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Conserved domains on  [gi|502864108|ref|WP_013099084|]
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MULTISPECIES: Hsp33 family molecular chaperone HslO [Enterobacter]

Protein Classification

Hsp33 family molecular chaperone HslO( domain architecture ID 11478100)

Hsp33 family molecular chaperone HslO is redox regulated and protects both thermally-unfolding and oxidatively-damaged proteins from irreversible aggregation

Gene Symbol:  hslO
Gene Ontology:  GO:0006457|GO:0051082
PubMed:  10025400|10359689
SCOP:  4003643

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hslO PRK00114
Hsp33 family molecular chaperone HslO;
3-285 1.45e-156

Hsp33 family molecular chaperone HslO;


:

Pssm-ID: 234643  Cd Length: 293  Bit Score: 438.06  E-value: 1.45e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   3 QHDQLHRYLFEQFAVRGELVTVSETWKQILENHNYPLPVKTLLGELLVATSLLTATLKFAGDITVQLQGDGPMSLAVING 82
Cdd:PRK00114   1 MADYLVRALAEDGAVRGEAVDTTETVQEAQERHDYPPTATAALGRTLTATSLLTATLKFDGDITVQIQGDGPLGLIVVDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  83 NNQQQMRGVARVQGDVPE-----NADLKTLVGNGYLVITISPEEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIR 157
Cdd:PRK00114  81 NADGQVRGYVRNPGVDLElnadgKLDVGQAVGNGYLVVTKDPGLGEPYQGVVPLVSGEIGEDLAYYFARSEQTPSAVGLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108 158 TGEVDG--QPAAGGMLLQVLPAQDaqtNDFEHLATLTETIKAEELFNL------SATDVLWRLYHEEEVTVYDPQAVEFK 229
Cdd:PRK00114 161 VLVNEDdsIKAAGGFLLQVLPGAA---EDFEHLATLEERIKEEELFSLllesglTAEELLYRLYHEEDVKILEPQPVEFK 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502864108 230 CTCSRERCAGALKTLPDEEIDSIMAEDGEIDMHCDYCGTHYVFNSMDIAEIRNNAS 285
Cdd:PRK00114 238 CDCSRERSANALKSLGKEELQEMIAEDGGAEMVCQFCGNKYLFDEEDLEELIAEAS 293
 
Name Accession Description Interval E-value
hslO PRK00114
Hsp33 family molecular chaperone HslO;
3-285 1.45e-156

Hsp33 family molecular chaperone HslO;


Pssm-ID: 234643  Cd Length: 293  Bit Score: 438.06  E-value: 1.45e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   3 QHDQLHRYLFEQFAVRGELVTVSETWKQILENHNYPLPVKTLLGELLVATSLLTATLKFAGDITVQLQGDGPMSLAVING 82
Cdd:PRK00114   1 MADYLVRALAEDGAVRGEAVDTTETVQEAQERHDYPPTATAALGRTLTATSLLTATLKFDGDITVQIQGDGPLGLIVVDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  83 NNQQQMRGVARVQGDVPE-----NADLKTLVGNGYLVITISPEEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIR 157
Cdd:PRK00114  81 NADGQVRGYVRNPGVDLElnadgKLDVGQAVGNGYLVVTKDPGLGEPYQGVVPLVSGEIGEDLAYYFARSEQTPSAVGLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108 158 TGEVDG--QPAAGGMLLQVLPAQDaqtNDFEHLATLTETIKAEELFNL------SATDVLWRLYHEEEVTVYDPQAVEFK 229
Cdd:PRK00114 161 VLVNEDdsIKAAGGFLLQVLPGAA---EDFEHLATLEERIKEEELFSLllesglTAEELLYRLYHEEDVKILEPQPVEFK 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502864108 230 CTCSRERCAGALKTLPDEEIDSIMAEDGEIDMHCDYCGTHYVFNSMDIAEIRNNAS 285
Cdd:PRK00114 238 CDCSRERSANALKSLGKEELQEMIAEDGGAEMVCQFCGNKYLFDEEDLEELIAEAS 293
HslO COG1281
Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein ...
4-283 4.08e-140

Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440892  Cd Length: 291  Bit Score: 396.44  E-value: 4.08e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   4 HDQLHRYLFEQFAVRGELVTVSETWKQILENHNYPLPVKTLLGELLVATSLLTATLKFAGDITVQLQGDGPMSLAVINGN 83
Cdd:COG1281    1 DDYLVRFLFEDGDVRGEAVRLTETVQEALARHDYPPPVTALLGEALAAAALLGATLKFDGRLTLQIQGDGPLGLLVADAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  84 NQQQMRGVARVQGDVPE-----NADLKTLVGNGYLVITISPEEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRT 158
Cdd:COG1281   81 SDGEVRGYARNPEVELPlnekgKLDVGELVGNGYLAVTIDPGLGEPYQGIVPLVGGELAEDLEYYFAQSEQLPTRVWLGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108 159 GEVDGQPAAGGMLLQVLPAQD----AQTNDFEHLATLTETIKAEELF--NLSATDVLWRLYHEEEVTVYDPQAVEFKCTC 232
Cdd:COG1281  161 LVDEDGWRAGGLLLQLLPGADeeaiDDEDAWERAVALAATLTISELLdpGLTPEELLYRLFHEEDVRVFEPQPVRFRCSC 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502864108 233 SRERCAGALKTLPDEEIDSIMAEDGEIDMHCDYCGTHYVFNSMDIAEIRNN 283
Cdd:COG1281  241 SRERVENALKSLGREELEDMLEEDGGIEVTCEFCNEKYRFDPEELEELFAE 291
Hsp33 cd00498
Heat shock protein 33 (Hsp33): Cytosolic protein that acts as a molecular chaperone under ...
7-273 3.51e-120

Heat shock protein 33 (Hsp33): Cytosolic protein that acts as a molecular chaperone under oxidative conditions. In normal (reducing) cytosolic conditions, four conserved Cys residues are coordinated by a Zn ion. Under oxidative stress (such as heat shock), the Cys are reversibly oxidized to disulfide bonds, which causes the chaperone activity to be turned on. Hsp33 is homodimeric in its functional form.


Pssm-ID: 238278  Cd Length: 275  Bit Score: 345.37  E-value: 3.51e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   7 LHRYLFEQFAVRGELVTVSETWKQILENHNYPLPVKTLLGELLVATSLLTATLKFAGDITVQLQGDGPMSLAVINGNNQQ 86
Cdd:cd00498    1 LVRFIADDGDVRGEAVRLTETVQEALRRHDYPPTATALLGRTLVAAALLGASLKFDGRLTVQIQGDGPVGLIVADADADG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  87 QMRGVARVQG-DVPEN----ADLKTLVGNGYLVITISPEEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRTGEV 161
Cdd:cd00498   81 TVRGYVRNPEvDLPLNedgkLDVGDAVGNGYLAVTKDLGLGEPYQGVVPLVSGEIAEDLEYYFAQSEQLPSAVGLGVLVN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108 162 --DGQPAAGGMLLQVLP-AQDAQTNDFEHLATLTETIKAEELFNLSATDVLWRLYHEEEVTVYDPQAVEFKCTCSRERCA 238
Cdd:cd00498  161 pdGTVKAAGGLLLQVLPgADEEDIDAWEKVIKLMPTVSALELLGLSPEELLYRLFHEEEVRILEKQPVRFRCDCSRERVA 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 502864108 239 GALKTLPDEEIDSIMAEDGEIDMHCDYCGTHYVFN 273
Cdd:cd00498  241 AALLTLGKEELADMIEEDGGIEVTCEFCGEKYHFD 275
HSP33 pfam01430
Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones ...
11-273 7.49e-105

Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidising conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.


Pssm-ID: 460209  Cd Length: 271  Bit Score: 306.37  E-value: 7.49e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   11 LFEQFAVRGELVTVSETWKQILENHNYPLPVKTLLGELLVATSLLTATLKFAGD-ITVQLQGDGPMSLAVINGNNQQQMR 89
Cdd:pfam01430   1 LAEDGNVRGFAVRLTELVEEALARHDYPPVATAALGRALAAAALLGATLKFEDGrLTLQIQGDGPLGLLVADADSDGNVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   90 GVARV-QGDVPENA---DLKTLVGNGYLVITISPEEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRTG-EVDGQ 164
Cdd:pfam01430  81 GYVRNpAVELPLNEkglDVGGAVGDGYLAVTKDLGLKEPYQGIVPLVSGEIAEDLTYYFAQSEQIPSAVGLGVLvDKDGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  165 P-AAGGMLLQVLPAQDAQTNDF--EHLATLTeTIKAEELFNLSATDVLWRLYHEEEVTVYDPQAVEFKCTCSRERCAGAL 241
Cdd:pfam01430 161 VkAAGGLLLQLLPGADEETIDDleERLKALP-TVTDEELLELPAEELLERLFHEEDVRILEPQPVRFKCRCSRERVENAL 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 502864108  242 KTLPDEEIDSIMAEDGEIDMHCDYCGTHYVFN 273
Cdd:pfam01430 240 ISLGKEELEEIIEEDGKIEVTCHFCNKKYRFD 271
 
Name Accession Description Interval E-value
hslO PRK00114
Hsp33 family molecular chaperone HslO;
3-285 1.45e-156

Hsp33 family molecular chaperone HslO;


Pssm-ID: 234643  Cd Length: 293  Bit Score: 438.06  E-value: 1.45e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   3 QHDQLHRYLFEQFAVRGELVTVSETWKQILENHNYPLPVKTLLGELLVATSLLTATLKFAGDITVQLQGDGPMSLAVING 82
Cdd:PRK00114   1 MADYLVRALAEDGAVRGEAVDTTETVQEAQERHDYPPTATAALGRTLTATSLLTATLKFDGDITVQIQGDGPLGLIVVDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  83 NNQQQMRGVARVQGDVPE-----NADLKTLVGNGYLVITISPEEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIR 157
Cdd:PRK00114  81 NADGQVRGYVRNPGVDLElnadgKLDVGQAVGNGYLVVTKDPGLGEPYQGVVPLVSGEIGEDLAYYFARSEQTPSAVGLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108 158 TGEVDG--QPAAGGMLLQVLPAQDaqtNDFEHLATLTETIKAEELFNL------SATDVLWRLYHEEEVTVYDPQAVEFK 229
Cdd:PRK00114 161 VLVNEDdsIKAAGGFLLQVLPGAA---EDFEHLATLEERIKEEELFSLllesglTAEELLYRLYHEEDVKILEPQPVEFK 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502864108 230 CTCSRERCAGALKTLPDEEIDSIMAEDGEIDMHCDYCGTHYVFNSMDIAEIRNNAS 285
Cdd:PRK00114 238 CDCSRERSANALKSLGKEELQEMIAEDGGAEMVCQFCGNKYLFDEEDLEELIAEAS 293
HslO COG1281
Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein ...
4-283 4.08e-140

Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440892  Cd Length: 291  Bit Score: 396.44  E-value: 4.08e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   4 HDQLHRYLFEQFAVRGELVTVSETWKQILENHNYPLPVKTLLGELLVATSLLTATLKFAGDITVQLQGDGPMSLAVINGN 83
Cdd:COG1281    1 DDYLVRFLFEDGDVRGEAVRLTETVQEALARHDYPPPVTALLGEALAAAALLGATLKFDGRLTLQIQGDGPLGLLVADAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  84 NQQQMRGVARVQGDVPE-----NADLKTLVGNGYLVITISPEEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRT 158
Cdd:COG1281   81 SDGEVRGYARNPEVELPlnekgKLDVGELVGNGYLAVTIDPGLGEPYQGIVPLVGGELAEDLEYYFAQSEQLPTRVWLGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108 159 GEVDGQPAAGGMLLQVLPAQD----AQTNDFEHLATLTETIKAEELF--NLSATDVLWRLYHEEEVTVYDPQAVEFKCTC 232
Cdd:COG1281  161 LVDEDGWRAGGLLLQLLPGADeeaiDDEDAWERAVALAATLTISELLdpGLTPEELLYRLFHEEDVRVFEPQPVRFRCSC 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502864108 233 SRERCAGALKTLPDEEIDSIMAEDGEIDMHCDYCGTHYVFNSMDIAEIRNN 283
Cdd:COG1281  241 SRERVENALKSLGREELEDMLEEDGGIEVTCEFCNEKYRFDPEELEELFAE 291
Hsp33 cd00498
Heat shock protein 33 (Hsp33): Cytosolic protein that acts as a molecular chaperone under ...
7-273 3.51e-120

Heat shock protein 33 (Hsp33): Cytosolic protein that acts as a molecular chaperone under oxidative conditions. In normal (reducing) cytosolic conditions, four conserved Cys residues are coordinated by a Zn ion. Under oxidative stress (such as heat shock), the Cys are reversibly oxidized to disulfide bonds, which causes the chaperone activity to be turned on. Hsp33 is homodimeric in its functional form.


Pssm-ID: 238278  Cd Length: 275  Bit Score: 345.37  E-value: 3.51e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   7 LHRYLFEQFAVRGELVTVSETWKQILENHNYPLPVKTLLGELLVATSLLTATLKFAGDITVQLQGDGPMSLAVINGNNQQ 86
Cdd:cd00498    1 LVRFIADDGDVRGEAVRLTETVQEALRRHDYPPTATALLGRTLVAAALLGASLKFDGRLTVQIQGDGPVGLIVADADADG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  87 QMRGVARVQG-DVPEN----ADLKTLVGNGYLVITISPEEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRTGEV 161
Cdd:cd00498   81 TVRGYVRNPEvDLPLNedgkLDVGDAVGNGYLAVTKDLGLGEPYQGVVPLVSGEIAEDLEYYFAQSEQLPSAVGLGVLVN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108 162 --DGQPAAGGMLLQVLP-AQDAQTNDFEHLATLTETIKAEELFNLSATDVLWRLYHEEEVTVYDPQAVEFKCTCSRERCA 238
Cdd:cd00498  161 pdGTVKAAGGLLLQVLPgADEEDIDAWEKVIKLMPTVSALELLGLSPEELLYRLFHEEEVRILEKQPVRFRCDCSRERVA 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 502864108 239 GALKTLPDEEIDSIMAEDGEIDMHCDYCGTHYVFN 273
Cdd:cd00498  241 AALLTLGKEELADMIEEDGGIEVTCEFCGEKYHFD 275
HSP33 pfam01430
Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones ...
11-273 7.49e-105

Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidising conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.


Pssm-ID: 460209  Cd Length: 271  Bit Score: 306.37  E-value: 7.49e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   11 LFEQFAVRGELVTVSETWKQILENHNYPLPVKTLLGELLVATSLLTATLKFAGD-ITVQLQGDGPMSLAVINGNNQQQMR 89
Cdd:pfam01430   1 LAEDGNVRGFAVRLTELVEEALARHDYPPVATAALGRALAAAALLGATLKFEDGrLTLQIQGDGPLGLLVADADSDGNVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108   90 GVARV-QGDVPENA---DLKTLVGNGYLVITISPEEGERYQGVVGLEGDTLAACLEDYFMRSEQLPTRLFIRTG-EVDGQ 164
Cdd:pfam01430  81 GYVRNpAVELPLNEkglDVGGAVGDGYLAVTKDLGLKEPYQGIVPLVSGEIAEDLTYYFAQSEQIPSAVGLGVLvDKDGS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  165 P-AAGGMLLQVLPAQDAQTNDF--EHLATLTeTIKAEELFNLSATDVLWRLYHEEEVTVYDPQAVEFKCTCSRERCAGAL 241
Cdd:pfam01430 161 VkAAGGLLLQLLPGADEETIDDleERLKALP-TVTDEELLELPAEELLERLFHEEDVRILEPQPVRFKCRCSRERVENAL 239
                         250       260       270
                  ....*....|....*....|....*....|..
gi 502864108  242 KTLPDEEIDSIMAEDGEIDMHCDYCGTHYVFN 273
Cdd:pfam01430 240 ISLGKEELEEIIEEDGKIEVTCHFCNKKYRFD 271
hslO PRK01402
Hsp33-like chaperonin; Reviewed
17-272 9.31e-68

Hsp33-like chaperonin; Reviewed


Pssm-ID: 234952  Cd Length: 328  Bit Score: 213.65  E-value: 9.31e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  17 VRGELVTVSETWKQILENHNYPLPVKTLLGELLVATSLLTATLKFAGDITVQLQGDGPMSLAVINGNNQQQMRGVAR--- 93
Cdd:PRK01402  29 VRGRAVRLGPALDEILTRHDYPEPVARLLGEAVVLTVLLGSSLKFEGRFILQTQGDGPVDMLVVDFSTPDRLRAYARfde 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108  94 ------VQGDVpenADLKTLVGNGYLVITIspEEG---ERYQGVVGLEGDTLAACLEDYFMRSEQLPTRlfIR------- 157
Cdd:PRK01402 109 erlaaaIAAGE---TSPEALLGKGHLAMTI--DQGpdmQRYQGIVALDGSTLEEAAHQYFRQSEQIPTR--VRlavaeli 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108 158 TGEVDGQPA--AGGMLLQVLP-------AQDAQTND--------------FEHLATLTETIKAEELFN--LSATDVLWRL 212
Cdd:PRK01402 182 TGGGAGKPRwrAGGLLIQFLPqaperarQADLHPGDapegteiavpeddaWVEARSLVETIEDDELIDptVSSERLLYRL 261
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502864108 213 YHEEEVTVYDPQAVEFKCTCSRERCAGALKTLPDEEIDSiMAEDGEIDMHCDYCGTHYVF 272
Cdd:PRK01402 262 FHERGVRVFDPQPVIARCSCSREKIAGVLKGFSAEERAD-MVEDGKISVTCEFCSRVYRF 320
 
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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