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Conserved domains on  [gi|1712969826|ref|XP_029991382|]
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inositol 1,4,5-trisphosphate receptor type 1-like isoform X11 [Sphaeramia orbicularis]

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 super family cl49619
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 224-458 6.83e-145

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.


The actual alignment was detected with superfamily member cd23287:

Pssm-ID: 483959 [Multi-domain]  Cd Length: 222  Bit Score: 449.52  E-value: 6.83e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  224 MKWSDNKETILKGGDVVRLFHAEQEKFLTCDDHRKKQYVFLRTTGRQSATSATSSKALWEVEVVHHDPCRGGAGYWNSLF 303
Cdd:cd23287      1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  304 RFKHLATGCYLAAEVgevNPDFEEESAEQRSSVvdftpfnfqlDADNEALRGRLRAPQEKIMYTLVPVPDGMDISSIFEL 383
Cdd:cd23287     81 RFKHLATGHYLAAEV---DPDFEEECLEFQPSV----------DPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFEL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712969826  384 DPTTLRGGDSMVPRSSYVRLRHLCTNTWVHSTNNPIDKEEEKPVMLRIGTSAVKEDKEAFAIVPVPPAEVRDLDF 458
Cdd:cd23287    148 DPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 5-229 2.83e-102

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: 327.15  E-value: 2.83e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826    5 MSSFLHIGDICSLYAEGSTSGFISTLGLVDDRCVVQPDTGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKA--AKPGGNS 82
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAgnRSPNGNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826   83 TTDTvllnkLHHAADLEKKQNesenrkllgtvIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDSAGN-EGSWF 161
Cdd:pfam08709   81 LTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWF 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712969826  162 YIQPFYKLRSLGDSVVIGDKVVLNPVNAGQPLH-ASSHQLVDNPGcNEVNSVNCNTSWKVVLFMKWSDN 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 ...
 489-683 1.71e-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: 267.14  E-value: 1.71e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  489 LLEDLVFFVVDIPNS---GQDVLEIMVNKPNRERQKLMREQNILKQIFK---LLQAPFTdsgdGPMLRLEELGDQRHAPF 562
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  563 RHICRLCYRVLRHSQQDYRKNQEYIAKQFRFMQKQIGYDVLAE---DTITALLHNNRKLLEKHITAAEIDTFVTLVRKN- 638
Cdd:pfam01365   77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKHg 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1712969826  639 REPRFLDYLSDLCVSMNKSIPVTQELICNAVLDpaNADILIETKL 683
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1936-2043 8.50e-29

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: 112.23  E-value: 8.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 1936 ITIMQPILRLMQLLCENHNRDLQNFLRNQNNKNNYN-LVCETLQFLDCICGSttgglgllglyINEKNVGLINQTVESLT 2014
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYnLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 1712969826 2015 EYCQGPCHENQNCIatHECNGIDIIIALI 2043
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2342-2600 2.60e-20

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: 92.72  E-value: 2.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 2342 EPTLLLLGGFNLCNKVIFLMSFV------GNRGTFTRGYKAMIMDVEFLYHLLYLIICSLGVFVHV----FFYSLLLFDL 2411
Cdd:pfam00520   29 EPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPWNILDFVVVLPSLISLVLSSVGSLSGLrvlrLLRLLRLLRL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 2412 VYREETLLNVIKSVTRNGRSIVLTAVLALILVYLFSIVGYIFFKDDFilavdripnktlehgasmvgeffsggvcqkeng 2491
Cdd:pfam00520  109 IRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL--------------------------------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 2492 encstegvmdGTWTEVkaslavqpsavviEDKERTCDSLLMCIVTVLShgLRSGGGVGDVLRKPSKEEPLFAArVIYDLL 2571
Cdd:pfam00520  156 ----------KTWENP-------------DNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVS 209

                          250       260
                   ....*....|....*....|....*....
gi 1712969826 2572 FFFMVIIIVLNLIFGVIIDTFADLRSEKQ 2600
Cdd:pfam00520  210 FIILGGFLLLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR super family cl03182
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1212-1325 1.17e-06

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


The actual alignment was detected with superfamily member pfam01365:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 51.43  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 1212 KQQQRLLRNMGAHSVVLE---LLQIPYeKGEDVRMQE-----------IMKLAHEFLQNFCAGNQQNQALLHKHINLFLN 1277
Cdd:pfam01365   32 RQRQNLMREQGVLETVMEvidLLGAPF-TGALLFAEDlgeeknapwkkIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQS 110

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1712969826 1278 P--------GILEavTMQHIFMNNFQLC-SEINERVVQHFVHCIESHGRHVQYLKFL 1325
Cdd:pfam01365  111 QlgspslaeGTLD--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) ...
 224-458 6.83e-145

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: 449.52  E-value: 6.83e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  224 MKWSDNKETILKGGDVVRLFHAEQEKFLTCDDHRKKQYVFLRTTGRQSATSATSSKALWEVEVVHHDPCRGGAGYWNSLF 303
Cdd:cd23287      1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  304 RFKHLATGCYLAAEVgevNPDFEEESAEQRSSVvdftpfnfqlDADNEALRGRLRAPQEKIMYTLVPVPDGMDISSIFEL 383
Cdd:cd23287     81 RFKHLATGHYLAAEV---DPDFEEECLEFQPSV----------DPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFEL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712969826  384 DPTTLRGGDSMVPRSSYVRLRHLCTNTWVHSTNNPIDKEEEKPVMLRIGTSAVKEDKEAFAIVPVPPAEVRDLDF 458
Cdd:cd23287    148 DPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 5-229 2.83e-102

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: 327.15  E-value: 2.83e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826    5 MSSFLHIGDICSLYAEGSTSGFISTLGLVDDRCVVQPDTGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKA--AKPGGNS 82
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAgnRSPNGNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826   83 TTDTvllnkLHHAADLEKKQNesenrkllgtvIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDSAGN-EGSWF 161
Cdd:pfam08709   81 LTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWF 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712969826  162 YIQPFYKLRSLGDSVVIGDKVVLNPVNAGQPLH-ASSHQLVDNPGcNEVNSVNCNTSWKVVLFMKWSDN 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 ...
 489-683 1.71e-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: 267.14  E-value: 1.71e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  489 LLEDLVFFVVDIPNS---GQDVLEIMVNKPNRERQKLMREQNILKQIFK---LLQAPFTdsgdGPMLRLEELGDQRHAPF 562
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  563 RHICRLCYRVLRHSQQDYRKNQEYIAKQFRFMQKQIGYDVLAE---DTITALLHNNRKLLEKHITAAEIDTFVTLVRKN- 638
Cdd:pfam01365   77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKHg 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1712969826  639 REPRFLDYLSDLCVSMNKSIPVTQELICNAVLDpaNADILIETKL 683
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 233-446 3.51e-69

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: 231.10  E-value: 3.51e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  233 ILKGGDVVRLFHAEQEKFLTCDDHRKKQYvFLRTTGRQSATSATSSKALWEVEVVHHDPCRGGAGYWNSLFRFKHLATGC 312
Cdd:pfam02815    2 YLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  313 YLAAEVgevnpdfeeesaEQRSSVVDftpfnfqldadnealrgRLRAPQEKIMYTLVPVPDGMDISSIFELDPTTLRGGD 392
Cdd:pfam02815   81 YLHSHE------------EQKPPLVE-----------------KEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSD 131

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1712969826  393 SMVPRSSYVRLRHLCTNTWVHSTNNPIDKEEEKPVMLRIGTSAVKEDKEAFAIV 446
Cdd:pfam02815  132 RIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1936-2043 8.50e-29

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: 112.23  E-value: 8.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 1936 ITIMQPILRLMQLLCENHNRDLQNFLRNQNNKNNYN-LVCETLQFLDCICGSttgglgllglyINEKNVGLINQTVESLT 2014
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYnLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 1712969826 2015 EYCQGPCHENQNCIatHECNGIDIIIALI 2043
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2342-2600 2.60e-20

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: 92.72  E-value: 2.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 2342 EPTLLLLGGFNLCNKVIFLMSFV------GNRGTFTRGYKAMIMDVEFLYHLLYLIICSLGVFVHV----FFYSLLLFDL 2411
Cdd:pfam00520   29 EPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPWNILDFVVVLPSLISLVLSSVGSLSGLrvlrLLRLLRLLRL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 2412 VYREETLLNVIKSVTRNGRSIVLTAVLALILVYLFSIVGYIFFKDDFilavdripnktlehgasmvgeffsggvcqkeng 2491
Cdd:pfam00520  109 IRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL--------------------------------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 2492 encstegvmdGTWTEVkaslavqpsavviEDKERTCDSLLMCIVTVLShgLRSGGGVGDVLRKPSKEEPLFAArVIYDLL 2571
Cdd:pfam00520  156 ----------KTWENP-------------DNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVS 209

                          250       260
                   ....*....|....*....|....*....
gi 1712969826 2572 FFFMVIIIVLNLIFGVIIDTFADLRSEKQ 2600
Cdd:pfam00520  210 FIILGGFLLLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1212-1325 1.17e-06

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


Pssm-ID: 460175  Cd Length: 199  Bit Score: 51.43  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 1212 KQQQRLLRNMGAHSVVLE---LLQIPYeKGEDVRMQE-----------IMKLAHEFLQNFCAGNQQNQALLHKHINLFLN 1277
Cdd:pfam01365   32 RQRQNLMREQGVLETVMEvidLLGAPF-TGALLFAEDlgeeknapwkkIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQS 110

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1712969826 1278 P--------GILEavTMQHIFMNNFQLC-SEINERVVQHFVHCIESHGRHVQYLKFL 1325
Cdd:pfam01365  111 QlgspslaeGTLD--VLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
112-166 3.88e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 3.88e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1712969826   112 GTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTL--DSAGNEGSWFYIQPF 166
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGygNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
231-287 2.48e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 43.87  E-value: 2.48e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712969826   231 ETILKGGDVVRLFHAEQEKFLTCDDHR------KKQYVFLRTTGRQSATSatsskaLWEVEVV 287
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlppwgdGQQEVTGYGNPAIDANT------LWLIEPV 57
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 104-199 1.28e-03

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


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 41.99  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  104 ESENRKLlGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDSAGNEGSWFYIQPFYKLRSLGDSVVIGDKVV 183
Cdd:cd23263     49 ESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDKSSLFKFEPIGSTKYKQKYVKKDSYFR 127

                           90
                   ....*....|....*.
gi 1712969826  184 LNPVNAGQPLHasSHQ 199
Cdd:cd23263    128 LKHVNTNFWLH--SHE 141
 
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) ...
 224-458 6.83e-145

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: 449.52  E-value: 6.83e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  224 MKWSDNKETILKGGDVVRLFHAEQEKFLTCDDHRKKQYVFLRTTGRQSATSATSSKALWEVEVVHHDPCRGGAGYWNSLF 303
Cdd:cd23287      1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  304 RFKHLATGCYLAAEVgevNPDFEEESAEQRSSVvdftpfnfqlDADNEALRGRLRAPQEKIMYTLVPVPDGMDISSIFEL 383
Cdd:cd23287     81 RFKHLATGHYLAAEV---DPDFEEECLEFQPSV----------DPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFEL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1712969826  384 DPTTLRGGDSMVPRSSYVRLRHLCTNTWVHSTNNPIDKEEEKPVMLRIGTSAVKEDKEAFAIVPVPPAEVRDLDF 458
Cdd:cd23287    148 DPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 224-453 7.30e-132

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: 411.36  E-value: 7.30e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  224 MKWSDNKETILKGGDVVRLFHAEQEKFLTCDDHRKKQYVFLRTTGRQSATSATSSKALWEVEVVHHDPCRGGAGYWNSLF 303
Cdd:cd23277      1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  304 RFKHLATGCYLAAevgEVNPDFEEesaeqrssvvdftpfnfqldadnEALRGRLRAPQEKIMYTLVPVPDGMDISSIFEL 383
Cdd:cd23277     81 RFKHLATGQYLAA---EVDPDPTP-----------------------DPTRSKLRGAPGKPVYCLVSVPHGNDIASIFEL 134

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  384 DPTTLRGGDSMVPRSSYVRLRHLCTNTWVHSTNNPIDKEEEKPVMLRIGTSAVKEDKEAFAIVPVPPAEV 453
Cdd:cd23277    135 DPTTLQRGDSLVPRSSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 218-453 3.58e-117

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: 370.14  E-value: 3.58e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  218 WKVVLFMKWSDNKETILKGGDVVRLFHAEQEKFLTCDDHRKKQYVFLRTTGRQSATSATSSKALWEVEVVHHDPCRGGAG 297
Cdd:cd23288      1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  298 YWNSLFRFKHLATGCYLAAevgEVNPDFEEESAEQRSSVVDFTPFNfqldadnealrGRLRAPQEKIMYTLVPVPDGMDI 377
Cdd:cd23288     81 QWNSLFRFKHLATGNYLAA---EVNPDYRDAQNEGKAVNDGDSPTS-----------KKKRQAAEKIMYTLVSVPHGNDI 146

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712969826  378 SSIFELDPTTLRGGDSMVPRSSYVRLRHLCTNTWVHSTNNPIDKEEEKPVMLRIGTSAVKEDKEAFAIVPVPPAEV 453
Cdd:cd23288    147 ASLFELDATTLQRADCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 224-453 2.35e-105

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: 336.25  E-value: 2.35e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  224 MKWSDNKETILKGGDVVRLFHAEQEKFLTCDDHRKKQYVFLRTTGRQSATSATSSKALWEVEVVHHDPCRGGAGYWNSLF 303
Cdd:cd23289      1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  304 RFKHLATGCYLAAevgEVNPDFEEESAEQRSSVVdftpfnfqldaDNEALRGRlRAPQEKIMYTLVPVPDGMDISSIFEL 383
Cdd:cd23289     81 RFKHLATGNYLAA---EENPSYKGDASDPKAAGM-----------GAQSRTGR-RNAGEKIKYCLVAVPHGNDIASLFEL 145

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  384 DPTTLRGGDSMVPRSSYVRLRHLCTNTWVHSTNNPIDKEEEKPVMLRIGTSAVKEDKEAFAIVPVPPAEV 453
Cdd:cd23289    146 DPTTLQKTDSFVPRNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 5-229 2.83e-102

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: 327.15  E-value: 2.83e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826    5 MSSFLHIGDICSLYAEGSTSGFISTLGLVDDRCVVQPDTGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKA--AKPGGNS 82
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAgnRSPNGNS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826   83 TTDTvllnkLHHAADLEKKQNesenrkllgtvIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDSAGN-EGSWF 161
Cdd:pfam08709   81 LTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWF 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1712969826  162 YIQPFYKLRSLGDSVVIGDKVVLNPVNAGQPLH-ASSHQLVDNPGcNEVNSVNCNTSWKVVLFMKWSDN 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 ...
 489-683 1.71e-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: 267.14  E-value: 1.71e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  489 LLEDLVFFVVDIPNS---GQDVLEIMVNKPNRERQKLMREQNILKQIFK---LLQAPFTdsgdGPMLRLEELGDQRHAPF 562
Cdd:pfam01365    1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  563 RHICRLCYRVLRHSQQDYRKNQEYIAKQFRFMQKQIGYDVLAE---DTITALLHNNRKLLEKHITAAEIDTFVTLVRKN- 638
Cdd:pfam01365   77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRKHg 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1712969826  639 REPRFLDYLSDLCVSMNKSIPVTQELICNAVLDpaNADILIETKL 683
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 233-446 3.51e-69

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: 231.10  E-value: 3.51e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  233 ILKGGDVVRLFHAEQEKFLTCDDHRKKQYvFLRTTGRQSATSATSSKALWEVEVVHHDPCRGGAGYWNSLFRFKHLATGC 312
Cdd:pfam02815    2 YLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  313 YLAAEVgevnpdfeeesaEQRSSVVDftpfnfqldadnealrgRLRAPQEKIMYTLVPVPDGMDISSIFELDPTTLRGGD 392
Cdd:pfam02815   81 YLHSHE------------EQKPPLVE-----------------KEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSD 131

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1712969826  393 SMVPRSSYVRLRHLCTNTWVHSTNNPIDKEEEKPVMLRIGTSAVKEDKEAFAIV 446
Cdd:pfam02815  132 RIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 231-453 3.06e-30

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: 120.18  E-value: 3.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  231 ETILKGGDVVRLFHAEQEKFLTCD--------DHRKKQYV-FLRTTGRQSATSATSSKALWEVEVVHhDPCRGGAGYWNS 301
Cdd:cd23280      4 ENFLKGGDVVRLFHKELEAYLSAEgsfvdevlTEDVHLRVrPVDDRKPRTLFPPTSGDTFWQIEKED-TPLKGGVIKWGD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  302 LFRFKHLATGCYLAAEVGEVNpdfeeesaeqrssvvdftpfnfqldadnealrgrlrapqekimYTLVPVPDGMDISSIF 381
Cdd:cd23280     83 QCRLRHLPTGKYLAVDDKTGN-------------------------------------------GKVVLTSDPSDPSTVF 119

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  382 ELDPTTlRGGDSMVPRSSYVRLRHLCTNTWVHSTNNPIDKEEEKPVML---------RIGTSAVKEDKEAFAIVPVPPAE 452
Cdd:cd23280    120 RLHPVT-KETSEEVKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGlswdgaklrKVSLSLERQDDDAFTIQEVDPDL 198


                   .
gi 1712969826  453 V 453
Cdd:cd23280    199 V 199
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 1936-2043 8.50e-29

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: 112.23  E-value: 8.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 1936 ITIMQPILRLMQLLCENHNRDLQNFLRNQNNKNNYN-LVCETLQFLDCICGSttgglgllglyINEKNVGLINQTVESLT 2014
Cdd:pfam08454    3 VKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYnLVEETVDLLKAYCKS-----------INEKNIELIIQCLDTLT 71

                           90       100
                   ....*....|....*....|....*....
gi 1712969826 2015 EYCQGPCHENQNCIatHECNGIDIIIALI 2043
Cdd:pfam08454   72 EFIQGPCIENQIAL--CESKFLEIANDLL 98
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 237-424 9.69e-25

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: 103.23  E-value: 9.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  237 GDVVRLFHAEQEKFLTCDDHR-----KKQYVFLRTTGRQsatsaTSSKALWEVEVVHHDPcrGGAGYWNSLFRFKHLATG 311
Cdd:cd23263      1 GDVIWLKHSETGKYLHSHRKNyptgsGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  312 CYLAAEVGEVNPdfeeesaeqrssvvdftpfnfqLDADNEALrgrlrapqekimyTLVPVPdgmDISSIFELDPTTLRGG 391
Cdd:cd23263     74 KYLSSEEGKKSP----------------------KSNHQEVL-------------CLTDNP---DKSSLFKFEPIGSTKY 115

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1712969826  392 -DSMVPRSSYVRLRHLCTNTWVHSTNNPIDKEEE 424
Cdd:cd23263    116 kQKYVKKDSYFRLKHVNTNFWLHSHEKKFNINNK 149
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2342-2600 2.60e-20

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: 92.72  E-value: 2.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 2342 EPTLLLLGGFNLCNKVIFLMSFV------GNRGTFTRGYKAMIMDVEFLYHLLYLIICSLGVFVHV----FFYSLLLFDL 2411
Cdd:pfam00520   29 EPLTTVLEILDYVFTGIFTLEMLlkiiaaGFKKRYFRSPWNILDFVVVLPSLISLVLSSVGSLSGLrvlrLLRLLRLLRL 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 2412 VYREETLLNVIKSVTRNGRSIVLTAVLALILVYLFSIVGYIFFKDDFilavdripnktlehgasmvgeffsggvcqkeng 2491
Cdd:pfam00520  109 IRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL--------------------------------- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 2492 encstegvmdGTWTEVkaslavqpsavviEDKERTCDSLLMCIVTVLShgLRSGGGVGDVLRKPSKEEPLFAArVIYDLL 2571
Cdd:pfam00520  156 ----------KTWENP-------------DNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVS 209

                          250       260
                   ....*....|....*....|....*....
gi 1712969826 2572 FFFMVIIIVLNLIFGVIIDTFADLRSEKQ 2600
Cdd:pfam00520  210 FIILGGFLLLNLFIAVIIDNFQELTERTE 238
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 237-314 2.30e-07

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: 53.49  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  237 GDVVRLFHAEQEKFLTCDDHR----KKQYvflRTTGRQSATSATSSKALWEVEVVhHDPCRGGAGYWNSL---FRFKHLA 309
Cdd:cd23276     69 GDEVRLLHKETNRYLRTHDAAapvtSKHK---EVSAYPDENEDGDDNDLWVVEIV-KDEGKLEDKRIKPLttrFRLRNKK 144


                   ....*
gi 1712969826  310 TGCYL 314
Cdd:cd23276    145 TGCYL 149
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1212-1325 1.17e-06

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


Pssm-ID: 460175  Cd Length: 199  Bit Score: 51.43  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826 1212 KQQQRLLRNMGAHSVVLE---LLQIPYeKGEDVRMQE-----------IMKLAHEFLQNFCAGNQQNQALLHKHINLFLN 1277
Cdd:pfam01365   32 RQRQNLMREQGVLETVMEvidLLGAPF-TGALLFAEDlgeeknapwkkIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQS 110

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1712969826 1278 P--------GILEavTMQHIFMNNFQLC-SEINERVVQHFVHCIESHGRHVQYLKFL 1325
Cdd:pfam01365  111 QlgspslaeGTLD--VLTALLMDNPELLlNYIKECHIKSFISLLRKHGRDPRYLDFL 165
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 179-314 1.96e-06

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: 50.46  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  179 GDKVVLNPVNAGQPLHASSHQLVDNPGCNEVN------SVNCNTSWKVvlfMKWSDNKETILKGGDVVRLFHAEQEKFLT 252
Cdd:cd23263      1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTfesssrKGDTNGLWII---ESENGKQGGPVKWGDKIRLRHLSTGKYLS 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712969826  253 CDDH---RKKQYVFLRTTGRQSATSAtsskaLWEVEVVHHDPcrGGAGYW--NSLFRFKHLATGCYL 314
Cdd:cd23263     78 SEEGkksPKSNHQEVLCLTDNPDKSS-----LFKFEPIGSTK--YKQKYVkkDSYFRLKHVNTNFWL 137
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
112-166 3.88e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 3.88e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1712969826   112 GTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTL--DSAGNEGSWFYIQPF 166
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGygNPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
231-287 2.48e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 43.87  E-value: 2.48e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712969826   231 ETILKGGDVVRLFHAEQEKFLTCDDHR------KKQYVFLRTTGRQSATSatsskaLWEVEVV 287
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlppwgdGQQEVTGYGNPAIDANT------LWLIEPV 57
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 234-315 8.23e-05

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: 46.06  E-value: 8.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  234 LKGGDVVRLFHAEQEKF-LTCDDHRKKQYvflRTTGRQSATSATSSKALWEVEvvhhdPCR----GGAGYWNSLFRFKHL 308
Cdd:cd23292      3 LLGGHVVRLFHGHDECLtIPSTDQSDEQH---RVVNYEAGGAGTRARSLWRLE-----PLRiswsGSHIRWGQTFRLRHL 74


                   ....*..
gi 1712969826  309 ATGCYLA 315
Cdd:cd23292     75 TTGHYLA 81
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 236-352 8.64e-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: 45.76  E-value: 8.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  236 GGDVVRLFHAEQEKFLTC-------DDHRKKQYvflrttgrQSATSATSSKALWEVEVVHHDPCrGGAGYWNSLFRFKHL 308
Cdd:cd23278      1 GGDVLRLFHGHMDECLTIpaagskeDQHRTVIY--------EGGAVSTHARSLWRLELLRIKWS-GSHIGWGQPFRLRHV 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1712969826  309 ATGCYLAaevgeVNPDFEEESAEQRSSVVDFTPFNFQLDADNEA 352
Cdd:cd23278     72 TTGRYLA-----LTEDRGLVLVPKEKADVKATAFCFRQSKDDKK 110
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
173-220 1.68e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.56  E-value: 1.68e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1712969826   173 GDSVVIGDKVVLNPVNAGQPLHASSHQL-VDNPGCNEVNSV-----NCNTSWKV 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, ...
 231-317 1.80e-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: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  231 ETILKGGDVVRLFHAEQEKFLTC-----DDHRkkqyvflRTTGRQSATSATSSKALWEVEvvhhdPCR----GGAGYWNS 301
Cdd:cd23290      5 EGYVTGGHVLRLFHGHMDECLTIsaadsDDQR-------RLVYYEGGAVCTHARSLWRLE-----PLRiswsGSHLRWGQ 72

                           90
                   ....*....|....*.
gi 1712969826  302 LFRFKHLATGCYLAAE 317
Cdd:cd23290     73 PLRIRHVTTGRYLALT 88
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
294-317 2.15e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.17  E-value: 2.15e-04
                            10        20
                    ....*....|....*....|....
gi 1712969826   294 GGAGYWNSLFRFKHLATGCYLAAE 317
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSH 24
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 236-412 8.41e-04

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: 43.11  E-value: 8.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  236 GGDVVRLFHAEQEKFLTC--DDHRKKQYvflRTTGRQSATSATSSKALWEVEVVHHdPCRGGAGYWNSLFRFKHLATGCY 313
Cdd:cd23291      1 GGDVLRLLHGHMDECLTVpsGEHGEEQR---RTVHYEGGAVSVHARSLWRLETLRV-AWSGSHIRWGQPFRLRHVTTGKY 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  314 LAAEVGEVNPDFEEESAEQRSSVVDFtpfnfqldadnealrgrlRAPQEKIMYTLVPVPDGMDISSIfeldpttlRGGDS 393
Cdd:cd23291     77 LSLMEDKNLLLMDKEKADVKSTAFTF------------------RSSKEKLDVGVRKEVDGMGTSEI--------KYGDS 130

                          170
                   ....*....|....*....
gi 1712969826  394 MvprsSYVrlRHLCTNTWV 412
Cdd:cd23291    131 V----CYI--QHVDTGLWL 143
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 104-199 1.28e-03

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


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 41.99  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712969826  104 ESENRKLlGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDSAGNEGSWFYIQPFYKLRSLGDSVVIGDKVV 183
Cdd:cd23263     49 ESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDKSSLFKFEPIGSTKYKQKYVKKDSYFR 127

                           90
                   ....*....|....*.
gi 1712969826  184 LNPVNAGQPLHasSHQ 199
Cdd:cd23263    128 LKHVNTNFWLH--SHE 141
 
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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