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Conserved domains on  [gi|2462512296|ref|XP_054194077|]
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ryanodine receptor 2 isoform X11 [Homo sapiens]

Protein Classification

ryanodine receptor( domain architecture ID 11696383)

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; similar to human ryanodine receptor 2, also called cardiac muscle ryanodine receptor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 230-413 1.83e-119

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: 375.92  E-value: 1.83e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  230 GGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 309
Cdd:cd23291      1 GGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  310 EDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSIQR 389
Cdd:cd23291     81 EDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSIQR 160

                          170       180
                   ....*....|....*....|....
gi 2462512296  390 KAIMHHEGHMDDGISLSRSQHEES 413
Cdd:cd23291    161 KAIMHHEGHMDDGLNLSRSQHEES 184
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4260-4526 4.47e-108

Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 family.


:

Pssm-ID: 461918  Cd Length: 282  Bit Score: 347.46  E-value: 4.47e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4260 NMPDPTQDEVRGDGEEGERKPLEAALPSEDLTDLKELTEESDLLSDIFGLDLKREGGQYKLIPHNPNAGLSDLMSNPV-- 4337
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLADAAGGEEEEDLLSDIFGLILKKEGGQYKVVPHDPEAGLGDLSETTAee 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4338 PMPEVQEKFQEQKAKEEEKEEKE-----------ETKSEPEKAEGEDGEKEEKAKEDKGKQKLRQLHTHRYGEPEVPESA 4406
Cdd:pfam06459   81 PPPLLKRKLQESEEAEDEEEEEEepkpepiekadGENGEKEEKPKEEETESEAPEEEEMKKKQRKRHSKKKEEPEAQGSA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4407 FWKKIIAYQQKLLNYFARNFYNMRMLALFVAFAINFILLFYKVSTSS-VVEGKELPTRSSSENAKVTSLDSS-SHRIIAV 4484
Cdd:pfam06459  161 FWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPpDEEEEEGSGWGDSGSGSGGGSGEDeEEEEGPV 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462512296 4485 HYVLEESSGYMEPTLRILAILHTVISFFCIIGYYCLKVPLVI 4526
Cdd:pfam06459  241 YFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 455-648 9.29e-92

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: 297.19  E-value: 9.29e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  455 SLQDLIGYFHPPDEHLEHEDKQNRL---RALKNRQNLFQEEGMINLVLECIDRLH-VYSSAAHFADVAGREAGESWKSIL 530
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  531 NSLYELLAALIRGNRKNCAQFSGSLDWLISRLERLEASSGILEVLHCVLVESPE-ALNIIKEGHIKSIISLLDKHGRNHK 609
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462512296  610 VLDVLCSLCVCHGVAVRSNQHLICDNLLPGRDLLLQTRL 648
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1086-1218 6.47e-87

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1


:

Pssm-ID: 240458  Cd Length: 133  Bit Score: 280.34  E-value: 6.47e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1086 RIFRAEKTYAVKAGRWYFEFETVTAGDMRVGWSRPGCQPDQELGSDERAFAFDGFKAQRWHQGNEHYGRSWQAGDVVGCM 1165
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462512296 1166 VDMNEHTMMFTLNGEILLDDSGSELAFKDFDVGDGFIPVCSLGVAQVGRMNFG 1218
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2135-2346 1.13e-80

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: 265.22  E-value: 1.13e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2135 QIRSLLSVRMGKEEEKLMIRGLGDIMNNKVFYQHPNLMRALGMHETVMEVMvNVLGG------------GESKEITFPKM 2202
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlGEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2203 VANCCRFLCYFCRISRQNQKAMFDHLSYLLENssvgLASPAMRGSTpLDVAAASVMDNNELALalrepdlekvvRYLAGC 2282
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKEC 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462512296 2283 GLQSCQMLVSKGYPDigwnpvegERYLDFLRFAVFCNGESVEENANVVVRLLIRRPECFGPALR 2346
Cdd:pfam01365  144 HIKSFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 654-805 2.53e-80

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs.


:

Pssm-ID: 240457  Cd Length: 151  Bit Score: 262.25  E-value: 2.53e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  654 SMRPNIFLGVSEGSAQYKKWYYELMVDHTEPFVTaEATHLRVGWASTEGYSPYPGGGEEWGGNGVGDDLFSYGFDGLHLW 733
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTH-QPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462512296  734 SGCIARTVSSPNQHLLRTDDVISCCLDLSAPSISFRINGQPVQGMFENFNIDGLFFPVVSFSAGIKVRFLLG 805
Cdd:cd12877     80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1412-1568 2.76e-78

SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this third SPRY domain of the RyRs.


:

Pssm-ID: 293937  Cd Length: 151  Bit Score: 256.46  E-value: 2.76e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1412 DDRDDYDFLMQTSTYYYSVRIFPGQEPANVWVGWITSDFHQYDTGFDLDRVRTVTVTLGDEKGKVHESfaidslcgfgIK 1491
Cdd:cd12879      1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYES----------IK 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1492 RSNCYMVCAGESMSPGQ----GRNNNGLEIGCVVDAASGLLTFIANGKELSTYYQVEPSTKLFPAVFAQATSPNVFQFEL 1567
Cdd:cd12879     71 RQNCYMVCAGELLAEVGqdssGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFEL 150


                   .
gi 2462512296 1568 G 1568
Cdd:cd12879    151 G 151
Ins145_P3_rec super family cl48031
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 13-222 3.68e-74

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: 247.41  E-value: 3.68e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   13 FLRTDDEVVLQCTATIhkeqqKLCLAAEGFGNRLCFLESTSNSKNVPP-DLSICTFVLEQSLSVRALQEML--ANTVEKS 89
Cdd:pfam08709    4 FLHIGDIVSLSCEESV-----NGFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWsaGNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   90 EGQVDVEKWkfmmkTAQGGGHRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTGEACWWTIHPASKQR 169
Cdd:pfam08709   79 NSLTDALKH-----ASNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQR 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512296  170 SEGEKVRVGDDLILVSVSSERYLHLS-----YGNGSLHVDAAFQQTLWSVAPISSGSE 222
Cdd:pfam08709  154 SEGDNVCVGDEVILVPVSAPIFLHTTssselRDNPGKEVNASFGQTSWKMEPFMSGCE 211
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2711-2800 1.95e-47

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 165.75  E-value: 1.95e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2711 FNPQPVDTSNITIPEKLEYFINKYAEHSHDKWSMDKLANGWIYGEIYSDSSKVQPLMKPYKLLSEKEKEIYRWPIKESLK 2790
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296 2791 TMLAWGWRIE 2800
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 862-951 7.34e-46

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 161.13  E-value: 7.34e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  862 FTPIPVDTSQIVLPPHLERIREKLAENIHELWVMNKIELGWQYGPVRDDNKRQHPCLVEFSKLPEQERNYNLQMSLETLK 941
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296  942 TLLALGCHVG 951
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 976-1065 2.24e-41

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 148.42  E-value: 2.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  976 YKPAPMDLSFIKLTPSQEAMVDKLAENAHNVWARDRIRQGWTYGIQQDVKNRRNPRLVPYTLLDDRTKKSNKDSLREAVR 1055
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296 1056 TLLGYGYNLE 1065
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3758-3875 3.57e-40

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


:

Pssm-ID: 462482  Cd Length: 98  Bit Score: 145.36  E-value: 3.57e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 3758 QDDEFTCDLFRFLQLLCEGHNSDFQNYLRTQTGNNTTVNIIISTVDYLLRVQESISdfywyysgkdvideqgqrnfSKAI 3837
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN--------------------EKNI 60

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462512296 3838 QVAKQVFNTLTEYIQGPCTGNQQSLAHSRLWDAVVGFL 3875
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2831-2914 2.11e-34

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 128.39  E-value: 2.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2831 YSPRAIDMSNVTLSRDLHAMAEMMAENYHNIWAKKKKMELESKGGG------NHPLLVPYDTLTAKEKAKDREKAQDILK 2904
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296 2905 FLQINGYAVS 2914
Cdd:pfam02026   81 TLLALGYTIE 90
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4645-4805 4.81e-17

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: 83.86  E-value: 4.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4645 SFLYLAWYMTMSVLG-HYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKS 4723
Cdd:pfam00520   79 SLISLVLSSVGSLSGlRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTW 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4724 EDGDTPDMKCDDMLTCYMFHMYVgvRAGGGIGDEIEDPAGDEYEIYRIIFDITFFFFVIVILLAIIQGLIIDAFGELRDQ 4803
Cdd:pfam00520  159 ENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTER 236


                   ..
gi 2462512296 4804 QE 4805
Cdd:pfam00520  237 TE 238
EF-hand_7 pfam13499
EF-hand domain pair;
3959-4014 3.78e-06

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 3.78e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512296 3959 FKEYDPDGKGVISKRDFHKAMESH---KHYTQSETEFLLSCAETDENETLDYEEFVKRF 4014
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRKLeegEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 230-413 1.83e-119

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: 375.92  E-value: 1.83e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  230 GGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 309
Cdd:cd23291      1 GGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  310 EDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSIQR 389
Cdd:cd23291     81 EDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSIQR 160

                          170       180
                   ....*....|....*....|....
gi 2462512296  390 KAIMHHEGHMDDGISLSRSQHEES 413
Cdd:cd23291    161 KAIMHHEGHMDDGLNLSRSQHEES 184
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4260-4526 4.47e-108

Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 family.


Pssm-ID: 461918  Cd Length: 282  Bit Score: 347.46  E-value: 4.47e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4260 NMPDPTQDEVRGDGEEGERKPLEAALPSEDLTDLKELTEESDLLSDIFGLDLKREGGQYKLIPHNPNAGLSDLMSNPV-- 4337
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLADAAGGEEEEDLLSDIFGLILKKEGGQYKVVPHDPEAGLGDLSETTAee 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4338 PMPEVQEKFQEQKAKEEEKEEKE-----------ETKSEPEKAEGEDGEKEEKAKEDKGKQKLRQLHTHRYGEPEVPESA 4406
Cdd:pfam06459   81 PPPLLKRKLQESEEAEDEEEEEEepkpepiekadGENGEKEEKPKEEETESEAPEEEEMKKKQRKRHSKKKEEPEAQGSA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4407 FWKKIIAYQQKLLNYFARNFYNMRMLALFVAFAINFILLFYKVSTSS-VVEGKELPTRSSSENAKVTSLDSS-SHRIIAV 4484
Cdd:pfam06459  161 FWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPpDEEEEEGSGWGDSGSGSGGGSGEDeEEEEGPV 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462512296 4485 HYVLEESSGYMEPTLRILAILHTVISFFCIIGYYCLKVPLVI 4526
Cdd:pfam06459  241 YFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 455-648 9.29e-92

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: 297.19  E-value: 9.29e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  455 SLQDLIGYFHPPDEHLEHEDKQNRL---RALKNRQNLFQEEGMINLVLECIDRLH-VYSSAAHFADVAGREAGESWKSIL 530
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  531 NSLYELLAALIRGNRKNCAQFSGSLDWLISRLERLEASSGILEVLHCVLVESPE-ALNIIKEGHIKSIISLLDKHGRNHK 609
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462512296  610 VLDVLCSLCVCHGVAVRSNQHLICDNLLPGRDLLLQTRL 648
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1086-1218 6.47e-87

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1


Pssm-ID: 240458  Cd Length: 133  Bit Score: 280.34  E-value: 6.47e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1086 RIFRAEKTYAVKAGRWYFEFETVTAGDMRVGWSRPGCQPDQELGSDERAFAFDGFKAQRWHQGNEHYGRSWQAGDVVGCM 1165
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462512296 1166 VDMNEHTMMFTLNGEILLDDSGSELAFKDFDVGDGFIPVCSLGVAQVGRMNFG 1218
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2135-2346 1.13e-80

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: 265.22  E-value: 1.13e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2135 QIRSLLSVRMGKEEEKLMIRGLGDIMNNKVFYQHPNLMRALGMHETVMEVMvNVLGG------------GESKEITFPKM 2202
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlGEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2203 VANCCRFLCYFCRISRQNQKAMFDHLSYLLENssvgLASPAMRGSTpLDVAAASVMDNNELALalrepdlekvvRYLAGC 2282
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKEC 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462512296 2283 GLQSCQMLVSKGYPDigwnpvegERYLDFLRFAVFCNGESVEENANVVVRLLIRRPECFGPALR 2346
Cdd:pfam01365  144 HIKSFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 654-805 2.53e-80

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs.


Pssm-ID: 240457  Cd Length: 151  Bit Score: 262.25  E-value: 2.53e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  654 SMRPNIFLGVSEGSAQYKKWYYELMVDHTEPFVTaEATHLRVGWASTEGYSPYPGGGEEWGGNGVGDDLFSYGFDGLHLW 733
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTH-QPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462512296  734 SGCIARTVSSPNQHLLRTDDVISCCLDLSAPSISFRINGQPVQGMFENFNIDGLFFPVVSFSAGIKVRFLLG 805
Cdd:cd12877     80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1412-1568 2.76e-78

SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this third SPRY domain of the RyRs.


Pssm-ID: 293937  Cd Length: 151  Bit Score: 256.46  E-value: 2.76e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1412 DDRDDYDFLMQTSTYYYSVRIFPGQEPANVWVGWITSDFHQYDTGFDLDRVRTVTVTLGDEKGKVHESfaidslcgfgIK 1491
Cdd:cd12879      1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYES----------IK 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1492 RSNCYMVCAGESMSPGQ----GRNNNGLEIGCVVDAASGLLTFIANGKELSTYYQVEPSTKLFPAVFAQATSPNVFQFEL 1567
Cdd:cd12879     71 RQNCYMVCAGELLAEVGqdssGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFEL 150


                   .
gi 2462512296 1568 G 1568
Cdd:cd12879    151 G 151
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 226-406 4.07e-75

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: 248.82  E-value: 4.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  226 GYLIGGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRV-AWSGSHIRWGQPFRLRHVTTGK 304
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  305 YLSLMEDKNLLLMDKEKADVKSTAFTFRSS---KEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKS 381
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFpgdNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....*
gi 2462512296  382 VRMGSIQRKAIMHHEGHMDDGISLS 406
Cdd:pfam02815  161 WGFGPEQQKVTCAKEGHMDDALTLP 185
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 13-222 3.68e-74

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: 247.41  E-value: 3.68e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   13 FLRTDDEVVLQCTATIhkeqqKLCLAAEGFGNRLCFLESTSNSKNVPP-DLSICTFVLEQSLSVRALQEML--ANTVEKS 89
Cdd:pfam08709    4 FLHIGDIVSLSCEESV-----NGFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWsaGNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   90 EGQVDVEKWkfmmkTAQGGGHRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTGEACWWTIHPASKQR 169
Cdd:pfam08709   79 NSLTDALKH-----ASNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQR 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512296  170 SEGEKVRVGDDLILVSVSSERYLHLS-----YGNGSLHVDAAFQQTLWSVAPISSGSE 222
Cdd:pfam08709  154 SEGDNVCVGDEVILVPVSAPIFLHTTssselRDNPGKEVNASFGQTSWKMEPFMSGCE 211
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2711-2800 1.95e-47

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


Pssm-ID: 460419  Cd Length: 90  Bit Score: 165.75  E-value: 1.95e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2711 FNPQPVDTSNITIPEKLEYFINKYAEHSHDKWSMDKLANGWIYGEIYSDSSKVQPLMKPYKLLSEKEKEIYRWPIKESLK 2790
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296 2791 TMLAWGWRIE 2800
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 862-951 7.34e-46

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


Pssm-ID: 460419  Cd Length: 90  Bit Score: 161.13  E-value: 7.34e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  862 FTPIPVDTSQIVLPPHLERIREKLAENIHELWVMNKIELGWQYGPVRDDNKRQHPCLVEFSKLPEQERNYNLQMSLETLK 941
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296  942 TLLALGCHVG 951
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 976-1065 2.24e-41

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


Pssm-ID: 460419  Cd Length: 90  Bit Score: 148.42  E-value: 2.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  976 YKPAPMDLSFIKLTPSQEAMVDKLAENAHNVWARDRIRQGWTYGIQQDVKNRRNPRLVPYTLLDDRTKKSNKDSLREAVR 1055
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296 1056 TLLGYGYNLE 1065
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3758-3875 3.57e-40

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


Pssm-ID: 462482  Cd Length: 98  Bit Score: 145.36  E-value: 3.57e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 3758 QDDEFTCDLFRFLQLLCEGHNSDFQNYLRTQTGNNTTVNIIISTVDYLLRVQESISdfywyysgkdvideqgqrnfSKAI 3837
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN--------------------EKNI 60

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462512296 3838 QVAKQVFNTLTEYIQGPCTGNQQSLAHSRLWDAVVGFL 3875
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2831-2914 2.11e-34

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


Pssm-ID: 460419  Cd Length: 90  Bit Score: 128.39  E-value: 2.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2831 YSPRAIDMSNVTLSRDLHAMAEMMAENYHNIWAKKKKMELESKGGG------NHPLLVPYDTLTAKEKAKDREKAQDILK 2904
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296 2905 FLQINGYAVS 2914
Cdd:pfam02026   81 TLLALGYTIE 90
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1099-1220 3.83e-33

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 126.26  E-value: 3.83e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  1099 GRWYFEFETVTAGDMRVGWSRPGCQPDQE--LGSDERAFAFDGFKAQRWHQGN-EHYGRSWQ-AGDVVGCMVDMNEHTMM 1174
Cdd:smart00449    2 GRHYFEVEIGDGGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNSTgPEYGLPLQePGDVIGCFLDLEAGTIS 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 2462512296  1175 FTLNGEILlddsgSELAFKDFDVGDGFIPVCSLGVAQVGRMNFGKD 1220
Cdd:smart00449   82 FYKNGKYL-----HGLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1100-1220 6.20e-28

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 111.28  E-value: 6.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1100 RWYFEFE--TVTAGDMRVGWSRPGCQ--PDQELGSDERAFAFDGFKAQR-WHQGNEHYGR-SWQAGDVVGCMVDMNEHTM 1173
Cdd:pfam00622    1 RHYFEVEifGQDGGGWRVGWATKSVPrkGERFLGDESGSWGYDGWTGKKyWASTSPLTGLpLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462512296 1174 MFTLNGEILlddsgsELAFKDFDVGDGFIPVCSLGVAQVGRMNFGKD 1220
Cdd:pfam00622   81 SFTKNGKSL------GYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 672-807 3.48e-26

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 106.27  E-value: 3.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  672 KWYYELMVDHTEPfvtaeaTHLRVGWAsTEGYSPYPGGGEEwggngvgDDLFSYGFDGlhlWSG--CIARTVSSPNQHLL 749
Cdd:pfam00622    1 RHYFEVEIFGQDG------GGWRVGWA-TKSVPRKGERFLG-------DESGSWGYDG---WTGkkYWASTSPLTGLPLF 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512296  750 RTDDVISCCLDLSAPSISFRINGQPVQGMFENFNIDGLFFPVVSFSAGIKVRFLLGGR 807
Cdd:pfam00622   64 EPGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 672-806 4.69e-23

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 97.37  E-value: 4.69e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   672 KWYYELMVDHTepfvtaeaTHLRVGWASTEGYSPYpgggeewgGNGVGDDLFSYGFDGLHLwSGCIARTVSSPNQHLLRT 751
Cdd:smart00449    3 RHYFEVEIGDG--------GHWRVGVATKSVPRGY--------FALLGEDKGSWGYDGDGG-KKYHNSTGPEYGLPLQEP 65

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462512296   752 DDVISCCLDLSAPSISFRINGQPVQGM-FENFNIDGLFFPVVSFSAGIKVRFLLGG 806
Cdd:smart00449   66 GDVIGCFLDLEAGTISFYKNGKYLHGLaFFDVKFSGPLYPAFSLGSGNSVRLNFGP 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1425-1570 4.87e-21

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 91.64  E-value: 4.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1425 TYYYSVRIFpGQEPANVWVGWITSDFHQYDTGFdldrvrtvtvtLGDEKGkvheSFAIDslcgfgikrsNCYMVCAGESM 1504
Cdd:pfam00622    1 RHYFEVEIF-GQDGGGWRVGWATKSVPRKGERF-----------LGDESG----SWGYD----------GWTGKKYWAST 54

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512296 1505 SPGQGRNNN--GLEIGCVVDAASGLLTFIANGKELSTYYQVEPST-KLFPAVFAQatSPNVFQFELGRI 1570
Cdd:pfam00622   55 SPLTGLPLFepGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSLG--AGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1425-1570 3.26e-17

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 80.80  E-value: 3.26e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  1425 TYYYSVRIFpgqEPANVWVGWITSDFHqydtgfdldrvRTVTVTLGDEKGkvheSFAIDslcgfGIKRSNCYMVCAGESM 1504
Cdd:smart00449    3 RHYFEVEIG---DGGHWRVGVATKSVP-----------RGYFALLGEDKG----SWGYD-----GDGGKKYHNSTGPEYG 59

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512296  1505 SPGQGRnnnGLEIGCVVDAASGLLTFIANGKELS--TYYQVEPSTKLFPAVFAQatSPNVFQFELGRI 1570
Cdd:smart00449   60 LPLQEP---GDVIGCFLDLEAGTISFYKNGKYLHglAFFDVKFSGPLYPAFSLG--SGNSVRLNFGPL 122
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4645-4805 4.81e-17

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: 83.86  E-value: 4.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4645 SFLYLAWYMTMSVLG-HYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKS 4723
Cdd:pfam00520   79 SLISLVLSSVGSLSGlRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTW 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4724 EDGDTPDMKCDDMLTCYMFHMYVgvRAGGGIGDEIEDPAGDEYEIYRIIFDITFFFFVIVILLAIIQGLIIDAFGELRDQ 4803
Cdd:pfam00520  159 ENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTER 236


                   ..
gi 2462512296 4804 QE 4805
Cdd:pfam00520  237 TE 238
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
286-376 9.00e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.88  E-value: 9.00e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   286 GSHIRWGQPFRLRHVTTGKYLSLMEDKNLllmdkekadvkstaftfRSSKEKldvgvrKEVDGMGTSEIkygdsvcyiqh 365
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLP-----------------PWGDGQ------QEVTGYGNPAI----------- 46

                            90
                    ....*....|.
gi 2462512296   366 VDTGLWLTYQS 376
Cdd:smart00472   47 DANTLWLIEPV 57
EF-hand_7 pfam13499
EF-hand domain pair;
3959-4014 3.78e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 3.78e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512296 3959 FKEYDPDGKGVISKRDFHKAMESH---KHYTQSETEFLLSCAETDENETLDYEEFVKRF 4014
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRKLeegEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
3959-4019 1.06e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.25  E-value: 1.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462512296 3959 FKEYDPDGKGVISKRDFHKAMESHkHYTQSETEFLLSCAETDENETLDYEEFV---KRFHEPAK 4019
Cdd:COG5126     75 FDLLDTDGDGKISADEFRRLLTAL-GVSEEEADELFARLDTDGDGKISFEEFVaavRDYYTPDA 137
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 3957-4012 2.82e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 41.76  E-value: 2.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462512296 3957 DTFKEYDPDGKGVISKRDFHKAMESH-KHYTQSETEFLLSCAETDENETLDYEEFVK 4012
Cdd:cd00051      4 EAFRLFDKDGDGTISADELKAALKSLgEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
110-165 7.57e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.40  E-value: 7.57e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462512296   110 HRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTG-EACWWTIHPA 165
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 95-197 8.48e-04

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: 43.91  E-value: 8.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   95 VEKWKFMMKtaqgGGhrTLLYGHAILLRHSYSGMYLCclstsrSSTDKLAFDVGLQEDTTGEACWWTIHPASKQRSEGek 174
Cdd:cd23280     66 IEKEDTPLK----GG--VIKWGDQCRLRHLPTGKYLA------VDDKTGNGKVVLTSDPSDPSTVFRLHPVTKETSEE-- 131

                           90       100
                   ....*....|....*....|...
gi 2462512296  175 VRVGDDLILVSVSSERYLHLSYG 197
Cdd:cd23280    132 VKFGSYVRIEHVATGTWLHAETD 154
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 230-413 1.83e-119

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: 375.92  E-value: 1.83e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  230 GGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 309
Cdd:cd23291      1 GGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  310 EDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSIQR 389
Cdd:cd23291     81 EDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSIQR 160

                          170       180
                   ....*....|....*....|....
gi 2462512296  390 KAIMHHEGHMDDGISLSRSQHEES 413
Cdd:cd23291    161 KAIMHHEGHMDDGLNLSRSQHEES 184
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 230-409 5.18e-113

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: 357.00  E-value: 5.18e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  230 GGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 309
Cdd:cd23278      1 GGDVLRLFHGHMDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  310 EDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSIQR 389
Cdd:cd23278     81 EDRGLVLVPKEKADVKATAFCFRQSKDDKKVLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVETKKRVGGVEER 160

                          170       180
                   ....*....|....*....|
gi 2462512296  390 KAIMHHEGHMDDGISLSRSQ 409
Cdd:cd23278    161 KAILHAEGHMDDGLSLSRAQ 180
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4260-4526 4.47e-108

Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 family.


Pssm-ID: 461918  Cd Length: 282  Bit Score: 347.46  E-value: 4.47e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4260 NMPDPTQDEVRGDGEEGERKPLEAALPSEDLTDLKELTEESDLLSDIFGLDLKREGGQYKLIPHNPNAGLSDLMSNPV-- 4337
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLADAAGGEEEEDLLSDIFGLILKKEGGQYKVVPHDPEAGLGDLSETTAee 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4338 PMPEVQEKFQEQKAKEEEKEEKE-----------ETKSEPEKAEGEDGEKEEKAKEDKGKQKLRQLHTHRYGEPEVPESA 4406
Cdd:pfam06459   81 PPPLLKRKLQESEEAEDEEEEEEepkpepiekadGENGEKEEKPKEEETESEAPEEEEMKKKQRKRHSKKKEEPEAQGSA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4407 FWKKIIAYQQKLLNYFARNFYNMRMLALFVAFAINFILLFYKVSTSS-VVEGKELPTRSSSENAKVTSLDSS-SHRIIAV 4484
Cdd:pfam06459  161 FWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPpDEEEEEGSGWGDSGSGSGGGSGEDeEEEEGPV 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2462512296 4485 HYVLEESSGYMEPTLRILAILHTVISFFCIIGYYCLKVPLVI 4526
Cdd:pfam06459  241 YFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 221-413 9.83e-102

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: 325.30  E-value: 9.83e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  221 SEAAQGYLIGGDVLRLLHGHMDECLTVPSGEhGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHV 300
Cdd:cd23290      1 SCCEEGYVTGGHVLRLFHGHMDECLTISAAD-SDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  301 TTGKYLSLMEDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVK 380
Cdd:cd23290     80 TTGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPK 159

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2462512296  381 SVRMGSIQRKAIMHHEGHMDDGISLSRSQHEES 413
Cdd:cd23290    160 ALRLGVLKKKAILHQEGHMDDALFLTRCQQEES 192
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 226-413 1.65e-97

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: 313.00  E-value: 1.65e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  226 GYLIGGDVLRLLHGHmDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKY 305
Cdd:cd23292      1 GYLLGGHVVRLFHGH-DECLTIPSTDQSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  306 LSLMEDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMG 385
Cdd:cd23292     80 LALTEDQGLILQDRAKSDTKSTAFCFRASKEKLESGPKRDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSRLG 159

                          170       180
                   ....*....|....*....|....*...
gi 2462512296  386 SIQRKAIMHHEGHMDDGISLSRSQHEES 413
Cdd:cd23292    160 PLKRRAILHQEGHMDDGLTLQRCQHEES 187
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 455-648 9.29e-92

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: 297.19  E-value: 9.29e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  455 SLQDLIGYFHPPDEHLEHEDKQNRL---RALKNRQNLFQEEGMINLVLECIDRLH-VYSSAAHFADVAGREAGESWKSIL 530
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  531 NSLYELLAALIRGNRKNCAQFSGSLDWLISRLERLEASSGILEVLHCVLVESPE-ALNIIKEGHIKSIISLLDKHGRNHK 609
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2462512296  610 VLDVLCSLCVCHGVAVRSNQHLICDNLLPGRDLLLQTRL 648
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1086-1218 6.47e-87

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1


Pssm-ID: 240458  Cd Length: 133  Bit Score: 280.34  E-value: 6.47e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1086 RIFRAEKTYAVKAGRWYFEFETVTAGDMRVGWSRPGCQPDQELGSDERAFAFDGFKAQRWHQGNEHYGRSWQAGDVVGCM 1165
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462512296 1166 VDMNEHTMMFTLNGEILLDDSGSELAFKDFDVGDGFIPVCSLGVAQVGRMNFG 1218
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2135-2346 1.13e-80

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: 265.22  E-value: 1.13e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2135 QIRSLLSVRMGKEEEKLMIRGLGDIMNNKVFYQHPNLMRALGMHETVMEVMvNVLGG------------GESKEITFPKM 2202
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlGEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2203 VANCCRFLCYFCRISRQNQKAMFDHLSYLLENssvgLASPAMRGSTpLDVAAASVMDNNELALalrepdlekvvRYLAGC 2282
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKEC 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462512296 2283 GLQSCQMLVSKGYPDigwnpvegERYLDFLRFAVFCNGESVEENANVVVRLLIRRPECFGPALR 2346
Cdd:pfam01365  144 HIKSFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 654-805 2.53e-80

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs.


Pssm-ID: 240457  Cd Length: 151  Bit Score: 262.25  E-value: 2.53e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  654 SMRPNIFLGVSEGSAQYKKWYYELMVDHTEPFVTaEATHLRVGWASTEGYSPYPGGGEEWGGNGVGDDLFSYGFDGLHLW 733
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTH-QPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462512296  734 SGCIARTVSSPNQHLLRTDDVISCCLDLSAPSISFRINGQPVQGMFENFNIDGLFFPVVSFSAGIKVRFLLG 805
Cdd:cd12877     80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1412-1568 2.76e-78

SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this third SPRY domain of the RyRs.


Pssm-ID: 293937  Cd Length: 151  Bit Score: 256.46  E-value: 2.76e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1412 DDRDDYDFLMQTSTYYYSVRIFPGQEPANVWVGWITSDFHQYDTGFDLDRVRTVTVTLGDEKGKVHESfaidslcgfgIK 1491
Cdd:cd12879      1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYES----------IK 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1492 RSNCYMVCAGESMSPGQ----GRNNNGLEIGCVVDAASGLLTFIANGKELSTYYQVEPSTKLFPAVFAQATSPNVFQFEL 1567
Cdd:cd12879     71 RQNCYMVCAGELLAEVGqdssGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFEL 150


                   .
gi 2462512296 1568 G 1568
Cdd:cd12879    151 G 151
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 226-406 4.07e-75

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: 248.82  E-value: 4.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  226 GYLIGGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRV-AWSGSHIRWGQPFRLRHVTTGK 304
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  305 YLSLMEDKNLLLMDKEKADVKSTAFTFRSS---KEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKS 381
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFpgdNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....*
gi 2462512296  382 VRMGSIQRKAIMHHEGHMDDGISLS 406
Cdd:pfam02815  161 WGFGPEQQKVTCAKEGHMDDALTLP 185
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 13-222 3.68e-74

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: 247.41  E-value: 3.68e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   13 FLRTDDEVVLQCTATIhkeqqKLCLAAEGFGNRLCFLESTSNSKNVPP-DLSICTFVLEQSLSVRALQEML--ANTVEKS 89
Cdd:pfam08709    4 FLHIGDIVSLSCEESV-----NGFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWsaGNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   90 EGQVDVEKWkfmmkTAQGGGHRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTGEACWWTIHPASKQR 169
Cdd:pfam08709   79 NSLTDALKH-----ASNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQR 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512296  170 SEGEKVRVGDDLILVSVSSERYLHLS-----YGNGSLHVDAAFQQTLWSVAPISSGSE 222
Cdd:pfam08709  154 SEGDNVCVGDEVILVPVSAPIFLHTTssselRDNPGKEVNASFGQTSWKMEPFMSGCE 211
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2711-2800 1.95e-47

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


Pssm-ID: 460419  Cd Length: 90  Bit Score: 165.75  E-value: 1.95e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2711 FNPQPVDTSNITIPEKLEYFINKYAEHSHDKWSMDKLANGWIYGEIYSDSSKVQPLMKPYKLLSEKEKEIYRWPIKESLK 2790
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296 2791 TMLAWGWRIE 2800
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 862-951 7.34e-46

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


Pssm-ID: 460419  Cd Length: 90  Bit Score: 161.13  E-value: 7.34e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  862 FTPIPVDTSQIVLPPHLERIREKLAENIHELWVMNKIELGWQYGPVRDDNKRQHPCLVEFSKLPEQERNYNLQMSLETLK 941
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296  942 TLLALGCHVG 951
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 976-1065 2.24e-41

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


Pssm-ID: 460419  Cd Length: 90  Bit Score: 148.42  E-value: 2.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  976 YKPAPMDLSFIKLTPSQEAMVDKLAENAHNVWARDRIRQGWTYGIQQDVKNRRNPRLVPYTLLDDRTKKSNKDSLREAVR 1055
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296 1056 TLLGYGYNLE 1065
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3758-3875 3.57e-40

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


Pssm-ID: 462482  Cd Length: 98  Bit Score: 145.36  E-value: 3.57e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 3758 QDDEFTCDLFRFLQLLCEGHNSDFQNYLRTQTGNNTTVNIIISTVDYLLRVQESISdfywyysgkdvideqgqrnfSKAI 3837
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN--------------------EKNI 60

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462512296 3838 QVAKQVFNTLTEYIQGPCTGNQQSLAHSRLWDAVVGFL 3875
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2831-2914 2.11e-34

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown.


Pssm-ID: 460419  Cd Length: 90  Bit Score: 128.39  E-value: 2.11e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 2831 YSPRAIDMSNVTLSRDLHAMAEMMAENYHNIWAKKKKMELESKGGG------NHPLLVPYDTLTAKEKAKDREKAQDILK 2904
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462512296 2905 FLQINGYAVS 2914
Cdd:pfam02026   81 TLLALGYTIE 90
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1099-1220 3.83e-33

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 126.26  E-value: 3.83e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  1099 GRWYFEFETVTAGDMRVGWSRPGCQPDQE--LGSDERAFAFDGFKAQRWHQGN-EHYGRSWQ-AGDVVGCMVDMNEHTMM 1174
Cdd:smart00449    2 GRHYFEVEIGDGGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNSTgPEYGLPLQePGDVIGCFLDLEAGTIS 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 2462512296  1175 FTLNGEILlddsgSELAFKDFDVGDGFIPVCSLGVAQVGRMNFGKD 1220
Cdd:smart00449   82 FYKNGKYL-----HGLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1099-1216 7.35e-29

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 113.68  E-value: 7.35e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1099 GRWYFEF--ETVTAGDMRVGWSRPGCQPDQE--LGSDERAFAFDGFKAQRWHQG-NEHYGRSWQAGDVVGCMVDMNEHTM 1173
Cdd:cd11709      1 GKWYWEVrvDSGNGGLIQVGWATKSFSLDGEggVGDDEESWGYDGSRLRKGHGGsSGPGGRPWKSGDVVGCLLDLDEGTL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2462512296 1174 MFTLNGEILlddsGSelAFKDFDV-GDGFIPVCSLGVAQVGRMN 1216
Cdd:cd11709     81 SFSLNGKDL----GV--AFTNLFLkGGGLYPAVSLGSGQGVTIN 118
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1100-1220 6.20e-28

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 111.28  E-value: 6.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1100 RWYFEFE--TVTAGDMRVGWSRPGCQ--PDQELGSDERAFAFDGFKAQR-WHQGNEHYGR-SWQAGDVVGCMVDMNEHTM 1173
Cdd:pfam00622    1 RHYFEVEifGQDGGGWRVGWATKSVPrkGERFLGDESGSWGYDGWTGKKyWASTSPLTGLpLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462512296 1174 MFTLNGEILlddsgsELAFKDFDVGDGFIPVCSLGVAQVGRMNFGKD 1220
Cdd:pfam00622   81 SFTKNGKSL------GYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 672-807 3.48e-26

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 106.27  E-value: 3.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  672 KWYYELMVDHTEPfvtaeaTHLRVGWAsTEGYSPYPGGGEEwggngvgDDLFSYGFDGlhlWSG--CIARTVSSPNQHLL 749
Cdd:pfam00622    1 RHYFEVEIFGQDG------GGWRVGWA-TKSVPRKGERFLG-------DESGSWGYDG---WTGkkYWASTSPLTGLPLF 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512296  750 RTDDVISCCLDLSAPSISFRINGQPVQGMFENFNIDGLFFPVVSFSAGIKVRFLLGGR 807
Cdd:pfam00622   64 EPGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 231-398 8.46e-26

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


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 107.08  E-value: 8.46e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  231 GDVLRLLHGHMDECLTVPSGEHG-EEQRRTVHYEGGAVSVHARSLWRLETLRVAWsGSHIRWGQPFRLRHVTTGKYLSLM 309
Cdd:cd23263      1 GDVIWLKHSETGKYLHSHRKNYPtGSGQQEVTFESSSRKGDTNGLWIIESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  310 ED-KNLLLMDKE-----KADVKSTAFTFRSSKekldvgvrkevDGMGTSEIKYGDSVCYIQHVDTGLWLtyQSVDVKSVR 383
Cdd:cd23263     80 EGkKSPKSNHQEvlcltDNPDKSSLFKFEPIG-----------STKYKQKYVKKDSYFRLKHVNTNFWL--HSHEKKFNI 146

                          170
                   ....*....|....*
gi 2462512296  384 MGSIQRKAIMHHEGH 398
Cdd:cd23263    147 NNKTQQEVICHGERE 161
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 1095-1218 8.69e-24

SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1).


Pssm-ID: 293940  Cd Length: 128  Bit Score: 99.71  E-value: 8.69e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1095 AVKAGRWYFEFETVTAGDMRVGWSRPGCQPDQELG-SDER-AFAFDGFKAQRWHQGNEHYGRSWQAGDVVGCMVDMNEHT 1172
Cdd:cd12882      7 CVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGvGDTRdSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDLDKGT 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462512296 1173 MMFTLNGEILlddsgsELAFKDFDVGDG--FIPVCSLGVAQVGRMNFG 1218
Cdd:cd12882     87 ISFYRNGRSL------GVAFDNVRRGPGlaYFPAVSLSFGERLELNFG 128
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 672-806 4.69e-23

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 97.37  E-value: 4.69e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   672 KWYYELMVDHTepfvtaeaTHLRVGWASTEGYSPYpgggeewgGNGVGDDLFSYGFDGLHLwSGCIARTVSSPNQHLLRT 751
Cdd:smart00449    3 RHYFEVEIGDG--------GHWRVGVATKSVPRGY--------FALLGEDKGSWGYDGDGG-KKYHNSTGPEYGLPLQEP 65

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462512296   752 DDVISCCLDLSAPSISFRINGQPVQGM-FENFNIDGLFFPVVSFSAGIKVRFLLGG 806
Cdd:smart00449   66 GDVIGCFLDLEAGTISFYKNGKYLHGLaFFDVKFSGPLYPAFSLGSGNSVRLNFGP 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1425-1570 4.87e-21

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 91.64  E-value: 4.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1425 TYYYSVRIFpGQEPANVWVGWITSDFHQYDTGFdldrvrtvtvtLGDEKGkvheSFAIDslcgfgikrsNCYMVCAGESM 1504
Cdd:pfam00622    1 RHYFEVEIF-GQDGGGWRVGWATKSVPRKGERF-----------LGDESG----SWGYD----------GWTGKKYWAST 54

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512296 1505 SPGQGRNNN--GLEIGCVVDAASGLLTFIANGKELSTYYQVEPST-KLFPAVFAQatSPNVFQFELGRI 1570
Cdd:pfam00622   55 SPLTGLPLFepGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSLG--AGEGLKFNFGLR 121
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 1099-1218 4.85e-20

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development.


Pssm-ID: 293941  Cd Length: 121  Bit Score: 88.56  E-value: 4.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1099 GRWYFEFETVTAGDMRVGWSRPGCQPDQE----LGSDERAFAFDGFKAQRWH--QGNEHYGRSWQAGDVVGCMVDMNEHT 1172
Cdd:cd12883      1 GVWYYEVTVLTSGVMQIGWATKDSKFLNHegygIGDDEYSCAYDGCRQLIWYnaKSKPHTHPRWKPGDVLGCLLDLNKKQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2462512296 1173 MMFTLNGEILLDDSGSELAFKdfdvgDGFIPVCSLGVAQVGRMNFG 1218
Cdd:cd12883     81 MIFSLNGNRLPPERQVFTSAK-----SGFFAAASFMSFQQCEFNFG 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 672-803 2.98e-19

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 86.33  E-value: 2.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  672 KWYYELMVDHTEPfvtaeaTHLRVGWAsTEGYSPYPGGGEEwggngvgDDLFSYGFDG--LHLWSGCIartvSSPNQHLL 749
Cdd:cd11709      2 KWYWEVRVDSGNG------GLIQVGWA-TKSFSLDGEGGVG-------DDEESWGYDGsrLRKGHGGS----SGPGGRPW 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462512296  750 RTDDVISCCLDLSAPSISFRINGQPVQGMFENFN-IDGLFFPVVSFSAGIKVRFL 803
Cdd:cd11709     64 KSGDVVGCLLDLDEGTLSFSLNGKDLGVAFTNLFlKGGGLYPAVSLGSGQGVTIN 118
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 222-412 3.74e-19

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: 88.98  E-value: 3.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  222 EAAQGYLIGGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHY----------EGGAVSVHARSLWRLETLRVAWSGSHIRW 291
Cdd:cd23280      1 KENENFLKGGDVVRLFHKELEAYLSAEGSFVDEVLTEDVHLrvrpvddrkpRTLFPPTSGDTFWQIEKEDTPLKGGVIKW 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  292 GQPFRLRHVTTGKYLSLMEDKNLL-LMDKEKADVKSTAFTFRSskekldvgvrkeVDGMGTSEIKYGdSVCYIQHVDTGL 370
Cdd:cd23280     81 GDQCRLRHLPTGKYLAVDDKTGNGkVVLTSDPSDPSTVFRLHP------------VTKETSEEVKFG-SYVRIEHVATGT 147

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462512296  371 WLtyqSVDVKSVRMGSIQRKAIMHHEGHMDDGISLSRSQHEE 412
Cdd:cd23280    148 WL---HAETDEELRRSKKSPAGLSWDGAKLRKVSLSLERQDD 186
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1425-1570 3.26e-17

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 80.80  E-value: 3.26e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  1425 TYYYSVRIFpgqEPANVWVGWITSDFHqydtgfdldrvRTVTVTLGDEKGkvheSFAIDslcgfGIKRSNCYMVCAGESM 1504
Cdd:smart00449    3 RHYFEVEIG---DGGHWRVGVATKSVP-----------RGYFALLGEDKG----SWGYD-----GDGGKKYHNSTGPEYG 59

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512296  1505 SPGQGRnnnGLEIGCVVDAASGLLTFIANGKELS--TYYQVEPSTKLFPAVFAQatSPNVFQFELGRI 1570
Cdd:smart00449   60 LPLQEP---GDVIGCFLDLEAGTISFYKNGKYLHglAFFDVKFSGPLYPAFSLG--SGNSVRLNFGPL 122
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4645-4805 4.81e-17

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: 83.86  E-value: 4.81e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4645 SFLYLAWYMTMSVLG-HYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKS 4723
Cdd:pfam00520   79 SLISLVLSSVGSLSGlRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTW 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 4724 EDGDTPDMKCDDMLTCYMFHMYVgvRAGGGIGDEIEDPAGDEYEIYRIIFDITFFFFVIVILLAIIQGLIIDAFGELRDQ 4803
Cdd:pfam00520  159 ENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTER 236


                   ..
gi 2462512296 4804 QE 4805
Cdd:pfam00520  237 TE 238
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 1081-1220 7.00e-14

SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis.


Pssm-ID: 293932  Cd Length: 150  Bit Score: 72.17  E-value: 7.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1081 TGER-FRIFRAekTYAVKAGRWYFEFETVTAGDM-----RVGWSRPGCQPDQELGSDERAFAFDGFKAQRWHQGN-EHYG 1153
Cdd:cd12872     11 TGEKgYRMARA--NHGVREGKWYFEVKILEGGGTetghvRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFHQSRgKPYG 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512296 1154 RSW-QAGDVVGCMVDMNEhtMMFTLNGEILlddsgsELAFKDFDVGDGFIPVCSL-GVAQVgRMNFGKD 1220
Cdd:cd12872     89 EPGfKEGDVIGFLITLPK--IEFFKNGKSQ------GVAFEDIYGTGGYYPAVSLyKGATV-TINFGPD 148
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 1093-1218 1.53e-13

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay.


Pssm-ID: 293933  Cd Length: 155  Bit Score: 71.07  E-value: 1.53e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1093 TYAVKA-GRWYFEFETVTAGDMRVGWSRPGCqpDQELGSDERAFAFDGfKAQRWHQGN-EHYGRSWQAGDVVGCMVDMNE 1170
Cdd:cd12873     33 TKGVKGkGKYYYEVTVTDEGLCRVGWSTEDA--SLDLGTDKFGFGYGG-TGKKSHGRQfDDYGEPFGLGDVIGCYLDLDN 109

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2462512296 1171 HTMMFTLNGEILlddsGSELAFKDFDVGDGFIPVCSLGVAQVgRMNFG 1218
Cdd:cd12873    110 GTISFSKNGKDL----GKAFDIPPHLRNSALFPAVCLKNAEV-EFNFG 152
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 1086-1218 5.12e-13

SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate.


Pssm-ID: 293943  Cd Length: 132  Bit Score: 68.85  E-value: 5.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1086 RIFRAEKTYAVKAGRWYFEFETV---TAGDMRVGWSRPGCQPDQELGSDERAFAFDGFKAQRWHQG--NEHYGRSWQAGD 1160
Cdd:cd12885      1 GSVRADHPIPPKVPVFYFEVTILdlgEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGgeGENYGPPFGTGD 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512296 1161 VVGCMVDMNEHTMMFTLNGEILlddsGSelAFKDFDVGDgFIPVCSLGVAQVG-RMNFG 1218
Cdd:cd12885     81 VVGCGINFKTGEVFFTKNGELL----GT--AFENVVKGR-LYPTVGLGSPGVKvRVNFG 132
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 1074-1218 5.00e-10

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs.


Pssm-ID: 240457  Cd Length: 151  Bit Score: 61.17  E-value: 5.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1074 RAEVCSGTGERFRIFRaektyavkagRWYFEFE-------TVTAGDMRVGWSR-------PGCQPD---QELGSDERAFA 1136
Cdd:cd12877      3 RPNIFVGVVEGSAQYK----------KWYFEVEvdhveqfTHQPAHLRVGWANtsgyvpyPGGGEGwggNGVGDDLYSYG 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1137 FDGF------KAQRWHQGNEHYGRSwqaGDVVGCMVDMNEHTMMFTLNGEILlddSGSelaFKDFDVGDGFIPVCSLGVA 1210
Cdd:cd12877     73 FDGLhlwtggRSRRVTSGTQHLLKK---GDVVGCCLDLSVPSISFRVNGRPV---QGM---FENFNLDGMFFPVMSFSAG 143


                   ....*...
gi 2462512296 1211 QVGRMNFG 1218
Cdd:cd12877    144 VSCRFLLG 151
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 1081-1182 6.85e-10

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation.


Pssm-ID: 293942  Cd Length: 177  Bit Score: 61.45  E-value: 6.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1081 TGERFRIF----RAekTYAVKAGRWYFE-------------FETVTAGDMRVGWSRPGCQPdqELGSDERAFAFDGfKAQ 1143
Cdd:cd12884     25 TDEGFAYLwagaRA--TYGVTKGKVCFEvkvtenlpvkhlpTEETDPHVVRVGWSVDSSSL--QLGEEEFSYGYGS-TGK 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462512296 1144 RWHQGN-EHYGRSWQAGDVVGCMVDMNEH--TMMFTLNGEIL 1182
Cdd:cd12884    100 KSTNCKfEDYGEPFGENDVIGCYLDFESEpvEISFSKNGKDL 141
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 672-805 5.76e-09

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1


Pssm-ID: 240458  Cd Length: 133  Bit Score: 57.31  E-value: 5.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  672 KWYYElmvdhtepFVTAEATHLRVGWASTEGYSPYPGGGeewggngvgDDLfSYGFDGL-----HLWSGCIARTvsspnq 746
Cdd:cd12878     15 KWYFE--------FEVLTSGYMRVGWARPGFRPDLELGS---------DDL-SYAFDGFlarkwHQGSESFGKQ------ 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462512296  747 hlLRTDDVISCCLDLSAPSISFRINGQPVQG------MFENFNIDGLFFPVVSFSAGIKVRFLLG 805
Cdd:cd12878     71 --WQPGDVVGCMLDLVDRTISFTLNGELLIDssgsevAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 662-802 8.18e-09

SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis.


Pssm-ID: 293932  Cd Length: 150  Bit Score: 57.53  E-value: 8.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  662 GVSEGsaqykKWYYELMVDHTEPFVTAeatHLRVGWASTE-------GYspypgggeewggngvgdDLFSYGF---DG-- 729
Cdd:cd12872     24 GVREG-----KWYFEVKILEGGGTETG---HVRVGWSRREaslqapvGY-----------------DKYSYAIrdkDGsk 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462512296  730 LHLWSGciaRTVSSPNqhlLRTDDVISCCLDLsaPSISFRINGQPvQG-MFENFNIDGLFFPVVSFSAGIKVRF 802
Cdd:cd12872     79 FHQSRG---KPYGEPG---FKEGDVIGFLITL--PKIEFFKNGKS-QGvAFEDIYGTGGYYPAVSLYKGATVTI 143
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1426-1553 2.53e-07

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 52.43  E-value: 2.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1426 YYYSVRIFPGQEPaNVWVGWITSDFHQYDTGfdldrvrtvtvTLGDEkgkvHESFAIDslcgfGIKRSNCYmvcaGESMS 1505
Cdd:cd11709      3 WYWEVRVDSGNGG-LIQVGWATKSFSLDGEG-----------GVGDD----EESWGYD-----GSRLRKGH----GGSSG 57

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1506 PGQGRNNNGLEIGCVVDAASGLLTFIANGKELSTYYQVEPSTK--LFPAV 1553
Cdd:cd11709     58 PGGRPWKSGDVVGCLLDLDEGTLSFSLNGKDLGVAFTNLFLKGggLYPAV 107
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
286-376 9.00e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.88  E-value: 9.00e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   286 GSHIRWGQPFRLRHVTTGKYLSLMEDKNLllmdkekadvkstaftfRSSKEKldvgvrKEVDGMGTSEIkygdsvcyiqh 365
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLP-----------------PWGDGQ------QEVTGYGNPAI----------- 46

                            90
                    ....*....|.
gi 2462512296   366 VDTGLWLTYQS 376
Cdd:smart00472   47 DANTLWLIEPV 57
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
 1099-1194 3.55e-06

PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM9 proteins. TRIM9 protein is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. It has been shown that TRIM9 is localized to the neurons in the normal human brain and its immunoreactivity in affected brain areas in Parkinson's disease and dementia with Lewy bodies is severely decreased, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis.


Pssm-ID: 293947  Cd Length: 172  Bit Score: 50.32  E-value: 3.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1099 GRWYFEFeTV----TAGDMRVGWSRPGCQPDQELGSDERAFA--FDGfkaQR-WHQ-GNEHYGRS---WQAGDVVGCMVD 1167
Cdd:cd12889     49 GVHYWEV-TIdrydGHPDPAFGVARIDVNKDKMLGKDDKGWSmyIDN---NRsWFLhNNEHSNRTeggITVGSVVGVLLD 124

                           90       100
                   ....*....|....*....|....*..
gi 2462512296 1168 MNEHTMMFTLNGEillddSGSELAFKD 1194
Cdd:cd12889    125 LDRHTLSFYVNDE-----PQGPIAFRN 146
EF-hand_7 pfam13499
EF-hand domain pair;
3959-4014 3.78e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 3.78e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462512296 3959 FKEYDPDGKGVISKRDFHKAMESH---KHYTQSETEFLLSCAETDENETLDYEEFVKRF 4014
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRKLeegEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 673-805 6.21e-06

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development.


Pssm-ID: 293941  Cd Length: 121  Bit Score: 48.50  E-value: 6.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  673 WYYELMVdhtepfVTAEAthLRVGWAST-------EGYSpypgggeewggngVGDDLFSYGFDGLH--LWSGciARtvSS 743
Cdd:cd12883      3 WYYEVTV------LTSGV--MQIGWATKdskflnhEGYG-------------IGDDEYSCAYDGCRqlIWYN--AK--SK 57

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462512296  744 PNQHL-LRTDDVISCCLDLSAPSISFRINGQPVQGMFENFNI--DGlFFPVVSFSAGIKVRFLLG 805
Cdd:cd12883     58 PHTHPrWKPGDVLGCLLDLNKKQMIFSLNGNRLPPERQVFTSakSG-FFAAASFMSFQQCEFNFG 121
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 228-372 7.23e-06

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: 50.45  E-value: 7.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  228 LIGGDVLRLLHGHMDECLTvpSGEHGEEQR---RTVHYEGGAVSVHARSLWRLETLRV-AWSGSHIRWGQPFRLRHVTTG 303
Cdd:cd23287     11 LKGGDVVRLFHAEQEKFLT--CDEHRKKQHvflRTTGRQSATSATSSKALWEVEVVQHdPCRGGAGYWNSLFRFKHLATG 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  304 KYLSL-----MEDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEI--------KYGDSVC----YI--Q 364
Cdd:cd23287     89 HYLAAevdpdFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIfeldpttlRGGDSLVprnsYVrlR 168


                   ....*...
gi 2462512296  365 HVDTGLWL 372
Cdd:cd23287    169 HLCTNTWV 176
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
3959-4019 1.06e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.25  E-value: 1.06e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462512296 3959 FKEYDPDGKGVISKRDFHKAMESHkHYTQSETEFLLSCAETDENETLDYEEFV---KRFHEPAK 4019
Cdd:COG5126     75 FDLLDTDGDGKISADEFRRLLTAL-GVSEEEADELFARLDTDGDGKISFEEFVaavRDYYTPDA 137
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 212-381 1.80e-05

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: 49.27  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  212 WSVAPISSGSEAAQGYLIGGDVLRLLHGHMDECLTVpsGEHGEEQR---RTVHYEGGAVSVHARSLWRLETLRV-AWSGS 287
Cdd:cd23288      1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTC--DEYKKKQHiflRTTLRQSATSATSSKALWEIEVVHYdPCRGG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  288 HIRWGQPFRLRHVTTGKYLS---------------LMEDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDgmgTS 352
Cdd:cd23288     79 AGQWNSLFRFKHLATGNYLAaevnpdyrdaqnegkAVNDGDSPTSKKKRQAAEKIMYTLVSVPHGNDIASLFELD---AT 155

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2462512296  353 EIKYGD------SVCYIQHVDTGLWLTYQSVDVKS 381
Cdd:cd23288    156 TLQRADclvprnSYVRLRHLCTNTWVTSTSIPIDT 190
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 181-307 2.29e-05

MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The SDF-2 family includes mammalian SDF-2 and SDF2-like protein 1 (SDF2L1) as well as similar proteins from plant, such as Arabidopsis thaliana stromal cell-derived factor 2-like protein (AtSDF2). SDF-2 is a secretory protein involved in multiple endoplasmic reticulum (ER) functions, including the misfolded protein catabolic process, protein glycosylation, and ER protein quality control. SDF2L1, also called PWP1-interacting protein 8, is an endoplasmic reticulum (ER)-localized protein that plays a role in ER-associated degradation (ERAD) of misfolded proinsulin in pancreatic beta-cells. It is a component of the endoplasmic reticulum (ER) chaperone complex and interacts with alpha- and beta-defensins. SDF2L1 may also act as a tumor suppressor that play an important role in a variety of cancers, such as breast cancer and ovarian cancer. AtSDF2, also called SDF2-like protein, acts as crucial component of the unfolded protein response (UPR) in Arabidopsis thaliana. It is involved in the endoplasmic reticulum (ER) protein quality control and unfolded protein response. It may be involved in the quality control of glycoproteins. AtSDF2 forms a complex in the ER with ERDJ3B and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467750 [Multi-domain]  Cd Length: 173  Bit Score: 48.06  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  181 LILVSVSSERYLH---LSYGNGSlhvdaaFQQ------------TLWSVAPISSGSEAAQGYLIG-GDVLRL-------- 236
Cdd:cd23279      5 IKLKHVNSGYRLHsheVSYGSGS------GQQsvtavpsaddanSLWTVLPGLGEPCQEQGKPVKcGDIIRLqhvntrkn 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462512296  237 LHGHMdecLTVPSGEHGEeqrrtvhyeggaVSVHARS------LWRLETLRVawSGSHIRWGQPFRLRHVTTGKYLS 307
Cdd:cd23279     79 LHSHN---HSSPLSGNQE------------VSAFGGGdedsgdNWIVECEGK--KAKFWKRGEPVRLKHVDTGKYLS 138
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 3957-4012 2.82e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 41.76  E-value: 2.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462512296 3957 DTFKEYDPDGKGVISKRDFHKAMESH-KHYTQSETEFLLSCAETDENETLDYEEFVK 4012
Cdd:cd00051      4 EAFRLFDKDGDGTISADELKAALKSLgEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
110-165 7.57e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.40  E-value: 7.57e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462512296   110 HRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTG-EACWWTIHPA 165
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 95-197 8.48e-04

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: 43.91  E-value: 8.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296   95 VEKWKFMMKtaqgGGhrTLLYGHAILLRHSYSGMYLCclstsrSSTDKLAFDVGLQEDTTGEACWWTIHPASKQRSEGek 174
Cdd:cd23280     66 IEKEDTPLK----GG--VIKWGDQCRLRHLPTGKYLA------VDDKTGNGKVVLTSDPSDPSTVFRLHPVTKETSEE-- 131

                           90       100
                   ....*....|....*....|...
gi 2462512296  175 VRVGDDLILVSVSSERYLHLSYG 197
Cdd:cd23280    132 VKFGSYVRIEHVATGTWLHAETD 154
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 672-797 1.98e-03

SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1).


Pssm-ID: 293940  Cd Length: 128  Bit Score: 41.54  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  672 KWYYELMVdHTEPFvtaeathLRVGWAS-------TEGYSpypgggeewggngvgDDLFSYGFDG--LHLWSGCiartvS 742
Cdd:cd12882     12 KWMYEVTL-GTKGI-------MQIGWATiscrftqEEGVG---------------DTRDSYAYDGnrVRKWNVS-----T 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462512296  743 SPNQHLLRTDDVISCCLDLSAPSISFRINGQPVQGMFENFNI-DGL-FFPVVSFSAG 797
Cdd:cd12882     64 QKYGEPWVAGDVIGCCIDLDKGTISFYRNGRSLGVAFDNVRRgPGLaYFPAVSLSFG 120
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 221-311 3.33e-03

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: 42.34  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296  221 SEAAQGYLIGGDVLRLLHGHMDECLTvpSGEHGEEQR---RTVHYEGGAVSVHARSLWRLETL-----RvawsGSHIRWG 292
Cdd:cd23277      4 KENLEDVLKGGDVVRLFHAEQEKFLT--CDEYKKKQYvflRTTGRTSATSATSSKALWEVEVVqhdpcR----GGAGHWN 77

                           90
                   ....*....|....*....
gi 2462512296  293 QPFRLRHVTTGKYLSLMED 311
Cdd:cd23277     78 SLFRFKHLATGQYLAAEVD 96
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 1099-1199 6.58e-03

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.


Pssm-ID: 293966  Cd Length: 144  Bit Score: 40.20  E-value: 6.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512296 1099 GRWYFEFETVTAGD---MRVGWSRPGCQPDQELGSDERAFAF---DG--FKAQrwHQGnEHYGRSWQAGDVVGCMVDMNE 1170
Cdd:cd12909     25 GIYYFEVKIISKGRdgyIGIGFSTKDVNLNRLPGWEPHSWGYhgdDGhsFCSS--GTG-KPYGPTFTTGDVIGCGINFRD 101

                           90       100
                   ....*....|....*....|....*....
gi 2462512296 1171 HTMMFTLNGEILlddsgsELAFKDFDVGD 1199
Cdd:cd12909    102 NTAFYTKNGVNL------GIAFRDIKKGN 124
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
172-217 7.88e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 37.71  E-value: 7.88e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462512296   172 GEKVRVGDDLILVSVSSERYLHLS----YGNGSLH-------VDAAFQQTLWSVAPI 217
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHdeklPPWGDGQqevtgygNPAIDANTLWLIEPV 57
 
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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