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Conserved domains on  [gi|1720417179|ref|XP_030111059|]
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inositol 1,4,5-trisphosphate receptor type 1 isoform X13 [Mus musculus]

Protein Classification

MIR and RYDR_ITPR domain-containing protein( domain architecture ID 11696449)

protein containing domains MIR, RYDR_ITPR, RIH_assoc, and Ion_trans

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 162-383 3.91e-163

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: 501.91  E-value: 3.91e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  162 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 241
Cdd:cd23287      1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  242 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 321
Cdd:cd23287     81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417179  322 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 383
Cdd:cd23287    161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 414-608 4.51e-81

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: 265.60  E-value: 4.51e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  414 LLEDLVYFVTGGTNS---GQDVLEVVFSKPNRERQKLMREQNILKQIFK---LLQAPFTdcgdGPMLRLEELGDQRHAPF 487
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  488 RHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAE---DTITALLHNNRKLLEKHITAAEIDTFVSLVRKN- 563
Cdd:pfam01365   77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKHg 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720417179  564 REPRFLDYLSDLCVSMNKSIPVTQELICKAVLNptNADILIETKL 608
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
Ins145_P3_rec super family cl48031
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 1-167 1.70e-67

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.


The actual alignment was detected with superfamily member pfam08709:

Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 227.38  E-value: 1.70e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179    1 MNRYSAQKQFWKA--AKPGANSTTDAvllnkLHHAADLEKKQNetenrkllgtvIQYGNVIQLLHLKSNKYLTVNKRLPA 78
Cdd:pfam08709   59 ANSYAAQKELWSAgnRSPNGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179   79 LLEKNAMRVTLDEAGN-EGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLH-ASSHQLVDNPGcNEVNSVNCNTSW 156
Cdd:pfam08709  123 LRDKNAMRVVLDEAGNgEGCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSW 201

                          170
                   ....*....|.
gi 1720417179  157 KIVLFMKWSDN 167
Cdd:pfam08709  202 KMEPFMSGCEN 212
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1909-2016 1.20e-39

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815.


:

Pssm-ID: 462482  Cd Length: 98  Bit Score: 143.05  E-value: 1.20e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 1909 ITIMQPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINEKNVALINQTLESLT 1987
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 1720417179 1988 EYCQGPCHENQNCIatHESNGIDIITALI 2016
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2297-2547 2.13e-22

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


:

Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 98.49  E-value: 2.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2297 QPTLFLLGAFNVCNKIIFLMSFV------GNCGTFTRGYRAMVLDVEFLYHLLYLLICAM----GLFVHEFFYSLLLFDL 2366
Cdd:pfam00520   29 EPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPWNILDFVVVLPSLISLVLSSVgslsGLRVLRLLRLLRLLRL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2367 VYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFilevdrlpnetavpetgeslandflysdvcrve 2446
Cdd:pfam00520  109 IRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL--------------------------------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2447 tgenctspapkeellPAEETEQDKEHTCETLLMCIVTVLShgLRSGGGVGDVLRKPSKEEPLFAArVIYDLLFFFMVIII 2526
Cdd:pfam00520  156 ---------------KTWENPDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFL 217

                          250       260
                   ....*....|....*....|.
gi 1720417179 2527 VLNLIFGVIIDTFADLRSEKQ 2547
Cdd:pfam00520  218 LLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR super family cl03182
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1140-1259 2.02e-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: 53.74  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 1140 SVRKSRKQQQRLLRNMGAHAVVLE---LLQIPY-------EKAEDTKM---QEIMRLAHEFLQNFCAGNQQNQALLHKHI 1206
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMEvidLLGAPFtgallfaEDLGEEKNapwKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417179 1207 NLFLNP--------GILEavTMQHIFMNNFQLC-SEINERVVQHFVHCIETHGRNVQYIKFL 1259
Cdd:pfam01365  106 DWLQSQlgspslaeGTLD--VLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 162-383 3.91e-163

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: 501.91  E-value: 3.91e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  162 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 241
Cdd:cd23287      1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  242 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 321
Cdd:cd23287     81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417179  322 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 383
Cdd:cd23287    161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 414-608 4.51e-81

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: 265.60  E-value: 4.51e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  414 LLEDLVYFVTGGTNS---GQDVLEVVFSKPNRERQKLMREQNILKQIFK---LLQAPFTdcgdGPMLRLEELGDQRHAPF 487
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  488 RHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAE---DTITALLHNNRKLLEKHITAAEIDTFVSLVRKN- 563
Cdd:pfam01365   77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKHg 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720417179  564 REPRFLDYLSDLCVSMNKSIPVTQELICKAVLNptNADILIETKL 608
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 170-371 1.83e-76

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: 251.90  E-value: 1.83e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  170 DILKGGDVVRLFHAEQEKFLTCDEHRKKQHvFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATG 249
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  250 HYLAAEVDPdfeeeclefqpsvdpdQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLR 329
Cdd:pfam02815   80 RYLHSHEEQ----------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQ 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720417179  330 HLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIV 371
Cdd:pfam02815  144 HVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 1-167 1.70e-67

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: 227.38  E-value: 1.70e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179    1 MNRYSAQKQFWKA--AKPGANSTTDAvllnkLHHAADLEKKQNetenrkllgtvIQYGNVIQLLHLKSNKYLTVNKRLPA 78
Cdd:pfam08709   59 ANSYAAQKELWSAgnRSPNGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179   79 LLEKNAMRVTLDEAGN-EGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLH-ASSHQLVDNPGcNEVNSVNCNTSW 156
Cdd:pfam08709  123 LRDKNAMRVVLDEAGNgEGCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSW 201

                          170
                   ....*....|.
gi 1720417179  157 KIVLFMKWSDN 167
Cdd:pfam08709  202 KMEPFMSGCEN 212
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1909-2016 1.20e-39

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815.


Pssm-ID: 462482  Cd Length: 98  Bit Score: 143.05  E-value: 1.20e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 1909 ITIMQPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINEKNVALINQTLESLT 1987
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 1720417179 1988 EYCQGPCHENQNCIatHESNGIDIITALI 2016
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2297-2547 2.13e-22

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 98.49  E-value: 2.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2297 QPTLFLLGAFNVCNKIIFLMSFV------GNCGTFTRGYRAMVLDVEFLYHLLYLLICAM----GLFVHEFFYSLLLFDL 2366
Cdd:pfam00520   29 EPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPWNILDFVVVLPSLISLVLSSVgslsGLRVLRLLRLLRLLRL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2367 VYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFilevdrlpnetavpetgeslandflysdvcrve 2446
Cdd:pfam00520  109 IRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL--------------------------------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2447 tgenctspapkeellPAEETEQDKEHTCETLLMCIVTVLShgLRSGGGVGDVLRKPSKEEPLFAArVIYDLLFFFMVIII 2526
Cdd:pfam00520  156 ---------------KTWENPDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFL 217

                          250       260
                   ....*....|....*....|.
gi 1720417179 2527 VLNLIFGVIIDTFADLRSEKQ 2547
Cdd:pfam00520  218 LLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1140-1259 2.02e-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: 53.74  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 1140 SVRKSRKQQQRLLRNMGAHAVVLE---LLQIPY-------EKAEDTKM---QEIMRLAHEFLQNFCAGNQQNQALLHKHI 1206
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMEvidLLGAPFtgallfaEDLGEEKNapwKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417179 1207 NLFLNP--------GILEavTMQHIFMNNFQLC-SEINERVVQHFVHCIETHGRNVQYIKFL 1259
Cdd:pfam01365  106 DWLQSQlgspslaeGTLD--VLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
169-225 2.47e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.57  E-value: 2.47e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720417179   169 DDILKGGDVVRLFHAEQEKFLTCDEHR------KKQHVFLRTTGRQSATSatsskaLWEVEVV 225
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlppwgdGQQEVTGYGNPAIDANT------LWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
50-104 3.22e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.57  E-value: 3.22e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417179    50 GTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDE--AGNEGSWFYIQPF 104
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGnpAIDANTLWLIEPV 57
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 42-121 4.33e-04

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: 43.53  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179   42 ETENRKLlGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPfYKLRSIGDSVVIGDKVV 121
Cdd:cd23263     49 ESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDKSSLFKFEP-IGSTKYKQKYVKKDSYF 126
AglD2 COG0392
Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis] ...
 2221-2420 3.60e-03

Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440161  Cd Length: 289  Bit Score: 41.86  E-value: 3.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2221 FWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIAL----PKPHGIRALIASTILRLI----- 2291
Cdd:COG0392     86 ALERLTDLLGLLLLAGLGLLFGPGALPGLGNLPGALLLLLLGLALLAAVLLYLlllaFRPRLLLRLRRWKLLRKIrekle 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2292 ------FSVGLQPTLFLLgafnvcnkiIFLMSFVGNCGTFTRGY---RAMVLDVEFLYHLL-YLLICAMGLFVH------ 2355
Cdd:COG0392    166 rfleglRRLRLSPRLLLL---------QLLLSLLDWLLAALILYfllPALGVDVSFLAVLAvFLLASLAGLLPPtpgglg 236

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417179 2356 --EFFYSLLLfdlvyreeTLLNViksvtrnGRSIILTAVLA--LILVYLFSIVGYLFFkddFILEVDRL 2420
Cdd:COG0392    237 vfEAALLLLL--------SLFGV-------PAAAALAALLLyrLIYYLLPLLLGLLLL---LLLELRRR 287
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 162-383 3.91e-163

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: 501.91  E-value: 3.91e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  162 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 241
Cdd:cd23287      1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  242 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 321
Cdd:cd23287     81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417179  322 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 383
Cdd:cd23287    161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 162-378 8.30e-144

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: 445.65  E-value: 8.30e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  162 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 241
Cdd:cd23277      1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  242 RFKHLATGHYLAAEVDPdfeeeclefqpsvDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 321
Cdd:cd23277     81 RFKHLATGQYLAAEVDP-------------DPTPDPTRSKLRGAPGKPVYCLVSVPHGNDIASIFELDPTTLQRGDSLVP 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417179  322 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEV 378
Cdd:cd23277    148 RSSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 156-378 4.28e-126

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: 395.95  E-value: 4.28e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  156 WKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAG 235
Cdd:cd23288      1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  236 YWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRlRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRG 315
Cdd:cd23288     81 QWNSLFRFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKK-RQAAEKIMYTLVSVPHGNDIASLFELDATTLQR 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720417179  316 GDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEV 378
Cdd:cd23288    160 ADCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 162-378 5.52e-113

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: 357.82  E-value: 5.52e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  162 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 241
Cdd:cd23289      1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  242 RFKHLATGHYLAAEVDPDFEEECLEfqPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 321
Cdd:cd23289     81 RFKHLATGNYLAAEENPSYKGDASD--PKAAGMGAQSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVP 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417179  322 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEV 378
Cdd:cd23289    159 RNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 414-608 4.51e-81

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: 265.60  E-value: 4.51e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  414 LLEDLVYFVTGGTNS---GQDVLEVVFSKPNRERQKLMREQNILKQIFK---LLQAPFTdcgdGPMLRLEELGDQRHAPF 487
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  488 RHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAE---DTITALLHNNRKLLEKHITAAEIDTFVSLVRKN- 563
Cdd:pfam01365   77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKHg 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1720417179  564 REPRFLDYLSDLCVSMNKSIPVTQELICKAVLNptNADILIETKL 608
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 170-371 1.83e-76

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: 251.90  E-value: 1.83e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  170 DILKGGDVVRLFHAEQEKFLTCDEHRKKQHvFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATG 249
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  250 HYLAAEVDPdfeeeclefqpsvdpdQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLR 329
Cdd:pfam02815   80 RYLHSHEEQ----------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQ 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720417179  330 HLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIV 371
Cdd:pfam02815  144 HVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 1-167 1.70e-67

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: 227.38  E-value: 1.70e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179    1 MNRYSAQKQFWKA--AKPGANSTTDAvllnkLHHAADLEKKQNetenrkllgtvIQYGNVIQLLHLKSNKYLTVNKRLPA 78
Cdd:pfam08709   59 ANSYAAQKELWSAgnRSPNGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPS 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179   79 LLEKNAMRVTLDEAGN-EGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLH-ASSHQLVDNPGcNEVNSVNCNTSW 156
Cdd:pfam08709  123 LRDKNAMRVVLDEAGNgEGCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSW 201

                          170
                   ....*....|.
gi 1720417179  157 KIVLFMKWSDN 167
Cdd:pfam08709  202 KMEPFMSGCEN 212
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1909-2016 1.20e-39

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815.


Pssm-ID: 462482  Cd Length: 98  Bit Score: 143.05  E-value: 1.20e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 1909 ITIMQPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINEKNVALINQTLESLT 1987
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 1720417179 1988 EYCQGPCHENQNCIatHESNGIDIITALI 2016
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 169-378 5.64e-32

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: 124.80  E-value: 5.64e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  169 DDILKGGDVVRLFHAEQEKFLTCDEH--------RKKQHV-FLRTTGRQSATSATSSKALWEVEVVqHDPCRGGAGYWNS 239
Cdd:cd23280      4 ENFLKGGDVVRLFHKELEAYLSAEGSfvdevlteDVHLRVrPVDDRKPRTLFPPTSGDTFWQIEKE-DTPLKGGVIKWGD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  240 LFRFKHLATGHYLAAEVDPDFEEECLEfqpsvdpdqdasrsrlrnaqekmvyslvsvPEGNDISSIFELDPTTLRGGDSl 319
Cdd:cd23280     83 QCRLRHLPTGKYLAVDDKTGNGKVVLT------------------------------SDPSDPSTVFRLHPVTKETSEE- 131

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720417179  320 VPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVML---------KIGTSPLKEDKEAFAIVPVSPAEV 378
Cdd:cd23280    132 VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGlswdgaklrKVSLSLERQDDDAFTIQEVDPDLV 199
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 175-349 4.36e-26

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: 107.08  E-value: 4.36e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  175 GDVVRLFHAEQEKFLTCDEHR-----KKQHVFLRTTGRQsatsaTSSKALWEVEVVQHDPcrGGAGYWNSLFRFKHLATG 249
Cdd:cd23263      1 GDVIWLKHSETGKYLHSHRKNyptgsGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  250 HYLAAEVDPdfeeeclefqpsvdpdqdasRSRLRNAQEKMVYSlvsvpEGNDISSIFELDPTTLRGG-DSLVPRNSYVRL 328
Cdd:cd23263     74 KYLSSEEGK--------------------KSPKSNHQEVLCLT-----DNPDKSSLFKFEPIGSTKYkQKYVKKDSYFRL 128

                          170       180
                   ....*....|....*....|.
gi 1720417179  329 RHLCTNTWVHSTNIPIDKEEE 349
Cdd:cd23263    129 KHVNTNFWLHSHEKKFNINNK 149
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2297-2547 2.13e-22

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 98.49  E-value: 2.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2297 QPTLFLLGAFNVCNKIIFLMSFV------GNCGTFTRGYRAMVLDVEFLYHLLYLLICAM----GLFVHEFFYSLLLFDL 2366
Cdd:pfam00520   29 EPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPWNILDFVVVLPSLISLVLSSVgslsGLRVLRLLRLLRLLRL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2367 VYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFilevdrlpnetavpetgeslandflysdvcrve 2446
Cdd:pfam00520  109 IRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL--------------------------------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2447 tgenctspapkeellPAEETEQDKEHTCETLLMCIVTVLShgLRSGGGVGDVLRKPSKEEPLFAArVIYDLLFFFMVIII 2526
Cdd:pfam00520  156 ---------------KTWENPDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFL 217

                          250       260
                   ....*....|....*....|.
gi 1720417179 2527 VLNLIFGVIIDTFADLRSEKQ 2547
Cdd:pfam00520  218 LLNLFIAVIIDNFQELTERTE 238
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 117-252 4.13e-08

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: 55.08  E-value: 4.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  117 GDKVVLNPVNAGQPLHASSHQLVDNPGCNEVN------SVNCNTSWKIvlfMKWSDNKDDILKGGDVVRLFHAEQEKFLT 190
Cdd:cd23263      1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTfesssrKGDTNGLWII---ESENGKQGGPVKWGDKIRLRHLSTGKYLS 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417179  191 CDEH---RKKQHVFLRTTGRQSATSatsskALWEVEVVQHDPcrGGAGYW--NSLFRFKHLATGHYL 252
Cdd:cd23263     78 SEEGkksPKSNHQEVLCLTDNPDKS-----SLFKFEPIGSTK--YKQKYVkkDSYFRLKHVNTNFWL 137
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 172-337 7.30e-08

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: 54.92  E-value: 7.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  172 LKGGDVVRLFHAEQEKF-LTCDEHRKKQHvflRTTGRQSATSATSSKALWEVEvvqhdPCR----GGAGYWNSLFRFKHL 246
Cdd:cd23292      3 LLGGHVVRLFHGHDECLtIPSTDQSDEQH---RVVNYEAGGAGTRARSLWRLE-----PLRiswsGSHIRWGQTFRLRHL 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  247 ATGHYLAAEvdpdfEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIfeldpttlRGGDSLvprnsyV 326
Cdd:cd23292     75 TTGHYLALT-----EDQGLILQDRAKSDTKSTAFCFRASKEKLESGPKRDIDGMGIAEI--------KYGDSV------C 135

                          170
                   ....*....|.
gi 1720417179  327 RLRHLCTNTWV 337
Cdd:cd23292    136 FVQHVASGLWL 146
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1140-1259 2.02e-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: 53.74  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 1140 SVRKSRKQQQRLLRNMGAHAVVLE---LLQIPY-------EKAEDTKM---QEIMRLAHEFLQNFCAGNQQNQALLHKHI 1206
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMEvidLLGAPFtgallfaEDLGEEKNapwKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720417179 1207 NLFLNP--------GILEavTMQHIFMNNFQLC-SEINERVVQHFVHCIETHGRNVQYIKFL 1259
Cdd:pfam01365  106 DWLQSQlgspslaeGTLD--VLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
169-225 2.47e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.57  E-value: 2.47e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720417179   169 DDILKGGDVVRLFHAEQEKFLTCDEHR------KKQHVFLRTTGRQSATSatsskaLWEVEVV 225
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlppwgdGQQEVTGYGNPAIDANT------LWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
50-104 3.22e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.57  E-value: 3.22e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720417179    50 GTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDE--AGNEGSWFYIQPF 104
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGnpAIDANTLWLIEPV 57
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 174-357 1.76e-05

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: 47.69  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  174 GGDVVRLFHAEQEKFLTCDE--HRKKQHvflRTTGRQSATSATSSKALWEVEVVQHDPCrGGAGYWNSLFRFKHLATGHY 251
Cdd:cd23278      1 GGDVLRLFHGHMDECLTIPAagSKEDQH---RTVIYEGGAVSTHARSLWRLELLRIKWS-GSHIGWGQPFRLRHVTTGRY 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  252 LAAEVDPDfeeecLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGndissifeLDPTTLRGGDSLvprnsyVRLRHL 331
Cdd:cd23278     77 LALTEDRG-----LVLVPKEKADVKATAFCFRQSKDDKKVLDEKEDEG--------MGTPEIKYGDSL------VFIQHV 137

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720417179  332 CTNTW-----VHSTNIPIDKEEEKPVMLKIG 357
Cdd:cd23278    138 DTGLWlsyqaVETKKRVGGVEERKAILHAEG 168
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 175-252 2.17e-05

MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein mannosyltransferase (PMT); The PMT (EC 2.4.1.109) family includes mammalian protein O-mannosyl-transferases (POMT1 and POMT2) and yeast PMT1-7. PMTs are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. Members in this family contain a 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: 467747 [Multi-domain]  Cd Length: 185  Bit Score: 47.71  E-value: 2.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  175 GDVVRLFHAEQEKFLTCDEHR---KKQHvfLRTTGRQSATSATSSKALWEVEVVQhDPCRGGAGYWNSL---FRFKHLAT 248
Cdd:cd23276     69 GDEVRLLHKETNRYLRTHDAAapvTSKH--KEVSAYPDENEDGDDNDLWVVEIVK-DEGKLEDKRIKPLttrFRLRNKKT 145


                   ....
gi 1720417179  249 GHYL 252
Cdd:cd23276    146 GCYL 149
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 174-337 3.84e-05

MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, also called RYR-2, or cardiac muscle ryanodine receptor-calcium release channel, or cardiac muscle ryanodine receptor, or type 2 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 cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity of RYR-2 is modulated by formation of heterotetramers with RYR-3. RYR-2 is required for cellular calcium ion homeostasis. it plays an essential role in embryonic heart development. RYR-2 forms homotetramer and also forms heterotetramers with RYR-1 and RYR-3. RYR-2 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: 467762 [Multi-domain]  Cd Length: 184  Bit Score: 46.96  E-value: 3.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  174 GGDVVRLFHAEQEKFLTC--DEHRKKQHvflRTTGRQSATSATSSKALWEVEVVQHdPCRGGAGYWNSLFRFKHLATGHY 251
Cdd:cd23291      1 GGDVLRLLHGHMDECLTVpsGEHGEEQR---RTVHYEGGAVSVHARSLWRLETLRV-AWSGSHIRWGQPFRLRHVTTGKY 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  252 LAAevdpdFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIfeldpttlRGGDSLvprnSYVrlRHL 331
Cdd:cd23291     77 LSL-----MEDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEI--------KYGDSV----CYI--QHV 137


                   ....*.
gi 1720417179  332 CTNTWV 337
Cdd:cd23291    138 DTGLWL 143
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
111-158 1.28e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.94  E-value: 1.28e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1720417179   111 GDSVVIGDKVVLNPVNAGQPLHASSHQL-VDNPGCNEVNSV-----NCNTSWKI 158
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLpPWGDGQQEVTGYgnpaiDANTLWLI 54
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 172-257 1.76e-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: 44.88  E-value: 1.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  172 LKGGDVVRLFHAEQEKFLTC-----DEHRkkqhvflRTTGRQSATSATSSKALWEVEvvqhdPCR----GGAGYWNSLFR 242
Cdd:cd23290      8 VTGGHVLRLFHGHMDECLTIsaadsDDQR-------RLVYYEGGAVCTHARSLWRLE-----PLRiswsGSHLRWGQPLR 75

                           90
                   ....*....|....*
gi 1720417179  243 FKHLATGHYLAAEVD 257
Cdd:cd23290     76 IRHVTTGRYLALTED 90
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 42-121 4.33e-04

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: 43.53  E-value: 4.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179   42 ETENRKLlGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPfYKLRSIGDSVVIGDKVV 121
Cdd:cd23263     49 ESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDKSSLFKFEP-IGSTKYKQKYVKKDSYF 126
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
232-259 7.44e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 39.63  E-value: 7.44e-04
                            10        20
                    ....*....|....*....|....*...
gi 1720417179   232 GGAGYWNSLFRFKHLATGHYLAAEVDPD 259
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKL 28
beta-trefoil_Ricin_EndoBetaGal-like cd23432
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1, ...
 209-285 1.49e-03

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1,4-Gal-releasing endo-beta-galactosidase (Endo-beta-Gal(GnGa)) and similar proteins; Endo-beta-Gal(GnGa) can release disaccharide GlcNAc-alpha-1,4Gal from O-glycans expressed in the gastric gland mucous cell-type mucin. It contains a C-terminal ricin B-type lectin domain with a 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. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467310  Cd Length: 127  Bit Score: 40.79  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  209 SATSATSSKALWEVEVVqhdpcrgGAGYwnslFRFKHLATGHYLAAEVDPDFeEECLEFQPSVDPDQ------DASRSRL 282
Cdd:cd23432     24 GTPPEDDTSAQWIIEDV-------GDGY----VRIKNRATGHYLHIENNTGY-LESGPIPPGWWSAQwtlepvGTGYVRI 91


                   ...
gi 1720417179  283 RNA 285
Cdd:cd23432     92 RNR 94
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 112-254 3.17e-03

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 2 (PMT2) and similar proteins; Dolichyl-phosphate-mannose-protein mannosyltransferases (EC 2.4.1.109), also called PMTs, are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. In Saccharomyces cerevisiae, a family of protein mannosyltransferases coded for by seven genes (PMT1-7). The family includes PMT2, PMT3 and PMT6. PMT2 forms a heterodimeric complex with PMT1 and more rarely with PMT5. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. It is required for incorporation of proteins in the cell wall. PMT3 form a functional heterodimer with PMT5 and more rarely with PMT1. It may have redundant activity to PMT2. PMT6 may form a heterodimer with PMT4. Members in this family contain a 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: 467755 [Multi-domain]  Cd Length: 192  Bit Score: 41.15  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  112 DSVVIGDKVVL-NPVNAGQPLHASSHQLvdnPGCNEVNSVNC------NTSWKIVL---FMKWSDNKDDI--LKGGDVVR 179
Cdd:cd23284      2 LDVAYGSKVTIkNQGLGGGLLHSHVQTY---PEGSNQQQVTCyghkdsNNEWIFERprgLPSWDENDTDIefIKDGDIVR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  180 LFHAEQEKFLtcDEHRKKQHVflrtTGRQSATSA------TSSKALWEVEVVQHDpcrgGAGYWNSL------FRFKHLA 247
Cdd:cd23284     79 LVHKQTGRNL--HSHPVPAPI----SKSDYEVSGygdltvGDEKDNWVIEIVKQV----GSEDPKKLhtlttsFRLRHEV 148


                   ....*..
gi 1720417179  248 TGHYLAA 254
Cdd:cd23284    149 LGCYLAQ 155
AglD2 COG0392
Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis] ...
 2221-2420 3.60e-03

Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440161  Cd Length: 289  Bit Score: 41.86  E-value: 3.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2221 FWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIAL----PKPHGIRALIASTILRLI----- 2291
Cdd:COG0392     86 ALERLTDLLGLLLLAGLGLLFGPGALPGLGNLPGALLLLLLGLALLAAVLLYLlllaFRPRLLLRLRRWKLLRKIrekle 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2292 ------FSVGLQPTLFLLgafnvcnkiIFLMSFVGNCGTFTRGY---RAMVLDVEFLYHLL-YLLICAMGLFVH------ 2355
Cdd:COG0392    166 rfleglRRLRLSPRLLLL---------QLLLSLLDWLLAALILYfllPALGVDVSFLAVLAvFLLASLAGLLPPtpgglg 236

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720417179 2356 --EFFYSLLLfdlvyreeTLLNViksvtrnGRSIILTAVLA--LILVYLFSIVGYLFFkddFILEVDRL 2420
Cdd:COG0392    237 vfEAALLLLL--------SLFGV-------PAAAALAALLLyrLIYYLLPLLLGLLLL---LLLELRRR 287
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 55-222 6.55e-03

MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The SDF-2 family includes mammalian SDF-2 and SDF2-like protein 1 (SDF2L1) as well as similar proteins from plant, such as Arabidopsis thaliana stromal cell-derived factor 2-like protein (AtSDF2). SDF-2 is a secretory protein involved in multiple endoplasmic reticulum (ER) functions, including the misfolded protein catabolic process, protein glycosylation, and ER protein quality control. SDF2L1, also called PWP1-interacting protein 8, is an endoplasmic reticulum (ER)-localized protein that plays a role in ER-associated degradation (ERAD) of misfolded proinsulin in pancreatic beta-cells. It is a component of the endoplasmic reticulum (ER) chaperone complex and interacts with alpha- and beta-defensins. SDF2L1 may also act as a tumor suppressor that play an important role in a variety of cancers, such as breast cancer and ovarian cancer. AtSDF2, also called SDF2-like protein, acts as crucial component of the unfolded protein response (UPR) in Arabidopsis thaliana. It is involved in the endoplasmic reticulum (ER) protein quality control and unfolded protein response. It may be involved in the quality control of glycoproteins. AtSDF2 forms a complex in the ER with ERDJ3B and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity. Members in this family contain a 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: 467750 [Multi-domain]  Cd Length: 173  Bit Score: 39.97  E-value: 6.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179   55 YGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFY--KLRSIGDSVVIGDKVVLNPVNAGQPLH 132
Cdd:cd23279      1 YGSAIKLKHVNSGYRLHSHEVSYGSGSGQQSVTAVPSADDANSLWTVLPGLgePCQEQGKPVKCGDIIRLQHVNTRKNLH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179  133 ASSHQlvdNPGCN--EVNSVNCNTS-----WKIVLFmkwsDNKDDILKGGDVVRLFHAEQEKFLTCdehrKKQHVFLRT- 204
Cdd:cd23279     81 SHNHS---SPLSGnqEVSAFGGGDEdsgdnWIVECE----GKKAKFWKRGEPVRLKHVDTGKYLSA----SKTHKFTQQp 149

                          170       180
                   ....*....|....*....|.
gi 1720417179  205 -TGRQ--SATSATSSKALWEV 222
Cdd:cd23279    150 iAGQLevSAASSKDSDSQWKA 170
MnhB COG2111
Multisubunit Na+/H+ antiporter, MnhB subunit [Inorganic ion transport and metabolism];
2229-2409 9.07e-03

Multisubunit Na+/H+ antiporter, MnhB subunit [Inorganic ion transport and metabolism];


Pssm-ID: 441714 [Multi-domain]  Cd Length: 750  Bit Score: 41.62  E-value: 9.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2229 LAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALpkphgIRALIASTILRLIFSVGLQPTLFLLGAFNV 2308
Cdd:COG2111    462 LLLLALLLLLLLAVAALVALLLLLLLLLLLLLVLVLLLLLLLLLL-----LLLLLLLLLLRAAARAALLALAAAAAGAAA 536

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720417179 2309 CNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLLICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSII 2388
Cdd:COG2111    537 YALALGLLLVAAASTTGGGGGGLLLGLLGVVVVVVVLVLVLLLLALGLVLLLLLARLGALALLLLLLLALLVAAAAASLI 616

                          170       180
                   ....*....|....*....|...
gi 1720417179 2389 LTAVLALIL--VYLFSIvgYLFF 2409
Cdd:COG2111    617 LSRLTRVLLpgILGFSV--YLFF 637
 
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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