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Conserved domains on  [gi|767988212|ref|XP_011544014|]
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serine/threonine-protein kinase/endoribonuclease IRE2 isoform X3 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase/endoribonuclease IRE( domain architecture ID 10176810)

serine/threonine-protein kinase/endoribonuclease IRE is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side; it acts as an ER stress sensor, undergoing trans-autophosphorylation during ER stress, leading to activation of the endoribonuclease domain, which splices HAC1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Luminal_IRE1 cd09769
The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, ...
 38-366 6.39e-80

The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, Inositol-requiring protein 1; The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), a serine/threonine protein kinase (STK) and a type I transmembrane protein that is localized in the endoplasmic reticulum (ER). IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is a kinase receptor that also contains an endoribonuclease domain in the cytoplasmic side. It plays roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1 acts as an ER stress sensor and is the oldest and most conserved component of the UPR in eukaryotes. During ER stress, IRE1 dimerizes through its luminal domain and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). IRE1alpha is expressed in all cells and tissues while IRE1beta is found only in intestinal epithelial cells.


:

Pssm-ID: 188875 [Multi-domain]  Cd Length: 295  Bit Score: 252.62  E-value: 6.39e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212  38 ENLLLVSTLDGSLHALSKQTGDLKWTL-RDDPVIEGPMY----VTEMAFLSDPADGSLYILGtQKQQGLMKLPFTIPELV 112
Cdd:cd09769    1 EDLLLVSTVDGGLHAVDRKTGKILWSLkAEDPLVEVPHHstlsIDGPTFIVEPRDGSLYVLN-PGNEGLKKLPFTIPQLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 113 HASPCRSSDGVFYTGRKQDAWFVVDPESGETQMTLTTEGP--------------------STPRLYIGRTQYTVTMHDPR 172
Cdd:cd09769   80 QSSPCRSSDGILYTGSKQTTWYTVDPRTGEKIQVLGSGGAdsncpescvdpdddeqsecsSSSTIYIGRTEYTVTIYDSK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 173 APALRWNTTYRRYSAPPMDGSPGKYMS------HLASCGMGLLLTVDPGSGTVLWTQDLGVPVMGVYTWHQ--DGLRQLP 244
Cdd:cd09769  160 TREPIWNVTYSDYTPNSNDRDLQSQYSktydlrYIASSSDGSLVTFDRDTGRVLWVQNLPSPVVAVFDVLRpePGLVKLP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 245 HLTLARDTLHFLAlrwghirlpasgprDTATLFSTLDTQLLMTLYVGK-DETGFYvskalvhtgvalvprgltlapadgp 323
Cdd:cd09769  240 FPPVALETLQYLE--------------DESPDFSSSEDKLRPTVYIGQtENGGLY------------------------- 280

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 767988212 324 ttdevtlqvsgeregspstavrypsgsvALPSQWLLIGHHELP 366
Cdd:cd09769  281 ----------------------------ALSSKELLIGVHELP 295
 
Name Accession Description Interval E-value
Luminal_IRE1 cd09769
The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, ...
 38-366 6.39e-80

The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, Inositol-requiring protein 1; The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), a serine/threonine protein kinase (STK) and a type I transmembrane protein that is localized in the endoplasmic reticulum (ER). IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is a kinase receptor that also contains an endoribonuclease domain in the cytoplasmic side. It plays roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1 acts as an ER stress sensor and is the oldest and most conserved component of the UPR in eukaryotes. During ER stress, IRE1 dimerizes through its luminal domain and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). IRE1alpha is expressed in all cells and tissues while IRE1beta is found only in intestinal epithelial cells.


Pssm-ID: 188875 [Multi-domain]  Cd Length: 295  Bit Score: 252.62  E-value: 6.39e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212  38 ENLLLVSTLDGSLHALSKQTGDLKWTL-RDDPVIEGPMY----VTEMAFLSDPADGSLYILGtQKQQGLMKLPFTIPELV 112
Cdd:cd09769    1 EDLLLVSTVDGGLHAVDRKTGKILWSLkAEDPLVEVPHHstlsIDGPTFIVEPRDGSLYVLN-PGNEGLKKLPFTIPQLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 113 HASPCRSSDGVFYTGRKQDAWFVVDPESGETQMTLTTEGP--------------------STPRLYIGRTQYTVTMHDPR 172
Cdd:cd09769   80 QSSPCRSSDGILYTGSKQTTWYTVDPRTGEKIQVLGSGGAdsncpescvdpdddeqsecsSSSTIYIGRTEYTVTIYDSK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 173 APALRWNTTYRRYSAPPMDGSPGKYMS------HLASCGMGLLLTVDPGSGTVLWTQDLGVPVMGVYTWHQ--DGLRQLP 244
Cdd:cd09769  160 TREPIWNVTYSDYTPNSNDRDLQSQYSktydlrYIASSSDGSLVTFDRDTGRVLWVQNLPSPVVAVFDVLRpePGLVKLP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 245 HLTLARDTLHFLAlrwghirlpasgprDTATLFSTLDTQLLMTLYVGK-DETGFYvskalvhtgvalvprgltlapadgp 323
Cdd:cd09769  240 FPPVALETLQYLE--------------DESPDFSSSEDKLRPTVYIGQtENGGLY------------------------- 280

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 767988212 324 ttdevtlqvsgeregspstavrypsgsvALPSQWLLIGHHELP 366
Cdd:cd09769  281 ----------------------------ALSSKELLIGVHELP 295
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
 30-192 2.22e-03

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 40.69  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212   30 PQVHtlrpENLLLVSTLDGSLHALSKQTGDLKWTL-RDDPVI----EGPMYVTEMAFLSDPADGSLYIL----GTQKQQG 100
Cdd:TIGR03300 141 PLVA----NGLVVVRTNDGRLTALDAATGERLWTYsRVTPPLtlrgSASPVIADGGVLVGFAGGKLVALdlqtGQPLWEQ 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212  101 LMKLPFTIPEL-----VHASPCRSSDGVF---YTGRKqdawFVVDPESGETQMTLTTEGPSTP-----RLYIGRTQYTVT 167
Cdd:TIGR03300 217 RVALPKGRTELerlvdVDGDPVVDGGQVYavsYQGRV----AALDLRSGRVLWKRDASSYQGPavddnRLYVTDADGVVV 292

                         170       180
                  ....*....|....*....|....*...
gi 767988212  168 MHDPRAPALRWNTT---YRRYSAPPMDG 192
Cdd:TIGR03300 293 ALDRRSGSELWKNDelkYRQLTAPAVLG 320
PQQ smart00564
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ...
 38-63 4.23e-03

beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.


Pssm-ID: 128836 [Multi-domain]  Cd Length: 33  Bit Score: 34.82  E-value: 4.23e-03
                           10        20
                   ....*....|....*....|....*.
gi 767988212    38 ENLLLVSTLDGSLHALSKQTGDLKWT 63
Cdd:smart00564   6 DGTVYVGSTDGTLYALDAKTGEILWT 31
 
Name Accession Description Interval E-value
Luminal_IRE1 cd09769
The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, ...
 38-366 6.39e-80

The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, Inositol-requiring protein 1; The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), a serine/threonine protein kinase (STK) and a type I transmembrane protein that is localized in the endoplasmic reticulum (ER). IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is a kinase receptor that also contains an endoribonuclease domain in the cytoplasmic side. It plays roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1 acts as an ER stress sensor and is the oldest and most conserved component of the UPR in eukaryotes. During ER stress, IRE1 dimerizes through its luminal domain and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). IRE1alpha is expressed in all cells and tissues while IRE1beta is found only in intestinal epithelial cells.


Pssm-ID: 188875 [Multi-domain]  Cd Length: 295  Bit Score: 252.62  E-value: 6.39e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212  38 ENLLLVSTLDGSLHALSKQTGDLKWTL-RDDPVIEGPMY----VTEMAFLSDPADGSLYILGtQKQQGLMKLPFTIPELV 112
Cdd:cd09769    1 EDLLLVSTVDGGLHAVDRKTGKILWSLkAEDPLVEVPHHstlsIDGPTFIVEPRDGSLYVLN-PGNEGLKKLPFTIPQLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 113 HASPCRSSDGVFYTGRKQDAWFVVDPESGETQMTLTTEGP--------------------STPRLYIGRTQYTVTMHDPR 172
Cdd:cd09769   80 QSSPCRSSDGILYTGSKQTTWYTVDPRTGEKIQVLGSGGAdsncpescvdpdddeqsecsSSSTIYIGRTEYTVTIYDSK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 173 APALRWNTTYRRYSAPPMDGSPGKYMS------HLASCGMGLLLTVDPGSGTVLWTQDLGVPVMGVYTWHQ--DGLRQLP 244
Cdd:cd09769  160 TREPIWNVTYSDYTPNSNDRDLQSQYSktydlrYIASSSDGSLVTFDRDTGRVLWVQNLPSPVVAVFDVLRpePGLVKLP 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 245 HLTLARDTLHFLAlrwghirlpasgprDTATLFSTLDTQLLMTLYVGK-DETGFYvskalvhtgvalvprgltlapadgp 323
Cdd:cd09769  240 FPPVALETLQYLE--------------DESPDFSSSEDKLRPTVYIGQtENGGLY------------------------- 280

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 767988212 324 ttdevtlqvsgeregspstavrypsgsvALPSQWLLIGHHELP 366
Cdd:cd09769  281 ----------------------------ALSSKELLIGVHELP 295
Luminal_IRE1_like cd09213
The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The ...
 40-233 1.98e-21

The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), eukaryotic translation Initiation Factor 2-Alpha Kinase 3 (EIF2AK3), and similar proteins. IRE1 and EIF2AK3 are serine/threonine protein kinases (STKs) and are type I transmembrane proteins that are localized in the endoplasmic reticulum (ER). They are kinase receptors that are activated through the release of BiP, a chaperone bound to their luminal domains under unstressed conditions. This results in dimerization through their luminal domains, allowing trans-autophosphorylation of their kinase domains and activation. They play roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), contains an endoribonuclease domain in its cytoplasmic side and acts as an ER stress sensor. It is the oldest and most conserved component of the UPR in eukaryotes. Its activation results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. EIF2AK3, also called PKR-like Endoplasmic Reticulum Kinase (PERK), phosphorylates the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. It functions as the central regulator of translational control during the UPR pathway. In addition to the eIF-2 alpha subunit, EIF2AK3 also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR.


Pssm-ID: 188873 [Multi-domain]  Cd Length: 312  Bit Score: 95.25  E-value: 1.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212  40 LLLVSTLDGSLHALSKQTGDLKWTLRD-DPVIE-------GPMYVTEMAFLSDP-ADGSLYILGtQKQQGLMKLPFTIPE 110
Cdd:cd09213    1 LLLVATLDGTIYAVDASSGEIQWSFDGgGPLYSsyqssrdGNAESSSTMLIPSLdGDGNLYQHD-KGHGSLQRLPLTIED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 111 LVHASPCRS---SDGVFYTGRKQDAWFVVDPESGETQMTLTTEGP---------------------STPRLYIGRTQYTV 166
Cdd:cd09213   80 LVEASPLVSdtnEDDVVVVGSKRTSVFALDAKTGKIIKTYRADGLpstggsdsdgnstpgpdelqeEEELLYIGRTDYVL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767988212 167 TMHDPRAPALRWNTTYRRYSA---PPMDGSPGKY--MSHLAS------CGMGLLLtVDPGSGTVLWTQDLGVPVMGVY 233
Cdd:cd09213  160 QAIDPRSGKELWNVTYGEYEAltlDADELGTSSSssPLSASFrisenePVPAVYL-LGLQGGKSLWEHLFDSPIVSAF 236
Luminal_EIF2AK3 cd09768
The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, eukaryotic ...
 39-243 3.26e-09

The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3; The Luminal domain is a dimerization domain present in eukaryotic translation Initiation Factor 2-Alpha Kinase 3 (EIF2AK3), also called PKR-like Endoplasmic Reticulum Kinase (PERK). EIF2AK3 is a serine/threonine protein kinase (STK) and a type I transmembrane protein that is localized in the endoplasmic reticulum (ER). As a EIF2AK, it phosphorylates the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis: General Control Non-derepressible-2 (GCN2), protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PERK. PERK contains a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize through its luminal domain and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR.


Pssm-ID: 188874 [Multi-domain]  Cd Length: 301  Bit Score: 58.18  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212  39 NLLLVSTLDGSLHALS-KQTGDLKWTLrddPVIEGPMYVTEmafLSDPA--------------DGSLYilgtQKQQGLMK 103
Cdd:cd09768    1 SLIIVSTLDGKLTALDiENSGKKVWSL---DAGSGPLVSSS---LSTLElinngksvrlipslDGSLY----QFDGESIE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 104 -LPFTIPELVHASpCRSSDGVFYTGRKQDAWFVVDPESGETQMTLTTEG--PST--------PRLYIGRTQYTVTMHDPR 172
Cdd:cd09768   71 aIPFTAESLLSSS-YKLGDDSVLVGGKEVTSYGINPYTGKLRYICSAEGckSSDteenesndDVLIVRRTTQTVRAVDPR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212 173 APALRWNTTYRRYS---APPMDGSPG------KYMSH---LASCGMGLLLTVDPGS-GTVLWTQDLGVPVMGVYTWHQDG 239
Cdd:cd09768  150 TGSERWNLSVGQYElslVGSIECKLGeedesnSAVSDveiKVSVPDGKIMAVSKSApGRLIWEYKFESPIASAWQLSDGK 229


                 ....
gi 767988212 240 LRQL 243
Cdd:cd09768  230 LRPI 233
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
 30-192 2.22e-03

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 40.69  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212   30 PQVHtlrpENLLLVSTLDGSLHALSKQTGDLKWTL-RDDPVI----EGPMYVTEMAFLSDPADGSLYIL----GTQKQQG 100
Cdd:TIGR03300 141 PLVA----NGLVVVRTNDGRLTALDAATGERLWTYsRVTPPLtlrgSASPVIADGGVLVGFAGGKLVALdlqtGQPLWEQ 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767988212  101 LMKLPFTIPEL-----VHASPCRSSDGVF---YTGRKqdawFVVDPESGETQMTLTTEGPSTP-----RLYIGRTQYTVT 167
Cdd:TIGR03300 217 RVALPKGRTELerlvdVDGDPVVDGGQVYavsYQGRV----AALDLRSGRVLWKRDASSYQGPavddnRLYVTDADGVVV 292

                         170       180
                  ....*....|....*....|....*...
gi 767988212  168 MHDPRAPALRWNTT---YRRYSAPPMDG 192
Cdd:TIGR03300 293 ALDRRSGSELWKNDelkYRQLTAPAVLG 320
PQQ smart00564
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ...
 38-63 4.23e-03

beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.


Pssm-ID: 128836 [Multi-domain]  Cd Length: 33  Bit Score: 34.82  E-value: 4.23e-03
                           10        20
                   ....*....|....*....|....*.
gi 767988212    38 ENLLLVSTLDGSLHALSKQTGDLKWT 63
Cdd:smart00564   6 DGTVYVGSTDGTLYALDAKTGEILWT 31
PQQ smart00564
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ...
 116-148 6.46e-03

beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.


Pssm-ID: 128836 [Multi-domain]  Cd Length: 33  Bit Score: 34.43  E-value: 6.46e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767988212   116 PCRSSDGVFYTGRKQDAWFVVDPESGETQMTLT 148
Cdd:smart00564   1 PVVLSDGTVYVGSTDGTLYALDAKTGEILWTYK 33
 
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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