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Conserved domains on  [gi|17380349|sp|P29994|]
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RecName: Full=Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1; AltName: Full=IP3 receptor isoform 1; Short=IP3R 1; Short=InsP3R1; AltName: Full=Inositol 1,4,5-trisphosphate receptor; Short=IP-3-R; AltName: Full=Inositol 1,4,5-trisphosphate receptor type 1; AltName: Full=Type 1 inositol 1,4,5-trisphosphate receptor; Short=Type 1 InsP3 receptor

Protein Classification

inositol 1,4,5-trisphosphate receptor( domain architecture ID 12096418)

inositol 1,4,5-trisphosphate receptor is an intracellular channel receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium

Gene Ontology:  GO:0005220|GO:0070679|GO:0070588
PubMed:  26830355|16102823|22453946
TCDB:  1.A.3

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) ...
 224-445 4.15e-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: 4.15e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  224 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 303
Cdd:cd23287    1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  304 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 383
Cdd:cd23287   81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17380349  384 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 445
Cdd:cd23287  161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 5-229 1.73e-105

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: 336.39  E-value: 1.73e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349      5 MSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKA--AKPGANS 82
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAgnRSPNGNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349     83 TTDAvllnkLHHAADLEKKQNetenrkllgtvIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGN-EGSWF 161
Cdd:pfam08709   81 LTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWF 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17380349    162 YIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLH-ASSHQLVDNPGcNEVNSVNCNTSWKIVLFMKWSDN 229
Cdd:pfam08709  145 IITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 476-670 3.16e-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: 266.37  E-value: 3.16e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349    476 LLEDLVYFVTGGTNS---GQDVLEVVFSKPNRERQKLMREQNILKQIFK---LLQAPFTdcgdGPMLRLEELGDQRHAPF 549
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349    550 RHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAE---DTITALLHNNRKLLEKHITAAEIDTFVSLVRKN- 625
Cdd:pfam01365   77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKHg 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 17380349    626 REPRFLDYLSDLCVSMNKSIPVTQELICKAVLNptNADILIETKL 670
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1963-2070 8.39e-40

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: 143.43  E-value: 8.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   1963 ITIMQPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINEKNVALINQTLESLT 2041
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 17380349   2042 EYCQGPCHENQNCIatHESNGIDIITALI 2070
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2351-2601 1.24e-21

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: 96.57  E-value: 1.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   2351 QPTLFLLGAFNVCNKIIFLMSFV------GNCGTFTRGYRAMVLDVEFLYHLLYLLICAM----GLFVHEFFYSLLLFDL 2420
Cdd:pfam00520   29 EPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPWNILDFVVVLPSLISLVLSSVgslsGLRVLRLLRLLRLLRL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   2421 VYREETLLNVIKSVTRNGRPIILTAALALILVYLFSIVGYLFFKDDFilevdrlpnetagpetgeslandflysdvcrve 2500
Cdd:pfam00520  109 IRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL--------------------------------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   2501 tgenctspapkeellPVEETEQDKEHTCETLLMCIVTVLShgLRSGGGVGDVLRKPSKEEPLFAArVIYDLLFFFMVIII 2580
Cdd:pfam00520  156 ---------------KTWENPDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFL 217

                          250       260
                   ....*....|....*....|.
gi 17380349   2581 VLNLIFGVIIDTFADLRSEKQ 2601
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 ...
 1193-1312 1.84e-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: 54.13  E-value: 1.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   1193 SVRKSRKQQQRLLRNMGAHAVVLE---LLQIPY-------EKAEDTKM---QEIMRLAHEFLQNFCAGNQQNQALLHKHI 1259
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMEvidLLGAPFtgallfaEDLGEEKNapwKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17380349   1260 NLFLNP--------GILEavTMQHIFMNNFQLC-SEINERVVQHFVHCIETHGRNVQYIKFL 1312
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) ...
 224-445 4.15e-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: 4.15e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  224 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 303
Cdd:cd23287    1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  304 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 383
Cdd:cd23287   81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17380349  384 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 445
Cdd:cd23287  161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 5-229 1.73e-105

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: 336.39  E-value: 1.73e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349      5 MSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKA--AKPGANS 82
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAgnRSPNGNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349     83 TTDAvllnkLHHAADLEKKQNetenrkllgtvIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGN-EGSWF 161
Cdd:pfam08709   81 LTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWF 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17380349    162 YIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLH-ASSHQLVDNPGcNEVNSVNCNTSWKIVLFMKWSDN 229
Cdd:pfam08709  145 IITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 476-670 3.16e-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: 266.37  E-value: 3.16e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349    476 LLEDLVYFVTGGTNS---GQDVLEVVFSKPNRERQKLMREQNILKQIFK---LLQAPFTdcgdGPMLRLEELGDQRHAPF 549
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349    550 RHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAE---DTITALLHNNRKLLEKHITAAEIDTFVSLVRKN- 625
Cdd:pfam01365   77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKHg 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 17380349    626 REPRFLDYLSDLCVSMNKSIPVTQELICKAVLNptNADILIETKL 670
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 232-433 1.45e-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: 252.28  E-value: 1.45e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349    232 DILKGGDVVRLFHAEQEKFLTCDEHRKKQHvFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATG 311
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349    312 HYLAAEVDPdfeeeclefqpsvdpdQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLR 391
Cdd:pfam02815   80 RYLHSHEEQ----------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQ 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 17380349    392 HLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIV 433
Cdd:pfam02815  144 HVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1963-2070 8.39e-40

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: 143.43  E-value: 8.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   1963 ITIMQPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINEKNVALINQTLESLT 2041
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 17380349   2042 EYCQGPCHENQNCIatHESNGIDIITALI 2070
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2351-2601 1.24e-21

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: 96.57  E-value: 1.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   2351 QPTLFLLGAFNVCNKIIFLMSFV------GNCGTFTRGYRAMVLDVEFLYHLLYLLICAM----GLFVHEFFYSLLLFDL 2420
Cdd:pfam00520   29 EPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPWNILDFVVVLPSLISLVLSSVgslsGLRVLRLLRLLRLLRL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   2421 VYREETLLNVIKSVTRNGRPIILTAALALILVYLFSIVGYLFFKDDFilevdrlpnetagpetgeslandflysdvcrve 2500
Cdd:pfam00520  109 IRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL--------------------------------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   2501 tgenctspapkeellPVEETEQDKEHTCETLLMCIVTVLShgLRSGGGVGDVLRKPSKEEPLFAArVIYDLLFFFMVIII 2580
Cdd:pfam00520  156 ---------------KTWENPDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFL 217

                          250       260
                   ....*....|....*....|.
gi 17380349   2581 VLNLIFGVIIDTFADLRSEKQ 2601
Cdd:pfam00520  218 LLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1193-1312 1.84e-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: 54.13  E-value: 1.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   1193 SVRKSRKQQQRLLRNMGAHAVVLE---LLQIPY-------EKAEDTKM---QEIMRLAHEFLQNFCAGNQQNQALLHKHI 1259
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMEvidLLGAPFtgallfaEDLGEEKNapwKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17380349   1260 NLFLNP--------GILEavTMQHIFMNNFQLC-SEINERVVQHFVHCIETHGRNVQYIKFL 1312
Cdd:pfam01365  106 DWLQSQlgspslaeGTLD--VLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
231-287 2.52e-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: 2.52e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17380349     231 DDILKGGDVVRLFHAEQEKFLTCDEHR------KKQHVFLRTTGRQSATSatsskaLWEVEVV 287
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlppwgdGQQEVTGYGNPAIDANT------LWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
112-166 3.28e-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: 3.28e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 17380349     112 GTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDE--AGNEGSWFYIQPF 166
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGnpAIDANTLWLIEPV 57
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 104-183 3.74e-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: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  104 ETENRKLlGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPfYKLRSIGDSVVIGDKVV 183
Cdd:cd23263   49 ESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDKSSLFKFEP-IGSTKYKQKYVKKDSYF 126
AglD2 COG0392
Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis] ...
 2275-2474 6.13e-03

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


Pssm-ID: 440161  Cd Length: 289  Bit Score: 41.47  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349 2275 FWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIAL----PKPHGIRALIASTILRLI----- 2345
Cdd:COG0392   86 ALERLTDLLGLLLLAGLGLLFGPGALPGLGNLPGALLLLLLGLALLAAVLLYLlllaFRPRLLLRLRRWKLLRKIrekle 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349 2346 ------FSVGLQPTLFLLgafnvcnkiIFLMSFVGNCGTFTRGY---RAMVLDVEFLYHLL-YLLICAMGLFVH------ 2409
Cdd:COG0392  166 rfleglRRLRLSPRLLLL---------QLLLSLLDWLLAALILYfllPALGVDVSFLAVLAvFLLASLAGLLPPtpgglg 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17380349 2410 --EFFYSLLLfdlvyreeTLLNViksvtrnGRPIILTAALA--LILVYLFSIVGYLFFkddFILEVDRL 2474
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) ...
 224-445 4.15e-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: 4.15e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  224 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 303
Cdd:cd23287    1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  304 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 383
Cdd:cd23287   81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17380349  384 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 445
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 ...
 224-440 8.50e-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: 8.50e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  224 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 303
Cdd:cd23277    1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  304 RFKHLATGHYLAAEVDPdfeeeclefqpsvDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 383
Cdd:cd23277   81 RFKHLATGQYLAAEVDP-------------DPTPDPTRSKLRGAPGKPVYCLVSVPHGNDIASIFELDPTTLQRGDSLVP 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17380349  384 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEV 440
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) ...
 218-440 4.37e-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: 4.37e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  218 WKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAG 297
Cdd:cd23288    1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  298 YWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRlRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRG 377
Cdd:cd23288   81 QWNSLFRFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKK-RQAAEKIMYTLVSVPHGNDIASLFELDATTLQR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17380349  378 GDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEV 440
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) ...
 224-440 5.64e-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: 5.64e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  224 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 303
Cdd:cd23289    1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  304 RFKHLATGHYLAAEVDPDFEEECLEfqPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 383
Cdd:cd23289   81 RFKHLATGNYLAAEENPSYKGDASD--PKAAGMGAQSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVP 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17380349  384 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEV 440
Cdd:cd23289  159 RNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 5-229 1.73e-105

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: 336.39  E-value: 1.73e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349      5 MSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKA--AKPGANS 82
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAgnRSPNGNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349     83 TTDAvllnkLHHAADLEKKQNetenrkllgtvIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGN-EGSWF 161
Cdd:pfam08709   81 LTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWF 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17380349    162 YIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLH-ASSHQLVDNPGcNEVNSVNCNTSWKIVLFMKWSDN 229
Cdd:pfam08709  145 IITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 476-670 3.16e-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: 266.37  E-value: 3.16e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349    476 LLEDLVYFVTGGTNS---GQDVLEVVFSKPNRERQKLMREQNILKQIFK---LLQAPFTdcgdGPMLRLEELGDQRHAPF 549
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349    550 RHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAE---DTITALLHNNRKLLEKHITAAEIDTFVSLVRKN- 625
Cdd:pfam01365   77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKHg 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 17380349    626 REPRFLDYLSDLCVSMNKSIPVTQELICKAVLNptNADILIETKL 670
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 232-433 1.45e-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: 252.28  E-value: 1.45e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349    232 DILKGGDVVRLFHAEQEKFLTCDEHRKKQHvFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATG 311
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349    312 HYLAAEVDPdfeeeclefqpsvdpdQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLR 391
Cdd:pfam02815   80 RYLHSHEEQ----------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQ 143

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 17380349    392 HLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIV 433
Cdd:pfam02815  144 HVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1963-2070 8.39e-40

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: 143.43  E-value: 8.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   1963 ITIMQPILRFLQLLCENHNRDLQNFLRCQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINEKNVALINQTLESLT 2041
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 17380349   2042 EYCQGPCHENQNCIatHESNGIDIITALI 2070
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 ...
 231-440 4.53e-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: 125.19  E-value: 4.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  231 DDILKGGDVVRLFHAEQEKFLTCDEH--------RKKQHV-FLRTTGRQSATSATSSKALWEVEVVqHDPCRGGAGYWNS 301
Cdd:cd23280    4 ENFLKGGDVVRLFHKELEAYLSAEGSfvdevlteDVHLRVrPVDDRKPRTLFPPTSGDTFWQIEKE-DTPLKGGVIKWGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  302 LFRFKHLATGHYLAAEVDPDFEEECLEfqpsvdpdqdasrsrlrnaqekmvyslvsvPEGNDISSIFELDPTTLRGGDSl 381
Cdd:cd23280   83 QCRLRHLPTGKYLAVDDKTGNGKVVLT------------------------------SDPSDPSTVFRLHPVTKETSEE- 131

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17380349  382 VPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVML---------KIGTSPLKEDKEAFAIVPVSPAEV 440
Cdd:cd23280  132 VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGlswdgaklrKVSLSLERQDDDAFTIQEVDPDLV 199
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 237-411 2.88e-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: 107.47  E-value: 2.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  237 GDVVRLFHAEQEKFLTCDEHR-----KKQHVFLRTTGRQsatsaTSSKALWEVEVVQHDPcrGGAGYWNSLFRFKHLATG 311
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHRKNyptgsGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  312 HYLAAEVDPdfeeeclefqpsvdpdqdasRSRLRNAQEKMVYSlvsvpEGNDISSIFELDPTTLRGG-DSLVPRNSYVRL 390
Cdd:cd23263   74 KYLSSEEGK--------------------KSPKSNHQEVLCLT-----DNPDKSSLFKFEPIGSTKYkQKYVKKDSYFRL 128

                        170       180
                 ....*....|....*....|.
gi 17380349  391 RHLCTNTWVHSTNIPIDKEEE 411
Cdd:cd23263  129 KHVNTNFWLHSHEKKFNINNK 149
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2351-2601 1.24e-21

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: 96.57  E-value: 1.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   2351 QPTLFLLGAFNVCNKIIFLMSFV------GNCGTFTRGYRAMVLDVEFLYHLLYLLICAM----GLFVHEFFYSLLLFDL 2420
Cdd:pfam00520   29 EPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPWNILDFVVVLPSLISLVLSSVgslsGLRVLRLLRLLRLLRL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   2421 VYREETLLNVIKSVTRNGRPIILTAALALILVYLFSIVGYLFFKDDFilevdrlpnetagpetgeslandflysdvcrve 2500
Cdd:pfam00520  109 IRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL--------------------------------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   2501 tgenctspapkeellPVEETEQDKEHTCETLLMCIVTVLShgLRSGGGVGDVLRKPSKEEPLFAArVIYDLLFFFMVIII 2580
Cdd:pfam00520  156 ---------------KTWENPDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFL 217

                          250       260
                   ....*....|....*....|.
gi 17380349   2581 VLNLIFGVIIDTFADLRSEKQ 2601
Cdd:pfam00520  218 LLNLFIAVIIDNFQELTERTE 238
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 179-314 3.35e-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: 55.47  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  179 GDKVVLNPVNAGQPLHASSHQLVDNPGCNEVN------SVNCNTSWKIvlfMKWSDNKDDILKGGDVVRLFHAEQEKFLT 252
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTfesssrKGDTNGLWII---ESENGKQGGPVKWGDKIRLRHLSTGKYLS 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17380349  253 CDEH---RKKQHVFLRTTGRQSATSatsskALWEVEVVQHDPcrGGAGYW--NSLFRFKHLATGHYL 314
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, ...
 234-399 7.45e-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: 7.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  234 LKGGDVVRLFHAEQEKF-LTCDEHRKKQHvflRTTGRQSATSATSSKALWEVEvvqhdPCR----GGAGYWNSLFRFKHL 308
Cdd:cd23292    3 LLGGHVVRLFHGHDECLtIPSTDQSDEQH---RVVNYEAGGAGTRARSLWRLE-----PLRiswsGSHIRWGQTFRLRHL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  309 ATGHYLAAEvdpdfEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIfeldpttlRGGDSLvprnsyV 388
Cdd:cd23292   75 TTGHYLALT-----EDQGLILQDRAKSDTKSTAFCFRASKEKLESGPKRDIDGMGIAEI--------KYGDSV------C 135

                        170
                 ....*....|.
gi 17380349  389 RLRHLCTNTWV 399
Cdd:cd23292  136 FVQHVASGLWL 146
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1193-1312 1.84e-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: 54.13  E-value: 1.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349   1193 SVRKSRKQQQRLLRNMGAHAVVLE---LLQIPY-------EKAEDTKM---QEIMRLAHEFLQNFCAGNQQNQALLHKHI 1259
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMEvidLLGAPFtgallfaEDLGEEKNapwKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17380349   1260 NLFLNP--------GILEavTMQHIFMNNFQLC-SEINERVVQHFVHCIETHGRNVQYIKFL 1312
Cdd:pfam01365  106 DWLQSQlgspslaeGTLD--VLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
231-287 2.52e-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: 2.52e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17380349     231 DDILKGGDVVRLFHAEQEKFLTCDEHR------KKQHVFLRTTGRQSATSatsskaLWEVEVV 287
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlppwgdGQQEVTGYGNPAIDANT------LWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
112-166 3.28e-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: 3.28e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 17380349     112 GTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDE--AGNEGSWFYIQPF 166
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 ...
 236-419 1.80e-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: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  236 GGDVVRLFHAEQEKFLTCDE--HRKKQHvflRTTGRQSATSATSSKALWEVEVVQHDPCrGGAGYWNSLFRFKHLATGHY 313
Cdd:cd23278    1 GGDVLRLFHGHMDECLTIPAagSKEDQH---RTVIYEGGAVSTHARSLWRLELLRIKWS-GSHIGWGQPFRLRHVTTGRY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  314 LAAEVDPDfeeecLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGndissifeLDPTTLRGGDSLvprnsyVRLRHL 393
Cdd:cd23278   77 LALTEDRG-----LVLVPKEKADVKATAFCFRQSKDDKKVLDEKEDEG--------MGTPEIKYGDSL------VFIQHV 137

                        170       180       190
                 ....*....|....*....|....*....|.
gi 17380349  394 CTNTW-----VHSTNIPIDKEEEKPVMLKIG 419
Cdd:cd23278  138 DTGLWlsyqaVETKKRVGGVEERKAILHAEG 168
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 237-314 2.00e-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: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  237 GDVVRLFHAEQEKFLTCDEHR---KKQHvfLRTTGRQSATSATSSKALWEVEVVQhDPCRGGAGYWNSL---FRFKHLAT 310
Cdd:cd23276   69 GDEVRLLHKETNRYLRTHDAAapvTSKH--KEVSAYPDENEDGDDNDLWVVEIVK-DEGKLEDKRIKPLttrFRLRNKKT 145


                 ....
gi 17380349  311 GHYL 314
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, ...
 236-399 3.47e-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: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  236 GGDVVRLFHAEQEKFLTC--DEHRKKQHvflRTTGRQSATSATSSKALWEVEVVQHdPCRGGAGYWNSLFRFKHLATGHY 313
Cdd:cd23291    1 GGDVLRLLHGHMDECLTVpsGEHGEEQR---RTVHYEGGAVSVHARSLWRLETLRV-AWSGSHIRWGQPFRLRHVTTGKY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  314 LAAevdpdFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIfeldpttlRGGDSLvprnSYVrlRHL 393
Cdd:cd23291   77 LSL-----MEDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEI--------KYGDSV----CYI--QHV 137


                 ....*.
gi 17380349  394 CTNTWV 399
Cdd:cd23291  138 DTGLWL 143
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
173-220 1.30e-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: 1.30e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 17380349     173 GDSVVIGDKVVLNPVNAGQPLHASSHQL-VDNPGCNEVNSV-----NCNTSWKI 220
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, ...
 234-319 1.78e-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: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  234 LKGGDVVRLFHAEQEKFLTC-----DEHRkkqhvflRTTGRQSATSATSSKALWEVEvvqhdPCR----GGAGYWNSLFR 304
Cdd:cd23290    8 VTGGHVLRLFHGHMDECLTIsaadsDDQR-------RLVYYEGGAVCTHARSLWRLE-----PLRiswsGSHLRWGQPLR 75

                         90
                 ....*....|....*
gi 17380349  305 FKHLATGHYLAAEVD 319
Cdd:cd23290   76 IRHVTTGRYLALTED 90
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 104-183 3.74e-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: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  104 ETENRKLlGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPfYKLRSIGDSVVIGDKVV 183
Cdd:cd23263   49 ESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDKSSLFKFEP-IGSTKYKQKYVKKDSYF 126
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
294-321 7.59e-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: 7.59e-04
                            10        20
                    ....*....|....*....|....*...
gi 17380349     294 GGAGYWNSLFRFKHLATGHYLAAEVDPD 321
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, ...
 271-347 1.52e-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: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  271 SATSATSSKALWEVEVVqhdpcrgGAGYwnslFRFKHLATGHYLAAEVDPDFeEECLEFQPSVDPDQ------DASRSRL 344
Cdd:cd23432   24 GTPPEDDTSAQWIIEDV-------GDGY----VRIKNRATGHYLHIENNTGY-LESGPIPPGWWSAQwtlepvGTGYVRI 91


                 ...
gi 17380349  345 RNA 347
Cdd:cd23432   92 RNR 94
AglD2 COG0392
Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis] ...
 2275-2474 6.13e-03

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


Pssm-ID: 440161  Cd Length: 289  Bit Score: 41.47  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349 2275 FWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIAL----PKPHGIRALIASTILRLI----- 2345
Cdd:COG0392   86 ALERLTDLLGLLLLAGLGLLFGPGALPGLGNLPGALLLLLLGLALLAAVLLYLlllaFRPRLLLRLRRWKLLRKIrekle 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349 2346 ------FSVGLQPTLFLLgafnvcnkiIFLMSFVGNCGTFTRGY---RAMVLDVEFLYHLL-YLLICAMGLFVH------ 2409
Cdd:COG0392  166 rfleglRRLRLSPRLLLL---------QLLLSLLDWLLAALILYfllPALGVDVSFLAVLAvFLLASLAGLLPPtpgglg 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17380349 2410 --EFFYSLLLfdlvyreeTLLNViksvtrnGRPIILTAALA--LILVYLFSIVGYLFFkddFILEVDRL 2474
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 ...
 117-284 6.69e-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: 6.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  117 YGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFY--KLRSIGDSVVIGDKVVLNPVNAGQPLH 194
Cdd:cd23279    1 YGSAIKLKHVNSGYRLHSHEVSYGSGSGQQSVTAVPSADDANSLWTVLPGLgePCQEQGKPVKCGDIIRLQHVNTRKNLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17380349  195 ASSHQlvdNPGCN--EVNSVNCNTS-----WKIVLFmkwsDNKDDILKGGDVVRLFHAEQEKFLTCdehrKKQHVFLRT- 266
Cdd:cd23279   81 SHNHS---SPLSGnqEVSAFGGGDEdsgdnWIVECE----GKKAKFWKRGEPVRLKHVDTGKYLSA----SKTHKFTQQp 149

                        170       180
                 ....*....|....*....|.
gi 17380349  267 -TGRQ--SATSATSSKALWEV 284
Cdd:cd23279  150 iAGQLevSAASSKDSDSQWKA 170
 
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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