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Conserved domains on  [gi|488692564|ref|WP_002616704|]
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MULTISPECIES: ATP-binding protein [Leptospira]

Protein Classification

anti-sigma regulatory factor( domain architecture ID 10005496)

anti-sigma regulatory factor similar to Mycobacterium tuberculosis RsbW, a putative ATPase/GTPase with serine-protein kinase activity that functions as a cognate anti-sigma factor for alternative sigma factor SigF

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
14-140 1.65e-31

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


:

Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 108.85  E-value: 1.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  14 RLQIPSHPRYLSIIRSLIHNLAFENGFTTSDSADLKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFGDQ 93
Cdd:COG2172    1 SLSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDPDGPVEVELELDPDGLEIEVRDEGPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488692564  94 KNLSEIRGYEPNDyREEGIGLYLVKKLTDHFYLDqSLPEGNRLILTK 140
Cdd:COG2172   81 FDPEDLPDPYSTL-AEGGRGLFLIRRLMDEVEYE-SDPGGTTVRLVK 125
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
14-140 1.65e-31

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 108.85  E-value: 1.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  14 RLQIPSHPRYLSIIRSLIHNLAFENGFTTSDSADLKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFGDQ 93
Cdd:COG2172    1 SLSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDPDGPVEVELELDPDGLEIEVRDEGPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488692564  94 KNLSEIRGYEPNDyREEGIGLYLVKKLTDHFYLDqSLPEGNRLILTK 140
Cdd:COG2172   81 FDPEDLPDPYSTL-AEGGRGLFLIRRLMDEVEYE-SDPGGTTVRLVK 125
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
17-140 1.19e-25

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 93.89  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564   17 IPSHPRYLSIIRSLIHNLAFENGFTTSDSADLKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFGDQKNL 96
Cdd:pfam13581   1 FPADPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHAYREGPEGPVEVRLTSDGGGLVVTVADSGPPFDP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 488692564   97 SEIRGYEPN----DYREEGIGLYLVKKLTDHFYLDQSlPEGNRLILTK 140
Cdd:pfam13581  81 LTLPPPDLEepdeDRKEGGRGLALIRGLMDDVEYTRG-GEGNTVRMRK 127
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
 15-122 2.26e-20

serine-protein kinase RsbW; Provisional


Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 81.51  E-value: 2.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  15 LQIPSHPRYLSIIRSLIHNLAFENGFTTSDSADLKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFG--- 91
Cdd:PRK04069  10 MKIPAKAEYVSIIRLTLSGVANRMGFSYDDIEDMKIAVSEACTNAVQHAYKEDEVGEIHIRFEIYEDRLEIVVADNGvsf 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488692564  92 DQKNLSEIRG-YEPN----DYREEGIGLYLVKKLTD 122
Cdd:PRK04069  90 DYETLKSKLGpYDISkpieDLREGGLGLFLIETLMD 125
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 48-140 6.53e-17

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 70.37  E-value: 6.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  48 LKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFGDQKNLSEIRGYEPNDyREEGIGLYLVKKLTDHFYLd 127
Cdd:cd16936    1 VELAVSEAVTNAVRHAYRHDGPGPVRLELDLDPDRLRVEVTDSGPGFDPLRPADPDAGL-REGGRGLALIRALMDEVGY- 78

                         90
                 ....*....|...
gi 488692564 128 QSLPEGNRLILTK 140
Cdd:cd16936   79 RRTPGGKTVWLEL 91
 
Name Accession Description Interval E-value
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
14-140 1.65e-31

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 108.85  E-value: 1.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  14 RLQIPSHPRYLSIIRSLIHNLAFENGFTTSDSADLKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFGDQ 93
Cdd:COG2172    1 SLSLPADLEDLGLARRAVRALLRELGLDEDDADDLVLAVSEAVTNAVRHAYGGDPDGPVEVELELDPDGLEIEVRDEGPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488692564  94 KNLSEIRGYEPNDyREEGIGLYLVKKLTDHFYLDqSLPEGNRLILTK 140
Cdd:COG2172   81 FDPEDLPDPYSTL-AEGGRGLFLIRRLMDEVEYE-SDPGGTTVRLVK 125
HATPase_c_2 pfam13581
Histidine kinase-like ATPase domain;
17-140 1.19e-25

Histidine kinase-like ATPase domain;


Pssm-ID: 433327 [Multi-domain]  Cd Length: 127  Bit Score: 93.89  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564   17 IPSHPRYLSIIRSLIHNLAFENGFTTSDSADLKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFGDQKNL 96
Cdd:pfam13581   1 FPADPEQLRAARRVLEAVLRRAGLPEELLDEVELAVGEACTNAVEHAYREGPEGPVEVRLTSDGGGLVVTVADSGPPFDP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 488692564   97 SEIRGYEPN----DYREEGIGLYLVKKLTDHFYLDQSlPEGNRLILTK 140
Cdd:pfam13581  81 LTLPPPDLEepdeDRKEGGRGLALIRGLMDDVEYTRG-GEGNTVRMRK 127
PRK04069 PRK04069
serine-protein kinase RsbW; Provisional
 15-122 2.26e-20

serine-protein kinase RsbW; Provisional


Pssm-ID: 235217 [Multi-domain]  Cd Length: 161  Bit Score: 81.51  E-value: 2.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  15 LQIPSHPRYLSIIRSLIHNLAFENGFTTSDSADLKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFG--- 91
Cdd:PRK04069  10 MKIPAKAEYVSIIRLTLSGVANRMGFSYDDIEDMKIAVSEACTNAVQHAYKEDEVGEIHIRFEIYEDRLEIVVADNGvsf 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488692564  92 DQKNLSEIRG-YEPN----DYREEGIGLYLVKKLTD 122
Cdd:PRK04069  90 DYETLKSKLGpYDISkpieDLREGGLGLFLIETLMD 125
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
 48-140 6.53e-17

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 70.37  E-value: 6.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  48 LKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFGDQKNLSEIRGYEPNDyREEGIGLYLVKKLTDHFYLd 127
Cdd:cd16936    1 VELAVSEAVTNAVRHAYRHDGPGPVRLELDLDPDRLRVEVTDSGPGFDPLRPADPDAGL-REGGRGLALIRALMDEVGY- 78

                         90
                 ....*....|...
gi 488692564 128 QSLPEGNRLILTK 140
Cdd:cd16936   79 RRTPGGKTVWLEL 91
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 44-139 6.86e-07

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 45.05  E-value: 6.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564   44 DSADLKLAVGECLLNVIKHSYSGRKnlpIFIEISlFDDRIEIRIRDFG---DQKNLSEIRG----YEPNDYREEGIGLYL 116
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGE---ITVTLS-EGGELTLTVEDNGigiPPEDLPRIFEpfstADKRGGGGTGLGLSI 77

                          90       100
                  ....*....|....*....|....*..
gi 488692564  117 VKKLTD----HFYLDQSLPEGNRLILT 139
Cdd:pfam02518  78 VRKLVEllggTITVESEPGGGTTVTLT 104
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
51-114 6.06e-06

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 44.22  E-value: 6.06e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488692564  51 AVGECLLNVIKHSYSGRknlpIFIEISLFDDRIEIRIRDFGdqknlseiRGYEPNDYREEGIGL 114
Cdd:COG4585  166 IVQEALTNALKHAGATR----VTVTLEVDDGELTLTVRDDG--------VGFDPEAAPGGGLGL 217
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 43-122 1.14e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 41.89  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  43 SDSADLKLAVGECLLNVIKHSYSGRKnlpifIEISLFDD--RIEIRIRDFG---DQKNLSEI--RGYEPNDYREE----G 111
Cdd:cd16948    1 TDAKWLSFIIGQIVSNALKYSKQGGK-----IEIYSETNeqGVVLSIKDFGigiPEEDLPRVfdKGFTGENGRNFqestG 75

                         90
                 ....*....|.
gi 488692564 112 IGLYLVKKLTD 122
Cdd:cd16948   76 MGLYLVKKLCD 86
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
13-122 5.41e-05

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 41.43  E-value: 5.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  13 FRLQIPSHPRYLSIirslihNLAFENGFTTSDSADLKLAVGECLLNVIKHSYSGRknlPIFIEISLFDDRIEIRIRDFG- 91
Cdd:COG2205  104 LRPLAEEKGIRLEL------DLPPELPLVYADPELLEQVLANLLDNAIKYSPPGG---TITISARREGDGVRISVSDNGp 174

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488692564  92 -----DQKNLSEiRGYEPNDYREE---GIGLYLVKKLTD 122
Cdd:COG2205  175 gipeeELERIFE-RFYRGDNSRGEggtGLGLAIVKRIVE 212
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
43-122 8.73e-04

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 37.97  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  43 SDSADLKLAVGECLLNVIKHSYSGRknlPIFIEISLFDDRIEIRIRDFG---DQKNLSEI-----RGYEPNDYREEGIGL 114
Cdd:COG0642  219 GDPDRLRQVLLNLLSNAIKYTPEGG---TVTVSVRREGDRVRISVEDTGpgiPPEDLERIfepffRTDPSRRGGGTGLGL 295


                 ....*...
gi 488692564 115 YLVKKLTD 122
Cdd:COG0642  296 AIVKRIVE 303
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
 41-140 1.60e-03

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 36.36  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  41 TTSDSADLKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFG-DQKNLSEIRgyEP-----NDYREEGIGL 114
Cdd:cd16942   32 TIDELTEIKTVVSEAVTNAIIHGYNNDPNGIVSISVIIEDGVVHLTVRDEGvGIPDIEEAR--QPlfttkPELERSGMGF 109

                         90       100
                 ....*....|....*....|....*.
gi 488692564 115 YLVKKLTDHFYLDQSLPEGNRLILTK 140
Cdd:cd16942  110 TIMENFMDEVIVESEVNKGTTVYLKK 135
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 52-92 4.38e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 34.45  E-value: 4.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 488692564  52 VGECLLNVIKHSYSGRknlpIFIEISLFDDRIEIRIRDFGD 92
Cdd:cd16917    5 VQEALTNALKHAGASR----VRVTLSYTADELTLTVVDDGV 41
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 48-139 6.54e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 34.70  E-value: 6.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488692564  48 LKLAVGECLLNVIKHSYSGRKNLPIFIEISLFDDRIEIRIRDFGdqknlseiRGY-EPNDYREEG-IGLYLVKKLT---- 121
Cdd:cd16951   40 IGLVVNELLQNALKHAFSDREGGTITIRSVVDGDYLRITVIDDG--------VGLpQDEDWPNKGsLGLQIVRSLVegel 111

                         90
                 ....*....|....*...
gi 488692564 122 DHFYLDQSLPEGNRLILT 139
Cdd:cd16951  112 KAFLEVQSAENGTRVNID 129
 
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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