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Conserved domains on  [gi|74689511|sp|Q6C6T1|]
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RecName: Full=Diphthamide biosynthesis protein 4

Protein Classification

DnaJ and zf-CSL domain-containing protein( domain architecture ID 10245160)

DnaJ and zf-CSL domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-CSL pfam05207
CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which ...
 88-158 1.37e-14

CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which chelate zinc. This domain is often found associated with a pfam00226 domain. This domain is named after the conserved motif of the final cysteine.


:

Pssm-ID: 398744  Cd Length: 55  Bit Score: 64.18  E-value: 1.37e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74689511    88 DVFDLTELEEREDADgmfSWYKPCRCGEAggYVLTEEHLENNEkyyegvdvqfheIVVQCGTCSLWITVQY 158
Cdd:pfam05207   1 DEVELEDFEFDEEEE---SYYYPCRCGDE--FEITEEDLEEGE------------VVVQCPSCSLWIKVIY 54
DnaJ super family cl02542
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 2-71 2.48e-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: 50.55  E-value: 2.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511     2 NHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKLQEREAYTGSVQItaITTAYACLSNSKLKKEYD 71
Cdd:pfam00226   1 DYYEILGVS-----PDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKE--INEAYEVLSDPEKRAIYD 63
 
Name Accession Description Interval E-value
zf-CSL pfam05207
CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which ...
 88-158 1.37e-14

CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which chelate zinc. This domain is often found associated with a pfam00226 domain. This domain is named after the conserved motif of the final cysteine.


Pssm-ID: 398744  Cd Length: 55  Bit Score: 64.18  E-value: 1.37e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74689511    88 DVFDLTELEEREDADgmfSWYKPCRCGEAggYVLTEEHLENNEkyyegvdvqfheIVVQCGTCSLWITVQY 158
Cdd:pfam05207   1 DEVELEDFEFDEEEE---SYYYPCRCGDE--FEITEEDLEEGE------------VVVQCPSCSLWIKVIY 54
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 2-71 2.48e-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: 50.55  E-value: 2.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511     2 NHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKLQEREAYTGSVQItaITTAYACLSNSKLKKEYD 71
Cdd:pfam00226   1 DYYEILGVS-----PDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKE--INEAYEVLSDPEKRAIYD 63
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
2-87 3.78e-09

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 50.87  E-value: 3.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511   2 NHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKlQEREAYTGSVQITAITTAYACLSNSKLKKEYDLSLKNGANGV 81
Cdd:COG2214   6 DHYAVLGVP-----PDASLEEIRQAYRRLAKLLHPDR-GGELKALAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKGS 79


                ....*.
gi 74689511  82 KSGPGS 87
Cdd:COG2214  80 ASQPSA 85
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1-65 4.63e-08

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 47.23  E-value: 4.63e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74689511      1 MNHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKLQEREAyTGSVQITAITTAYACLSNSK 65
Cdd:smart00271   1 TDYYEILGVP-----RDASLDEIKKAYRKLALKYHPDKNPGDKE-EAEEKFKEINEAYEVLSDPE 59
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 2-105 1.88e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 49.46  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    2 NHYTILGLSEpphvpELTSADLKTAYKQALLKNHPDKLQEREAytgSVQITAITTAYACLSNSKLKKEYDLSLKNGANGV 81
Cdd:PRK14298   6 DYYEILGLSK-----DASVEDIKKAYRKLAMKYHPDKNKEPDA---EEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQ 77

                         90       100
                 ....*....|....*....|....
gi 74689511   82 KSgpGSDVFDLTELEEREDADGMF 105
Cdd:PRK14298  78 YS--AEDIFRGADFGGFGDIFEMF 99
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 2-63 2.24e-07

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: 45.23  E-value: 2.24e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74689511   2 NHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKLQEREAYTGsvQITAITTAYACLSN 63
Cdd:cd06257   1 DYYDILGVP-----PDASDEEIKKAYRKLALKYHPDKNPDDPEAEE--KFKEINEAYEVLSD 55
 
Name Accession Description Interval E-value
zf-CSL pfam05207
CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which ...
 88-158 1.37e-14

CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which chelate zinc. This domain is often found associated with a pfam00226 domain. This domain is named after the conserved motif of the final cysteine.


Pssm-ID: 398744  Cd Length: 55  Bit Score: 64.18  E-value: 1.37e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74689511    88 DVFDLTELEEREDADgmfSWYKPCRCGEAggYVLTEEHLENNEkyyegvdvqfheIVVQCGTCSLWITVQY 158
Cdd:pfam05207   1 DEVELEDFEFDEEEE---SYYYPCRCGDE--FEITEEDLEEGE------------VVVQCPSCSLWIKVIY 54
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 2-71 2.48e-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: 50.55  E-value: 2.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511     2 NHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKLQEREAYTGSVQItaITTAYACLSNSKLKKEYD 71
Cdd:pfam00226   1 DYYEILGVS-----PDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKE--INEAYEVLSDPEKRAIYD 63
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
2-87 3.78e-09

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 50.87  E-value: 3.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511   2 NHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKlQEREAYTGSVQITAITTAYACLSNSKLKKEYDLSLKNGANGV 81
Cdd:COG2214   6 DHYAVLGVP-----PDASLEEIRQAYRRLAKLLHPDR-GGELKALAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKGS 79


                ....*.
gi 74689511  82 KSGPGS 87
Cdd:COG2214  80 ASQPSA 85
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 2-71 3.81e-09

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: 52.40  E-value: 3.81e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511   2 NHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKLQEREAYTgsVQITAITTAYACLSNSKLKKEYD 71
Cdd:COG0484   1 DYYEILGVS-----RDASAEEIKKAYRKLAKKYHPDRNPGDPEAE--EKFKEINEAYEVLSDPEKRAAYD 63
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1-65 2.31e-08

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 48.64  E-value: 2.31e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74689511   1 MNHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKL------QEREAytgSVQ-ITAITTAYACLSNSK 65
Cdd:COG1076   4 DDAFELLGLP-----PDADDAELKRAYRKLQREHHPDRLaaglpeEEQRL---ALQkAAAINEAYETLKDPR 67
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1-65 4.63e-08

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 47.23  E-value: 4.63e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74689511      1 MNHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKLQEREAyTGSVQITAITTAYACLSNSK 65
Cdd:smart00271   1 TDYYEILGVP-----RDASLDEIKKAYRKLALKYHPDKNPGDKE-EAEEKFKEINEAYEVLSDPE 59
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 2-105 1.88e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 49.46  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    2 NHYTILGLSEpphvpELTSADLKTAYKQALLKNHPDKLQEREAytgSVQITAITTAYACLSNSKLKKEYDLSLKNGANGV 81
Cdd:PRK14298   6 DYYEILGLSK-----DASVEDIKKAYRKLAMKYHPDKNKEPDA---EEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQ 77

                         90       100
                 ....*....|....*....|....
gi 74689511   82 KSgpGSDVFDLTELEEREDADGMF 105
Cdd:PRK14298  78 YS--AEDIFRGADFGGFGDIFEMF 99
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 2-63 2.24e-07

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: 45.23  E-value: 2.24e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74689511   2 NHYTILGLSepphvPELTSADLKTAYKQALLKNHPDKLQEREAYTGsvQITAITTAYACLSN 63
Cdd:cd06257   1 DYYDILGVP-----PDASDEEIKKAYRKLALKYHPDKNPDDPEAEE--KFKEINEAYEVLSD 55
PRK14295 PRK14295
molecular chaperone DnaJ;
2-95 8.10e-07

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 47.54  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    2 NHYTILGLSEpphvpELTSADLKTAYKQALLKNHPDklqereAYTGSVQ----ITAITTAYACLSNSKLKKEYDLSLK-N 76
Cdd:PRK14295  10 DYYKVLGVPK-----DATEAEIKKAYRKLAREYHPD------ANKGDAKaeerFKEISEAYDVLSDEKKRKEYDEARSlF 78

                         90       100
                 ....*....|....*....|....
gi 74689511   77 GANGVKSGPGSDV-----FDLTEL 95
Cdd:PRK14295  79 GNGGFRPGPGGGGgggfnFDLGDL 102
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 1-90 1.54e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 46.81  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    1 MNHYTILGLSEPPhvpelTSADLKTAYKQALLKNHPDKLQEREAytgSVQITAITTAYACLSNSKLKKEYDlslKNGANG 80
Cdd:PRK14292   2 MDYYELLGVSRTA-----SADEIKSAYRKLALKYHPDRNKEKGA---AEKFAQINEAYAVLSDAEKRAHYD---RFGTAP 70

                         90
                 ....*....|
gi 74689511   81 VKSGPGSDVF 90
Cdd:PRK14292  71 GAGMPGGDPF 80
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 4-92 9.80e-06

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 44.43  E-value: 9.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    4 YTILGLSEpphvpELTSADLKTAYKQALLKNHPDKLQEREAYtgsvqiTAITTAYACLSNSKLKKEYDLSLKNG-ANGVK 82
Cdd:PTZ00037  31 YEVLNLSK-----DCTTSEIKKAYRKLAIKHHPDKGGDPEKF------KEISRAYEVLSDPEKRKIYDEYGEEGlEGGEQ 99

                         90
                 ....*....|
gi 74689511   83 SGPGSDVFDL 92
Cdd:PTZ00037 100 PADASDLFDL 109
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 3-90 5.38e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 42.28  E-value: 5.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    3 HYTILGLSEPPHVPELtsadlKTAYKQALLKNHPDKLQ-EREAytgSVQITAITTAYACLSNSKLKKEYDLSLKNGANGV 81
Cdd:PRK14286   6 YYDILGVSKSANDEEI-----KSAYRKLAIKYHPDKNKgNKES---EEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAG 77

                         90
                 ....*....|....*.
gi 74689511   82 KSGPG-------SDVF 90
Cdd:PRK14286  78 AGGFGqgaytdfSDIF 93
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 2-92 6.22e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 38.84  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    2 NHYTILGLSEPPhvpelTSADLKTAYKQALLKNHPDKLQEREAytgSVQITAITTAYACLSNSKLKKEYDL----SLKN- 76
Cdd:PRK14300   4 DYYQILGVSKTA-----SQADLKKAYLKLAKQYHPDTTDAKDA---EKKFKEINAAYDVLKDEQKRAAYDRfghdAFQNq 75

                         90
                 ....*....|....*....
gi 74689511   77 ---GANGVKSGPGSDVFDL 92
Cdd:PRK14300  76 qsrGGGGNHGGFHPDINDI 94
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 2-91 1.72e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 37.66  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    2 NHYTILGLSEPPhvpelTSADLKTAYKQALLKNHPDKLQEREAyTGSVQITAiTTAYACLSNSKLKKEYD----LSLKNG 77
Cdd:PRK14285   4 DYYEILGLSKGA-----SKDEIKKAYRKIAIKYHPDKNKGNKE-AESIFKEA-TEAYEVLIDDNKRAQYDrfghTAFEGG 76

                         90
                 ....*....|....*...
gi 74689511   78 A--NGVKSGPG--SDVFD 91
Cdd:PRK14285  77 GgfEGFSGGFSgfSDIFE 94
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 2-91 2.39e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 37.34  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    2 NHYTILGLSEpphvpELTSADLKTAYKQALLKNHPD-----KLQEReaytgsvqITAITTAYACLSNSKLKKEYDLS--- 73
Cdd:PRK14278   4 DYYGLLGVSR-----NASDAEIKRAYRKLARELHPDvnpdeEAQEK--------FKEISVAYEVLSDPEKRRIVDLGgdp 70

                         90       100
                 ....*....|....*....|...
gi 74689511   74 LKNGA---NGVKSGPG--SDVFD 91
Cdd:PRK14278  71 LESAGgggGGFGGGFGglGDVFE 93
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 2-71 2.42e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 37.11  E-value: 2.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    2 NHYTILGLSEpphvpELTSADLKTAYKQALLKNHPDKLQEREAytgSVQITAITTAYACLSNSKLKKEYD 71
Cdd:PRK14283   6 DYYEVLGVDR-----NADKKEIKKAYRKLARKYHPDVSEEEGA---EEKFKEISEAYAVLSDDEKRQRYD 67
hscB PRK01356
co-chaperone HscB; Provisional
 2-76 2.69e-03

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 36.39  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    2 NHYTILGLsepphvPELTSADLKTAYKQAL---LKNHPDK---LQEREAYtgsVQITA-ITTAYACLSNSKLKKEYDLSL 74
Cdd:PRK01356   3 NYFQLLGL------PQEYNIDLKILEKQYFamqVKYHPDKaktLQEKEQN---LIIASeLNNAYSTLKDALKRAEYMLLL 73


                 ..
gi 74689511   75 KN 76
Cdd:PRK01356  74 QN 75
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 2-92 3.45e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 36.71  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74689511    2 NHYTILGLSEpphvpELTSADLKTAYKQALLKNHPDK-LQEREAytgSVQITAITTAYACLSNSKLKKEYDL-------- 72
Cdd:PRK14281   4 DYYEVLGVSR-----SADKDEIKKAYRKLALKYHPDKnPDNKEA---EEHFKEVNEAYEVLSNDDKRRRYDQfghagvgs 75

                         90       100
                 ....*....|....*....|
gi 74689511   73 SLKNGANGVKSGPGSDVFDL 92
Cdd:PRK14281  76 SAASGGGPGYGGGGGDFNDI 95
 
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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