 7.61e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 37.61  E-value: 7.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAAK---INEA 110
Cdd:PRK14299   1 MAYKDYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKfkeINEA 52
djlA PRK09430
co-chaperone DjlA;
70-106 9.08e-04

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 37.10  E-value: 9.08e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 386770961  70 ILGVSPSASKIKIKDAHKKIMLLNHPDRggspyLAAK 106
Cdd:PRK09430 205 VLGVSESDDDQEIKRAYRKLMSEHHPDK-----LVAK 236
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 64-107 1.24e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 36.89  E-value: 1.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 386770961  64 KREASLILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAAKI 107
Cdd:PRK14285   2 KRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESI 45
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 62-112 1.27e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 36.89  E-value: 1.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDRG-GSPYLAAKINEAKD 112
Cdd:PRK14286   1 MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNkGNKESEEKFKEATE 52
PRK14295 PRK14295
molecular chaperone DnaJ;
70-118 2.03e-03

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 36.37  E-value: 2.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 386770961  70 ILGVSPSASKIKIKDAHKKIMLLNHPD-RGGSPYLAAK---INEAKDFLDKAK 118
Cdd:PRK14295  14 VLGVPKDATEAEIKKAYRKLAREYHPDaNKGDAKAEERfkeISEAYDVLSDEK 66
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 62-97 2.74e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 35.92  E-value: 2.74e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDR 97
Cdd:PRK14282   1 REKKDYYEILGVSRNATQEEIKRAYKRLVKEWHPDR 36
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 62-109 4.20e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 35.19  E-value: 4.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 386770961  62 MNKREASLILGVSPSASKIKIKDAHKKIMLLNHPDRGGSPYLAAKINE 109
Cdd:PRK14283   2 AEKRDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKE 49
 
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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