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Conserved domains on  [gi|1958771641|ref|XP_038964357|]
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inositol 1,4,5-trisphosphate receptor type 2 isoform X4 [Rattus norvegicus]

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_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 156-377 6.06e-159

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: 489.94  E-value: 6.06e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  156 WKITLFMKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAG 235
Cdd:cd23288      1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  236 QWNSLFRFKHLATGNYLAAELNPDYRDAQNEGKTVRDGELPTSKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRA 315
Cdd:cd23288     81 QWNSLFRFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKKRQAAEKIMYTLVSVPHGNDIASLFELDATTLQRA 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958771641  316 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEV 377
Cdd:cd23288    161 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 413-608 3.60e-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: 265.99  E-value: 3.60e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  413 LLEDLIFFVADVTNN---GQDVLDVVITKPNRERQKLMREQNILAQVFG---ILKAPFKekageGSMLRLEDLGDQRYAP 486
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT-----GALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  487 YKYVLRLCYRVLRHSQQDYRKNQEYIAKNFCVMQSQIGYDILAE---DTITALLHNNRKLLEKHITAKEIETFVSLLRRN 563
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958771641  564 -REPRFLDYLSDLCVSNSTAIPVTQELICKFMLSpgNADILIQTKL 608
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
Ins145_P3_rec super family cl48031
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 1-166 4.37e-62

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: 211.97  E-value: 4.37e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641    1 MNRYSAQKQYWKAKQAKQGNHteaALLKKLQHAAELEQKQNesenrkllgeiVKYSNVIQLLHIKSNKYLTVNKRLPALL 80
Cdd:pfam08709   59 ANSYAAQKELWSAGNRSPNGN---SLTDALKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLR 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641   81 EKNAMRVSLDAAGN-EGSWFYIHPFWKLRSEGDNIVVGDKVVLMPVNAGQPLH-ASNVELLDNPGcKEVNAVNCNTSWKI 158
Cdd:pfam08709  125 DKNAMRVVLDEAGNgEGCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKM 203


                   ....*...
gi 1958771641  159 TLFMKFSS 166
Cdd:pfam08709  204 EPFMSGCE 211
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1853-1960 1.91e-38

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: 139.58  E-value: 1.91e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 1853 ITIMRPILRFLQLLCENHNRELQNFLRNQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINEKNVALVNQTLESLT 1931
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 1958771641 1932 EYCQGPCHENQTCIatHESNGIDIIIALI 1960
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2228-2491 8.41e-12

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: 67.68  E-value: 8.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2228 FLVSIMLRSI------YTIGLGPTLILLGAANLCNKIVFLVSFV------GNRGTFTRGYRaVILDMA-----FLYHVAY 2290
Cdd:pfam00520    8 ILLLILLNTIflaletYFQPEEPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPW-NILDFVvvlpsLISLVLS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2291 VLVCMLGLFVHEFFYSFLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIIGFLFLKDDFtmevdrlknrt 2370
Cdd:pfam00520   87 SVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL----------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2371 pvtgsndgvptmtltsmlgtcpkencsptipssnaAGEGGEDGIERTCDTLLMCIVTVLNqgLRNGGGVGDVLRRPSKDE 2450
Cdd:pfam00520  156 -----------------------------------KTWENPDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGK 198

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1958771641 2451 PLFAArVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQ 2491
Cdd:pfam00520  199 GEFWA-YIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR super family cl03182
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1140-1282 3.57e-09

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: 59.13  E-value: 3.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 1140 QHQRLLKNMGAHSVVL---DLLQIPY-----------EKTDEKMNEVMDLAHTFLQNFCRGNPQNQVLLHKHLNLFLTP- 1204
Cdd:pfam01365   33 QRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQl 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 1205 -------GLLeaETMRHIFMNNYHLC-NEISERVVQHFVHCIETHGRHVEYLRFLQTIVKADGKYVKKCQDMVMTELINg 1276
Cdd:pfam01365  113 gspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP- 189


                   ....*.
gi 1958771641 1277 GEDVLI 1282
Cdd:pfam01365  190 NPDLLL 195
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 156-377 6.06e-159

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: 489.94  E-value: 6.06e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  156 WKITLFMKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAG 235
Cdd:cd23288      1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  236 QWNSLFRFKHLATGNYLAAELNPDYRDAQNEGKTVRDGELPTSKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRA 315
Cdd:cd23288     81 QWNSLFRFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKKRQAAEKIMYTLVSVPHGNDIASLFELDATTLQRA 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958771641  316 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEV 377
Cdd:cd23288    161 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 413-608 3.60e-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: 265.99  E-value: 3.60e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  413 LLEDLIFFVADVTNN---GQDVLDVVITKPNRERQKLMREQNILAQVFG---ILKAPFKekageGSMLRLEDLGDQRYAP 486
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT-----GALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  487 YKYVLRLCYRVLRHSQQDYRKNQEYIAKNFCVMQSQIGYDILAE---DTITALLHNNRKLLEKHITAKEIETFVSLLRRN 563
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958771641  564 -REPRFLDYLSDLCVSNSTAIPVTQELICKFMLSpgNADILIQTKL 608
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 170-370 8.58e-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: 249.97  E-value: 8.58e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  170 DVLKGGDVVRLFHAEQEKFLTCDDYEKKQHiFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLFRFKHLATG 249
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  250 NYLAAELNPdyrdaqnegktvrdgELPTSKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPRNSYVRLRH 329
Cdd:pfam02815   80 RYLHSHEEQ---------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQH 144

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958771641  330 LCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIV 370
Cdd:pfam02815  145 VCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 1-166 4.37e-62

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: 211.97  E-value: 4.37e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641    1 MNRYSAQKQYWKAKQAKQGNHteaALLKKLQHAAELEQKQNesenrkllgeiVKYSNVIQLLHIKSNKYLTVNKRLPALL 80
Cdd:pfam08709   59 ANSYAAQKELWSAGNRSPNGN---SLTDALKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLR 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641   81 EKNAMRVSLDAAGN-EGSWFYIHPFWKLRSEGDNIVVGDKVVLMPVNAGQPLH-ASNVELLDNPGcKEVNAVNCNTSWKI 158
Cdd:pfam08709  125 DKNAMRVVLDEAGNgEGCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKM 203


                   ....*...
gi 1958771641  159 TLFMKFSS 166
Cdd:pfam08709  204 EPFMSGCE 211
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1853-1960 1.91e-38

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: 139.58  E-value: 1.91e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 1853 ITIMRPILRFLQLLCENHNRELQNFLRNQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINEKNVALVNQTLESLT 1931
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 1958771641 1932 EYCQGPCHENQTCIatHESNGIDIIIALI 1960
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2228-2491 8.41e-12

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: 67.68  E-value: 8.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2228 FLVSIMLRSI------YTIGLGPTLILLGAANLCNKIVFLVSFV------GNRGTFTRGYRaVILDMA-----FLYHVAY 2290
Cdd:pfam00520    8 ILLLILLNTIflaletYFQPEEPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPW-NILDFVvvlpsLISLVLS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2291 VLVCMLGLFVHEFFYSFLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIIGFLFLKDDFtmevdrlknrt 2370
Cdd:pfam00520   87 SVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL----------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2371 pvtgsndgvptmtltsmlgtcpkencsptipssnaAGEGGEDGIERTCDTLLMCIVTVLNqgLRNGGGVGDVLRRPSKDE 2450
Cdd:pfam00520  156 -----------------------------------KTWENPDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGK 198

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1958771641 2451 PLFAArVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQ 2491
Cdd:pfam00520  199 GEFWA-YIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1140-1282 3.57e-09

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: 59.13  E-value: 3.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 1140 QHQRLLKNMGAHSVVL---DLLQIPY-----------EKTDEKMNEVMDLAHTFLQNFCRGNPQNQVLLHKHLNLFLTP- 1204
Cdd:pfam01365   33 QRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQl 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 1205 -------GLLeaETMRHIFMNNYHLC-NEISERVVQHFVHCIETHGRHVEYLRFLQTIVKADGKYVKKCQDMVMTELINg 1276
Cdd:pfam01365  113 gspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP- 189


                   ....*.
gi 1958771641 1277 GEDVLI 1282
Cdd:pfam01365  190 NPDLLL 195
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
232-262 1.53e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.64  E-value: 1.53e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1958771641   232 GGAGQWNSLFRFKHLATGNYLAAELNPDYRD 262
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPW 31
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
50-104 4.46e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 43.10  E-value: 4.46e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958771641    50 GEIVKYSNVIQLLHIKSNKYLTVNKRLPALLEKNAMRVSL--DAAGNEGSWFYIHPF 104
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGygNPAIDANTLWLIEPV 57
glyco_rpt_poly TIGR04370
oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic ...
 2146-2356 8.11e-04

oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic proteins, with few highly conserved residues, all may act to polymerize the oligosaccharide repeat units of surface polysaccharides, including O-antigen in Gram-negative bacteria such as Leptospira (assign gene symbol wzy) and capsular polysaccharide in Gram-positive bacteria such as Streptococcus. O-antigen biosynthesis enzymes produce a repeat unit, usually an oligosaccharide, which itself is polymerized. O-antigen polymerase, usually designated Wzy. This family bears homology to the O-antigen ligase WaaL, but known examples of WaaL fall outside the bounds defined here. This model is much broader than pfam14296. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 275163 [Multi-domain]  Cd Length: 392  Bit Score: 44.46  E-value: 8.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2146 KWQKKIRNNPALFwfsrhISLWgSISFNLAVFINLAVALFYPFGDDgdegTLSPLFSALLWVAVAICTSMLFFFSKPVGI 2225
Cdd:TIGR04370    3 KKKKDILSPIILF-----SLIW-LLIFLLSLLLLSYLSFLYPLSDY----TYLIIILGILIFIFGSLFLSLSLKSKKRKT 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2226 RP----------------------FLVSIMLRSIYTIGLGPTLILLGAANLcnkivFLVSFVGNRGTFTRGYRAVILDMA 2283
Cdd:TIGR04370   73 RKkklskisisliilflfflililLLLIILLLLLYIISLIGILGILSLLGS-----ALGYLALSGSTFLSGLIILLYILI 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958771641 2284 FLYhvaYVLVCMLGLFVHEFFYSFLLFdlvyreetLLNVIKSVTRNGRSIILTAVLALILVYLFSIIGFLFLK 2356
Cdd:TIGR04370  148 ILL---LLLFLLLLLKKKRKKLLLLLI--------LLALLISLLTGSRTGLILLILSLLFIYYLFYKKKSLKK 209
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 156-377 6.06e-159

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: 489.94  E-value: 6.06e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  156 WKITLFMKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAG 235
Cdd:cd23288      1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  236 QWNSLFRFKHLATGNYLAAELNPDYRDAQNEGKTVRDGELPTSKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRA 315
Cdd:cd23288     81 QWNSLFRFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKKRQAAEKIMYTLVSVPHGNDIASLFELDATTLQRA 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958771641  316 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEV 377
Cdd:cd23288    161 DCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 162-377 3.16e-135

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: 420.99  E-value: 3.16e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  162 MKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLF 241
Cdd:cd23277      1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  242 RFKHLATGNYLAAELNPDYRDAqnegktvrdgelPTSKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPR 321
Cdd:cd23277     81 RFKHLATGQYLAAEVDPDPTPD------------PTRSKLRGAPGKPVYCLVSVPHGNDIASIFELDPTTLQRGDSLVPR 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958771641  322 NSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEV 377
Cdd:cd23277    149 SSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 162-377 1.55e-123

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: 388.25  E-value: 1.55e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  162 MKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLF 241
Cdd:cd23289      1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  242 RFKHLATGNYLAAELNPDYRDAQNEGKTVRDGElPTSKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPR 321
Cdd:cd23289     81 RFKHLATGNYLAAEENPSYKGDASDPKAAGMGA-QSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVPR 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958771641  322 NSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEV 377
Cdd:cd23289    160 NSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 162-382 1.50e-121

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: 382.88  E-value: 1.50e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  162 MKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHIFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLF 241
Cdd:cd23287      1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  242 RFKHLATGNYLAAELNPDYRDAQNEGKTVRDGELPTSKKK-RQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVP 320
Cdd:cd23287     81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRlRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958771641  321 RNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVCVPLSEVRDLDF 382
Cdd:cd23287    161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 413-608 3.60e-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: 265.99  E-value: 3.60e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  413 LLEDLIFFVADVTNN---GQDVLDVVITKPNRERQKLMREQNILAQVFG---ILKAPFKekageGSMLRLEDLGDQRYAP 486
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT-----GALLFAEDLGEEKNAP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  487 YKYVLRLCYRVLRHSQQDYRKNQEYIAKNFCVMQSQIGYDILAE---DTITALLHNNRKLLEKHITAKEIETFVSLLRRN 563
Cdd:pfam01365   76 WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKH 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958771641  564 -REPRFLDYLSDLCVSNSTAIPVTQELICKFMLSpgNADILIQTKL 608
Cdd:pfam01365  156 gRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 170-370 8.58e-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: 249.97  E-value: 8.58e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  170 DVLKGGDVVRLFHAEQEKFLTCDDYEKKQHiFLRTTLRQSATSATSSKALWEIEVVHHDPCRGGAGQWNSLFRFKHLATG 249
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  250 NYLAAELNPdyrdaqnegktvrdgELPTSKKKRQAGEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVPRNSYVRLRH 329
Cdd:pfam02815   80 RYLHSHEEQ---------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQH 144

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1958771641  330 LCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIV 370
Cdd:pfam02815  145 VCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 1-166 4.37e-62

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: 211.97  E-value: 4.37e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641    1 MNRYSAQKQYWKAKQAKQGNHteaALLKKLQHAAELEQKQNesenrkllgeiVKYSNVIQLLHIKSNKYLTVNKRLPALL 80
Cdd:pfam08709   59 ANSYAAQKELWSAGNRSPNGN---SLTDALKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLR 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641   81 EKNAMRVSLDAAGN-EGSWFYIHPFWKLRSEGDNIVVGDKVVLMPVNAGQPLH-ASNVELLDNPGcKEVNAVNCNTSWKI 158
Cdd:pfam08709  125 DKNAMRVVLDEAGNgEGCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIFLHtTSSSELRDNPG-KEVNASFGQTSWKM 203


                   ....*...
gi 1958771641  159 TLFMKFSS 166
Cdd:pfam08709  204 EPFMSGCE 211
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1853-1960 1.91e-38

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: 139.58  E-value: 1.91e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 1853 ITIMRPILRFLQLLCENHNRELQNFLRNQ-NNKTNYNLVCETLQFLDCICGSttgglgllglyINEKNVALVNQTLESLT 1931
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQtNNKNSYNLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 1958771641 1932 EYCQGPCHENQTCIatHESNGIDIIIALI 1960
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 ...
 169-377 1.84e-25

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: 106.32  E-value: 1.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  169 EDVLKGGDVVRLFHAEQEKFLTCD--------DYEKKQHIFLRTTLRQ-SATSATSSKALWEIEVVHhDPCRGGAGQWNS 239
Cdd:cd23280      4 ENFLKGGDVVRLFHKELEAYLSAEgsfvdevlTEDVHLRVRPVDDRKPrTLFPPTSGDTFWQIEKED-TPLKGGVIKWGD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  240 LFRFKHLATGNYLAAELNpdyrdaqnegktvrdgelptskkkrqageKIMYTLVSVPHGNDIASLFELDATTLQRADcLV 319
Cdd:cd23280     83 QCRLRHLPTGKYLAVDDK-----------------------------TGNGKVVLTSDPSDPSTVFRLHPVTKETSE-EV 132

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958771641  320 PRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVML---------KIGTCQTKEDKEAFAIVCVPLSEV 377
Cdd:cd23280    133 KFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGlswdgaklrKVSLSLERQDDDAFTIQEVDPDLV 199
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 175-372 1.21e-21

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: 94.37  E-value: 1.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  175 GDVVRLFHAEQEKFLTCDDY-----EKKQHIFLRTTLRQsatsaTSSKALWEIEVVHHDPcrGGAGQWNSLFRFKHLATG 249
Cdd:cd23263      1 GDVIWLKHSETGKYLHSHRKnyptgSGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  250 NYLAAELNpdyrdaqnegktvrdgelPTSKKKRQAgekimYTLVSVPHGnDIASLFELDAT-TLQRADCLVPRNSYVRLR 328
Cdd:cd23263     74 KYLSSEEG------------------KKSPKSNHQ-----EVLCLTDNP-DKSSLFKFEPIgSTKYKQKYVKKDSYFRLK 129

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958771641  329 HLCTNTWVTSTSIPIDTEEErpvMLKIGTCQtKEDKEAFAIVCV 372
Cdd:cd23263    130 HVNTNFWLHSHEKKFNINNK---TQQEVICH-GEREEVFKLWKA 169
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2228-2491 8.41e-12

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: 67.68  E-value: 8.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2228 FLVSIMLRSI------YTIGLGPTLILLGAANLCNKIVFLVSFV------GNRGTFTRGYRaVILDMA-----FLYHVAY 2290
Cdd:pfam00520    8 ILLLILLNTIflaletYFQPEEPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPW-NILDFVvvlpsLISLVLS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2291 VLVCMLGLFVHEFFYSFLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIIGFLFLKDDFtmevdrlknrt 2370
Cdd:pfam00520   87 SVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL----------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2371 pvtgsndgvptmtltsmlgtcpkencsptipssnaAGEGGEDGIERTCDTLLMCIVTVLNqgLRNGGGVGDVLRRPSKDE 2450
Cdd:pfam00520  156 -----------------------------------KTWENPDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGK 198

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1958771641 2451 PLFAArVVYDLLFFFIVIIIVLNLIFGVIIDTFADLRSEKQ 2491
Cdd:pfam00520  199 GEFWA-YIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1140-1282 3.57e-09

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: 59.13  E-value: 3.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 1140 QHQRLLKNMGAHSVVL---DLLQIPY-----------EKTDEKMNEVMDLAHTFLQNFCRGNPQNQVLLHKHLNLFLTP- 1204
Cdd:pfam01365   33 QRQNLMREQGVLETVMeviDLLGAPFtgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQl 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 1205 -------GLLeaETMRHIFMNNYHLC-NEISERVVQHFVHCIETHGRHVEYLRFLQTIVKADGKYVKKCQDMVMTELINg 1276
Cdd:pfam01365  113 gspslaeGTL--DVLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP- 189


                   ....*.
gi 1958771641 1277 GEDVLI 1282
Cdd:pfam01365  190 NPDLLL 195
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 172-253 3.58e-06

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: 49.91  E-value: 3.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  172 LKGGDVVRLFHAEQEKfLTCDDYEK--KQHiflRTTLRQSATSATSSKALWEIEvvhhdPCR----GGAGQWNSLFRFKH 245
Cdd:cd23292      3 LLGGHVVRLFHGHDEC-LTIPSTDQsdEQH---RVVNYEAGGAGTRARSLWRLE-----PLRiswsGSHIRWGQTFRLRH 73


                   ....*...
gi 1958771641  246 LATGNYLA 253
Cdd:cd23292     74 LTTGHYLA 81
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 153-252 8.95e-06

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: 48.87  E-value: 8.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  153 NTSWKI---TLFMKFSSYREDVLKGGDVVRLFHAEQEKFLTCDDYE---KKQHifLRTTLRQSATSATSSKALWEIEVVh 226
Cdd:cd23276     44 NNWWQIlkpRGDPSSNPPDPEYVRDGDEVRLLHKETNRYLRTHDAAapvTSKH--KEVSAYPDENEDGDDNDLWVVEIV- 120

                           90       100
                   ....*....|....*....|....*....
gi 1958771641  227 HDPCRGGAGQWNSL---FRFKHLATGNYL 252
Cdd:cd23276    121 KDEGKLEDKRIKPLttrFRLRNKKTGCYL 149
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 169-301 1.45e-05

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: 48.35  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  169 EDVLKGGDVVRLFHAEQEKFLTCDDYEKKQHifLRTTLRQSATSATSSKALWEIEvvhhdPCR----GGAGQWNSLFRFK 244
Cdd:cd23290      5 EGYVTGGHVLRLFHGHMDECLTISAADSDDQ--RRLVYYEGGAVCTHARSLWRLE-----PLRiswsGSHLRWGQPLRIR 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958771641  245 HLATGNYLAAElnpdyrdaQNEGKTVRDGELPTSKKK----RQAGEKImytlvSVPHGNDI 301
Cdd:cd23290     78 HVTTGRYLALT--------EDQGLVVVDACKAHTKATsfcfRVSKEKL-----DTAPKRDV 125
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
232-262 1.53e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.64  E-value: 1.53e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 1958771641   232 GGAGQWNSLFRFKHLATGNYLAAELNPDYRD 262
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPW 31
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 174-259 2.56e-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: 47.30  E-value: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  174 GGDVVRLFHAEQEKFLTC--DDYEKKQHiflRTTLRQSATSATSSKALWEIEVVHHDPCrGGAGQWNSLFRFKHLATGNY 251
Cdd:cd23278      1 GGDVLRLFHGHMDECLTIpaAGSKEDQH---RTVIYEGGAVSTHARSLWRLELLRIKWS-GSHIGWGQPFRLRHVTTGRY 76


                   ....*...
gi 1958771641  252 LAaeLNPD 259
Cdd:cd23278     77 LA--LTED 82
Yip1 pfam04893
Yip1 domain; The Yip1 integral membrane domain contains four transmembrane alpha helices. The ...
 2200-2349 4.33e-05

Yip1 domain; The Yip1 integral membrane domain contains four transmembrane alpha helices. The domain is characterized by the motifs DLYGP and GY. The Yip1 protein is a golgi protein involved in vesicular transport that interacts with GTPases.


Pssm-ID: 461468 [Multi-domain]  Cd Length: 173  Bit Score: 46.28  E-value: 4.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2200 LFSALLWVAVAICTSMLFFFSKPVGIRPFLVSIMLRSIYT-IGLGPTLILLGAAnlcnkIVFLVSFVGNRGTFTRGYRAV 2278
Cdd:pfam04893   26 LILLLLLALLAALALLIGGTQVGWALSLTQLSALAVAIGAlIGILLGLLILAAL-----LYWLGRLFGGRGSFKQTLAVA 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2279 ILDMA---------FLYHVAYVLVCMLGLFVHeFFYSFLLFdlvyreETLLNVIKSVTRNGRSIILTAVLALILVYLFSI 2349
Cdd:pfam04893  101 GYALLplilggllsGLLPLLWLPLSLVGLLFG-IWSLYLLY------LGLKEAHGLSSKKAAALIAALLLLLLLLLLVLL 173
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
50-104 4.46e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 43.10  E-value: 4.46e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958771641    50 GEIVKYSNVIQLLHIKSNKYLTVNKRLPALLEKNAMRVSL--DAAGNEGSWFYIHPF 104
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGygNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
111-158 5.21e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.02  E-value: 5.21e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1958771641   111 GDNIVVGDKVVLMPVNAGQPLHAS-NVELLDNPGCKEVNAV-----NCNTSWKI 158
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHdEKLPPWGDGQQEVTGYgnpaiDANTLWLI 54
glyco_rpt_poly TIGR04370
oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic ...
 2146-2356 8.11e-04

oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic proteins, with few highly conserved residues, all may act to polymerize the oligosaccharide repeat units of surface polysaccharides, including O-antigen in Gram-negative bacteria such as Leptospira (assign gene symbol wzy) and capsular polysaccharide in Gram-positive bacteria such as Streptococcus. O-antigen biosynthesis enzymes produce a repeat unit, usually an oligosaccharide, which itself is polymerized. O-antigen polymerase, usually designated Wzy. This family bears homology to the O-antigen ligase WaaL, but known examples of WaaL fall outside the bounds defined here. This model is much broader than pfam14296. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 275163 [Multi-domain]  Cd Length: 392  Bit Score: 44.46  E-value: 8.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2146 KWQKKIRNNPALFwfsrhISLWgSISFNLAVFINLAVALFYPFGDDgdegTLSPLFSALLWVAVAICTSMLFFFSKPVGI 2225
Cdd:TIGR04370    3 KKKKDILSPIILF-----SLIW-LLIFLLSLLLLSYLSFLYPLSDY----TYLIIILGILIFIFGSLFLSLSLKSKKRKT 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641 2226 RP----------------------FLVSIMLRSIYTIGLGPTLILLGAANLcnkivFLVSFVGNRGTFTRGYRAVILDMA 2283
Cdd:TIGR04370   73 RKkklskisisliilflfflililLLLIILLLLLYIISLIGILGILSLLGS-----ALGYLALSGSTFLSGLIILLYILI 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958771641 2284 FLYhvaYVLVCMLGLFVHEFFYSFLLFdlvyreetLLNVIKSVTRNGRSIILTAVLALILVYLFSIIGFLFLK 2356
Cdd:TIGR04370  148 ILL---LLLFLLLLLKKKRKKLLLLLI--------LLALLISLLTGSRTGLILLILSLLFIYYLFYKKKSLKK 209
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
169-225 1.26e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 39.25  E-value: 1.26e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958771641   169 EDVLKGGDVVRLFHAEQEKFLTCDD---YE---KKQHIFLRTTLRQSATSatsskaLWEIEVV 225
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDeklPPwgdGQQEVTGYGNPAIDANT------LWLIEPV 57
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 174-253 1.86e-03

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: 41.95  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958771641  174 GGDVVRLFHAEQEKFLTCDDYEKKQHIfLRTTLRQSATSATSSKALWEIEVVHHdPCRGGAGQWNSLFRFKHLATGNYLA 253
Cdd:cd23291      1 GGDVLRLLHGHMDECLTVPSGEHGEEQ-RRTVHYEGGAVSVHARSLWRLETLRV-AWSGSHIRWGQPFRLRHVTTGKYLS 78
 
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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