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Conserved domains on  [gi|17352467|ref|NP_476992|]
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ryanodine receptor, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 215-395 1.17e-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: 341.98  E-value: 1.17e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  215 GGDVLRFFHGG-DECLTIPSTWGREAGQNIVIYEGGVVMAQARSLWRLELARTKWTGGFINWYHPMRIRHITTGRYLGVN 293
Cdd:cd23278    1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  294 DSNELILVKKEEASIATTTFCLRQEKDDeKKVLEDKDLEVIGSPIIKYGDTTVIVQHCETSLWLSYKSYETKKKgVGKVE 373
Cdd:cd23278   81 EDRGLVLVPKEKADVKATAFCFRQSKDD-KKVLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVETKKR-VGGVE 158

                        170       180
                 ....*....|....*....|..
gi 17352467  374 EKQAILHEEGKMDDCLDFSRSQ 395
Cdd:cd23278  159 ERKAILHAEGHMDDGLSLSRAQ 180
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 12-206 5.45e-84

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: 275.53  E-value: 5.45e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467     12 DVSFLRTEDMVTLSCTATGeRVCLAAEGFGNRHCFLENIAD-KNVPP-DLSQCVFVIEQALSVRALQELVTAA-GSETGK 88
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESV-NGFISALGLGNDRCFVENKAGdLNDPPkKFRDCVFKICPANSYAAQKELWSAGnRSPNGN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467     89 G---------TGSGHRTLLYGNAILLRHHNSDMYLACLSTS-SSNDKLSFDVGLQEHSQGEACWWTVHPASKQRSEGEKV 158
Cdd:pfam08709   80 SltdalkhasNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSpSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDNV 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17352467    159 RVGDDLILVSVATERYLHTT-----KENEQSIVNASFHVTHWSVQPYGTGISR 206
Cdd:pfam08709  160 CVGDEVILVPVSAPIFLHTTssselRDNPGKEVNASFGQTSWKMEPFMSGCEN 212
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 647-799 1.83e-80

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


:

Pssm-ID: 240457  Cd Length: 151  Bit Score: 262.63  E-value: 1.83e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  647 SIRPNIFVGRVDGSSMYQKWYFEVTMDHIEQTTHMMPHLRIGWANTSGYVPYPGGGKKWGGNGVGDDLYSFGFDGAFLWT 726
Cdd:cd12877    1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTHQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLWT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17352467  727 GGRKTLVVDalPEEPFIRKGDVIGVAIDLSVPIITFTFNGVKVRGSFRDFNLDGMFFPVMSCSSKLSCRFLFG 799
Cdd:cd12877   81 GGRSRRVTS--GTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 443-641 3.66e-80

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


:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 264.06  E-value: 3.66e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    443 CLEDLINYFSQPEDDMEHEEKQNR---FRALRNRQDLFQEEGVLNLILEAIDKINIITSQGFLASFLAGDETGQSWDLIS 519
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKlmnNKPLRQRQNLMREQGVLETVMEVIDLLGAPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    520 TYLYQLLAAIIKGNHTNCAQFANSnrLNWLFSRLGSQASSEGSgmLDVLHCVLIDSPE-ALNMMRDEHIKVIISLLEKHG 598
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKH--LDWLQSQLGSPSLAEGT--LDVLTALLMDNPElLLNYIKECHIKSFISLLRKHG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 17352467    599 RDPKVLDVLCSLCVGNGVAVRSSQNNICDFLLPGKNLLLQTLL 641
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1518-1669 5.05e-78

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


:

Pssm-ID: 293937  Cd Length: 151  Bit Score: 255.69  E-value: 5.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1518 DEMFDAECLKLINEYFYGVRIFPGQDPTHVYVGWVTTQYHLHSREFNKNKVRRGSVYIEDDYEMAIERIDRQSCYVVRAD 1597
Cdd:cd12879    1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17352467 1598 ELFNEVTQDaSGKGASQGMFVGCFVDTATGIIRFTCEGKDTSHRWMMEPDTKLFPAIFVEATSKEILQIELG 1669
Cdd:cd12879   81 ELLAEVGQD-SSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1079-1213 4.95e-77

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: 252.22  E-value: 4.95e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1079 RTYRVERNYAVTSGKWYFEFEVLTSGPMRVGWARADCYPGAMLGSEDTSWAFDGHNVTKMHAGSiEHFGVRYEAGDVIGC 1158
Cdd:cd12878    1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGS-ESFGKQWQPGDVVGC 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17352467 1159 FIDVKEQTISFSLNGELLMDALGGETTFADVTAeGVGFVPACTLGVGQKARLIYG 1213
Cdd:cd12878   80 MLDLVDRTISFTLNGELLIDSSGSEVAFKDIEI-GEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2214-2443 2.01e-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: 2.01e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2214 QIRALLPVQMSQEEEELMRKRLWKLVNNATFFQHPDLIRILRVHENVMAVmMNTLGRRAQAQSDAPTqsevaegAPSKEK 2293
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEV-IDLLGAPFTGALLFAE-------DLGEEK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2294 DTS-HEMVVACCRFLCYFCRTGRQNQKAMFDHFDFLLDNanilLARPSLRGSTpLDVAYSSLMENTELALalrehyleki 2372
Cdd:pfam01365   73 NAPwKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL---------- 137

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17352467   2373 aVYLSRCGLQSNSELVEKGYPDlgwdpvegERYLDFLRY-CVwVNGESVEENANLVIRLLIRRPECLGPALR 2443
Cdd:pfam01365  138 -NYIKECHIKSFISLLRKHGRD--------PRYLDFLSDlCV-CNGEAVRENQNLICRLLLPNPDLLLQTLL 199
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4505-4747 4.20e-68

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: 232.67  E-value: 4.20e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4505 TVQAFGlDINKEENGMYKVVVHESPA---NSSMEEGGESSP-------EDGAAASGELVEGEPHQEPISIVDLLGGEAAK 4574
Cdd:pfam06459   44 LSDIFG-LILKKEGGQYKVVPHDPEAglgDLSETTAEEPPPllkrklqESEEAEDEEEEEEEPKPEPIEKADGENGEKEE 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4575 KA--------AQERQEAQKAQEAAMASIEAEAKKSSSAPQEtpavhqiDFSQYTHRAVSFLARNFYNLKYVALVLAFSIN 4646
Cdd:pfam06459  123 KPkeeeteseAPEEEEMKKKQRKRHSKKKEEPEAQGSAFWN-------ELEVYQTKLLNYLARNFYNLRFLALFVAFAIN 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4647 FMLLFYKVTSFTEEADSSAEEELILGSGSGGGADitgsgfggsgdggsGDGEMEDEIPELVHVDEDFFYMEHVLRIAACL 4726
Cdd:pfam06459  196 FILLFYKVSTSPPDEEEEEGSGWGDSGSGSGGGS--------------GEDEEEEEGPVYFVLEESTGYMEPTLRFLAIL 261

                          250       260
                   ....*....|....*....|.
gi 17352467   4727 HSLVSLAMLIAYYHLKVPLAI 4747
Cdd:pfam06459  262 HTIISFLCIIGYYCLKVPLVI 282
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2817-2906 1.13e-41

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 149.19  E-value: 1.13e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2817 YMPNPIDTNNVHLDNDLNSLVQKFSEHYHDAWASRRLEGGWTYGDIRSDNDRKHPRLKPYNMLSEYERERYRDPVRECLK 2896
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 17352467   2897 GLLAIGWTVE 2906
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 967-1056 2.39e-41

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 148.42  E-value: 2.39e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    967 YKPAPLDLSAVTLTPKLEELVDQLAENTHNLWARERIQQGWTYGLNEDSENHRSPHLVPYAKVDEAIKKANRDTASETVR 1046
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 17352467   1047 TLLVYGYVLD 1056
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 854-943 8.76e-41

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 146.88  E-value: 8.76e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    854 FVPKPVDTTGVTLPSSVDQIKEKLAENIHEMWALNKIEAGWSWGEHRDDYHRIHPCLTHFEKLPAAEKRYDNQLAVQTLK 933
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 17352467    934 TIISLGYYIT 943
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3992-4109 1.82e-36

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: 134.58  E-value: 1.82e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   3992 HDAEFTCALFRFIQLTCEGHNLEWQNYLRTQAGNTTTVNVVICTVDYLLRLQESImdfywhysskeiidpagkanFFKAI 4071
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSI--------------------NEKNI 60

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 17352467   4072 EVASQVFNTLTEVIQGPCTLNQQALAHSRLWDAVGGFL 4109
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2940-3022 4.26e-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: 124.92  E-value: 4.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2940 YNPHPVDMSNLTLSREMQNMAERLAENSHDIWAKKKNEELNGCGGV------IHPQLVPYDLLTDKEKKKDRERSQEFLK 3013
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 17352467   3014 YMQYQGYKL 3022
Cdd:pfam02026   81 TLLALGYTI 89
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4835-4958 1.34e-11

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


:

Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 67.68  E-value: 1.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4835 IFKYIMNIDWRYQVWKAGVT---FTDNAFLYSLWYFSFSVMG------------NFNNFFFAAHLLDVAVGFKTLRTILQ 4899
Cdd:pfam00520   41 VFTGIFTLEMLLKIIAAGFKkryFRSPWNILDFVVVLPSLISlvlssvgslsglRVLRLLRLLRLLRLIRRLEGLRTLVN 120

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4900 SVTHNGKQLVLTVMLLTIIVYIYTVIAFNFFR-KFYIQEEDEEVDKKCHDMLTCFVFHLY 4958
Cdd:pfam00520  121 SLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGgKLKTWENPDNGRTNFDNFPNAFLWLFQ 180
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 215-395 1.17e-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: 341.98  E-value: 1.17e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  215 GGDVLRFFHGG-DECLTIPSTWGREAGQNIVIYEGGVVMAQARSLWRLELARTKWTGGFINWYHPMRIRHITTGRYLGVN 293
Cdd:cd23278    1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  294 DSNELILVKKEEASIATTTFCLRQEKDDeKKVLEDKDLEVIGSPIIKYGDTTVIVQHCETSLWLSYKSYETKKKgVGKVE 373
Cdd:cd23278   81 EDRGLVLVPKEKADVKATAFCFRQSKDD-KKVLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVETKKR-VGGVE 158

                        170       180
                 ....*....|....*....|..
gi 17352467  374 EKQAILHEEGKMDDCLDFSRSQ 395
Cdd:cd23278  159 ERKAILHAEGHMDDGLSLSRAQ 180
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 12-206 5.45e-84

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: 275.53  E-value: 5.45e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467     12 DVSFLRTEDMVTLSCTATGeRVCLAAEGFGNRHCFLENIAD-KNVPP-DLSQCVFVIEQALSVRALQELVTAA-GSETGK 88
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESV-NGFISALGLGNDRCFVENKAGdLNDPPkKFRDCVFKICPANSYAAQKELWSAGnRSPNGN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467     89 G---------TGSGHRTLLYGNAILLRHHNSDMYLACLSTS-SSNDKLSFDVGLQEHSQGEACWWTVHPASKQRSEGEKV 158
Cdd:pfam08709   80 SltdalkhasNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSpSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDNV 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17352467    159 RVGDDLILVSVATERYLHTT-----KENEQSIVNASFHVTHWSVQPYGTGISR 206
Cdd:pfam08709  160 CVGDEVILVPVSAPIFLHTTssselRDNPGKEVNASFGQTSWKMEPFMSGCEN 212
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 647-799 1.83e-80

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


Pssm-ID: 240457  Cd Length: 151  Bit Score: 262.63  E-value: 1.83e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  647 SIRPNIFVGRVDGSSMYQKWYFEVTMDHIEQTTHMMPHLRIGWANTSGYVPYPGGGKKWGGNGVGDDLYSFGFDGAFLWT 726
Cdd:cd12877    1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTHQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLWT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17352467  727 GGRKTLVVDalPEEPFIRKGDVIGVAIDLSVPIITFTFNGVKVRGSFRDFNLDGMFFPVMSCSSKLSCRFLFG 799
Cdd:cd12877   81 GGRSRRVTS--GTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 443-641 3.66e-80

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


Pssm-ID: 460175  Cd Length: 199  Bit Score: 264.06  E-value: 3.66e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    443 CLEDLINYFSQPEDDMEHEEKQNR---FRALRNRQDLFQEEGVLNLILEAIDKINIITSQGFLASFLAGDETGQSWDLIS 519
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKlmnNKPLRQRQNLMREQGVLETVMEVIDLLGAPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    520 TYLYQLLAAIIKGNHTNCAQFANSnrLNWLFSRLGSQASSEGSgmLDVLHCVLIDSPE-ALNMMRDEHIKVIISLLEKHG 598
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKH--LDWLQSQLGSPSLAEGT--LDVLTALLMDNPElLLNYIKECHIKSFISLLRKHG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 17352467    599 RDPKVLDVLCSLCVGNGVAVRSSQNNICDFLLPGKNLLLQTLL 641
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1518-1669 5.05e-78

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


Pssm-ID: 293937  Cd Length: 151  Bit Score: 255.69  E-value: 5.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1518 DEMFDAECLKLINEYFYGVRIFPGQDPTHVYVGWVTTQYHLHSREFNKNKVRRGSVYIEDDYEMAIERIDRQSCYVVRAD 1597
Cdd:cd12879    1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17352467 1598 ELFNEVTQDaSGKGASQGMFVGCFVDTATGIIRFTCEGKDTSHRWMMEPDTKLFPAIFVEATSKEILQIELG 1669
Cdd:cd12879   81 ELLAEVGQD-SSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1079-1213 4.95e-77

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: 252.22  E-value: 4.95e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1079 RTYRVERNYAVTSGKWYFEFEVLTSGPMRVGWARADCYPGAMLGSEDTSWAFDGHNVTKMHAGSiEHFGVRYEAGDVIGC 1158
Cdd:cd12878    1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGS-ESFGKQWQPGDVVGC 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17352467 1159 FIDVKEQTISFSLNGELLMDALGGETTFADVTAeGVGFVPACTLGVGQKARLIYG 1213
Cdd:cd12878   80 MLDLVDRTISFTLNGELLIDSSGSEVAFKDIEI-GEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2214-2443 2.01e-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: 2.01e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2214 QIRALLPVQMSQEEEELMRKRLWKLVNNATFFQHPDLIRILRVHENVMAVmMNTLGRRAQAQSDAPTqsevaegAPSKEK 2293
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEV-IDLLGAPFTGALLFAE-------DLGEEK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2294 DTS-HEMVVACCRFLCYFCRTGRQNQKAMFDHFDFLLDNanilLARPSLRGSTpLDVAYSSLMENTELALalrehyleki 2372
Cdd:pfam01365   73 NAPwKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL---------- 137

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17352467   2373 aVYLSRCGLQSNSELVEKGYPDlgwdpvegERYLDFLRY-CVwVNGESVEENANLVIRLLIRRPECLGPALR 2443
Cdd:pfam01365  138 -NYIKECHIKSFISLLRKHGRD--------PRYLDFLSDlCV-CNGEAVRENQNLICRLLLPNPDLLLQTLL 199
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4505-4747 4.20e-68

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: 232.67  E-value: 4.20e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4505 TVQAFGlDINKEENGMYKVVVHESPA---NSSMEEGGESSP-------EDGAAASGELVEGEPHQEPISIVDLLGGEAAK 4574
Cdd:pfam06459   44 LSDIFG-LILKKEGGQYKVVPHDPEAglgDLSETTAEEPPPllkrklqESEEAEDEEEEEEEPKPEPIEKADGENGEKEE 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4575 KA--------AQERQEAQKAQEAAMASIEAEAKKSSSAPQEtpavhqiDFSQYTHRAVSFLARNFYNLKYVALVLAFSIN 4646
Cdd:pfam06459  123 KPkeeeteseAPEEEEMKKKQRKRHSKKKEEPEAQGSAFWN-------ELEVYQTKLLNYLARNFYNLRFLALFVAFAIN 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4647 FMLLFYKVTSFTEEADSSAEEELILGSGSGGGADitgsgfggsgdggsGDGEMEDEIPELVHVDEDFFYMEHVLRIAACL 4726
Cdd:pfam06459  196 FILLFYKVSTSPPDEEEEEGSGWGDSGSGSGGGS--------------GEDEEEEEGPVYFVLEESTGYMEPTLRFLAIL 261

                          250       260
                   ....*....|....*....|.
gi 17352467   4727 HSLVSLAMLIAYYHLKVPLAI 4747
Cdd:pfam06459  262 HTIISFLCIIGYYCLKVPLVI 282
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 211-392 8.84e-64

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: 216.46  E-value: 8.84e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    211 GYVFGGDVLRFFHGG-DECLTIPSTWGREAGQNIVIYEGGVVMAQARSLWRLELART-KWTGGFINWYHPMRIRHITTGR 288
Cdd:pfam02815    1 GYLKGGDVVRLFHSHqDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    289 YLGVNDSNELILVKKEEASIATTTFCLRQEK--DDEKKVLEDKDLEVIGSPIIKYGDTTVIVQHCETSLWLSYKSYETKK 366
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFPgdNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....*.
gi 17352467    367 KGVGKvEEKQAILHEEGKMDDCLDFS 392
Cdd:pfam02815  161 WGFGP-EQQKVTCAKEGHMDDALTLP 185
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2817-2906 1.13e-41

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 149.19  E-value: 1.13e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2817 YMPNPIDTNNVHLDNDLNSLVQKFSEHYHDAWASRRLEGGWTYGDIRSDNDRKHPRLKPYNMLSEYERERYRDPVRECLK 2896
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 17352467   2897 GLLAIGWTVE 2906
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 967-1056 2.39e-41

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 148.42  E-value: 2.39e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    967 YKPAPLDLSAVTLTPKLEELVDQLAENTHNLWARERIQQGWTYGLNEDSENHRSPHLVPYAKVDEAIKKANRDTASETVR 1046
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 17352467   1047 TLLVYGYVLD 1056
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 854-943 8.76e-41

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 146.88  E-value: 8.76e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    854 FVPKPVDTTGVTLPSSVDQIKEKLAENIHEMWALNKIEAGWSWGEHRDDYHRIHPCLTHFEKLPAAEKRYDNQLAVQTLK 933
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 17352467    934 TIISLGYYIT 943
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3992-4109 1.82e-36

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: 134.58  E-value: 1.82e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   3992 HDAEFTCALFRFIQLTCEGHNLEWQNYLRTQAGNTTTVNVVICTVDYLLRLQESImdfywhysskeiidpagkanFFKAI 4071
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSI--------------------NEKNI 60

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 17352467   4072 EVASQVFNTLTEVIQGPCTLNQQALAHSRLWDAVGGFL 4109
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1091-1215 1.76e-33

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 127.03  E-value: 1.76e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    1091 SGKWYFEFEVLTSGPMRVGWARADCYPG--AMLGSEDTSWAFDGHNVTKMHAGSIEHFGVRY-EAGDVIGCFIDVKEQTI 1167
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGyfALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLqEPGDVIGCFLDLEAGTI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 17352467    1168 SFSLNGELLMdalggETTFADVTAEGvGFVPACTLGVGQKARLIYGQD 1215
Cdd:smart00449   81 SFYKNGKYLH-----GLAFFDVKFSG-PLYPAFSLGSGNSVRLNFGPL 122
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2940-3022 4.26e-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: 124.92  E-value: 4.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2940 YNPHPVDMSNLTLSREMQNMAERLAENSHDIWAKKKNEELNGCGGV------IHPQLVPYDLLTDKEKKKDRERSQEFLK 3013
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 17352467   3014 YMQYQGYKL 3022
Cdd:pfam02026   81 TLLALGYTI 89
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1093-1215 5.59e-30

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: 117.06  E-value: 5.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   1093 KWYFEFEVL--TSGPMRVGWARADC--YPGAMLGSEDTSWAFDGHNVTKMHAGSIEHFGV-RYEAGDVIGCFIDVKEQTI 1167
Cdd:pfam00622    1 RHYFEVEIFgqDGGGWRVGWATKSVprKGERFLGDESGSWGYDGWTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 17352467   1168 SFSLNGELLMdalggeTTFADVTAEGvGFVPACTLGVGQKARLIYGQD 1215
Cdd:pfam00622   81 SFTKNGKSLG------YAFRDVPFAG-PLFPAVSLGAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 665-801 5.09e-28

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 111.67  E-value: 5.09e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    665 KWYFEVTMDHIEQTthmmpHLRIGWAntsgYVPYPGGGKKWGGngvgDDLYSFGFDGaflWTGGRKTLVVDALPEEPFIR 744
Cdd:pfam00622    1 RHYFEVEIFGQDGG-----GWRVGWA----TKSVPRKGERFLG----DESGSWGYDG---WTGKKYWASTSPLTGLPLFE 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 17352467    745 KGDVIGVAIDLSVPIITFTFNGVKVRGSFRDFNLDGMFFPVMSCSSKLSCRFLFGGD 801
Cdd:pfam00622   65 PGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 665-801 1.05e-21

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: 93.51  E-value: 1.05e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467     665 KWYFEVTmdhIEQTTHMmphlRIGWANTSGYVPYpgggkkwgGNGVGDDLYSFGFDG--AFLWTGGRKTLVVDALPEepf 742
Cdd:smart00449    3 RHYFEVE---IGDGGHW----RVGVATKSVPRGY--------FALLGEDKGSWGYDGdgGKKYHNSTGPEYGLPLQE--- 64

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467     743 irKGDVIGVAIDLSVPIITFTFNGVKVRG-SFRDFNLDGMFFPVMSCSSKLSCRFLFGGD 801
Cdd:smart00449   65 --PGDVIGCFLDLEAGTISFYKNGKYLHGlAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1532-1671 1.19e-19

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: 87.78  E-value: 1.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   1532 YFYGVRIFpGQDPTHVYVGWVTTQYHLHSREFnknkvrrgsvyIEDDYEMaierIDRQSCYVVRadelFNEVTQDASGKG 1611
Cdd:pfam00622    2 HYFEVEIF-GQDGGGWRVGWATKSVPRKGERF-----------LGDESGS----WGYDGWTGKK----YWASTSPLTGLP 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17352467   1612 -ASQGMFVGCFVDTATGIIRFTCEGKDTSHRWMMEPDT-KLFPAIFVeaTSKEILQIELGRT 1671
Cdd:pfam00622   62 lFEPGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSL--GAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1530-1670 1.28e-18

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: 84.65  E-value: 1.28e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    1530 NEYFYGVRIFpgqDPTHVYVGWVTTQYHLHsrefnknkvrRGSVYIEDDYEMAIERIDRQSCYVVRADELFNEVTQdasg 1609
Cdd:smart00449    2 GRHYFEVEIG---DGGHWRVGVATKSVPRG----------YFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQE---- 64

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17352467    1610 kgasQGMFVGCFVDTATGIIRFTCEGKDTSHR--WMMEPDTKLFPAIFVEatSKEILQIELGR 1670
Cdd:smart00449   65 ----PGDVIGCFLDLEAGTISFYKNGKYLHGLafFDVKFSGPLYPAFSLG--SGNSVRLNFGP 121
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4835-4958 1.34e-11

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 67.68  E-value: 1.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4835 IFKYIMNIDWRYQVWKAGVT---FTDNAFLYSLWYFSFSVMG------------NFNNFFFAAHLLDVAVGFKTLRTILQ 4899
Cdd:pfam00520   41 VFTGIFTLEMLLKIIAAGFKkryFRSPWNILDFVVVLPSLISlvlssvgslsglRVLRLLRLLRLLRLIRRLEGLRTLVN 120

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4900 SVTHNGKQLVLTVMLLTIIVYIYTVIAFNFFR-KFYIQEEDEEVDKKCHDMLTCFVFHLY 4958
Cdd:pfam00520  121 SLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGgKLKTWENPDNGRTNFDNFPNAFLWLFQ 180
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
270-305 2.06e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.94  E-value: 2.06e-04
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 17352467     270 GGFINWYHPMRIRHITTGRYLGVNDSNELILVKKEE 305
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQ 36
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
155-200 4.09e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.17  E-value: 4.09e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 17352467     155 GEKVRVGDDLILVSVATERYLHTTKENEQSIVNASFHVT-----------HWSVQPY 200
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 ...
 54-196 8.39e-04

MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate receptor Itr-1 and similar proteins; Itr-1, also called IP3 receptor, or IP3R, or InsP3R, or LET-23 fertility effector 1, is a receptor for inositol 1,4,5-trisphosphate, a second messenger that regulates intracellular calcium homeostasis. It binds in vitro to both inositol 1,4,5-trisphosphate (1,4,5-InsP3) and inositol 2,4,5-trisphosphate (2,4,5-InsP3) with high affinity. It can also bind inositol 1,3,4,5-tetrakisphosphate (1,3,4,5-InsP4) and inositol 4,5-bisphosphate (4,5-InsP2), but with lower affinity. Itr-1 acts as a timekeeper/rhythm generator via calcium signaling, affecting the defecation cycle and pharyngeal pumping. It affects normal hermaphrodite and male fertility as a participant in intracellular signaling by acting downstream of let-23/lin-3 which regulates ovulation, spermathecal valve dilation and male mating behavior. It plays an important role in early embryonic development. It controls epidermal cell migration and may also regulate filopodial protrusive activity during epithelial morphogenesis. Itr-1 functions as a component of inositol trisphosphate (IP3)-mediated downstream signaling pathways that controls amphid sensory neuronal (ASH)-mediated response to nose touch and benzaldehyde, but no other ASH-mediated responses. Itr-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467751 [Multi-domain]  Cd Length: 199  Bit Score: 43.91  E-value: 8.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   54 NVPPDLSQCVFVIEQAlsvralqelvtaagsetgKGTGSGHrTLLYGNAILLRHHNSDMYLAclstsSSNDKLSFDVGLQ 133
Cdd:cd23280   54 LFPPTSGDTFWQIEKE------------------DTPLKGG-VIKWGDQCRLRHLPTGKYLA-----VDDKTGNGKVVLT 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17352467  134 EHSQGEACWWTVHPASKQRSEGekVRVGDDLILVSVATERYLHTTKENEQSIVNASFHVTHWS 196
Cdd:cd23280  110 SDPSDPSTVFRLHPVTKETSEE--VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGLSWD 170
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 215-395 1.17e-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: 341.98  E-value: 1.17e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  215 GGDVLRFFHGG-DECLTIPSTWGREAGQNIVIYEGGVVMAQARSLWRLELARTKWTGGFINWYHPMRIRHITTGRYLGVN 293
Cdd:cd23278    1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  294 DSNELILVKKEEASIATTTFCLRQEKDDeKKVLEDKDLEVIGSPIIKYGDTTVIVQHCETSLWLSYKSYETKKKgVGKVE 373
Cdd:cd23278   81 EDRGLVLVPKEKADVKATAFCFRQSKDD-KKVLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVETKKR-VGGVE 158

                        170       180
                 ....*....|....*....|..
gi 17352467  374 EKQAILHEEGKMDDCLDFSRSQ 395
Cdd:cd23278  159 ERKAILHAEGHMDDGLSLSRAQ 180
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 12-206 5.45e-84

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: 275.53  E-value: 5.45e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467     12 DVSFLRTEDMVTLSCTATGeRVCLAAEGFGNRHCFLENIAD-KNVPP-DLSQCVFVIEQALSVRALQELVTAA-GSETGK 88
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESV-NGFISALGLGNDRCFVENKAGdLNDPPkKFRDCVFKICPANSYAAQKELWSAGnRSPNGN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467     89 G---------TGSGHRTLLYGNAILLRHHNSDMYLACLSTS-SSNDKLSFDVGLQEHSQGEACWWTVHPASKQRSEGEKV 158
Cdd:pfam08709   80 SltdalkhasNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSpSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDNV 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17352467    159 RVGDDLILVSVATERYLHTT-----KENEQSIVNASFHVTHWSVQPYGTGISR 206
Cdd:pfam08709  160 CVGDEVILVPVSAPIFLHTTssselRDNPGKEVNASFGQTSWKMEPFMSGCEN 212
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 647-799 1.83e-80

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


Pssm-ID: 240457  Cd Length: 151  Bit Score: 262.63  E-value: 1.83e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  647 SIRPNIFVGRVDGSSMYQKWYFEVTMDHIEQTTHMMPHLRIGWANTSGYVPYPGGGKKWGGNGVGDDLYSFGFDGAFLWT 726
Cdd:cd12877    1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTHQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLWT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17352467  727 GGRKTLVVDalPEEPFIRKGDVIGVAIDLSVPIITFTFNGVKVRGSFRDFNLDGMFFPVMSCSSKLSCRFLFG 799
Cdd:cd12877   81 GGRSRRVTS--GTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 443-641 3.66e-80

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


Pssm-ID: 460175  Cd Length: 199  Bit Score: 264.06  E-value: 3.66e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    443 CLEDLINYFSQPEDDMEHEEKQNR---FRALRNRQDLFQEEGVLNLILEAIDKINIITSQGFLASFLAGDETGQSWDLIS 519
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKlmnNKPLRQRQNLMREQGVLETVMEVIDLLGAPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    520 TYLYQLLAAIIKGNHTNCAQFANSnrLNWLFSRLGSQASSEGSgmLDVLHCVLIDSPE-ALNMMRDEHIKVIISLLEKHG 598
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKH--LDWLQSQLGSPSLAEGT--LDVLTALLMDNPElLLNYIKECHIKSFISLLRKHG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 17352467    599 RDPKVLDVLCSLCVGNGVAVRSSQNNICDFLLPGKNLLLQTLL 641
Cdd:pfam01365  157 RDPRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1518-1669 5.05e-78

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


Pssm-ID: 293937  Cd Length: 151  Bit Score: 255.69  E-value: 5.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1518 DEMFDAECLKLINEYFYGVRIFPGQDPTHVYVGWVTTQYHLHSREFNKNKVRRGSVYIEDDYEMAIERIDRQSCYVVRAD 1597
Cdd:cd12879    1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17352467 1598 ELFNEVTQDaSGKGASQGMFVGCFVDTATGIIRFTCEGKDTSHRWMMEPDTKLFPAIFVEATSKEILQIELG 1669
Cdd:cd12879   81 ELLAEVGQD-SSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1079-1213 4.95e-77

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: 252.22  E-value: 4.95e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1079 RTYRVERNYAVTSGKWYFEFEVLTSGPMRVGWARADCYPGAMLGSEDTSWAFDGHNVTKMHAGSiEHFGVRYEAGDVIGC 1158
Cdd:cd12878    1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGS-ESFGKQWQPGDVVGC 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17352467 1159 FIDVKEQTISFSLNGELLMDALGGETTFADVTAeGVGFVPACTLGVGQKARLIYG 1213
Cdd:cd12878   80 MLDLVDRTISFTLNGELLIDSSGSEVAFKDIEI-GEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2214-2443 2.01e-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: 2.01e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2214 QIRALLPVQMSQEEEELMRKRLWKLVNNATFFQHPDLIRILRVHENVMAVmMNTLGRRAQAQSDAPTqsevaegAPSKEK 2293
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEV-IDLLGAPFTGALLFAE-------DLGEEK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2294 DTS-HEMVVACCRFLCYFCRTGRQNQKAMFDHFDFLLDNanilLARPSLRGSTpLDVAYSSLMENTELALalrehyleki 2372
Cdd:pfam01365   73 NAPwKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL---------- 137

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17352467   2373 aVYLSRCGLQSNSELVEKGYPDlgwdpvegERYLDFLRY-CVwVNGESVEENANLVIRLLIRRPECLGPALR 2443
Cdd:pfam01365  138 -NYIKECHIKSFISLLRKHGRD--------PRYLDFLSDlCV-CNGEAVRENQNLICRLLLPNPDLLLQTLL 199
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4505-4747 4.20e-68

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: 232.67  E-value: 4.20e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4505 TVQAFGlDINKEENGMYKVVVHESPA---NSSMEEGGESSP-------EDGAAASGELVEGEPHQEPISIVDLLGGEAAK 4574
Cdd:pfam06459   44 LSDIFG-LILKKEGGQYKVVPHDPEAglgDLSETTAEEPPPllkrklqESEEAEDEEEEEEEPKPEPIEKADGENGEKEE 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4575 KA--------AQERQEAQKAQEAAMASIEAEAKKSSSAPQEtpavhqiDFSQYTHRAVSFLARNFYNLKYVALVLAFSIN 4646
Cdd:pfam06459  123 KPkeeeteseAPEEEEMKKKQRKRHSKKKEEPEAQGSAFWN-------ELEVYQTKLLNYLARNFYNLRFLALFVAFAIN 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4647 FMLLFYKVTSFTEEADSSAEEELILGSGSGGGADitgsgfggsgdggsGDGEMEDEIPELVHVDEDFFYMEHVLRIAACL 4726
Cdd:pfam06459  196 FILLFYKVSTSPPDEEEEEGSGWGDSGSGSGGGS--------------GEDEEEEEGPVYFVLEESTGYMEPTLRFLAIL 261

                          250       260
                   ....*....|....*....|.
gi 17352467   4727 HSLVSLAMLIAYYHLKVPLAI 4747
Cdd:pfam06459  262 HTIISFLCIIGYYCLKVPLVI 282
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 211-392 8.84e-64

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: 216.46  E-value: 8.84e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    211 GYVFGGDVLRFFHGG-DECLTIPSTWGREAGQNIVIYEGGVVMAQARSLWRLELART-KWTGGFINWYHPMRIRHITTGR 288
Cdd:pfam02815    1 GYLKGGDVVRLFHSHqDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    289 YLGVNDSNELILVKKEEASIATTTFCLRQEK--DDEKKVLEDKDLEVIGSPIIKYGDTTVIVQHCETSLWLSYKSYETKK 366
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFPgdNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....*.
gi 17352467    367 KGVGKvEEKQAILHEEGKMDDCLDFS 392
Cdd:pfam02815  161 WGFGP-EQQKVTCAKEGHMDDALTLP 185
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 211-399 5.97e-57

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: 197.03  E-value: 5.97e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  211 GYVFGGDVLRFFHGG-DECLTIPSTwGREAGQNIVIYEGGVVMAQARSLWRLELARTKWTGGFINWYHPMRIRHITTGRY 289
Cdd:cd23290    6 GYVTGGHVLRLFHGHmDECLTISAA-DSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  290 LGVNDSNELILVKKEEASIATTTFCLRQEKdDEKKVLEDKDLEVIGSPIIKYGDTTVIVQHCETSLWLSYKSYETKKKGV 369
Cdd:cd23290   85 LALTEDQGLVVVDACKAHTKATSFCFRVSK-EKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRL 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 17352467  370 GKVEEKqAILHEEGKMDDCLDFSRSQEEES 399
Cdd:cd23290  164 GVLKKK-AILHQEGHMDDALFLTRCQQEES 192
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 211-399 1.84e-55

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: 192.82  E-value: 1.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  211 GYVFGGDVLRFFHGGDECLTIPSTWGREAGQNIVIYEGGVVMAQARSLWRLELARTKWTGGFINWYHPMRIRHITTGRYL 290
Cdd:cd23292    1 GYLLGGHVVRLFHGHDECLTIPSTDQSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  291 GVNDSNELILVKKEEASIATTTFCLRQEKDDEKKVLEdKDLEVIGSPIIKYGDTTVIVQHCETSLWLSYKSYETKKKGVG 370
Cdd:cd23292   81 ALTEDQGLILQDRAKSDTKSTAFCFRASKEKLESGPK-RDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSRLG 159

                        170       180
                 ....*....|....*....|....*....
gi 17352467  371 KVEEKqAILHEEGKMDDCLDFSRSQEEES 399
Cdd:cd23292  160 PLKRR-AILHQEGHMDDGLTLQRCQHEES 187
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 215-399 4.63e-50

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: 177.16  E-value: 4.63e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  215 GGDVLRFFHGG-DECLTIPSTWGREAGQNIVIYEGGVVMAQARSLWRLELARTKWTGGFINWYHPMRIRHITTGRYLGVN 293
Cdd:cd23291    1 GGDVLRLLHGHmDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  294 DSNELILVKKEEASIATTTFCLRQEKdDEKKVLEDKDLEVIGSPIIKYGDTTVIVQHCETSLWLSYKSYETKKKGVGKVE 373
Cdd:cd23291   81 EDKNLLLMDKEKADVKSTAFTFRSSK-EKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSIQ 159

                        170       180
                 ....*....|....*....|....*.
gi 17352467  374 EKqAILHEEGKMDDCLDFSRSQEEES 399
Cdd:cd23291  160 RK-AIMHHEGHMDDGLNLSRSQHEES 184
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2817-2906 1.13e-41

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 149.19  E-value: 1.13e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2817 YMPNPIDTNNVHLDNDLNSLVQKFSEHYHDAWASRRLEGGWTYGDIRSDNDRKHPRLKPYNMLSEYERERYRDPVRECLK 2896
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 17352467   2897 GLLAIGWTVE 2906
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 967-1056 2.39e-41

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 148.42  E-value: 2.39e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    967 YKPAPLDLSAVTLTPKLEELVDQLAENTHNLWARERIQQGWTYGLNEDSENHRSPHLVPYAKVDEAIKKANRDTASETVR 1046
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 17352467   1047 TLLVYGYVLD 1056
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 854-943 8.76e-41

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 146.88  E-value: 8.76e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    854 FVPKPVDTTGVTLPSSVDQIKEKLAENIHEMWALNKIEAGWSWGEHRDDYHRIHPCLTHFEKLPAAEKRYDNQLAVQTLK 933
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 17352467    934 TIISLGYYIT 943
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3992-4109 1.82e-36

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: 134.58  E-value: 1.82e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   3992 HDAEFTCALFRFIQLTCEGHNLEWQNYLRTQAGNTTTVNVVICTVDYLLRLQESImdfywhysskeiidpagkanFFKAI 4071
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSI--------------------NEKNI 60

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 17352467   4072 EVASQVFNTLTEVIQGPCTLNQQALAHSRLWDAVGGFL 4109
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1091-1215 1.76e-33

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 127.03  E-value: 1.76e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    1091 SGKWYFEFEVLTSGPMRVGWARADCYPG--AMLGSEDTSWAFDGHNVTKMHAGSIEHFGVRY-EAGDVIGCFIDVKEQTI 1167
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGyfALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLqEPGDVIGCFLDLEAGTI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 17352467    1168 SFSLNGELLMdalggETTFADVTAEGvGFVPACTLGVGQKARLIYGQD 1215
Cdd:smart00449   81 SFYKNGKYLH-----GLAFFDVKFSG-PLYPAFSLGSGNSVRLNFGPL 122
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2940-3022 4.26e-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: 124.92  E-value: 4.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   2940 YNPHPVDMSNLTLSREMQNMAERLAENSHDIWAKKKNEELNGCGGV------IHPQLVPYDLLTDKEKKKDRERSQEFLK 3013
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 17352467   3014 YMQYQGYKL 3022
Cdd:pfam02026   81 TLLALGYTI 89
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1093-1215 5.59e-30

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: 117.06  E-value: 5.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   1093 KWYFEFEVL--TSGPMRVGWARADC--YPGAMLGSEDTSWAFDGHNVTKMHAGSIEHFGV-RYEAGDVIGCFIDVKEQTI 1167
Cdd:pfam00622    1 RHYFEVEIFgqDGGGWRVGWATKSVprKGERFLGDESGSWGYDGWTGKKYWASTSPLTGLpLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 17352467   1168 SFSLNGELLMdalggeTTFADVTAEGvGFVPACTLGVGQKARLIYGQD 1215
Cdd:pfam00622   81 SFTKNGKSLG------YAFRDVPFAG-PLFPAVSLGAGEGLKFNFGLR 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1092-1211 2.49e-29

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


Pssm-ID: 293931  Cd Length: 118  Bit Score: 115.22  E-value: 2.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1092 GKWYFEFEVLT--SGPMRVGWARADC--YPGAMLGSEDTSWAFDGHNVTKMHAGSIEHFGVRYEAGDVIGCFIDVKEQTI 1167
Cdd:cd11709    1 GKWYWEVRVDSgnGGLIQVGWATKSFslDGEGGVGDDEESWGYDGSRLRKGHGGSSGPGGRPWKSGDVVGCLLDLDEGTL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 17352467 1168 SFSLNGELLMDAlggettFADVTAEGVGFVPACTLGVGQKARLI 1211
Cdd:cd11709   81 SFSLNGKDLGVA------FTNLFLKGGGLYPAVSLGSGQGVTIN 118
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 665-801 5.09e-28

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 111.67  E-value: 5.09e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    665 KWYFEVTMDHIEQTthmmpHLRIGWAntsgYVPYPGGGKKWGGngvgDDLYSFGFDGaflWTGGRKTLVVDALPEEPFIR 744
Cdd:pfam00622    1 RHYFEVEIFGQDGG-----GWRVGWA----TKSVPRKGERFLG----DESGSWGYDG---WTGKKYWASTSPLTGLPLFE 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 17352467    745 KGDVIGVAIDLSVPIITFTFNGVKVRGSFRDFNLDGMFFPVMSCSSKLSCRFLFGGD 801
Cdd:pfam00622   65 PGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 665-801 1.05e-21

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: 93.51  E-value: 1.05e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467     665 KWYFEVTmdhIEQTTHMmphlRIGWANTSGYVPYpgggkkwgGNGVGDDLYSFGFDG--AFLWTGGRKTLVVDALPEepf 742
Cdd:smart00449    3 RHYFEVE---IGDGGHW----RVGVATKSVPRGY--------FALLGEDKGSWGYDGdgGKKYHNSTGPEYGLPLQE--- 64

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467     743 irKGDVIGVAIDLSVPIITFTFNGVKVRG-SFRDFNLDGMFFPVMSCSSKLSCRFLFGGD 801
Cdd:smart00449   65 --PGDVIGCFLDLEAGTISFYKNGKYLHGlAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 1086-1213 8.04e-20

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: 88.54  E-value: 8.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1086 NYAVTSGKWYFEFEVLTSGPMRVGWARADCYPGAMLGSEDT--SWAFDGHNVTKMHAGSIEhFGVRYEAGDVIGCFIDVK 1163
Cdd:cd12882    5 NACVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDTrdSYAYDGNRVRKWNVSTQK-YGEPWVAGDVIGCCIDLD 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17352467 1164 EQTISFSLNGEllmdALGgeTTFADVTA-EGVGFVPACTLGVGQKARLIYG 1213
Cdd:cd12882   84 KGTISFYRNGR----SLG--VAFDNVRRgPGLAYFPAVSLSFGERLELNFG 128
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1532-1671 1.19e-19

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: 87.78  E-value: 1.19e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   1532 YFYGVRIFpGQDPTHVYVGWVTTQYHLHSREFnknkvrrgsvyIEDDYEMaierIDRQSCYVVRadelFNEVTQDASGKG 1611
Cdd:pfam00622    2 HYFEVEIF-GQDGGGWRVGWATKSVPRKGERF-----------LGDESGS----WGYDGWTGKK----YWASTSPLTGLP 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17352467   1612 -ASQGMFVGCFVDTATGIIRFTCEGKDTSHRWMMEPDT-KLFPAIFVeaTSKEILQIELGRT 1671
Cdd:pfam00622   62 lFEPGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSL--GAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1530-1670 1.28e-18

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: 84.65  E-value: 1.28e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467    1530 NEYFYGVRIFpgqDPTHVYVGWVTTQYHLHsrefnknkvrRGSVYIEDDYEMAIERIDRQSCYVVRADELFNEVTQdasg 1609
Cdd:smart00449    2 GRHYFEVEIG---DGGHWRVGVATKSVPRG----------YFALLGEDKGSWGYDGDGGKKYHNSTGPEYGLPLQE---- 64

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17352467    1610 kgasQGMFVGCFVDTATGIIRFTCEGKDTSHR--WMMEPDTKLFPAIFVEatSKEILQIELGR 1670
Cdd:smart00449   65 ----PGDVIGCFLDLEAGTISFYKNGKYLHGLafFDVKFSGPLYPAFSLG--SGNSVRLNFGP 121
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 1076-1202 4.92e-17

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: 81.47  E-value: 4.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1076 AGFRTyrverNYAVT-SGKWYFEFEVLTSGPMRVGWARADCYPGamLGSEDTSWAFDGHNvTKMHAGSIEHFGVRYEAGD 1154
Cdd:cd12873   28 QGCRA-----TKGVKgKGKYYYEVTVTDEGLCRVGWSTEDASLD--LGTDKFGFGYGGTG-KKSHGRQFDDYGEPFGLGD 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 17352467 1155 VIGCFIDVKEQTISFSLNGELLMDALggettFADVTAEGVGFVPACTL 1202
Cdd:cd12873  100 VIGCYLDLDNGTISFSKNGKDLGKAF-----DIPPHLRNSALFPAVCL 142
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 1072-1213 7.03e-16

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: 77.94  E-value: 7.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1072 RLKFAGFRTYRVER-NYAVTSGKWYFEFEVLTSGPM-----RVGWARADCYPGAMLGSEDTSWAFDGHNVTKMHAGSIEH 1145
Cdd:cd12872    7 RLTVTGEKGYRMARaNHGVREGKWYFEVKILEGGGTetghvRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFHQSRGKP 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17352467 1146 FGV-RYEAGDVIGCFIDVKEqtISFSLNGELLMdalggeTTFADVTAEGvGFVPACTLGVGQKARLIYG 1213
Cdd:cd12872   87 YGEpGFKEGDVIGFLITLPK--IEFFKNGKSQG------VAFEDIYGTG-GYYPAVSLYKGATVTINFG 146
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 1052-1176 2.04e-15

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: 77.24  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1052 GYVLDPPTGEGtEALLaeaqrlkFAGFRTyrverNYAVTSGKWYFEFEVLTSGPM-------------RVGWARADCYPg 1118
Cdd:cd12884   18 RYSASPLTDEG-FAYL-------WAGARA-----TYGVTKGKVCFEVKVTENLPVkhlpteetdphvvRVGWSVDSSSL- 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1119 aMLGSEDTSWAFDGhNVTKMHAGSIEHFGVRYEAGDVIGCFIDV--KEQTISFSLNGELL 1176
Cdd:cd12884   84 -QLGEEEFSYGYGS-TGKKSTNCKFEDYGEPFGENDVIGCYLDFesEPVEISFSKNGKDL 141
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 1092-1213 3.24e-15

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: 75.08  E-value: 3.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1092 GKWYFEFEVLTSGPMRVGWARADC----YPGAMLGSEDTSWAFDG------HNvtkmhAGSIEHFGVRYEAGDVIGCFID 1161
Cdd:cd12883    1 GVWYYEVTVLTSGVMQIGWATKDSkflnHEGYGIGDDEYSCAYDGcrqliwYN-----AKSKPHTHPRWKPGDVLGCLLD 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17352467 1162 VKEQTISFSLNGELLMDAlggETTFADVTAegvGFVPACTLGVGQKARLIYG 1213
Cdd:cd12883   76 LNKKQMIFSLNGNRLPPE---RQVFTSAKS---GFFAAASFMSFQQCEFNFG 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 665-797 1.14e-12

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: 67.46  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  665 KWYFEVTMDHIEqtthmMPHLRIGWAnTSGYVPYPGGGKKwggngvgDDLYSFGFDGA--FLWTGGRKTLVVDALpeepf 742
Cdd:cd11709    2 KWYWEVRVDSGN-----GGLIQVGWA-TKSFSLDGEGGVG-------DDEESWGYDGSrlRKGHGGSSGPGGRPW----- 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 17352467  743 iRKGDVIGVAIDLSVPIITFTFNGVKVRGSFRDFNLDGM-FFPVMSCSSKLSCRFL 797
Cdd:cd11709   64 -KSGDVVGCLLDLDEGTLSFSLNGKDLGVAFTNLFLKGGgLYPAVSLGSGQGVTIN 118
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 1089-1176 1.69e-12

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: 67.69  E-value: 1.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1089 VTSGKWYFEFEVL---TSGPMRVGWARADCYPGAMLGSEDTSWAFDGHNVTKMHAGS-IEHFGVRYEAGDVIGCFIDVKE 1164
Cdd:cd12885   11 PKVPVFYFEVTILdlgEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGeGENYGPPFGTGDVVGCGINFKT 90

                         90
                 ....*....|..
gi 17352467 1165 QTISFSLNGELL 1176
Cdd:cd12885   91 GEVFFTKNGELL 102
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 1093-1213 3.66e-12

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: 67.34  E-value: 3.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1093 KWYFEFEVL-----TSGP--MRVGWARAD---CYPGA-------MLGSEDTSWAFDGHNvtkMHAG----SIEHFGVRY- 1150
Cdd:cd12877   19 KWYFEVEVDhveqfTHQPahLRVGWANTSgyvPYPGGgegwggnGVGDDLYSYGFDGLH---LWTGgrsrRVTSGTQHLl 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17352467 1151 EAGDVIGCFIDVKEQTISFSLNGELLmdalggETTFADVTAEGvGFVPACTLGVGQKARLIYG 1213
Cdd:cd12877   96 KKGDVVGCCLDLSVPSISFRVNGRPV------QGMFENFNLDG-MFFPVMSFSAGVSCRFLLG 151
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4835-4958 1.34e-11

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 67.68  E-value: 1.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4835 IFKYIMNIDWRYQVWKAGVT---FTDNAFLYSLWYFSFSVMG------------NFNNFFFAAHLLDVAVGFKTLRTILQ 4899
Cdd:pfam00520   41 VFTGIFTLEMLLKIIAAGFKkryFRSPWNILDFVVVLPSLISlvlssvgslsglRVLRLLRLLRLLRLIRRLEGLRTLVN 120

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   4900 SVTHNGKQLVLTVMLLTIIVYIYTVIAFNFFR-KFYIQEEDEEVDKKCHDMLTCFVFHLY 4958
Cdd:pfam00520  121 SLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGgKLKTWENPDNGRTNFDNFPNAFLWLFQ 180
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 255-388 1.10e-10

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: 64.33  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  255 ARSLWRLELARTKWTGGFINWYHPMRIRHITTGRYLGVND---SNELILVKKEeaSIATTTFCLRQekddekkVLEDKDL 331
Cdd:cd23280   60 GDTFWQIEKEDTPLKGGVIKWGDQCRLRHLPTGKYLAVDDktgNGKVVLTSDP--SDPSTVFRLHP-------VTKETSE 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17352467  332 EvigspiIKYGDTTVIvQHCETSLWLS--YKSYETKKKGVGKVEEKQA------ILHEEGKMDDC 388
Cdd:cd23280  131 E------VKFGSYVRI-EHVATGTWLHaeTDEELRRSKKSPAGLSWDGaklrkvSLSLERQDDDA 188
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 666-799 2.74e-09

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: 58.13  E-value: 2.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  666 WYFEVTMdhieQTTHMMphlRIGWA-------NTSGYvpypgggkkwggnGVGDDLYSFGFDGAflwtggRKTLVVDALP 738
Cdd:cd12883    3 WYYEVTV----LTSGVM---QIGWAtkdskflNHEGY-------------GIGDDEYSCAYDGC------RQLIWYNAKS 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17352467  739 EE---PFIRKGDVIGVAIDLSVPIITFTFNGVKVRGSFRDFNL--DGmFFPVMSCSSKLSCRFLFG 799
Cdd:cd12883   57 KPhthPRWKPGDVLGCLLDLNKKQMIFSLNGNRLPPERQVFTSakSG-FFAAASFMSFQQCEFNFG 121
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 665-801 7.33e-09

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


Pssm-ID: 293932  Cd Length: 150  Bit Score: 57.53  E-value: 7.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  665 KWYFEVTMDhiEQTTHMMPHLRIGW----ANTSGYVPYpgggkkwggngvgdDLYSFGF-DgaflwTGGRKtlVVDALPE 739
Cdd:cd12872   29 KWYFEVKIL--EGGGTETGHVRVGWsrreASLQAPVGY--------------DKYSYAIrD-----KDGSK--FHQSRGK 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17352467  740 ---EPFIRKGDVIGVAIDLsvPIITFTFNGVKVRGSFRDFNLDGMFFPVMSCSSKLSCRFLFGGD 801
Cdd:cd12872   86 pygEPGFKEGDVIGFLITL--PKIEFFKNGKSQGVAFEDIYGTGGYYPAVSLYKGATVTINFGPD 148
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 659-799 6.80e-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: 54.23  E-value: 6.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  659 GSSMYQ----KWYFEVTMdhieQTTHMMphlRIGWANTSGYVPYPGGGkkwggngvgDDLySFGFDG--AFLWTGGrktl 732
Cdd:cd12878    5 AEKTYAvtsgKWYFEFEV----LTSGYM---RVGWARPGFRPDLELGS---------DDL-SYAFDGflARKWHQG---- 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17352467  733 vvdalpEEPF---IRKGDVIGVAIDLSVPIITFTFNGVKVRGS------FRDFNLDGMFFPVMSCSSKLSCRFLFG 799
Cdd:cd12878   64 ------SESFgkqWQPGDVVGCMLDLVDRTISFTLNGELLIDSsgsevaFKDIEIGEGFVPACSLGVGQKGRLNLG 133
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 1092-1203 1.83e-07

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: 52.89  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1092 GKWYFEFEVLTSGP---MRVGWARAD-CYPGAMLGSEDTSWAFDGHN---VTKMHAGSIEHFGVRYEAGDVIGCFIDVKE 1164
Cdd:cd12886    1 GKWYWEVTVVSSAAstyAGIGVANAAaTGNNGLNGIELSSIGYSLGVysgNKLSNGSSVATYGAGFTAGDVIGVALDLDA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 17352467 1165 QTISFSLNGELLmdaLGGETTFADVTAEGVG-FVPACTLG 1203
Cdd:cd12886   81 GKIWFYKNGVWQ---GGGDPAPGTNPAFAGTaMYPAVTGG 117
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
 1108-1202 3.16e-06

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


Pssm-ID: 293947  Cd Length: 172  Bit Score: 50.70  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1108 VGWARADCYPGAMLGSEDTSWA--FDGHNVTKMHAGsiEHFGvRYE----AGDVIGCFIDVKEQTISFSLNGEllmdaLG 1181
Cdd:cd12889   68 FGVARIDVNKDKMLGKDDKGWSmyIDNNRSWFLHNN--EHSN-RTEggitVGSVVGVLLDLDRHTLSFYVNDE-----PQ 139

                         90       100
                 ....*....|....*....|.
gi 17352467 1182 GETTFADVtaEGVgFVPACTL 1202
Cdd:cd12889  140 GPIAFRNL--PGV-FYPAVSL 157
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 1091-1176 2.38e-05

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: 47.52  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1091 SGKWYFEFEVL---TSGPMRVGWARADCYPGAMLGSEDTSWAF---DGHNVTKMHAGSieHFGVRYEAGDVIGCFIDVKE 1164
Cdd:cd12909   24 CGIYYFEVKIIskgRDGYIGIGFSTKDVNLNRLPGWEPHSWGYhgdDGHSFCSSGTGK--PYGPTFTTGDVIGCGINFRD 101

                         90
                 ....*....|..
gi 17352467 1165 QTISFSLNGELL 1176
Cdd:cd12909  102 NTAFYTKNGVNL 113
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 216-389 4.59e-05

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: 47.38  E-value: 4.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  216 GDVLRFFHGG-DECLTIPS-TWGREAGQNIVIYEGGVVMAQARSLWRLELARTKWtGGFINWYHPMRIRHITTGRYLGVN 293
Cdd:cd23263    1 GDVIWLKHSEtGKYLHSHRkNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  294 DSnelilvKKEEASIATTTFCLRQEKD--DEKKVLEDKDLEVIGSPIIKygDTTVIVQHCETSLWLSYKSYETKKKGVGK 371
Cdd:cd23263   80 EG------KKSPKSNHQEVLCLTDNPDksSLFKFEPIGSTKYKQKYVKK--DSYFRLKHVNTNFWLHSHEKKFNINNKTQ 151

                        170
                 ....*....|....*...
gi 17352467  372 VEekqAILHEEGKMDDCL 389
Cdd:cd23263  152 QE---VICHGEREEVFKL 166
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
 1088-1169 1.08e-04

PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67, TRIM76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67 and TRIM76. TRIM1 (also known as MID2) and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. Their coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in TRIM18 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects. TRIM9 is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. Its immunoreactivity is severely decreased in affected brain areas in Parkinson's disease and dementia with Lewy bodies, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM36 interacts with centromere protein-H, one of the kinetochore proteins and possibly associates with chromosome segregation; an excess of TRIM36 may cause chromosomal instability. TRIM46 has not yet been characterized. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It is possibly involved in protein kinase A signaling as well as vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293969 [Multi-domain]  Cd Length: 166  Bit Score: 46.12  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467 1088 AVTSGKWYFEFEVLTSGPMRVGWARADCYPGAMLGSEDTSWAF--DGHNVTKMHAGSIEHFGVRYEaGDVIGCFIDVKEQ 1165
Cdd:cd13734   50 AISSGRHYWEVSVSRSTSYRVGVAYKSAPRDEDLGKNSTSWCLsrDNNRYTARHDGKVVDLRVTGH-PARIGVLLDYDNG 128


                 ....
gi 17352467 1166 TISF 1169
Cdd:cd13734  129 TLSF 132
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
270-305 2.06e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.94  E-value: 2.06e-04
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 17352467     270 GGFINWYHPMRIRHITTGRYLGVNDSNELILVKKEE 305
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQ 36
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
155-200 4.09e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.17  E-value: 4.09e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 17352467     155 GEKVRVGDDLILVSVATERYLHTTKENEQSIVNASFHVT-----------HWSVQPY 200
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 ...
 54-196 8.39e-04

MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate receptor Itr-1 and similar proteins; Itr-1, also called IP3 receptor, or IP3R, or InsP3R, or LET-23 fertility effector 1, is a receptor for inositol 1,4,5-trisphosphate, a second messenger that regulates intracellular calcium homeostasis. It binds in vitro to both inositol 1,4,5-trisphosphate (1,4,5-InsP3) and inositol 2,4,5-trisphosphate (2,4,5-InsP3) with high affinity. It can also bind inositol 1,3,4,5-tetrakisphosphate (1,3,4,5-InsP4) and inositol 4,5-bisphosphate (4,5-InsP2), but with lower affinity. Itr-1 acts as a timekeeper/rhythm generator via calcium signaling, affecting the defecation cycle and pharyngeal pumping. It affects normal hermaphrodite and male fertility as a participant in intracellular signaling by acting downstream of let-23/lin-3 which regulates ovulation, spermathecal valve dilation and male mating behavior. It plays an important role in early embryonic development. It controls epidermal cell migration and may also regulate filopodial protrusive activity during epithelial morphogenesis. Itr-1 functions as a component of inositol trisphosphate (IP3)-mediated downstream signaling pathways that controls amphid sensory neuronal (ASH)-mediated response to nose touch and benzaldehyde, but no other ASH-mediated responses. Itr-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467751 [Multi-domain]  Cd Length: 199  Bit Score: 43.91  E-value: 8.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467   54 NVPPDLSQCVFVIEQAlsvralqelvtaagsetgKGTGSGHrTLLYGNAILLRHHNSDMYLAclstsSSNDKLSFDVGLQ 133
Cdd:cd23280   54 LFPPTSGDTFWQIEKE------------------DTPLKGG-VIKWGDQCRLRHLPTGKYLA-----VDDKTGNGKVVLT 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17352467  134 EHSQGEACWWTVHPASKQRSEGekVRVGDDLILVSVATERYLHTTKENEQSIVNASFHVTHWS 196
Cdd:cd23280  110 SDPSDPSTVFRLHPVTKETSEE--VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGLSWD 170
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 665-799 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 17352467  665 KWYFEVTMdhieQTTHMMphlRIGWANTSgyVPYpgggkkWGGNGVGDDLYSFGFDGAflwtgGRKTLVVDALPEEPFIR 744
Cdd:cd12882   12 KWMYEVTL----GTKGIM---QIGWATIS--CRF------TQEEGVGDTRDSYAYDGN-----RVRKWNVSTQKYGEPWV 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17352467  745 KGDVIGVAIDLSVPIITFTFNGVKVRGSFRDFN-LDGM-FFPVMSCSSKLSCRFLFG 799
Cdd:cd12882   72 AGDVIGCCIDLDKGTISFYRNGRSLGVAFDNVRrGPGLaYFPAVSLSFGERLELNFG 128
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 643-791 3.95e-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: 40.73  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17352467  643 DHVASIRPNIFvgrvdgssmyqkwYFEVTMDHIEQTthmmPHLRIGWAnTSGYvpypgggkkWGGNGVGDDLYSFGF--- 719
Cdd:cd12885    6 DHPIPPKVPVF-------------YFEVTILDLGEK----GIVSIGFC-TSGF---------PLNRMPGWEDGSYGYhgd 58

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17352467  720 DGAFLWTGGRKTLvvdalPEEPFiRKGDVIGVAIDLSVPIITFTFNGVKVrGSFRDFNLDGMFFPVMSCSSK 791
Cdd:cd12885   59 DGRVYLGGGEGEN-----YGPPF-GTGDVVGCGINFKTGEVFFTKNGELL-GTAFENVVKGRLYPTVGLGSP 123
 
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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