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Conserved domains on  [gi|1831513401|ref|NP_001367466|]
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Inositol 1,4,5-trisphosphate receptor itr-1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 33-271 6.52e-91

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity.


:

Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 294.02  E-value: 6.52e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401   33 NNGNLHIGDIISLYTESSSNqeqrGFLSTLGLVDDRCIVELKDGRPESPPKKFRDCLFKVCPVNRYAAQKHLWTEQKRFQ 112
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVN----GFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  113 TGDSMFDDdlmnkLKVAADKEREENesefqktlgnvIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKVYLDRAGN-E 191
Cdd:pfam08709   77 NGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgE 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  192 GSWFIIEPAYKHYAIGDNVSAGNKISLIPNSVSTTqaghvksqLHL-SSFNLLDHQSaAEVNCLNEPTEWQVFMFLLFDE 270
Cdd:pfam08709  141 GCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIF--------LHTtSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCE 211


                   .
gi 1831513401  271 N 271
Cdd:pfam08709  212 N 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 547-746 6.18e-65

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 218.99  E-value: 6.18e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  547 LLIDCILFVTNSSD---HLADPLKISDFSPSRDRQKLLREQEVLNQVF---LLLKAPFLprqgttelGPLLSsPSELSDS 620
Cdd:pfam01365    1 LLRDLIFFFAGPEEeelHEEDLLKLMNNKPLRQRQNLMREQGVLETVMeviDLLGAPFT--------GALLF-AEDLGEE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  621 RNEIFKTMFQLCYCLLKYSQVSYRKNQEFLAEKFGEIQEQIGFDLMAE---DTMTAVLHNNPKLLEKYVKTPHVERFVEL 697
Cdd:pfam01365   72 KNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISL 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1831513401  698 VRNNRQG-KFLDYLADLCVCRGEANKKIQELICTSVLSskHRDIFMDTKI 746
Cdd:pfam01365  152 LRKHGRDpRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 274-502 1.73e-57

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


:

Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 196.82  E-value: 1.73e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  274 NSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvvFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNKAYRFKH 353
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-----FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  354 LATDMYLSAEPSQvqvkpamngrrasliysktNNPMAMYSDGPNGVTNESTDTTQQNipsvwvlgptksefpeEDANLLF 433
Cdd:pfam02815   76 LTTGRYLHSHEEQ-------------------KPPLVEKEDWQKEVSAYGFRGFPGD----------------NDIVEIF 120

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513401  434 QLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATNATEKQNlhyssKNEKGWVKVICEKNRVDKETFAL 502
Cdd:pfam02815  121 EKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW-----GFGPEQQKVTCAKEGHMDDALTL 184
RYDR_ITPR super family cl03182
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1280-1427 9.30e-07

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


The actual alignment was detected with superfamily member pfam01365:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 51.43  E-value: 9.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401 1280 KPDTMNQQLLKNMRVYEVVLEFISV--------------PHDKKHDHdMMKLITLSHEFLRSFCKTNKENQSRLYKFISY 1345
Cdd:pfam01365   29 KPLRQRQNLMREQGVLETVMEVIDLlgapftgallfaedLGEEKNAP-WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDW 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401 1346 EKDAKEGMLRVETIEEVGTlvAIFRNNRELASN-VPEELIAHIVGLIEHNSRNPIFLELLQALvCVYDKE-IESGQekva 1423
Cdd:pfam01365  108 LQSQLGSPSLAEGTLDVLT--ALLMDNPELLLNyIKECHIKSFISLLRKHGRDPRYLDFLSDL-CVCNGEaVRENQ---- 180


                   ....
gi 1831513401 1424 NEIC 1427
Cdd:pfam01365  181 NLIC 184
 
Name Accession Description Interval E-value
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 33-271 6.52e-91

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity.


Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 294.02  E-value: 6.52e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401   33 NNGNLHIGDIISLYTESSSNqeqrGFLSTLGLVDDRCIVELKDGRPESPPKKFRDCLFKVCPVNRYAAQKHLWTEQKRFQ 112
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVN----GFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  113 TGDSMFDDdlmnkLKVAADKEREENesefqktlgnvIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKVYLDRAGN-E 191
Cdd:pfam08709   77 NGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgE 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  192 GSWFIIEPAYKHYAIGDNVSAGNKISLIPNSVSTTqaghvksqLHL-SSFNLLDHQSaAEVNCLNEPTEWQVFMFLLFDE 270
Cdd:pfam08709  141 GCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIF--------LHTtSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCE 211


                   .
gi 1831513401  271 N 271
Cdd:pfam08709  212 N 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 547-746 6.18e-65

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 218.99  E-value: 6.18e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  547 LLIDCILFVTNSSD---HLADPLKISDFSPSRDRQKLLREQEVLNQVF---LLLKAPFLprqgttelGPLLSsPSELSDS 620
Cdd:pfam01365    1 LLRDLIFFFAGPEEeelHEEDLLKLMNNKPLRQRQNLMREQGVLETVMeviDLLGAPFT--------GALLF-AEDLGEE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  621 RNEIFKTMFQLCYCLLKYSQVSYRKNQEFLAEKFGEIQEQIGFDLMAE---DTMTAVLHNNPKLLEKYVKTPHVERFVEL 697
Cdd:pfam01365   72 KNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISL 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1831513401  698 VRNNRQG-KFLDYLADLCVCRGEANKKIQELICTSVLSskHRDIFMDTKI 746
Cdd:pfam01365  152 LRKHGRDpRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 274-502 1.73e-57

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 196.82  E-value: 1.73e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  274 NSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvvFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNKAYRFKH 353
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-----FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  354 LATDMYLSAEPSQvqvkpamngrrasliysktNNPMAMYSDGPNGVTNESTDTTQQNipsvwvlgptksefpeEDANLLF 433
Cdd:pfam02815   76 LTTGRYLHSHEEQ-------------------KPPLVEKEDWQKEVSAYGFRGFPGD----------------NDIVEIF 120

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513401  434 QLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATNATEKQNlhyssKNEKGWVKVICEKNRVDKETFAL 502
Cdd:pfam02815  121 EKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW-----GFGPEQQKVTCAKEGHMDDALTL 184
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 268-510 5.69e-56

MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor (ITPR); Inositol 1,4,5 trisphosphate receptors (ITPRs) are a family of endoplasmic reticulum Ca2+ channels essential for the control of intracellular Ca2+ levels in virtually every mammalian cell type. Calcium-mediated signaling through ITPRs is essential for the regulation of numerous physiological processes, including fertilization, muscle contraction, apoptosis, secretion, and synaptic plasticity. The ITPR family includes three isoforms (ITPR1, ITPR2 and ITPR3), which can control different cellular processes due to their unique biophysical properties, subcellular localization, and tissue distribution. ITPRs contain an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467748 [Multi-domain]  Cd Length: 204  Bit Score: 193.34  E-value: 5.69e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  268 FDENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNpptdVVFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNK 347
Cdd:cd23277      3 YKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQ----YVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  348 AYRFKHLATDMYLSAEpsqvqvkpamngrrasLIYSKTNNPMAMYSDGPNGVTNESTDTTQQNipsvwvlgptksefpeE 427
Cdd:cd23277     79 LFRFKHLATGQYLAAE----------------VDPDPTPDPTRSKLRGAPGKPVYCLVSVPHG----------------N 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  428 DANLLFQLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATN-----ATEKQNLHyssknekgwvKVICEKNRVDKETFAL 502
Cdd:cd23277    127 DIASIFELDPTTLQRGDSLVPRSSYVRLRHLCTNTWVHSTNipidkEEEKPVML----------KVGTAPIKEDKEAFAI 196


                   ....*...
gi 1831513401  503 LPVNPDEV 510
Cdd:cd23277    197 VPVSPSEV 204
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 152-293 1.54e-09

MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) superfamily; The MIR superfamily includes dolichyl-phosphate-mannose-protein mannosyltransferases (PMTs), inositol 1,4,5-trisphosphate receptors (ITPRs/IP3R), ryanodine receptors (RyRs), and stromal cell-derived factor 2 (SDF-2)-like proteins. They all contain a MIR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The MIR domain may have a ligand transferase function.


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 58.93  E-value: 1.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  152 GSMVQLLHVKSNKYITVQKNSPAKRERNAMkVYL---DRAGNEGSWFIIEPayKHYAIGDNVSAGNKISLIpnsvsttqa 228
Cdd:cd23263      1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQE-VTFessSRKGDTNGLWIIES--ENGKQGGPVKWGDKIRLR--------- 68

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513401  229 gHVKSQLHLSSFNL-LDHQSAA-EVNCLNEP----TEWQvFMFLLFDENQQNSVKSGDVVRLFHADQQTFL 293
Cdd:cd23263     69 -HLSTGKYLSSEEGkKSPKSNHqEVLCLTDNpdksSLFK-FEPIGSTKYKQKYVKKDSYFRLKHVNTNFWL 137
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1280-1427 9.30e-07

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 51.43  E-value: 9.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401 1280 KPDTMNQQLLKNMRVYEVVLEFISV--------------PHDKKHDHdMMKLITLSHEFLRSFCKTNKENQSRLYKFISY 1345
Cdd:pfam01365   29 KPLRQRQNLMREQGVLETVMEVIDLlgapftgallfaedLGEEKNAP-WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDW 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401 1346 EKDAKEGMLRVETIEEVGTlvAIFRNNRELASN-VPEELIAHIVGLIEHNSRNPIFLELLQALvCVYDKE-IESGQekva 1423
Cdd:pfam01365  108 LQSQLGSPSLAEGTLDVLT--ALLMDNPELLLNyIKECHIKSFISLLRKHGRDPRYLDFLSDL-CVCNGEaVRENQ---- 180


                   ....
gi 1831513401 1424 NEIC 1427
Cdd:pfam01365  181 NLIC 184
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
146-200 2.74e-03

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 37.71  E-value: 2.74e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513401   146 GNVIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKV--YLDRAGNEGSWFIIEPA 200
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVtgYGNPAIDANTLWLIEPV 57
 
Name Accession Description Interval E-value
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 33-271 6.52e-91

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity.


Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 294.02  E-value: 6.52e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401   33 NNGNLHIGDIISLYTESSSNqeqrGFLSTLGLVDDRCIVELKDGRPESPPKKFRDCLFKVCPVNRYAAQKHLWTEQKRFQ 112
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVN----GFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  113 TGDSMFDDdlmnkLKVAADKEREENesefqktlgnvIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKVYLDRAGN-E 191
Cdd:pfam08709   77 NGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgE 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  192 GSWFIIEPAYKHYAIGDNVSAGNKISLIPNSVSTTqaghvksqLHL-SSFNLLDHQSaAEVNCLNEPTEWQVFMFLLFDE 270
Cdd:pfam08709  141 GCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIF--------LHTtSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCE 211


                   .
gi 1831513401  271 N 271
Cdd:pfam08709  212 N 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 547-746 6.18e-65

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 218.99  E-value: 6.18e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  547 LLIDCILFVTNSSD---HLADPLKISDFSPSRDRQKLLREQEVLNQVF---LLLKAPFLprqgttelGPLLSsPSELSDS 620
Cdd:pfam01365    1 LLRDLIFFFAGPEEeelHEEDLLKLMNNKPLRQRQNLMREQGVLETVMeviDLLGAPFT--------GALLF-AEDLGEE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  621 RNEIFKTMFQLCYCLLKYSQVSYRKNQEFLAEKFGEIQEQIGFDLMAE---DTMTAVLHNNPKLLEKYVKTPHVERFVEL 697
Cdd:pfam01365   72 KNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISL 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1831513401  698 VRNNRQG-KFLDYLADLCVCRGEANKKIQELICTSVLSskHRDIFMDTKI 746
Cdd:pfam01365  152 LRKHGRDpRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 274-502 1.73e-57

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 196.82  E-value: 1.73e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  274 NSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvvFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNKAYRFKH 353
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-----FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  354 LATDMYLSAEPSQvqvkpamngrrasliysktNNPMAMYSDGPNGVTNESTDTTQQNipsvwvlgptksefpeEDANLLF 433
Cdd:pfam02815   76 LTTGRYLHSHEEQ-------------------KPPLVEKEDWQKEVSAYGFRGFPGD----------------NDIVEIF 120

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831513401  434 QLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATNATEKQNlhyssKNEKGWVKVICEKNRVDKETFAL 502
Cdd:pfam02815  121 EKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW-----GFGPEQQKVTCAKEGHMDDALTL 184
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 268-510 5.69e-56

MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor (ITPR); Inositol 1,4,5 trisphosphate receptors (ITPRs) are a family of endoplasmic reticulum Ca2+ channels essential for the control of intracellular Ca2+ levels in virtually every mammalian cell type. Calcium-mediated signaling through ITPRs is essential for the regulation of numerous physiological processes, including fertilization, muscle contraction, apoptosis, secretion, and synaptic plasticity. The ITPR family includes three isoforms (ITPR1, ITPR2 and ITPR3), which can control different cellular processes due to their unique biophysical properties, subcellular localization, and tissue distribution. ITPRs contain an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467748 [Multi-domain]  Cd Length: 204  Bit Score: 193.34  E-value: 5.69e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  268 FDENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNpptdVVFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNK 347
Cdd:cd23277      3 YKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQ----YVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  348 AYRFKHLATDMYLSAEpsqvqvkpamngrrasLIYSKTNNPMAMYSDGPNGVTNESTDTTQQNipsvwvlgptksefpeE 427
Cdd:cd23277     79 LFRFKHLATGQYLAAE----------------VDPDPTPDPTRSKLRGAPGKPVYCLVSVPHG----------------N 126

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  428 DANLLFQLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATN-----ATEKQNLHyssknekgwvKVICEKNRVDKETFAL 502
Cdd:cd23277    127 DIASIFELDPTTLQRGDSLVPRSSYVRLRHLCTNTWVHSTNipidkEEEKPVML----------KVGTAPIKEDKEAFAI 196


                   ....*...
gi 1831513401  503 LPVNPDEV 510
Cdd:cd23277    197 VPVSPSEV 204
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 268-515 3.53e-50

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) and similar proteins; ITPR1, also called IP3 receptor isoform 1 (IP3R 1), or InsP3R1, or type 1 inositol 1,4,5-trisphosphate receptor, or type 1 InsP3 receptor, is an intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. It is involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1. It plays a role in endoplasmic reticulum (ER) stress-induced apoptosis. ITPR1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467758 [Multi-domain]  Cd Length: 222  Bit Score: 177.57  E-value: 3.53e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  268 FDENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvVFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNK 347
Cdd:cd23287      3 WSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQH----VFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  348 AYRFKHLATDMYLSAEPSQVQvkpamngrrasliySKTNNPMAMYSDGPNGVTNESTDTTQQNIPSVWVLGPTKSefpee 427
Cdd:cd23287     79 LFRFKHLATGHYLAAEVDPDF--------------EEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGN----- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  428 DANLLFQLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATNATekqnlhySSKNEKGWV--KVICEKNRVDKETFALLPV 505
Cdd:cd23287    140 DISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIP-------IDKEEEKPVmlKIGTSPLKEDKEAFAIVPV 212

                          250
                   ....*....|
gi 1831513401  506 NPDEVRDLDF 515
Cdd:cd23287    213 SPAEVRDLDF 222
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 260-510 1.62e-44

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) and similar proteins; ITPR2, also called IP3 receptor isoform 2 (IP3R 2), or InsP3R2, or type 2 inositol 1,4,5-trisphosphate receptor, or type 2 InsP3 receptor, is a key regulator for the activity of calcium ion transmembrane transportation, which plays a critical role in cell cycle and proliferation. It is a receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of cAMP-dependent protein kinase (PKA). ITPR2 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467759 [Multi-domain]  Cd Length: 222  Bit Score: 161.36  E-value: 1.62e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  260 WQVFMFLLFDENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvVFLRMTNRPSAADATSSRALWEVQVVQTNAYR 339
Cdd:cd23288      1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQH----IFLRTTLRQSATSATSSKALWEIEVVHYDPCR 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  340 GGTAKWNKAYRFKHLATDMYLSAEpsqvqVKPAmngrrasliYSKTNNPMAMYSDGpNGVTNESTDTTQQNIPSVWVLGP 419
Cdd:cd23288     77 GGAGQWNSLFRFKHLATGNYLAAE-----VNPD---------YRDAQNEGKAVNDG-DSPTSKKKRQAAEKIMYTLVSVP 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  420 TKSefpeeDANLLFQLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATnatekqNLHYSSKNEKG-WVKVICEKNRVDKE 498
Cdd:cd23288    142 HGN-----DIASLFELDATTLQRADCLVPRNSYVRLRHLCTNTWVTST------SIPIDTEEERPvMLKIGTCQTKEDKE 210

                          250
                   ....*....|..
gi 1831513401  499 TFALLPVNPDEV 510
Cdd:cd23288    211 AFAIVSVPLSEV 222
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 270-510 1.04e-38

MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate receptor Itr-1 and similar proteins; Itr-1, also called IP3 receptor, or IP3R, or InsP3R, or LET-23 fertility effector 1, is a receptor for inositol 1,4,5-trisphosphate, a second messenger that regulates intracellular calcium homeostasis. It binds in vitro to both inositol 1,4,5-trisphosphate (1,4,5-InsP3) and inositol 2,4,5-trisphosphate (2,4,5-InsP3) with high affinity. It can also bind inositol 1,3,4,5-tetrakisphosphate (1,3,4,5-InsP4) and inositol 4,5-bisphosphate (4,5-InsP2), but with lower affinity. Itr-1 acts as a timekeeper/rhythm generator via calcium signaling, affecting the defecation cycle and pharyngeal pumping. It affects normal hermaphrodite and male fertility as a participant in intracellular signaling by acting downstream of let-23/lin-3 which regulates ovulation, spermathecal valve dilation and male mating behavior. It plays an important role in early embryonic development. It controls epidermal cell migration and may also regulate filopodial protrusive activity during epithelial morphogenesis. Itr-1 functions as a component of inositol trisphosphate (IP3)-mediated downstream signaling pathways that controls amphid sensory neuronal (ASH)-mediated response to nose touch and benzaldehyde, but no other ASH-mediated responses. Itr-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467751 [Multi-domain]  Cd Length: 199  Bit Score: 143.68  E-value: 1.04e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  270 ENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNPPTDVV-----FLRMTNRPSAADATSSRALWEVQVVQTnAYRGGTAK 344
Cdd:cd23280      1 KENENFLKGGDVVRLFHKELEAYLSAEGSFVDEVLTEDVhlrvrPVDDRKPRTLFPPTSGDTFWQIEKEDT-PLKGGVIK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  345 WNKAYRFKHLATDMYLSAEPSqvqvkpamngrrasliysktnnpmamysdgpngvtnestdttqqNIPSVWVLGPTKSef 424
Cdd:cd23280     80 WGDQCRLRHLPTGKYLAVDDK--------------------------------------------TGNGKVVLTSDPS-- 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  425 peeDANLLFQLDPSTFMKSnKEVPRRSYVRLLHQSSDKWVHATNATEKQNLHYS----SKNEKGWVKVICEKNRVDKETF 500
Cdd:cd23280    114 ---DPSTVFRLHPVTKETS-EEVKFGSYVRIEHVATGTWLHAETDEELRRSKKSpaglSWDGAKLRKVSLSLERQDDDAF 189

                          250
                   ....*....|
gi 1831513401  501 ALLPVNPDEV 510
Cdd:cd23280    190 TIQEVDPDLV 199
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 266-510 1.47e-38

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) and similar proteins; ITPR3, also called IP3 receptor isoform 3 (IP3R 3), or InsP3R3, or type 3 inositol 1,4,5-trisphosphate receptor, or type 3 InsP3 receptor, acts as anti-oncogenic channel by propelling pro-apoptotic Ca2+ signals to mitochondria. It is the principal intracellular Ca2+ release channel in cholangiocytes and plays a particularly important role in cancer. ITPR3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467760 [Multi-domain]  Cd Length: 215  Bit Score: 144.03  E-value: 1.47e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  266 LLFDENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvVFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKW 345
Cdd:cd23289      1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQ----VFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  346 NKAYRFKHLATDMYLSAEpsqvqVKPAMNGRrasliySKTNNPMAMYSDGPNGVTNestdtTQQNIPSVWVLGPTKSefp 425
Cdd:cd23289     77 NGLYRFKHLATGNYLAAE-----ENPSYKGD------ASDPKAAGMGAQSRTGRRN-----AGEKIKYCLVAVPHGN--- 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  426 eeDANLLFQLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATNATekqnlhySSKNEKGWVKVI---CeKNRVDKETFAL 502
Cdd:cd23289    138 --DIASLFELDPTTLQKTDSFVPRNSYVRLRHLCTNTWIQSTNVP-------IDIEEERPIRLMlgtC-PTKEDKEAFAI 207


                   ....*...
gi 1831513401  503 LPVNPDEV 510
Cdd:cd23289    208 VSVPVSEI 215
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 279-507 2.48e-22

MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) superfamily; The MIR superfamily includes dolichyl-phosphate-mannose-protein mannosyltransferases (PMTs), inositol 1,4,5-trisphosphate receptors (ITPRs/IP3R), ryanodine receptors (RyRs), and stromal cell-derived factor 2 (SDF-2)-like proteins. They all contain a MIR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The MIR domain may have a ligand transferase function.


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 95.53  E-value: 2.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  279 GDVVRLFHADQQTFLTLDTIPKQ-NPPTDVVFLRMTNRPsaadaTSSRALWEVQVVQTNAyrGGTAKWNKAYRFKHLATD 357
Cdd:cd23263      1 GDVIWLKHSETGKYLHSHRKNYPtGSGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  358 MYLSAEPSQVQvkPAMNGRRasliysktnnpmamysdgpngvtnestdttqqnipsVWVLGptksefPEEDANLLFQLDP 437
Cdd:cd23263     74 KYLSSEEGKKS--PKSNHQE------------------------------------VLCLT------DNPDKSSLFKFEP 109

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513401  438 STFMK-SNKEVPRRSYVRLLHQSSDKWVHATNATEKQnlhysskNEKGWVKVICEKNRvdKETFALLPVNP 507
Cdd:cd23263    110 IGSTKyKQKYVKKDSYFRLKHVNTNFWLHSHEKKFNI-------NNKTQQEVICHGER--EEVFKLWKAEL 171
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 152-293 1.54e-09

MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) superfamily; The MIR superfamily includes dolichyl-phosphate-mannose-protein mannosyltransferases (PMTs), inositol 1,4,5-trisphosphate receptors (ITPRs/IP3R), ryanodine receptors (RyRs), and stromal cell-derived factor 2 (SDF-2)-like proteins. They all contain a MIR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The MIR domain may have a ligand transferase function.


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 58.93  E-value: 1.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  152 GSMVQLLHVKSNKYITVQKNSPAKRERNAMkVYL---DRAGNEGSWFIIEPayKHYAIGDNVSAGNKISLIpnsvsttqa 228
Cdd:cd23263      1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQE-VTFessSRKGDTNGLWIIES--ENGKQGGPVKWGDKIRLR--------- 68

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831513401  229 gHVKSQLHLSSFNL-LDHQSAA-EVNCLNEP----TEWQvFMFLLFDENQQNSVKSGDVVRLFHADQQTFL 293
Cdd:cd23263     69 -HLSTGKYLSSEEGkKSPKSNHqEVLCLTDNpdksSLFK-FEPIGSTKYKQKYVKKDSYFRLKHVNTNFWL 137
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1280-1427 9.30e-07

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3.


Pssm-ID: 460175  Cd Length: 199  Bit Score: 51.43  E-value: 9.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401 1280 KPDTMNQQLLKNMRVYEVVLEFISV--------------PHDKKHDHdMMKLITLSHEFLRSFCKTNKENQSRLYKFISY 1345
Cdd:pfam01365   29 KPLRQRQNLMREQGVLETVMEVIDLlgapftgallfaedLGEEKNAP-WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDW 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401 1346 EKDAKEGMLRVETIEEVGTlvAIFRNNRELASN-VPEELIAHIVGLIEHNSRNPIFLELLQALvCVYDKE-IESGQekva 1423
Cdd:pfam01365  108 LQSQLGSPSLAEGTLDVLT--ALLMDNPELLLNyIKECHIKSFISLLRKHGRDPRYLDFLSDL-CVCNGEaVRENQ---- 180


                   ....
gi 1831513401 1424 NEIC 1427
Cdd:pfam01365  181 NLIC 184
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 276-366 1.74e-04

MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, also called RYR-1, or skeletal muscle calcium release channel, or skeletal muscle ryanodine receptor, or skeletal muscle-type ryanodine receptor, or type 1 ryanodine receptor, is a calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. It can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. It is required for normal embryonic development of muscle fibers and skeletal muscle, as well as for normal heart morphogenesis, skin development and ossification during embryogenesis. RYR-1 forms homotetramer and can also form heterotetramers with RYR-2. RYR-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467761 [Multi-domain]  Cd Length: 192  Bit Score: 44.49  E-value: 1.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  276 VKSGDVVRLFHADQQTFLTLDTIPKQNPptdvvfLRMTNRPSAADATSSRALWEVQVVQTnAYRGGTAKWNKAYRFKHLA 355
Cdd:cd23290      8 VTGGHVLRLFHGHMDECLTISAADSDDQ------RRLVYYEGGAVCTHARSLWRLEPLRI-SWSGSHLRWGQPLRIRHVT 80

                           90
                   ....*....|.
gi 1831513401  356 TDMYLSAEPSQ 366
Cdd:cd23290     81 TGRYLALTEDQ 91
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 279-366 2.19e-04

MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, also called RYR-3, or brain ryanodine receptor-calcium release channel, or brain-type ryanodine receptor, or type 3 ryanodine receptor, is a calcium channel that plays a role in cellular calcium signaling. It mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. It also mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. RYR-3 forms homotetramer and also forms heterotetramer with RYR-2. RYR-3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467763 [Multi-domain]  Cd Length: 187  Bit Score: 44.13  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  279 GDVVRLFHADQQTFltldTIPKQNPpTDVVFlRMTNRPSAADATSSRALWEVQVVQTnAYRGGTAKWNKAYRFKHLATDM 358
Cdd:cd23292      6 GHVVRLFHGHDECL----TIPSTDQ-SDEQH-RVVNYEAGGAGTRARSLWRLEPLRI-SWSGSHIRWGQTFRLRHLTTGH 78


                   ....*...
gi 1831513401  359 YLSAEPSQ 366
Cdd:cd23292     79 YLALTEDQ 86
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 279-366 2.33e-03

MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also called RYRs) are intracellular Ca(2+) release channels located on the sarco/endoplasmic reticulum (SR/ER). They release calcium Ca(2+) intracellular stores to activate critical functions including muscle contraction and neurotransmitter release. The family includes three closely homologous proteins, RyR1, RyR2 and RyR3. RyR1 is present in skeletal muscle; RyR2 is in heart muscle; and RyR3 is expressed at low levels in many tissues including brain, smooth muscle, and slow-twitch skeletal muscle. RYR2 is the major cellular mediator of calcium-induced calcium release (CICR) in animal cells. RyR1 and RyR2 release Ca2+ from the ER in response to excitation of muscle membranes to promote muscle contraction. RYR3 is involved in force production and calcium handling in extraocular muscle. RYRs contain an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467749 [Multi-domain]  Cd Length: 180  Bit Score: 40.75  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  279 GDVVRLFHADQQTFLtldTIP----KQNPPTDVVFlrmtnrPSAADATSSRALWEVQVVQTnAYRGGTAKWNKAYRFKHL 354
Cdd:cd23278      2 GDVLRLFHGHMDECL---TIPaagsKEDQHRTVIY------EGGAVSTHARSLWRLELLRI-KWSGSHIGWGQPFRLRHV 71

                           90
                   ....*....|..
gi 1831513401  355 ATDMYLSAEPSQ 366
Cdd:cd23278     72 TTGRYLALTEDR 83
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
146-200 2.74e-03

Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 37.71  E-value: 2.74e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831513401   146 GNVIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKV--YLDRAGNEGSWFIIEPA 200
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVtgYGNPAIDANTLWLIEPV 57
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 138-262 5.36e-03

MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) superfamily; The MIR superfamily includes dolichyl-phosphate-mannose-protein mannosyltransferases (PMTs), inositol 1,4,5-trisphosphate receptors (ITPRs/IP3R), ryanodine receptors (RyRs), and stromal cell-derived factor 2 (SDF-2)-like proteins. They all contain a MIR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The MIR domain may have a ligand transferase function.


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 39.67  E-value: 5.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831513401  138 ESEfQKTLGNVIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKVYLDRAGNEGSWFIIEPAYKHYAIGDNVSAGNKIS 217
Cdd:cd23263     49 ESE-NGKQGGPVKWGDKIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDKSSLFKFEPIGSTKYKQKYVKKDSYFR 127

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1831513401  218 LIpnsvsttqagHVKSQLHLSSFNLLDHQSAA---EVNCLNEP----TEWQV 262
Cdd:cd23263    128 LK----------HVNTNFWLHSHEKKFNINNKtqqEVICHGEReevfKLWKA 169
 
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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