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Conserved domains on  [gi|30698003|ref|NP_851265|]
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Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

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 ...
 79-141 1.09e-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.


The actual alignment was detected with superfamily member pfam00226:

Pssm-ID: 413365 [Multi-domain]  Cd Length: 63  Bit Score: 54.02  E-value: 1.09e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30698003    79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNR-LPFADRALKIVSDAWFVLSDPFKKSFYD 141
Cdd:pfam00226   1 DYYEILGVSPDA-SDEEIKKAYRKLALKYHPDKNPgDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 79-141 1.09e-09

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: 54.02  E-value: 1.09e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30698003    79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNR-LPFADRALKIVSDAWFVLSDPFKKSFYD 141
Cdd:pfam00226   1 DYYEILGVSPDA-SDEEIKKAYRKLALKYHPDKNPgDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 79-142 6.32e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 53.79  E-value: 6.32e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30698003   79 DWYAVLRLGRLAQNPEhVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDR 142
Cdd:PRK14299   5 DYYAILGVPKNASQDE-IKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDT 67
DnaJ smart00271
DnaJ molecular chaperone homology domain;
78-136 6.69e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 43.38  E-value: 6.69e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30698003     78 PDWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNRL--PFADRALKIVSDAWFVLSDPFK 136
Cdd:smart00271   1 TDYYEILGVPRDA-SLDEIKKAYRKLALKYHPDKNPGdkEEAEEKFKEINEAYEVLSDPEK 60
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 79-190 1.04e-05

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: 45.08  E-value: 1.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698003  79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNRL-PFADRALKIVSDAWFVLSDPFKKSFYDrelqlsqlgQSGFHPQ 157
Cdd:COG0484   1 DYYEILGVSRDA-SAEEIKKAYRKLAKKYHPDRNPGdPEAEEKFKEINEAYEVLSDPEKRAAYD---------RFGHAAE 70

                        90       100       110
                ....*....|....*....|....*....|...
gi 30698003 158 TQSHQNFQWEPSSSTAVYPPPRSQSQAGTSADP 190
Cdd:COG0484  71 LLLATELAESAAAEAAAAEAKEEAAEAGASEYE 103
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 79-133 3.09e-05

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: 41.38  E-value: 3.09e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30698003  79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNR-LPFADRALKIVSDAWFVLSD 133
Cdd:cd06257   1 DYYDILGVPPDA-SDEEIKKAYRKLALKYHPDKNPdDPEAEEKFKEINEAYEVLSD 55
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 79-141 1.09e-09

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: 54.02  E-value: 1.09e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30698003    79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNR-LPFADRALKIVSDAWFVLSDPFKKSFYD 141
Cdd:pfam00226   1 DYYEILGVSPDA-SDEEIKKAYRKLALKYHPDKNPgDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 79-142 6.32e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 53.79  E-value: 6.32e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30698003   79 DWYAVLRLGRLAQNPEhVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDR 142
Cdd:PRK14299   5 DYYAILGVPKNASQDE-IKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYDT 67
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 79-164 1.44e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 53.23  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698003   79 DWYAVLRLGRLAQNPEhVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDrelqlsQLGQSGFHPQT 158
Cdd:PRK14291   4 DYYEILGVSRNATQEE-IKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYD------QFGHAAFSGSG 76


                 ....*.
gi 30698003  159 QSHQNF 164
Cdd:PRK14291  77 QQQQGQ 82
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 79-142 5.94e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 51.43  E-value: 5.94e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30698003   79 DWYAVLRLGRLAQNPEhVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDR 142
Cdd:PRK14292   3 DYYELLGVSRTASADE-IKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYDR 65
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 79-142 9.09e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 51.00  E-value: 9.09e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30698003   79 DWYAVLRLGRLAQNpEHVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDR 142
Cdd:PRK14298   6 DYYEILGLSKDASV-EDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYDR 68
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 79-142 1.09e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 50.78  E-value: 1.09e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30698003   79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDR 142
Cdd:PRK14287   5 DYYEVLGVDRNA-SVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYDQ 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 79-164 2.20e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 49.80  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698003   79 DWYAVLRLGRLAQNpEHVATQYRRLALLLNPSVNrlP---FADRALKIVSDAWFVLSDPFKKSFYDrelqlsQLGQSGFH 155
Cdd:PRK14277   6 DYYEILGVDRNATE-EEIKKAYRRLAKKYHPDLN--PgdkEAEQKFKEINEAYEILSDPQKRAQYD------QFGHAAFD 76


                 ....*....
gi 30698003  156 PQTQSHQNF 164
Cdd:PRK14277  77 PGGFGQGGF 85
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 79-167 2.30e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 49.44  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698003   79 DWYAVLRLGRLAQNPEhVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDrelQLSQLGQSGFhPQT 158
Cdd:PRK14283   6 DYYEVLGVDRNADKKE-IKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYD---QFGHAGMDGF-SQE 80


                 ....*....
gi 30698003  159 QSHQNFQWE 167
Cdd:PRK14283  81 DIFNNINFE 89
PRK14280 PRK14280
molecular chaperone DnaJ;
79-165 5.07e-06

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 48.56  E-value: 5.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698003   79 DWYAVLRLGRLAQNPEhVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDrelqlsQLG----QSGF 154
Cdd:PRK14280   5 DYYEVLGVSKSASKDE-IKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYD------QFGhagpNQGF 77

                         90
                 ....*....|.
gi 30698003  155 HPQTQSHQNFQ 165
Cdd:PRK14280  78 GGGGFGGGDFG 88
DnaJ smart00271
DnaJ molecular chaperone homology domain;
78-136 6.69e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 43.38  E-value: 6.69e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30698003     78 PDWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNRL--PFADRALKIVSDAWFVLSDPFK 136
Cdd:smart00271   1 TDYYEILGVPRDA-SLDEIKKAYRKLALKYHPDKNPGdkEEAEEKFKEINEAYEVLSDPEK 60
PRK10266 PRK10266
curved DNA-binding protein;
77-161 8.89e-06

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 47.51  E-value: 8.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698003   77 LPDWYAVLRLgRLAQNPEHVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDrelQLSQ-LGQSGFH 155
Cdd:PRK10266   3 LKDYYAIMGV-KPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYD---QLWQhRNDPQFN 78


                 ....*.
gi 30698003  156 PQTQSH 161
Cdd:PRK10266  79 RQFQHG 84
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 79-190 1.04e-05

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: 45.08  E-value: 1.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698003  79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNRL-PFADRALKIVSDAWFVLSDPFKKSFYDrelqlsqlgQSGFHPQ 157
Cdd:COG0484   1 DYYEILGVSRDA-SAEEIKKAYRKLAKKYHPDRNPGdPEAEEKFKEINEAYEVLSDPEKRAAYD---------RFGHAAE 70

                        90       100       110
                ....*....|....*....|....*....|...
gi 30698003 158 TQSHQNFQWEPSSSTAVYPPPRSQSQAGTSADP 190
Cdd:COG0484  71 LLLATELAESAAAEAAAAEAKEEAAEAGASEYE 103
PRK14293 PRK14293
molecular chaperone DnaJ;
79-154 1.83e-05

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 46.91  E-value: 1.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30698003   79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDR--ELQLSqlGQSGF 154
Cdd:PRK14293   4 DYYEILGVSRDA-DKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYDQfgEAGVS--GAAGF 78
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 79-141 1.90e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 46.58  E-value: 1.90e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30698003   79 DWYAVLRLGRLAQNPEhVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYD 141
Cdd:PRK14278   4 DYYGLLGVSRNASDAE-IKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 79-142 2.17e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 46.37  E-value: 2.17e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30698003   79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNrlP---FADRALKIVSDAWFVLSDPFKKSFYDR 142
Cdd:PRK14284   2 DYYTILGVSKTA-SPEEIKKAYRKLAVKYHPDKN--PgdaEAEKRFKEVSEAYEVLSDAQKRESYDR 65
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 79-133 3.09e-05

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: 41.38  E-value: 3.09e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30698003  79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNR-LPFADRALKIVSDAWFVLSD 133
Cdd:cd06257   1 DYYDILGVPPDA-SDEEIKKAYRKLALKYHPDKNPdDPEAEEKFKEINEAYEVLSD 55
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 79-153 4.73e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 45.46  E-value: 4.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30698003   79 DWYAVLRLGRLAQNPEhVATQYRRLALLLNPSVNRLPFADRALKIVSDAWFVLSDPFKKSFYDrelqlsQLGQSG 153
Cdd:PRK14276   5 EYYDRLGVSKDASQDE-IKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYD------QYGAAG 72
PRK14295 PRK14295
molecular chaperone DnaJ;
79-156 2.19e-04

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 43.30  E-value: 2.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30698003   79 DWYAVLRLGRLAQNPEhVATQYRRLALLLNPSVNR-LPFADRALKIVSDAWFVLSDPFKKSFYDRELQLsqLGQSGFHP 156
Cdd:PRK14295  10 DYYKVLGVPKDATEAE-IKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYDEARSL--FGNGGFRP 85
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 79-154 5.54e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 42.06  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698003   79 DWYAVLRLGRLAqNPEHVATQYRRLALLLNPSVNrlPF---ADRALKIVSDAWFVLSDPFKKSFYDR--ELQLSQLGQSG 153
Cdd:PRK14294   5 DYYEILGVTRDA-SEEEIKKSYRKLAMKYHPDRN--PGdkeAEELFKEAAEAYEVLSDPKKRGIYDQygHEGLSGTGFSG 81


                 .
gi 30698003  154 F 154
Cdd:PRK14294  82 F 82
PRK14297 PRK14297
molecular chaperone DnaJ;
79-142 8.03e-04

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 41.69  E-value: 8.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30698003   79 DWYAVLRLGRLAQNPEhVATQYRRLALLLNPSVNR-LPFADRALKIVSDAWFVLSDPFKKSFYDR 142
Cdd:PRK14297   5 DYYEVLGLEKGASDDE-IKKAFRKLAIKYHPDKNKgNKEAEEKFKEINEAYQVLSDPQKKAQYDQ 68
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 79-167 1.84e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 40.30  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30698003   79 DWYAVLRLGRLAQNpEHVATQYRRLALLLNPSVN--RLPFADRALKIVSDAWFVLSDPFKKSFYDrelqlsQLGQSGFHp 156
Cdd:PRK14290   4 DYYKILGVDRNASQ-EDIKKAFRELAKKWHPDLHpgNKAEAEEKFKEISEAYEVLSDPQKRRQYD------QTGTVDFG- 75

                         90
                 ....*....|.
gi 30698003  157 qtQSHQNFQWE 167
Cdd:PRK14290  76 --AGGSNFNWD 84
 
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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