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Conserved domains on  [gi|378523612|sp|F1LMY4|]
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RecName: Full=Ryanodine receptor 1; Short=RYR-1; Short=RyR1; AltName: Full=Skeletal muscle calcium release channel; AltName: Full=Skeletal muscle ryanodine receptor; AltName: Full=Skeletal muscle-type ryanodine receptor; AltName: Full=Type 1 ryanodine receptor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 208-399 2.50e-132

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: 413.13  E-value: 2.50e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  208 SCCEEGFVTGGHVLRLFHGHMDECLTISPSDSDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 287
Cdd:cd23290     1 SCCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  288 TGRYLALTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 367
Cdd:cd23290    81 TGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 378523612  368 LRLGVLKKKAMLHQEGHMDDALSLTRCQQEES 399
Cdd:cd23290   161 LRLGVLKKKAILHQEGHMDDALFLTRCQQEES 192
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4379-4668 1.39e-86

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: 285.83  E-value: 1.39e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4379 GMPDPTGDEVHGQQPSGAGSDAEGEGQGEGEGDAAEGVGDEEVAADQAGT-----GGADRTVAvadgspfrPEGAGGLGD 4453
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLADAAGGEEEEDLLSDIFGLilkkeGGQYKVVP--------HDPEAGLGD 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4454 MGDTTPVEPPtpegsPILKRKLGVDGEEEEPQPEPEPEPEPEPEKADTENGEKEVPEPPPEPPKKAPPPPPPKKEEAGGA 4533
Cdd:pfam06459   73 LSETTAEEPP-----PLLKRKLQESEEAEDEEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMKKKQRKRH 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4534 GLE---------EFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDIEGSGAGDMsgagsg 4604
Cdd:pfam06459  148 SKKkeepeaqgsAFWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGSGWGDS------ 221

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378523612  4605 dgsGWGSRASEEVEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVI 4668
Cdd:pfam06459  222 ---GSGSGGGSGEDEEEEEGPVYFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 445-638 5.01e-82

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: 269.45  E-value: 5.01e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   445 SLQDLIGYFEPPSEELQHEEKQTKL---RSLRNRQSLFQEEGMLSLVLNCIDRLN-VYTTAAHFAEFAGEEAAESWKEIV 520
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   521 NLLYELLASLIRGNRTNCALFSTNLDWLVSKLDRLEASSGILEVLYCVLIESPE-VLNIIQENHIKSIISLLDKHGRNHK 599
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 378523612   600 VLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNL 638
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 644-795 1.07e-78

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: 257.63  E-value: 1.07e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  644 SIRPNIFVGRAEGSTQYGKWYFEVMVDEVAPFlTAQATHLRVGWALSEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 723
Cdd:cd12877     1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378523612  724 TGHVARPVTSPGQHLLGPEDVVSCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGIKVRFLLG 795
Cdd:cd12877    80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
Ins145_P3_rec super family cl48031
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 12-211 1.29e-77

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: 257.04  E-value: 1.29e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612    12 VQFLRTDDEVVLQCSATVLkeqlkLCLAAEGFGNRLCFLEPTSNAQNVPP-DLAICCFILEQSLSVRALQEMLAN----- 85
Cdd:pfam08709    2 SSFLHIGDIVSLSCEESVN-----GFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWSAgnrsp 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612    86 ----TVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEG 161
Cdd:pfam08709   77 ngnsLTDALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 378523612   162 EKVRVGDDLILVSVSSERYLHLST-----ASGELQVDASFMQTLWNMNPICSCCE 211
Cdd:pfam08709  157 DNVCVGDEVILVPVSAPIFLHTTSsselrDNPGKEVNASFGQTSWKMEPFMSGCE 211
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1074-1205 2.71e-76

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: 249.91  E-value: 2.71e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1074 RIFRAEKSYAVQSGRWYFEFEAVTTGR-ELGWARPELRPDVELGADDLAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCM 1152
Cdd:cd12878     1 RTFRAEKTYAVTSGKWYFEFEVLTSGYmRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 378523612 1153 IDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLG 1205
Cdd:cd12878    81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1419-1567 4.01e-75

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: 247.60  E-value: 4.01e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1419 DNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMSFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGG 1498
Cdd:cd12879     1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378523612 1499 DFVSPGQQ--GRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVVQFDLR 1567
Cdd:cd12879    81 ELLAEVGQdsSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2160-2368 1.55e-71

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: 239.02  E-value: 1.55e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2160 QIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMvNVLGG------------GESKEIRFPKM 2227
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlGEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2228 VTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGiGLGMQGSTpLDVAAASVIDNNELALalqeqdlekvvSYLAGCGLQ 2307
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLG-SPSLAEGT-LDVLTALLMDNPELLL-----------NYIKECHIK 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378523612  2308 SCPMLLAKGYPDigwnpcggERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALR 2368
Cdd:pfam01365  147 SFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 852-941 3.21e-45

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: 159.59  E-value: 3.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   852 FVPCPVDTIQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVDFHSLPEPERNYNLQMSGETLK 931
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612   932 TLLALGCHVG 941
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2732-2821 4.65e-42

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: 150.35  E-value: 4.65e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2732 FDPRPVETLNVIIPEKLDSFINKFAEYAHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLK 2811
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612  2812 AMIAWEWTVE 2821
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 966-1055 2.60e-37

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: 136.86  E-value: 2.60e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   966 YKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVR 1045
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612  1046 TLLGYGYNIE 1055
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2852-2935 5.40e-33

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: 124.54  E-value: 5.40e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2852 YNPQPPDLSVVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGG------SHPLLVPYDTLTAKEKARDREKAQELLK 2925
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612  2926 FLQMNGYAVT 2935
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3880-3996 6.49e-32

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: 121.86  E-value: 6.49e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  3880 DDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISdfywyysgkdvieeqgkrnfSKAMS 3959
Cdd:pfam08454    2 EVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN--------------------EKNIE 61

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 378523612  3960 VAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFL 3996
Cdd:pfam08454   62 LIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4762-4946 2.11e-27

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: 113.90  E-value: 2.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4762 LLTWIMSIDVKYQIWKFGVI---FTDNSFLYLGWYMVMSLLG------------HYNNFFFAAHLLDIAMGVKTLRTILS 4826
Cdd:pfam00520   41 VFTGIFTLEMLLKIIAAGFKkryFRSPWNILDFVVVLPSLISlvlssvgslsglRVLRLLRLLRLLRLIRRLEGLRTLVN 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4827 SVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVgvRAGGGIGDEIEDPAGDE 4906
Cdd:pfam00520  121 SLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGK 198

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 378523612  4907 YELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQE 4946
Cdd:pfam00520  199 GEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 208-399 2.50e-132

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: 413.13  E-value: 2.50e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  208 SCCEEGFVTGGHVLRLFHGHMDECLTISPSDSDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 287
Cdd:cd23290     1 SCCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  288 TGRYLALTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 367
Cdd:cd23290    81 TGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 378523612  368 LRLGVLKKKAMLHQEGHMDDALSLTRCQQEES 399
Cdd:cd23290   161 LRLGVLKKKAILHQEGHMDDALFLTRCQQEES 192
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4379-4668 1.39e-86

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: 285.83  E-value: 1.39e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4379 GMPDPTGDEVHGQQPSGAGSDAEGEGQGEGEGDAAEGVGDEEVAADQAGT-----GGADRTVAvadgspfrPEGAGGLGD 4453
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLADAAGGEEEEDLLSDIFGLilkkeGGQYKVVP--------HDPEAGLGD 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4454 MGDTTPVEPPtpegsPILKRKLGVDGEEEEPQPEPEPEPEPEPEKADTENGEKEVPEPPPEPPKKAPPPPPPKKEEAGGA 4533
Cdd:pfam06459   73 LSETTAEEPP-----PLLKRKLQESEEAEDEEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMKKKQRKRH 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4534 GLE---------EFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDIEGSGAGDMsgagsg 4604
Cdd:pfam06459  148 SKKkeepeaqgsAFWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGSGWGDS------ 221

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378523612  4605 dgsGWGSRASEEVEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVI 4668
Cdd:pfam06459  222 ---GSGSGGGSGEDEEEEEGPVYFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 445-638 5.01e-82

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: 269.45  E-value: 5.01e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   445 SLQDLIGYFEPPSEELQHEEKQTKL---RSLRNRQSLFQEEGMLSLVLNCIDRLN-VYTTAAHFAEFAGEEAAESWKEIV 520
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   521 NLLYELLASLIRGNRTNCALFSTNLDWLVSKLDRLEASSGILEVLYCVLIESPE-VLNIIQENHIKSIISLLDKHGRNHK 599
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 378523612   600 VLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNL 638
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 644-795 1.07e-78

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: 257.63  E-value: 1.07e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  644 SIRPNIFVGRAEGSTQYGKWYFEVMVDEVAPFlTAQATHLRVGWALSEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 723
Cdd:cd12877     1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378523612  724 TGHVARPVTSPGQHLLGPEDVVSCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGIKVRFLLG 795
Cdd:cd12877    80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 12-211 1.29e-77

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: 257.04  E-value: 1.29e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612    12 VQFLRTDDEVVLQCSATVLkeqlkLCLAAEGFGNRLCFLEPTSNAQNVPP-DLAICCFILEQSLSVRALQEMLAN----- 85
Cdd:pfam08709    2 SSFLHIGDIVSLSCEESVN-----GFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWSAgnrsp 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612    86 ----TVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEG 161
Cdd:pfam08709   77 ngnsLTDALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 378523612   162 EKVRVGDDLILVSVSSERYLHLST-----ASGELQVDASFMQTLWNMNPICSCCE 211
Cdd:pfam08709  157 DNVCVGDEVILVPVSAPIFLHTTSsselrDNPGKEVNASFGQTSWKMEPFMSGCE 211
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1074-1205 2.71e-76

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: 249.91  E-value: 2.71e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1074 RIFRAEKSYAVQSGRWYFEFEAVTTGR-ELGWARPELRPDVELGADDLAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCM 1152
Cdd:cd12878     1 RTFRAEKTYAVTSGKWYFEFEVLTSGYmRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 378523612 1153 IDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLG 1205
Cdd:cd12878    81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1419-1567 4.01e-75

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: 247.60  E-value: 4.01e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1419 DNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMSFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGG 1498
Cdd:cd12879     1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378523612 1499 DFVSPGQQ--GRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVVQFDLR 1567
Cdd:cd12879    81 ELLAEVGQdsSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 213-391 1.70e-73

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: 244.20  E-value: 1.70e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   213 GFVTGGHVLRLFHGHMDECLTISPSDS-DDQRRLVYYEGGPVCTHARSLWRLEPLRI-SWSGSHLRWGQPLRIRHVTTGR 290
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQkQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   291 YLALTEDQGLVVVDASKAHTKATSFCFRIS---KEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 367
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFpgdNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....
gi 378523612   368 LRLGVLKKKAMLHQEGHMDDALSL 391
Cdd:pfam02815  161 WGFGPEQQKVTCAKEGHMDDALTL 184
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2160-2368 1.55e-71

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: 239.02  E-value: 1.55e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2160 QIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMvNVLGG------------GESKEIRFPKM 2227
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlGEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2228 VTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGiGLGMQGSTpLDVAAASVIDNNELALalqeqdlekvvSYLAGCGLQ 2307
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLG-SPSLAEGT-LDVLTALLMDNPELLL-----------NYIKECHIK 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378523612  2308 SCPMLLAKGYPDigwnpcggERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALR 2368
Cdd:pfam01365  147 SFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 852-941 3.21e-45

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: 159.59  E-value: 3.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   852 FVPCPVDTIQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVDFHSLPEPERNYNLQMSGETLK 931
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612   932 TLLALGCHVG 941
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2732-2821 4.65e-42

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: 150.35  E-value: 4.65e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2732 FDPRPVETLNVIIPEKLDSFINKFAEYAHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLK 2811
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612  2812 AMIAWEWTVE 2821
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 966-1055 2.60e-37

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: 136.86  E-value: 2.60e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   966 YKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVR 1045
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612  1046 TLLGYGYNIE 1055
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2852-2935 5.40e-33

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: 124.54  E-value: 5.40e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2852 YNPQPPDLSVVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGG------SHPLLVPYDTLTAKEKARDREKAQELLK 2925
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612  2926 FLQMNGYAVT 2935
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3880-3996 6.49e-32

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: 121.86  E-value: 6.49e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  3880 DDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISdfywyysgkdvieeqgkrnfSKAMS 3959
Cdd:pfam08454    2 EVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN--------------------EKNIE 61

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 378523612  3960 VAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFL 3996
Cdd:pfam08454   62 LIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1086-1207 2.07e-29

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: 115.47  E-value: 2.07e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   1086 SGRWYFEFEAVTTG--ReLGWARPELRPDVE--LGADDLAYVFNGHRGQRWHLG-SEPFGRPWQS-GDVVGCMIDLTENT 1159
Cdd:smart00449    1 SGRHYFEVEIGDGGhwR-VGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNStGPEYGLPLQEpGDVIGCFLDLEAGT 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 378523612   1160 IIFTLNGEVLMsdsgsETAFREIEIGDGFLPVCSLGPGQVGHLNLGQD 1207
Cdd:smart00449   80 ISFYKNGKYLH-----GLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4762-4946 2.11e-27

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: 113.90  E-value: 2.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4762 LLTWIMSIDVKYQIWKFGVI---FTDNSFLYLGWYMVMSLLG------------HYNNFFFAAHLLDIAMGVKTLRTILS 4826
Cdd:pfam00520   41 VFTGIFTLEMLLKIIAAGFKkryFRSPWNILDFVVVLPSLISlvlssvgslsglRVLRLLRLLRLLRLIRRLEGLRTLVN 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4827 SVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVgvRAGGGIGDEIEDPAGDE 4906
Cdd:pfam00520  121 SLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGK 198

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 378523612  4907 YELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQE 4946
Cdd:pfam00520  199 GEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 662-797 2.28e-27

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: 109.74  E-value: 2.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   662 KWYFEVMVDevapflTAQATHLRVGWAlsegYSPYPGGGEGWGGngvgDDLYSYGFDGlhlWTGHVARPVTSP--GQHLL 739
Cdd:pfam00622    1 RHYFEVEIF------GQDGGGWRVGWA----TKSVPRKGERFLG----DESGSWGYDG---WTGKKYWASTSPltGLPLF 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 378523612   740 GPEDVVSCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGIKVRFLLGGR 797
Cdd:pfam00622   64 EPGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1432-1564 3.01e-23

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: 97.80  E-value: 3.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  1432 TYYYSVRVFaGQEPSCVWVGWVTPDYHQHDMSFDlskvravtvtmGDEQGnvhsslkcSNCYMVWGGDFVSPGQQGRISH 1511
Cdd:pfam00622    1 RHYFEVEIF-GQDGGGWRVGWATKSVPRKGERFL-----------GDESG--------SWGYDGWTGKKYWASTSPLTGL 60

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 378523612  1512 ----TDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNT-KLFPAVFVlpTHQNVVQF 1564
Cdd:pfam00622   61 plfePGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSL--GAGEGLKF 116
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1431-1564 1.72e-22

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: 95.82  E-value: 1.72e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   1431 TTYYYSVRVFagqEPSCVWVGWVTPDYHQHDMSfdlskvravtvTMGDEQG-NVHSSLKCSNCYMVWGGDFVSPGQQgri 1509
Cdd:smart00449    2 GRHYFEVEIG---DGGHWRVGVATKSVPRGYFA-----------LLGEDKGsWGYDGDGGKKYHNSTGPEYGLPLQE--- 64

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 378523612   1510 shTDLVIGCLVDLATGLMTFTANGKESN--TFFQVEPNTKLFPAVFVLPTHQNVVQF 1564
Cdd:smart00449   65 --PGDVIGCFLDLEAGTISFYKNGKYLHglAFFDVKFSGPLYPAFSLGSGNSVRLNF 119
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1088-1207 3.94e-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: 92.02  E-value: 3.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  1088 RWYFEFEAVTTGRE---LGWARPE--LRPDVELGADDLAYVFNGHRGQR-WHLGSEPFGRP-WQSGDVVGCMIDLTENTI 1160
Cdd:pfam00622    1 RHYFEVEIFGQDGGgwrVGWATKSvpRKGERFLGDESGSWGYDGWTGKKyWASTSPLTGLPlFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 378523612  1161 IFTLNGEVLMsdsgseTAFREIEIGDGFLPVCSLGPGQVGHLNLGQD 1207
Cdd:pfam00622   81 SFTKNGKSLG------YAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 661-796 8.01e-20

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: 88.12  E-value: 8.01e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612    661 GKWYFEVMVDEvapfltaqATHLRVGWALSEGYSPYpgggegwgGNGVGDDLYSYGFDGLHLwTGHVARPVTSPGQHLLG 740
Cdd:smart00449    2 GRHYFEVEIGD--------GGHWRVGVATKSVPRGY--------FALLGEDKGSWGYDGDGG-KKYHNSTGPEYGLPLQE 64

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 378523612    741 PEDVVSCCLDLSVPSISFRINGCPVQGV-FESFNLDGLFFPVVSFSAGIKVRFLLGG 796
Cdd:smart00449   65 PGDVIGCFLDLEAGTISFYKNGKYLHGLaFFDVKFSGPLYPAFSLGSGNSVRLNFGP 121
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
272-360 1.03e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 51.57  E-value: 1.03e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612    272 GSHLRWGQPLRIRHVTTGRYLALTEDqglvvvdaskahtkatsfcfrisKEKLDVAPKRDVEGMGPPEIkygeslcfvqh 351
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDE-----------------------KLPPWGDGQQEVTGYGNPAI----------- 46


                    ....*....
gi 378523612    352 VASGLWLTY 360
Cdd:smart00472   47 DANTLWLIE 55
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
99-154 2.10e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.02  E-value: 2.10e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 378523612     99 HRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATG-EACWWTMHPA 154
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 ...
 45-186 2.83e-05

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: 48.15  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   45 NRLCFLEPTSNAQNVPPDLAICCFILEqslsvralqemlantveaGVESSQGGGhrTLLYGHAILLRHAHSRMYLsCLTt 124
Cdd:cd23280    41 LRVRPVDDRKPRTLFPPTSGDTFWQIE------------------KEDTPLKGG--VIKWGDQCRLRHLPTGKYL-AVD- 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378523612  125 srsmTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGekVRVGDDLILVSVSSERYLHLSTA 186
Cdd:cd23280    99 ----DKTGNGKVVLTSDPSDPSTVFRLHPVTKETSEE--VKFGSYVRIEHVATGTWLHAETD 154
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 208-399 2.50e-132

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: 413.13  E-value: 2.50e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  208 SCCEEGFVTGGHVLRLFHGHMDECLTISPSDSDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 287
Cdd:cd23290     1 SCCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  288 TGRYLALTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 367
Cdd:cd23290    81 TGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 378523612  368 LRLGVLKKKAMLHQEGHMDDALSLTRCQQEES 399
Cdd:cd23290   161 LRLGVLKKKAILHQEGHMDDALFLTRCQQEES 192
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 217-395 2.20e-107

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: 341.21  E-value: 2.20e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  217 GGHVLRLFHGHMDECLTISPSDS-DDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALT 295
Cdd:cd23278     1 GGDVLRLFHGHMDECLTIPAAGSkEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  296 EDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKK 375
Cdd:cd23278    81 EDRGLVLVPKEKADVKATAFCFRQSKDDKKVLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVETKKRVGGVEER 160

                         170       180
                  ....*....|....*....|
gi 378523612  376 KAMLHQEGHMDDALSLTRCQ 395
Cdd:cd23278   161 KAILHAEGHMDDGLSLSRAQ 180
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 213-399 7.02e-101

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: 322.63  E-value: 7.02e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  213 GFVTGGHVLRLFHGHmDECLTISPSD-SDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRY 291
Cdd:cd23292     1 GYLLGGHVVRLFHGH-DECLTIPSTDqSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  292 LALTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLG 371
Cdd:cd23292    80 LALTEDQGLILQDRAKSDTKSTAFCFRASKEKLESGPKRDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSRLG 159

                         170       180
                  ....*....|....*....|....*...
gi 378523612  372 VLKKKAMLHQEGHMDDALSLTRCQQEES 399
Cdd:cd23292   160 PLKRRAILHQEGHMDDGLTLQRCQHEES 187
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4379-4668 1.39e-86

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: 285.83  E-value: 1.39e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4379 GMPDPTGDEVHGQQPSGAGSDAEGEGQGEGEGDAAEGVGDEEVAADQAGT-----GGADRTVAvadgspfrPEGAGGLGD 4453
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLADAAGGEEEEDLLSDIFGLilkkeGGQYKVVP--------HDPEAGLGD 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4454 MGDTTPVEPPtpegsPILKRKLGVDGEEEEPQPEPEPEPEPEPEKADTENGEKEVPEPPPEPPKKAPPPPPPKKEEAGGA 4533
Cdd:pfam06459   73 LSETTAEEPP-----PLLKRKLQESEEAEDEEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMKKKQRKRH 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4534 GLE---------EFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDIEGSGAGDMsgagsg 4604
Cdd:pfam06459  148 SKKkeepeaqgsAFWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGSGWGDS------ 221

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378523612  4605 dgsGWGSRASEEVEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVI 4668
Cdd:pfam06459  222 ---GSGSGGGSGEDEEEEEGPVYFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 445-638 5.01e-82

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: 269.45  E-value: 5.01e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   445 SLQDLIGYFEPPSEELQHEEKQTKL---RSLRNRQSLFQEEGMLSLVLNCIDRLN-VYTTAAHFAEFAGEEAAESWKEIV 520
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   521 NLLYELLASLIRGNRTNCALFSTNLDWLVSKLDRLEASSGILEVLYCVLIESPE-VLNIIQENHIKSIISLLDKHGRNHK 599
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 378523612   600 VLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNL 638
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 217-399 1.83e-80

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: 264.21  E-value: 1.83e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  217 GGHVLRLFHGHMDECLTI-SPSDSDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALT 295
Cdd:cd23291     1 GGDVLRLLHGHMDECLTVpSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  296 EDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKK 375
Cdd:cd23291    81 EDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSIQR 160

                         170       180
                  ....*....|....*....|....
gi 378523612  376 KAMLHQEGHMDDALSLTRCQQEES 399
Cdd:cd23291   161 KAIMHHEGHMDDGLNLSRSQHEES 184
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 644-795 1.07e-78

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: 257.63  E-value: 1.07e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  644 SIRPNIFVGRAEGSTQYGKWYFEVMVDEVAPFlTAQATHLRVGWALSEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 723
Cdd:cd12877     1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378523612  724 TGHVARPVTSPGQHLLGPEDVVSCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGIKVRFLLG 795
Cdd:cd12877    80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 12-211 1.29e-77

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: 257.04  E-value: 1.29e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612    12 VQFLRTDDEVVLQCSATVLkeqlkLCLAAEGFGNRLCFLEPTSNAQNVPP-DLAICCFILEQSLSVRALQEMLAN----- 85
Cdd:pfam08709    2 SSFLHIGDIVSLSCEESVN-----GFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWSAgnrsp 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612    86 ----TVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEG 161
Cdd:pfam08709   77 ngnsLTDALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 378523612   162 EKVRVGDDLILVSVSSERYLHLST-----ASGELQVDASFMQTLWNMNPICSCCE 211
Cdd:pfam08709  157 DNVCVGDEVILVPVSAPIFLHTTSsselrDNPGKEVNASFGQTSWKMEPFMSGCE 211
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1074-1205 2.71e-76

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: 249.91  E-value: 2.71e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1074 RIFRAEKSYAVQSGRWYFEFEAVTTGR-ELGWARPELRPDVELGADDLAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCM 1152
Cdd:cd12878     1 RTFRAEKTYAVTSGKWYFEFEVLTSGYmRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 378523612 1153 IDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLG 1205
Cdd:cd12878    81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1419-1567 4.01e-75

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: 247.60  E-value: 4.01e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1419 DNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMSFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGG 1498
Cdd:cd12879     1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378523612 1499 DFVSPGQQ--GRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVVQFDLR 1567
Cdd:cd12879    81 ELLAEVGQdsSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 213-391 1.70e-73

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: 244.20  E-value: 1.70e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   213 GFVTGGHVLRLFHGHMDECLTISPSDS-DDQRRLVYYEGGPVCTHARSLWRLEPLRI-SWSGSHLRWGQPLRIRHVTTGR 290
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQkQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   291 YLALTEDQGLVVVDASKAHTKATSFCFRIS---KEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 367
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFpgdNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....
gi 378523612   368 LRLGVLKKKAMLHQEGHMDDALSL 391
Cdd:pfam02815  161 WGFGPEQQKVTCAKEGHMDDALTL 184
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2160-2368 1.55e-71

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: 239.02  E-value: 1.55e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2160 QIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMvNVLGG------------GESKEIRFPKM 2227
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlGEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2228 VTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGiGLGMQGSTpLDVAAASVIDNNELALalqeqdlekvvSYLAGCGLQ 2307
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLG-SPSLAEGT-LDVLTALLMDNPELLL-----------NYIKECHIK 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378523612  2308 SCPMLLAKGYPDigwnpcggERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALR 2368
Cdd:pfam01365  147 SFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 852-941 3.21e-45

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: 159.59  E-value: 3.21e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   852 FVPCPVDTIQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVDFHSLPEPERNYNLQMSGETLK 931
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612   932 TLLALGCHVG 941
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2732-2821 4.65e-42

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: 150.35  E-value: 4.65e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2732 FDPRPVETLNVIIPEKLDSFINKFAEYAHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLK 2811
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612  2812 AMIAWEWTVE 2821
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 966-1055 2.60e-37

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: 136.86  E-value: 2.60e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   966 YKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVR 1045
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612  1046 TLLGYGYNIE 1055
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2852-2935 5.40e-33

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: 124.54  E-value: 5.40e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  2852 YNPQPPDLSVVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGG------SHPLLVPYDTLTAKEKARDREKAQELLK 2925
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 378523612  2926 FLQMNGYAVT 2935
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3880-3996 6.49e-32

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: 121.86  E-value: 6.49e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  3880 DDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISdfywyysgkdvieeqgkrnfSKAMS 3959
Cdd:pfam08454    2 EVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN--------------------EKNIE 61

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 378523612  3960 VAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFL 3996
Cdd:pfam08454   62 LIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1086-1207 2.07e-29

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: 115.47  E-value: 2.07e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   1086 SGRWYFEFEAVTTG--ReLGWARPELRPDVE--LGADDLAYVFNGHRGQRWHLG-SEPFGRPWQS-GDVVGCMIDLTENT 1159
Cdd:smart00449    1 SGRHYFEVEIGDGGhwR-VGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNStGPEYGLPLQEpGDVIGCFLDLEAGT 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 378523612   1160 IIFTLNGEVLMsdsgsETAFREIEIGDGFLPVCSLGPGQVGHLNLGQD 1207
Cdd:smart00449   80 ISFYKNGKYLH-----GLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4762-4946 2.11e-27

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: 113.90  E-value: 2.11e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4762 LLTWIMSIDVKYQIWKFGVI---FTDNSFLYLGWYMVMSLLG------------HYNNFFFAAHLLDIAMGVKTLRTILS 4826
Cdd:pfam00520   41 VFTGIFTLEMLLKIIAAGFKkryFRSPWNILDFVVVLPSLISlvlssvgslsglRVLRLLRLLRLLRLIRRLEGLRTLVN 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  4827 SVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVgvRAGGGIGDEIEDPAGDE 4906
Cdd:pfam00520  121 SLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGK 198

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 378523612  4907 YELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQE 4946
Cdd:pfam00520  199 GEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 662-797 2.28e-27

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: 109.74  E-value: 2.28e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   662 KWYFEVMVDevapflTAQATHLRVGWAlsegYSPYPGGGEGWGGngvgDDLYSYGFDGlhlWTGHVARPVTSP--GQHLL 739
Cdd:pfam00622    1 RHYFEVEIF------GQDGGGWRVGWA----TKSVPRKGERFLG----DESGSWGYDG---WTGKKYWASTSPltGLPLF 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 378523612   740 GPEDVVSCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGIKVRFLLGGR 797
Cdd:pfam00622   64 EPGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1087-1203 4.20e-26

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: 105.98  E-value: 4.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1087 GRWYFEFEAVTTGRE---LGWARPELRPDVE--LGADDLAYVFNGHRGQRWHLG-SEPFGRPWQSGDVVGCMIDLTENTI 1160
Cdd:cd11709     1 GKWYWEVRVDSGNGGliqVGWATKSFSLDGEggVGDDEESWGYDGSRLRKGHGGsSGPGGRPWKSGDVVGCLLDLDEGTL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 378523612 1161 IFTLNGEVLMsdsgseTAFREI-EIGDGFLPVCSLGPGQVGHLN 1203
Cdd:cd11709    81 SFSLNGKDLG------VAFTNLfLKGGGLYPAVSLGSGQGVTIN 118
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1432-1564 3.01e-23

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: 97.80  E-value: 3.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  1432 TYYYSVRVFaGQEPSCVWVGWVTPDYHQHDMSFDlskvravtvtmGDEQGnvhsslkcSNCYMVWGGDFVSPGQQGRISH 1511
Cdd:pfam00622    1 RHYFEVEIF-GQDGGGWRVGWATKSVPRKGERFL-----------GDESG--------SWGYDGWTGKKYWASTSPLTGL 60

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 378523612  1512 ----TDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNT-KLFPAVFVlpTHQNVVQF 1564
Cdd:pfam00622   61 plfePGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSL--GAGEGLKF 116
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1431-1564 1.72e-22

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: 95.82  E-value: 1.72e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   1431 TTYYYSVRVFagqEPSCVWVGWVTPDYHQHDMSfdlskvravtvTMGDEQG-NVHSSLKCSNCYMVWGGDFVSPGQQgri 1509
Cdd:smart00449    2 GRHYFEVEIG---DGGHWRVGVATKSVPRGYFA-----------LLGEDKGsWGYDGDGGKKYHNSTGPEYGLPLQE--- 64

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 378523612   1510 shTDLVIGCLVDLATGLMTFTANGKESN--TFFQVEPNTKLFPAVFVLPTHQNVVQF 1564
Cdd:smart00449   65 --PGDVIGCFLDLEAGTISFYKNGKYLHglAFFDVKFSGPLYPAFSLGSGNSVRLNF 119
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 1083-1205 2.09e-22

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: 95.86  E-value: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1083 AVQSGRWYFEFEAVTTG-RELGWARPELRPDVELGADDL--AYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCMIDLTENT 1159
Cdd:cd12882     7 CVYKGKWMYEVTLGTKGiMQIGWATISCRFTQEEGVGDTrdSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDLDKGT 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 378523612 1160 IIFTLNGEVLmsdsgsETAFREIEIGDG--FLPVCSLGPGQVGHLNLG 1205
Cdd:cd12882    87 ISFYRNGRSL------GVAFDNVRRGPGlaYFPAVSLSFGERLELNFG 128
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1088-1207 3.94e-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: 92.02  E-value: 3.94e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  1088 RWYFEFEAVTTGRE---LGWARPE--LRPDVELGADDLAYVFNGHRGQR-WHLGSEPFGRP-WQSGDVVGCMIDLTENTI 1160
Cdd:pfam00622    1 RHYFEVEIFGQDGGgwrVGWATKSvpRKGERFLGDESGSWGYDGWTGKKyWASTSPLTGLPlFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 378523612  1161 IFTLNGEVLMsdsgseTAFREIEIGDGFLPVCSLGPGQVGHLNLGQD 1207
Cdd:pfam00622   81 SFTKNGKSLG------YAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 661-796 8.01e-20

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: 88.12  E-value: 8.01e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612    661 GKWYFEVMVDEvapfltaqATHLRVGWALSEGYSPYpgggegwgGNGVGDDLYSYGFDGLHLwTGHVARPVTSPGQHLLG 740
Cdd:smart00449    2 GRHYFEVEIGD--------GGHWRVGVATKSVPRGY--------FALLGEDKGSWGYDGDGG-KKYHNSTGPEYGLPLQE 64

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 378523612    741 PEDVVSCCLDLSVPSISFRINGCPVQGV-FESFNLDGLFFPVVSFSAGIKVRFLLGG 796
Cdd:smart00449   65 PGDVIGCFLDLEAGTISFYKNGKYLHGLaFFDVKFSGPLYPAFSLGSGNSVRLNFGP 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 661-793 1.60e-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: 87.10  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  661 GKWYFEVMVDevapflTAQATHLRVGWAlSEGYSPYPGGGEGwggngvgDDLYSYGFDGLHLWTGHVARPvtSPGQHLLG 740
Cdd:cd11709     1 GKWYWEVRVD------SGNGGLIQVGWA-TKSFSLDGEGGVG-------DDEESWGYDGSRLRKGHGGSS--GPGGRPWK 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 378523612  741 PEDVVSCCLDLSVPSISFRINGCPVQGVFESFNLD-GLFFPVVSFSAGIKVRFL 793
Cdd:cd11709    65 SGDVVGCLLDLDEGTLSFSLNGKDLGVAFTNLFLKgGGLYPAVSLGSGQGVTIN 118
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 212-392 6.94e-17

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: 82.43  E-value: 6.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  212 EGFVTGGHVLRLFHGHMDECLTISPSDSDDqrrlVYYEGGPVCTH---------------ARSLWRLEPLRISWSGSHLR 276
Cdd:cd23280     4 ENFLKGGDVVRLFHKELEAYLSAEGSFVDE----VLTEDVHLRVRpvddrkprtlfpptsGDTFWQIEKEDTPLKGGVIK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  277 WGQPLRIRHVTTGRYLALTEDQGLVVVDA-SKAHTKATSFCFriskekldvapkRDVEGMGPPEIKYGeSLCFVQHVASG 355
Cdd:cd23280    80 WGDQCRLRHLPTGKYLAVDDKTGNGKVVLtSDPSDPSTVFRL------------HPVTKETSEEVKFG-SYVRIEHVATG 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 378523612  356 LWLtYAAPDP-----KALRLGVLKKKAMLHQ-----EGHMDDALSLT 392
Cdd:cd23280   147 TWL-HAETDEelrrsKKSPAGLSWDGAKLRKvslslERQDDDAFTIQ 192
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 1081-1205 4.18e-12

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: 67.16  E-value: 4.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1081 SYAVQSGRWYFEFEaVTTGRE-------LGWARPELRPDVELGADDLAYVFNGHRGQRWHLG-SEPFGRPW-QSGDVVGC 1151
Cdd:cd12872    22 NHGVREGKWYFEVK-ILEGGGtetghvrVGWSRREASLQAPVGYDKYSYAIRDKDGSKFHQSrGKPYGEPGfKEGDVIGF 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 378523612 1152 MIDLTEntIIFTLNGEVLMsdsgseTAFREIEIGDGFLPVCSL-GPGQVgHLNLG 1205
Cdd:cd12872   101 LITLPK--IEFFKNGKSQG------VAFEDIYGTGGYYPAVSLyKGATV-TINFG 146
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 218-358 5.86e-11

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: 64.33  E-value: 5.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  218 GHVLRLFHGHMDECLTISPSD--SDDQRRLVYYEGGPVCTHARSLWRLEPLRISWsGSHLRWGQPLRIRHVTTGRYLAL- 294
Cdd:cd23263     1 GDVIWLKHSETGKYLHSHRKNypTGSGQQEVTFESSSRKGDTNGLWIIESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSe 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378523612  295 -------TEDQGLVVVDASKahTKATSFCFRISKEKLDVapkrdvegmgpPEIKYGESLCFVQHVASGLWL 358
Cdd:cd23263    80 egkkspkSNHQEVLCLTDNP--DKSSLFKFEPIGSTKYK-----------QKYVKKDSYFRLKHVNTNFWL 137
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 653-792 3.84e-10

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: 61.38  E-value: 3.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  653 RAEGSTQYGKWYFEVMVDEVAPFLTAqatHLRVGWALSE-------GYspypgggegwggngvgdDLYSYGFDGLHLWTG 725
Cdd:cd12872    20 RANHGVREGKWYFEVKILEGGGTETG---HVRVGWSRREaslqapvGY-----------------DKYSYAIRDKDGSKF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378523612  726 HVARPvTSPGQHLLGPEDVVSCCLDLsvPSISFRINGCPvQGV-FESFNLDGLFFPVVSFSAGIKVRF 792
Cdd:cd12872    80 HQSRG-KPYGEPGFKEGDVIGFLITL--PKIEFFKNGKS-QGVaFEDIYGTGGYYPAVSLYKGATVTI 143
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 1087-1205 4.04e-10

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: 60.44  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1087 GRWYFEFEAVTTG-RELGWARPELRPDVE----LGADDLAYVFNGHRGQRWH-LGSEPFGRP-WQSGDVVGCMIDLTENT 1159
Cdd:cd12883     1 GVWYYEVTVLTSGvMQIGWATKDSKFLNHegygIGDDEYSCAYDGCRQLIWYnAKSKPHTHPrWKPGDVLGCLLDLNKKQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 378523612 1160 IIFTLNGEVLMSDSGSETAFREieigdGFLPVCSLGPGQVGHLNLG 1205
Cdd:cd12883    81 MIFSLNGNRLPPERQVFTSAKS-----GFFAAASFMSFQQCEFNFG 121
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 1074-1205 1.17e-09

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: 59.60  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1074 RIFRAEKSYAVQSGRWYFEFEAVTTGRE----LGWARPELRPDVELGADDLAYVFNGHRGQ--RWHLGSEPFGRPWQSGD 1147
Cdd:cd12885     1 GSVRADHPIPPKVPVFYFEVTILDLGEKgivsIGFCTSGFPLNRMPGWEDGSYGYHGDDGRvyLGGGEGENYGPPFGTGD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 378523612 1148 VVGCMIDLTENTIIFTLNGEVLmsdsgsETAFREIEIGDgFLPVCSLG-PGQVGHLNLG 1205
Cdd:cd12885    81 VVGCGINFKTGEVFFTKNGELL------GTAFENVVKGR-LYPTVGLGsPGVKVRVNFG 132
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1433-1559 3.65e-09

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: 57.44  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1433 YYYSVRVFAGQePSCVWVGWVTPDyhqhdmsFDLSKVRAVtvtmGDeqgNVHS-SLKCSNCYMvwGGDFVSPGQQGRISH 1511
Cdd:cd11709     3 WYWEVRVDSGN-GGLIQVGWATKS-------FSLDGEGGV----GD---DEESwGYDGSRLRK--GHGGSSGPGGRPWKS 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 378523612 1512 TDlVIGCLVDLATGLMTFTANGKESNTFFQVEPNTK--LFPAVFVLPTHQ 1559
Cdd:cd11709    66 GD-VVGCLLDLDEGTLSFSLNGKDLGVAFTNLFLKGggLYPAVSLGSGQG 114
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 1077-1206 5.07e-09

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: 57.92  E-value: 5.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1077 RAEKSYAVQSGRWYFEFEAVTTGRE----LGWARPelrpDVEL----GADDLAYVFNGHRGQRWHlGS---EPFGRPWQS 1145
Cdd:cd12909    15 RANHPIPPQCGIYYFEVKIISKGRDgyigIGFSTK----DVNLnrlpGWEPHSWGYHGDDGHSFC-SSgtgKPYGPTFTT 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378523612 1146 GDVVGCMIDLTENTIIFTLNGEVLmsdsgsETAFREIEIGDgFLPVCSL-GPGQVGHLNLGQ 1206
Cdd:cd12909    90 GDVIGCGINFRDNTAFYTKNGVNL------GIAFRDIKKGN-LYPTVGLrTPGEHVEANFGQ 144
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 1072-1197 1.39e-08

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: 56.94  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1072 RARIFRAEKSYAVQSGRWYFEF-----EAVTTGR---ELGWA-----RPELRPDVELGA----DDL-AYVFNG------H 1127
Cdd:cd12877     3 RPNIFVGVVEGSAQYKKWYFEVevdhvEQFTHQPahlRVGWAntsgyVPYPGGGEGWGGngvgDDLySYGFDGlhlwtgG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1128 RGQRWHLGSEPFGRPwqsGDVVGCMIDLTENTIIFTLNGEVLmsdsgsETAFREIEIGDGFLPVCSLGPG 1197
Cdd:cd12877    83 RSRRVTSGTQHLLKK---GDVVGCCLDLSVPSISFRVNGRPV------QGMFENFNLDGMFFPVMSFSAG 143
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 653-795 4.38e-08

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: 55.00  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  653 RAEGSTQY--GKWYFEVMVdevapfLTAqaTHLRVGWALSEGYSPYPGGGegwggngvgDDLySYGFDGLHLWTGHVarp 730
Cdd:cd12878     4 RAEKTYAVtsGKWYFEFEV------LTS--GYMRVGWARPGFRPDLELGS---------DDL-SYAFDGFLARKWHQ--- 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 378523612  731 vtspGQHLLG----PEDVVSCCLDLSVPSISFRING---CPVQG---VFESFNLDGLFFPVVSFSAGIKVRFLLG 795
Cdd:cd12878    63 ----GSESFGkqwqPGDVVGCMLDLVDRTISFTLNGellIDSSGsevAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
272-360 1.03e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 51.57  E-value: 1.03e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612    272 GSHLRWGQPLRIRHVTTGRYLALTEDqglvvvdaskahtkatsfcfrisKEKLDVAPKRDVEGMGPPEIkygeslcfvqh 351
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDE-----------------------KLPPWGDGQQEVTGYGNPAI----------- 46


                    ....*....
gi 378523612    352 VASGLWLTY 360
Cdd:smart00472   47 DANTLWLIE 55
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
212-265 2.05e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 50.42  E-value: 2.05e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 378523612    212 EGFVTGGHVLRLFHGHMDECLTIS----PSDSDDQRRLVYYEGGpvCTHARSLWRLEP 265
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHdeklPPWGDGQQEVTGYGNP--AIDANTLWLIEP 56
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 1067-1206 3.08e-07

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: 52.96  E-value: 3.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1067 QSRGDRA-RIFRAEKSyAVQSGRWYFEFEAVTTG--ReLGWArpELRPDVELGADDLAYVFNGHrGQRWHLGS-EPFGRP 1142
Cdd:cd12873    20 QSREEKGwQGCRATKG-VKGKGKYYYEVTVTDEGlcR-VGWS--TEDASLDLGTDKFGFGYGGT-GKKSHGRQfDDYGEP 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 378523612 1143 WQSGDVVGCMIDLTENTIIFTLNGEVLmsdsgsETAFrEIE---IGDGFLPVCSLGPGQVGhLNLGQ 1206
Cdd:cd12873    95 FGLGDVIGCYLDLDNGTISFSKNGKDL------GKAF-DIPphlRNSALFPAVCLKNAEVE-FNFGD 153
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
 1120-1207 5.11e-06

SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor of SHR3 null mutation protein 4) and similar proteins. SSH4 is a component of the endosome-vacuole trafficking pathway that regulates nutrient transport and may be involved in processes determining whether plasma membrane proteins are degraded or routed to the plasma membrane. 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. In yeast, SSH4 and the homologous protein EAR1 (endosomal adapter of RSP5) recruit Rsp5p, an essential ubiquitin ligase of the Nedd4 family, and assist it in its function at multivesicular bodies by directing the ubiquitylation of specific cargoes.


Pssm-ID: 293967  Cd Length: 192  Bit Score: 50.44  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1120 LAYVF-NGHR--GQRWhlGSEPFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMS-DSGSETAFRE--IEIGDGFLPV-- 1191
Cdd:cd12910    96 LAVHSdDGHRyiNDPF--GGKDFTPPFREGDTIGIGYRFSSGTIFFTRNGKRLGGwDLGEELDAEDdgVTGLEGFHDLya 173

                          90
                  ....*....|....*....
gi 378523612 1192 ---CSLGPGQVgHLNLGQD 1207
Cdd:cd12910   174 aigVFGGECEV-HVNPGQW 191
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 661-795 5.98e-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: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  661 GKWYFEVMVdevapfLTAQAthLRVGWALS-------EGYSpypgggegwggngVGDDLYSYGFDGLH--LWtgHVARPV 731
Cdd:cd12883     1 GVWYYEVTV------LTSGV--MQIGWATKdskflnhEGYG-------------IGDDEYSCAYDGCRqlIW--YNAKSK 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378523612  732 TSPGQHLlGPEDVVSCCLDLSVPSISFRINGCPVQGVFESFNL--DGlFFPVVSFSAGIKVRFLLG 795
Cdd:cd12883    58 PHTHPRW-KPGDVLGCLLDLNKKQMIFSLNGNRLPPERQVFTSakSG-FFAAASFMSFQQCEFNFG 121
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
99-154 2.10e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.02  E-value: 2.10e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 378523612     99 HRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATG-EACWWTMHPA 154
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 ...
 45-186 2.83e-05

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: 48.15  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612   45 NRLCFLEPTSNAQNVPPDLAICCFILEqslsvralqemlantveaGVESSQGGGhrTLLYGHAILLRHAHSRMYLsCLTt 124
Cdd:cd23280    41 LRVRPVDDRKPRTLFPPTSGDTFWQIE------------------KEDTPLKGG--VIKWGDQCRLRHLPTGKYL-AVD- 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378523612  125 srsmTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGekVRVGDDLILVSVSSERYLHLSTA 186
Cdd:cd23280    99 ----DKTGNGKVVLTSDPSDPSTVFRLHPVTKETSEE--VKFGSYVRIEHVATGTWLHAETD 154
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 1087-1195 1.82e-04

SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in bacterial and are mostly uncharacterized. 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 eukaryotic 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).


Pssm-ID: 293944  Cd Length: 129  Bit Score: 44.42  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1087 GRWYFEFE----AVTTGRELGWARPELRPDVELGADDLA---YVFNGHRGQRWHLGSEP--FGRPWQSGDVVGCMIDLTE 1157
Cdd:cd12886     1 GKWYWEVTvvssAASTYAGIGVANAAATGNNGLNGIELSsigYSLGVYSGNKLSNGSSVatYGAGFTAGDVIGVALDLDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 378523612 1158 NTIIFTLNGeVLMSDSGSETAFREIEIGDGFLPVCSLG 1195
Cdd:cd12886    81 GKIWFYKNG-VWQGGGDPAPGTNPAFAGTAMYPAVTGG 117
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
161-206 2.83e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.56  E-value: 2.83e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 378523612    161 GEKVRVGDDLILVSVSSERYLHLSTA------SGELQVDAS-----FMQTLWNMNPI 206
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEklppwgDGQQEVTGYgnpaiDANTLWLIEPV 57
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 1433-1552 3.33e-04

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: 44.10  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1433 YYYSVRVfagQEPSCVWVGWVTPDyhqhdMSFDLSKvravtvtmgDEQGnvhsslkcsncymvWGgdFvspGQQGRISHT 1512
Cdd:cd12873    42 YYYEVTV---TDEGLCRVGWSTED-----ASLDLGT---------DKFG--------------FG--Y---GGTGKKSHG 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 378523612 1513 DL------------VIGCLVDLATGLMTFTANGKESNTFFQVEPNTK---LFPAV 1552
Cdd:cd12873    86 RQfddygepfglgdVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRnsaLFPAV 140
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 1077-1169 3.44e-04

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: 44.50  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1077 RAekSYAVQSGRWYFEF--------------EAVTTGRELGWARPelRPDVELGADDLAYVFNGhRGQRWHLG-SEPFGR 1141
Cdd:cd12884    37 RA--TYGVTKGKVCFEVkvtenlpvkhlpteETDPHVVRVGWSVD--SSSLQLGEEEFSYGYGS-TGKKSTNCkFEDYGE 111

                          90       100       110
                  ....*....|....*....|....*....|
gi 378523612 1142 PWQSGDVVGCMIDL--TENTIIFTLNGEVL 1169
Cdd:cd12884   112 PFGENDVIGCYLDFesEPVEISFSKNGKDL 141
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 644-787 1.06e-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: 42.31  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612  644 SIRPNIFVGRaegstqyGKWYFEVMVdevapfltAQATHLRVGWAL-------SEGYSpypgggegwggngvgDDLYSYG 716
Cdd:cd12882     1 SIRANACVYK-------GKWMYEVTL--------GTKGIMQIGWATiscrftqEEGVG---------------DTRDSYA 50

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378523612  717 FDGLHLWTGHVArpVTSPGQHLLgPEDVVSCCLDLSVPSISFRINGCPVQGVFESFN-LDGL-FFPVVSFSAG 787
Cdd:cd12882    51 YDGNRVRKWNVS--TQKYGEPWV-AGDVIGCCIDLDKGTISFYRNGRSLGVAFDNVRrGPGLaYFPAVSLSFG 120
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 1415-1552 1.27e-03

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: 41.88  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378523612 1415 VVPADNRddpeIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMsfdlskvravtvtMGDEQGNVhsSLKCSNCYM 1494
Cdd:cd12885     2 SVRADHP----IPPKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRM-------------PGWEDGSY--GYHGDDGRV 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 378523612 1495 VWGGDfvSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAV 1552
Cdd:cd12885    63 YLGGG--EGENYGPPFGTGDVVGCGINFKTGEVFFTKNGELLGTAFENVVKGRLYPTV 118
 
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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