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Conserved domains on  [gi|2462545459|ref|XP_054234573|]
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ryanodine receptor 3 isoform X14 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 216-405 3.71e-132

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: 412.38  E-value: 3.71e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  216 GYLLGGHVVRLFHGHDECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYL 295
Cdd:cd23292      1 GYLLGGHVVRLFHGHDECLTIPSTDQSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHYL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  296 ALTEDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKTSR 375
Cdd:cd23292     81 ALTEDQGLILQDRAKSDTKSTAFCFRAS---KEKLESGPKRDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSR 157

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462545459  376 LGPLKRKVILHQEGHMDDGLTLQRCQREES 405
Cdd:cd23292    158 LGPLKRRAILHQEGHMDDGLTLQRCQHEES 187
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 641-792 2.43e-85

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: 276.50  E-value: 2.43e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  641 SIRPNIFLGVAEGSAQYKKWYFELIIDQVDPFlTAEPTHLRVGWASSSGYAPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 720
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545459  721 SGRIPRAVASINQHLLRSDDVVSCCLDLGVPSISFRINGQPVQGMFENFNTDGLFFPVMSFSAGVKVRFLMG 792
Cdd:cd12877     80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 442-621 4.00e-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: 263.68  E-value: 4.00e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  442 TLQDLIAYFQPPEEEMRHEDKQNKL---RSLKNRQNLFKEEGMLALVLNCIDRLN-VYNSVAHFAGIAREESGMAWKEIL 517
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  518 NLLYKLLAALIRGNRNNCAQFSNNLDWLISKLDRLESSSGILEVLHCILTESPE-ALNLIAEGHIKSIISLLDKHGRNHK 596
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180
                   ....*....|....*....|....*
gi 2462545459  597 VLDILCSLCLCNGVAVRANQNLICD 621
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICR 185
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1072-1204 1.59e-79

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: 259.15  E-value: 1.59e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1072 RFFRVERSYAVRSGKWYFEFEVVTGGDMRVGWARPGCRPDVELGADDQAFVFEGNRGQRWHQGSGYFGRTWQPGDVVGCM 1151
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462545459 1152 INLDDASMIFTLNGELLITNKGSELAFADYEIENGFVPICCLGLSQIGRMNLG 1204
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2023-2233 2.69e-75

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: 249.81  E-value: 2.69e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2023 QIRSLLSVRMGKEEELLMINGLGDIMNNKVFYQHPNLMRVLGMHETVMEVMvNVLGT-------------EKSQIAFPKM 2089
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlgEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2090 VASCCRFLCYFCRISRQNQKAMFEHLSYLLENssvgLASPSMRGSTpLDVAASSVMDNNELALsleepdlekvvTYLAGC 2169
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKEC 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545459 2170 GLQSCPMLLAKGYPDvgwnpiegERYLSFLRFAVFVNSESVEENASVVVKLLIRRPECFGPALR 2233
Cdd:pfam01365  144 HIKSFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1324-1462 1.70e-72

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: 239.90  E-value: 1.70e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1324 TTTQCYYAIRIFAGQDPSCVWVGWVTPDYHLYSEKFDLNKNCTVTVTLGDERGRVHESVKRSNCYMVWGGDIVASSQR-- 1401
Cdd:cd12879     11 LVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAGELLAEVGQds 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545459 1402 SNRSNVDLEIGCLVDLAMGMLSFSANGKELGTCYQVEPNTKVFPAVFLQPTSTSLFQFELG 1462
Cdd:cd12879     91 SGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
Ins145_P3_rec super family cl48031
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 14-212 1.68e-65

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity.


The actual alignment was detected with superfamily member pfam08709:

Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 222.37  E-value: 1.68e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459   14 FLRTEDEVVLQCIATIhkeqrKFCLAAEGLGNRLCFLEPTSEAKYIPP-DLCVCNFVLEQSLSVRALQEML--ANTGENG 90
Cdd:pfam08709    4 FLHIGDIVSLSCEESV-----NGFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWsaGNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459   91 GEGAAQGG------GHRTLLYGHAVLLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATGEACWWTIHPASKQRSEGEK 164
Cdd:pfam08709   79 NSLTDALKhasnieGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDN 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462545459  165 VRIGDDLILVSVSSERYLHLSVS-----NGNIQVDASFMQTLWNVHPTCSGSS 212
Cdd:pfam08709  159 VCVGDEVILVPVSAPIFLHTTSSselrdNPGKEVNASFGQTSWKMEPFMSGCE 211
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 849-937 6.86e-46

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 161.13  E-value: 6.86e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  849 FIPCPVDTSQVILPPHLEKIRDRLAENIHELWGMNKIELGWTFGKIRDDNKRQHPCLVEFSKLPETEKNYNLQMSTETLK 928
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 2462545459  929 TLLALGCHI 937
Cdd:pfam02026   81 TLLALGYTI 89
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2598-2687 1.69e-45

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 159.98  E-value: 1.69e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2598 FDPKPINTMNFSLPEKLEYIVTKYAEHSHDKWACDKSQSGWKYGISLDENVKTHPLIRPFKTLTEKEKEIYRWPARESLK 2677
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462545459 2678 TMLAVGWTVE 2687
Cdd:pfam02026   81 TLLALGYTIE 90
RR_TM4-6 super family cl24183
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4230-4399 1.98e-43

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


The actual alignment was detected with superfamily member pfam06459:

Pssm-ID: 461918  Cd Length: 282  Bit Score: 161.41  E-value: 1.98e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 4230 DMPDPTQFGIHDDTMEAERAEVMEPGITTELVHfIKGEKGDTDIMSDLFGLHPKKEGSLK----HGPEVGLGDLSEIIGK 4305
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLAD-AAGGEEEEDLLSDIFGLILKKEGGQYkvvpHDPEAGLGDLSETTAE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 4306 DEPPTLEstvQKKRKAQAAEMKAANEAEGKVES-EKADMEDG-EKEDKDKEEEQAEYLW-TEVTKKKKRRCGQKVEKPEA 4382
Cdd:pfam06459   80 EPPPLLK---RKLQESEEAEDEEEEEEEPKPEPiEKADGENGeKEEKPKEEETESEAPEeEEMKKKQRKRHSKKKEEPEA 156

                          170
                   ....*....|....*..
gi 2462545459 4383 FTANFFKGLEIYQTKLL 4399
Cdd:pfam06459  157 QGSAFWNELEVYQTKLL 173
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 963-1052 6.39e-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: 146.88  E-value: 6.39e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  963 YKPAPLDLSDVKLLPPQEILVDKLAENAHNVWAKDRIKQGWTYGIQQDLKNKRNPRLVPYALLDERTKKSNRDSLREAVR 1042
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462545459 1043 TFVGYGYNIE 1052
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3723-3840 2.07e-35

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: 131.49  E-value: 2.07e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 3723 QNDEFTRDLFRFLQLLCEGHNSDFQNFLRTQMGNTTTVNVIISTVDYLLRLQESISdfywyysgkdiidesgQHNFSKAl 3802
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN----------------EKNIELI- 63

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462545459 3803 avtKQIFNSLTEYIQGPCIGNQQSLAHSRLWDAVVGFL 3840
Cdd:pfam08454   64 ---IQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR super family cl03409
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2716-2795 3.27e-25

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.


The actual alignment was detected with superfamily member pfam02026:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 102.20  E-value: 3.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2716 YSPAPLDLSNVVLSRELQGMVEVVAENYHNIWAKKKKLELESKGGG------SHPLLVPYDTLTAKEKFKDREKAQDLFK 2789
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*.
gi 2462545459 2790 FLQVNG 2795
Cdd:pfam02026   81 TLLALG 86
EF-hand_7 pfam13499
EF-hand domain pair;
3924-3979 3.13e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 3.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545459 3924 FKEYDPDGKGIISKKEFQKAM---EGQKQYTQSEIDFLLSCAEADENDMFNYVDFVDRF 3979
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLrklEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 216-405 3.71e-132

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: 412.38  E-value: 3.71e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  216 GYLLGGHVVRLFHGHDECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYL 295
Cdd:cd23292      1 GYLLGGHVVRLFHGHDECLTIPSTDQSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHYL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  296 ALTEDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKTSR 375
Cdd:cd23292     81 ALTEDQGLILQDRAKSDTKSTAFCFRAS---KEKLESGPKRDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSR 157

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462545459  376 LGPLKRKVILHQEGHMDDGLTLQRCQREES 405
Cdd:cd23292    158 LGPLKRRAILHQEGHMDDGLTLQRCQHEES 187
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 641-792 2.43e-85

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: 276.50  E-value: 2.43e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  641 SIRPNIFLGVAEGSAQYKKWYFELIIDQVDPFlTAEPTHLRVGWASSSGYAPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 720
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545459  721 SGRIPRAVASINQHLLRSDDVVSCCLDLGVPSISFRINGQPVQGMFENFNTDGLFFPVMSFSAGVKVRFLMG 792
Cdd:cd12877     80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 442-621 4.00e-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: 263.68  E-value: 4.00e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  442 TLQDLIAYFQPPEEEMRHEDKQNKL---RSLKNRQNLFKEEGMLALVLNCIDRLN-VYNSVAHFAGIAREESGMAWKEIL 517
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  518 NLLYKLLAALIRGNRNNCAQFSNNLDWLISKLDRLESSSGILEVLHCILTESPE-ALNLIAEGHIKSIISLLDKHGRNHK 596
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180
                   ....*....|....*....|....*
gi 2462545459  597 VLDILCSLCLCNGVAVRANQNLICD 621
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICR 185
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1072-1204 1.59e-79

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: 259.15  E-value: 1.59e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1072 RFFRVERSYAVRSGKWYFEFEVVTGGDMRVGWARPGCRPDVELGADDQAFVFEGNRGQRWHQGSGYFGRTWQPGDVVGCM 1151
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462545459 1152 INLDDASMIFTLNGELLITNKGSELAFADYEIENGFVPICCLGLSQIGRMNLG 1204
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 216-397 7.04e-77

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: 253.83  E-value: 7.04e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  216 GYLLGGHVVRLFHGH-DECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRI-SWSGSNIRWGQAFRLRHLTTGH 293
Cdd:pfam02815    1 GYLKGGDVVRLFHSHqDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  294 YLALTEDQGLILQDRAKSDTKSTAFSFRASKELKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKT 373
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....
gi 2462545459  374 SRLGPLKRKVILHQEGHMDDGLTL 397
Cdd:pfam02815  161 WGFGPEQQKVTCAKEGHMDDALTL 184
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2023-2233 2.69e-75

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: 249.81  E-value: 2.69e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2023 QIRSLLSVRMGKEEELLMINGLGDIMNNKVFYQHPNLMRVLGMHETVMEVMvNVLGT-------------EKSQIAFPKM 2089
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlgEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2090 VASCCRFLCYFCRISRQNQKAMFEHLSYLLENssvgLASPSMRGSTpLDVAASSVMDNNELALsleepdlekvvTYLAGC 2169
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKEC 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545459 2170 GLQSCPMLLAKGYPDvgwnpiegERYLSFLRFAVFVNSESVEENASVVVKLLIRRPECFGPALR 2233
Cdd:pfam01365  144 HIKSFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1324-1462 1.70e-72

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: 239.90  E-value: 1.70e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1324 TTTQCYYAIRIFAGQDPSCVWVGWVTPDYHLYSEKFDLNKNCTVTVTLGDERGRVHESVKRSNCYMVWGGDIVASSQR-- 1401
Cdd:cd12879     11 LVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAGELLAEVGQds 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545459 1402 SNRSNVDLEIGCLVDLAMGMLSFSANGKELGTCYQVEPNTKVFPAVFLQPTSTSLFQFELG 1462
Cdd:cd12879     91 SGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 14-212 1.68e-65

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: 222.37  E-value: 1.68e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459   14 FLRTEDEVVLQCIATIhkeqrKFCLAAEGLGNRLCFLEPTSEAKYIPP-DLCVCNFVLEQSLSVRALQEML--ANTGENG 90
Cdd:pfam08709    4 FLHIGDIVSLSCEESV-----NGFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWsaGNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459   91 GEGAAQGG------GHRTLLYGHAVLLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATGEACWWTIHPASKQRSEGEK 164
Cdd:pfam08709   79 NSLTDALKhasnieGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDN 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462545459  165 VRIGDDLILVSVSSERYLHLSVS-----NGNIQVDASFMQTLWNVHPTCSGSS 212
Cdd:pfam08709  159 VCVGDEVILVPVSAPIFLHTTSSselrdNPGKEVNASFGQTSWKMEPFMSGCE 211
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 849-937 6.86e-46

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 161.13  E-value: 6.86e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  849 FIPCPVDTSQVILPPHLEKIRDRLAENIHELWGMNKIELGWTFGKIRDDNKRQHPCLVEFSKLPETEKNYNLQMSTETLK 928
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 2462545459  929 TLLALGCHI 937
Cdd:pfam02026   81 TLLALGYTI 89
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2598-2687 1.69e-45

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 159.98  E-value: 1.69e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2598 FDPKPINTMNFSLPEKLEYIVTKYAEHSHDKWACDKSQSGWKYGISLDENVKTHPLIRPFKTLTEKEKEIYRWPARESLK 2677
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462545459 2678 TMLAVGWTVE 2687
Cdd:pfam02026   81 TLLALGYTIE 90
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4230-4399 1.98e-43

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: 161.41  E-value: 1.98e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 4230 DMPDPTQFGIHDDTMEAERAEVMEPGITTELVHfIKGEKGDTDIMSDLFGLHPKKEGSLK----HGPEVGLGDLSEIIGK 4305
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLAD-AAGGEEEEDLLSDIFGLILKKEGGQYkvvpHDPEAGLGDLSETTAE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 4306 DEPPTLEstvQKKRKAQAAEMKAANEAEGKVES-EKADMEDG-EKEDKDKEEEQAEYLW-TEVTKKKKRRCGQKVEKPEA 4382
Cdd:pfam06459   80 EPPPLLK---RKLQESEEAEDEEEEEEEPKPEPiEKADGENGeKEEKPKEEETESEAPEeEEMKKKQRKRHSKKKEEPEA 156

                          170
                   ....*....|....*..
gi 2462545459 4383 FTANFFKGLEIYQTKLL 4399
Cdd:pfam06459  157 QGSAFWNELEVYQTKLL 173
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 963-1052 6.39e-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: 146.88  E-value: 6.39e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  963 YKPAPLDLSDVKLLPPQEILVDKLAENAHNVWAKDRIKQGWTYGIQQDLKNKRNPRLVPYALLDERTKKSNRDSLREAVR 1042
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462545459 1043 TFVGYGYNIE 1052
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3723-3840 2.07e-35

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: 131.49  E-value: 2.07e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 3723 QNDEFTRDLFRFLQLLCEGHNSDFQNFLRTQMGNTTTVNVIISTVDYLLRLQESISdfywyysgkdiidesgQHNFSKAl 3802
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN----------------EKNIELI- 63

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462545459 3803 avtKQIFNSLTEYIQGPCIGNQQSLAHSRLWDAVVGFL 3840
Cdd:pfam08454   64 ---IQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1084-1206 1.28e-31

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: 121.63  E-value: 1.28e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  1084 SGKWYFEFEVVTGGDMRVGWARPGCRPDVE--LGADDQAFVFEGNRGQRWHQGSG-YFGRTWQ-PGDVVGCMINLDDASM 1159
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNSTGpEYGLPLQePGDVIGCFLDLEAGTI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 2462545459  1160 IFTLNGELLitnkgSELAFADYEIENGFVPICCLGLSQIGRMNLGTD 1206
Cdd:smart00449   81 SFYKNGKYL-----HGLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 659-794 3.18e-25

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: 103.19  E-value: 3.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  659 KWYFELIIDQvdpfltAEPTHLRVGWAsssgYAPYPGGGEGWGGngvgDDLYSYGFDGlhlWSGRI--PRAVASINQHLL 736
Cdd:pfam00622    1 RHYFEVEIFG------QDGGGWRVGWA----TKSVPRKGERFLG----DESGSWGYDG---WTGKKywASTSPLTGLPLF 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545459  737 RSDDVVSCCLDLGVPSISFRINGQPVQGMFENFNTDGLFFPVMSFSAGVKVRFLMGGR 794
Cdd:pfam00622   64 EPGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2716-2795 3.27e-25

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: 102.20  E-value: 3.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2716 YSPAPLDLSNVVLSRELQGMVEVVAENYHNIWAKKKKLELESKGGG------SHPLLVPYDTLTAKEKFKDREKAQDLFK 2789
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*.
gi 2462545459 2790 FLQVNG 2795
Cdd:pfam02026   81 TLLALG 86
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1086-1206 1.13e-21

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 93.18  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1086 KWYFEFEV--VTGGDMRVGWARPGCR--PDVELGADDQAFVFEGNRGQRWHQGSG--YFGRTWQPGDVVGCMINLDDASM 1159
Cdd:pfam00622    1 RHYFEVEIfgQDGGGWRVGWATKSVPrkGERFLGDESGSWGYDGWTGKKYWASTSplTGLPLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462545459 1160 IFTLNGELLITnkgselAFADYEIENGFVPICCLGLSQIGRMNLGTD 1206
Cdd:pfam00622   81 SFTKNGKSLGY------AFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1328-1463 5.62e-20

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: 88.55  E-value: 5.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1328 CYYAIRIFaGQDPSCVWVGWVTPDYHLYSEKFdlnknctvtvtLGDERGrvhesvkrSNCYMVWGGDIV-ASSQRSNRSN 1406
Cdd:pfam00622    2 HYFEVEIF-GQDGGGWRVGWATKSVPRKGERF-----------LGDESG--------SWGYDGWTGKKYwASTSPLTGLP 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545459 1407 V---DLEIGCLVDLAMGMLSFSANGKELGTCYQVEPNT-KVFPAVFLQPTSTslFQFELGK 1463
Cdd:pfam00622   62 LfepGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSLGAGEG--LKFNFGL 120
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1328-1464 3.27e-19

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: 86.19  E-value: 3.27e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  1328 CYYAIRIFagqDPSCVWVGWVTPDYHLYSEKfdlnknctvtvTLGDERG-RVHESVKRSNCYMVWGGDIVASSQRSNRsn 1406
Cdd:smart00449    4 HYFEVEIG---DGGHWRVGVATKSVPRGYFA-----------LLGEDKGsWGYDGDGGKKYHNSTGPEYGLPLQEPGD-- 67

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  1407 vdlEIGCLVDLAMGMLSFSANGKELG--TCYQVEPNTKVFPAVFLQPTSTSlfQFELGKL 1464
Cdd:smart00449   68 ---VIGCFLDLEAGTISFYKNGKYLHglAFFDVKFSGPLYPAFSLGSGNSV--RLNFGPL 122
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 659-793 3.99e-17

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 80.42  E-value: 3.99e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459   659 KWYFELIIDqvdpfltaEPTHLRVGWASSSGYAPYpgggegwgGNGVGDDLYSYGFDGLHLwSGRIPRAVASINQHLLRS 738
Cdd:smart00449    3 RHYFEVEIG--------DGGHWRVGVATKSVPRGY--------FALLGEDKGSWGYDGDGG-KKYHNSTGPEYGLPLQEP 65

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545459   739 DDVVSCCLDLGVPSISFRINGQPVQGM-FENFNTDGLFFPVMSFSAGVKVRFLMGG 793
Cdd:smart00449   66 GDVIGCFLDLEAGTISFYKNGKYLHGLaFFDVKFSGPLYPAFSLGSGNSVRLNFGP 121
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
275-368 7.70e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.88  E-value: 7.70e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459   275 GSNIRWGQAFRLRHLTTGHYLALTEDqglilqdraksdtkstafsfraskelKEKLDSSHKRDIEGMGVPEIKygdsvcf 354
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDE--------------------------KLPPWGDGQQEVTGYGNPAID------- 47

                            90
                    ....*....|....
gi 2462545459   355 vqhiASGLWVTYKA 368
Cdd:smart00472   48 ----ANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
100-155 1.13e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.41  E-value: 1.13e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545459   100 HRTLLYGHAVLLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATG-EACWWTIHPA 155
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57
EF-hand_7 pfam13499
EF-hand domain pair;
3924-3979 3.13e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 3.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545459 3924 FKEYDPDGKGIISKKEFQKAM---EGQKQYTQSEIDFLLSCAEADENDMFNYVDFVDRF 3979
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLrklEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 216-405 3.71e-132

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: 412.38  E-value: 3.71e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  216 GYLLGGHVVRLFHGHDECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYL 295
Cdd:cd23292      1 GYLLGGHVVRLFHGHDECLTIPSTDQSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHYL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  296 ALTEDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKTSR 375
Cdd:cd23292     81 ALTEDQGLILQDRAKSDTKSTAFCFRAS---KEKLESGPKRDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSR 157

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462545459  376 LGPLKRKVILHQEGHMDDGLTLQRCQREES 405
Cdd:cd23292    158 LGPLKRRAILHQEGHMDDGLTLQRCQHEES 187
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 220-401 9.50e-103

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: 327.73  E-value: 9.50e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  220 GGHVVRLFHGH-DECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYLALT 298
Cdd:cd23278      1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  299 EDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKTSRLGP 378
Cdd:cd23278     81 EDRGLVLVPKEKADVKATAFCFRQS---KDDKKVLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVETKKRVGGV 157

                          170       180
                   ....*....|....*....|...
gi 2462545459  379 LKRKVILHQEGHMDDGLTLQRCQ 401
Cdd:cd23278    158 EERKAILHAEGHMDDGLSLSRAQ 180
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 211-405 3.10e-102

MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, also called RYR-1, or skeletal muscle calcium release channel, or skeletal muscle ryanodine receptor, or skeletal muscle-type ryanodine receptor, or type 1 ryanodine receptor, is a calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. It can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. It is required for normal embryonic development of muscle fibers and skeletal muscle, as well as for normal heart morphogenesis, skin development and ossification during embryogenesis. RYR-1 forms homotetramer and can also form heterotetramers with RYR-2. RYR-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467761 [Multi-domain]  Cd Length: 192  Bit Score: 326.84  E-value: 3.10e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  211 SSIEEGYLLGGHVVRLFHGH-DECLTIPSTDQNDsQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHL 289
Cdd:cd23290      1 SCCEEGYVTGGHVLRLFHGHmDECLTISAADSDD-QRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  290 TTGHYLALTEDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQ 369
Cdd:cd23290     80 TTGRYLALTEDQGLVVVDACKAHTKATSFCFRVS---KEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAP 156

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462545459  370 DAKTSRLGPLKRKVILHQEGHMDDGLTLQRCQREES 405
Cdd:cd23290    157 DPKALRLGVLKKKAILHQEGHMDDALFLTRCQQEES 192
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 641-792 2.43e-85

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: 276.50  E-value: 2.43e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  641 SIRPNIFLGVAEGSAQYKKWYFELIIDQVDPFlTAEPTHLRVGWASSSGYAPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 720
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545459  721 SGRIPRAVASINQHLLRSDDVVSCCLDLGVPSISFRINGQPVQGMFENFNTDGLFFPVMSFSAGVKVRFLMG 792
Cdd:cd12877     80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 442-621 4.00e-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: 263.68  E-value: 4.00e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  442 TLQDLIAYFQPPEEEMRHEDKQNKL---RSLKNRQNLFKEEGMLALVLNCIDRLN-VYNSVAHFAGIAREESGMAWKEIL 517
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  518 NLLYKLLAALIRGNRNNCAQFSNNLDWLISKLDRLESSSGILEVLHCILTESPE-ALNLIAEGHIKSIISLLDKHGRNHK 596
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180
                   ....*....|....*....|....*
gi 2462545459  597 VLDILCSLCLCNGVAVRANQNLICD 621
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICR 185
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1072-1204 1.59e-79

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: 259.15  E-value: 1.59e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1072 RFFRVERSYAVRSGKWYFEFEVVTGGDMRVGWARPGCRPDVELGADDQAFVFEGNRGQRWHQGSGYFGRTWQPGDVVGCM 1151
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462545459 1152 INLDDASMIFTLNGELLITNKGSELAFADYEIENGFVPICCLGLSQIGRMNLG 1204
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 220-405 5.06e-77

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: 254.20  E-value: 5.06e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  220 GGHVVRLFHGH-DECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYLALT 298
Cdd:cd23291      1 GGDVLRLLHGHmDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  299 EDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKTSRLGP 378
Cdd:cd23291     81 EDKNLLLMDKEKADVKSTAFTFRSS---KEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGS 157

                          170       180
                   ....*....|....*....|....*..
gi 2462545459  379 LKRKVILHQEGHMDDGLTLQRCQREES 405
Cdd:cd23291    158 IQRKAIMHHEGHMDDGLNLSRSQHEES 184
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 216-397 7.04e-77

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: 253.83  E-value: 7.04e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  216 GYLLGGHVVRLFHGH-DECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRI-SWSGSNIRWGQAFRLRHLTTGH 293
Cdd:pfam02815    1 GYLKGGDVVRLFHSHqDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  294 YLALTEDQGLILQDRAKSDTKSTAFSFRASKELKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKT 373
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....
gi 2462545459  374 SRLGPLKRKVILHQEGHMDDGLTL 397
Cdd:pfam02815  161 WGFGPEQQKVTCAKEGHMDDALTL 184
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2023-2233 2.69e-75

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: 249.81  E-value: 2.69e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2023 QIRSLLSVRMGKEEELLMINGLGDIMNNKVFYQHPNLMRVLGMHETVMEVMvNVLGT-------------EKSQIAFPKM 2089
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlgEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2090 VASCCRFLCYFCRISRQNQKAMFEHLSYLLENssvgLASPSMRGSTpLDVAASSVMDNNELALsleepdlekvvTYLAGC 2169
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKEC 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545459 2170 GLQSCPMLLAKGYPDvgwnpiegERYLSFLRFAVFVNSESVEENASVVVKLLIRRPECFGPALR 2233
Cdd:pfam01365  144 HIKSFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1324-1462 1.70e-72

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: 239.90  E-value: 1.70e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1324 TTTQCYYAIRIFAGQDPSCVWVGWVTPDYHLYSEKFDLNKNCTVTVTLGDERGRVHESVKRSNCYMVWGGDIVASSQR-- 1401
Cdd:cd12879     11 LVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAGELLAEVGQds 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545459 1402 SNRSNVDLEIGCLVDLAMGMLSFSANGKELGTCYQVEPNTKVFPAVFLQPTSTSLFQFELG 1462
Cdd:cd12879     91 SGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 14-212 1.68e-65

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: 222.37  E-value: 1.68e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459   14 FLRTEDEVVLQCIATIhkeqrKFCLAAEGLGNRLCFLEPTSEAKYIPP-DLCVCNFVLEQSLSVRALQEML--ANTGENG 90
Cdd:pfam08709    4 FLHIGDIVSLSCEESV-----NGFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWsaGNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459   91 GEGAAQGG------GHRTLLYGHAVLLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATGEACWWTIHPASKQRSEGEK 164
Cdd:pfam08709   79 NSLTDALKhasnieGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDN 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462545459  165 VRIGDDLILVSVSSERYLHLSVS-----NGNIQVDASFMQTLWNVHPTCSGSS 212
Cdd:pfam08709  159 VCVGDEVILVPVSAPIFLHTTSSselrdNPGKEVNASFGQTSWKMEPFMSGCE 211
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 849-937 6.86e-46

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 161.13  E-value: 6.86e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  849 FIPCPVDTSQVILPPHLEKIRDRLAENIHELWGMNKIELGWTFGKIRDDNKRQHPCLVEFSKLPETEKNYNLQMSTETLK 928
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 2462545459  929 TLLALGCHI 937
Cdd:pfam02026   81 TLLALGYTI 89
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2598-2687 1.69e-45

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 159.98  E-value: 1.69e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2598 FDPKPINTMNFSLPEKLEYIVTKYAEHSHDKWACDKSQSGWKYGISLDENVKTHPLIRPFKTLTEKEKEIYRWPARESLK 2677
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462545459 2678 TMLAVGWTVE 2687
Cdd:pfam02026   81 TLLALGYTIE 90
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4230-4399 1.98e-43

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: 161.41  E-value: 1.98e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 4230 DMPDPTQFGIHDDTMEAERAEVMEPGITTELVHfIKGEKGDTDIMSDLFGLHPKKEGSLK----HGPEVGLGDLSEIIGK 4305
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLAD-AAGGEEEEDLLSDIFGLILKKEGGQYkvvpHDPEAGLGDLSETTAE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 4306 DEPPTLEstvQKKRKAQAAEMKAANEAEGKVES-EKADMEDG-EKEDKDKEEEQAEYLW-TEVTKKKKRRCGQKVEKPEA 4382
Cdd:pfam06459   80 EPPPLLK---RKLQESEEAEDEEEEEEEPKPEPiEKADGENGeKEEKPKEEETESEAPEeEEMKKKQRKRHSKKKEEPEA 156

                          170
                   ....*....|....*..
gi 2462545459 4383 FTANFFKGLEIYQTKLL 4399
Cdd:pfam06459  157 QGSAFWNELEVYQTKLL 173
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 963-1052 6.39e-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: 146.88  E-value: 6.39e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  963 YKPAPLDLSDVKLLPPQEILVDKLAENAHNVWAKDRIKQGWTYGIQQDLKNKRNPRLVPYALLDERTKKSNRDSLREAVR 1042
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2462545459 1043 TFVGYGYNIE 1052
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3723-3840 2.07e-35

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: 131.49  E-value: 2.07e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 3723 QNDEFTRDLFRFLQLLCEGHNSDFQNFLRTQMGNTTTVNVIISTVDYLLRLQESISdfywyysgkdiidesgQHNFSKAl 3802
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN----------------EKNIELI- 63

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462545459 3803 avtKQIFNSLTEYIQGPCIGNQQSLAHSRLWDAVVGFL 3840
Cdd:pfam08454   64 ---IQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1084-1206 1.28e-31

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: 121.63  E-value: 1.28e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  1084 SGKWYFEFEVVTGGDMRVGWARPGCRPDVE--LGADDQAFVFEGNRGQRWHQGSG-YFGRTWQ-PGDVVGCMINLDDASM 1159
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNSTGpEYGLPLQePGDVIGCFLDLEAGTI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 2462545459  1160 IFTLNGELLitnkgSELAFADYEIENGFVPICCLGLSQIGRMNLGTD 1206
Cdd:smart00449   81 SFYKNGKYL-----HGLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1085-1202 6.56e-26

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


Pssm-ID: 293931  Cd Length: 118  Bit Score: 105.21  E-value: 6.56e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1085 GKWYFEFEVVT--GGDMRVGWARPGCRPDVE--LGADDQAFVFEGNRGQRWHQG-SGYFGRTWQPGDVVGCMINLDDASM 1159
Cdd:cd11709      1 GKWYWEVRVDSgnGGLIQVGWATKSFSLDGEggVGDDEESWGYDGSRLRKGHGGsSGPGGRPWKSGDVVGCLLDLDEGTL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2462545459 1160 IFTLNGELLITnkgselAFAD-YEIENGFVPICCLGLSQIGRMN 1202
Cdd:cd11709     81 SFSLNGKDLGV------AFTNlFLKGGGLYPAVSLGSGQGVTIN 118
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 659-794 3.18e-25

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: 103.19  E-value: 3.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  659 KWYFELIIDQvdpfltAEPTHLRVGWAsssgYAPYPGGGEGWGGngvgDDLYSYGFDGlhlWSGRI--PRAVASINQHLL 736
Cdd:pfam00622    1 RHYFEVEIFG------QDGGGWRVGWA----TKSVPRKGERFLG----DESGSWGYDG---WTGKKywASTSPLTGLPLF 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545459  737 RSDDVVSCCLDLGVPSISFRINGQPVQGMFENFNTDGLFFPVMSFSAGVKVRFLMGGR 794
Cdd:pfam00622   64 EPGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2716-2795 3.27e-25

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: 102.20  E-value: 3.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 2716 YSPAPLDLSNVVLSRELQGMVEVVAENYHNIWAKKKKLELESKGGG------SHPLLVPYDTLTAKEKFKDREKAQDLFK 2789
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*.
gi 2462545459 2790 FLQVNG 2795
Cdd:pfam02026   81 TLLALG 86
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1086-1206 1.13e-21

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 93.18  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1086 KWYFEFEV--VTGGDMRVGWARPGCR--PDVELGADDQAFVFEGNRGQRWHQGSG--YFGRTWQPGDVVGCMINLDDASM 1159
Cdd:pfam00622    1 RHYFEVEIfgQDGGGWRVGWATKSVPrkGERFLGDESGSWGYDGWTGKKYWASTSplTGLPLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462545459 1160 IFTLNGELLITnkgselAFADYEIENGFVPICCLGLSQIGRMNLGTD 1206
Cdd:pfam00622   81 SFTKNGKSLGY------AFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1328-1463 5.62e-20

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: 88.55  E-value: 5.62e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1328 CYYAIRIFaGQDPSCVWVGWVTPDYHLYSEKFdlnknctvtvtLGDERGrvhesvkrSNCYMVWGGDIV-ASSQRSNRSN 1406
Cdd:pfam00622    2 HYFEVEIF-GQDGGGWRVGWATKSVPRKGERF-----------LGDESG--------SWGYDGWTGKKYwASTSPLTGLP 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462545459 1407 V---DLEIGCLVDLAMGMLSFSANGKELGTCYQVEPNT-KVFPAVFLQPTSTslFQFELGK 1463
Cdd:pfam00622   62 LfepGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSLGAGEG--LKFNFGL 120
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1328-1464 3.27e-19

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: 86.19  E-value: 3.27e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  1328 CYYAIRIFagqDPSCVWVGWVTPDYHLYSEKfdlnknctvtvTLGDERG-RVHESVKRSNCYMVWGGDIVASSQRSNRsn 1406
Cdd:smart00449    4 HYFEVEIG---DGGHWRVGVATKSVPRGYFA-----------LLGEDKGsWGYDGDGGKKYHNSTGPEYGLPLQEPGD-- 67

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  1407 vdlEIGCLVDLAMGMLSFSANGKELG--TCYQVEPNTKVFPAVFLQPTSTSlfQFELGKL 1464
Cdd:smart00449   68 ---VIGCFLDLEAGTISFYKNGKYLHglAFFDVKFSGPLYPAFSLGSGNSV--RLNFGPL 122
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 659-790 6.29e-19

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


Pssm-ID: 293931  Cd Length: 118  Bit Score: 85.18  E-value: 6.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  659 KWYFELIIDqvdpflTAEPTHLRVGWASSSgyapypggGEGWGGNGVGDDLYSYGFDG--LHLWSGRIPRAvasiNQHLL 736
Cdd:cd11709      2 KWYWEVRVD------SGNGGLIQVGWATKS--------FSLDGEGGVGDDEESWGYDGsrLRKGHGGSSGP----GGRPW 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462545459  737 RSDDVVSCCLDLGVPSISFRINGQPVQGMFENFNTD-GLFFPVMSFSAGVKVRFL 790
Cdd:cd11709     64 KSGDVVGCLLDLDEGTLSFSLNGKDLGVAFTNLFLKgGGLYPAVSLGSGQGVTIN 118
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 215-398 1.53e-18

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: 87.06  E-value: 1.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  215 EGYLLGGHVVRLFH-------GHDECLTIPSTDQNDSQHRRIFYEAGGAG----TRARSLWRVEPLRISWSGSNIRWGQA 283
Cdd:cd23280      4 ENFLKGGDVVRLFHkeleaylSAEGSFVDEVLTEDVHLRVRPVDDRKPRTlfppTSGDTFWQIEKEDTPLKGGVIKWGDQ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  284 FRLRHLTTGHYLALTEDQG---LILQDraKSDTKSTAFSFRASkeLKEKLDsshkrdiegmgvpEIKYGdSVCFVQHIAS 360
Cdd:cd23280     84 CRLRHLPTGKYLAVDDKTGngkVVLTS--DPSDPSTVFRLHPV--TKETSE-------------EVKFG-SYVRIEHVAT 145

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2462545459  361 GLWV-----TYKAQDAKTSRLGP----LKRKVILHQEGHMDDGLTLQ 398
Cdd:cd23280    146 GTWLhaetdEELRRSKKSPAGLSwdgaKLRKVSLSLERQDDDAFTIQ 192
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 1081-1165 3.00e-18

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: 83.53  E-value: 3.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1081 AVRSGKWYFEFEVVTGGDMRVGWARPGCRPDVELGADD--QAFVFEGNRGQRWHQGSGYFGRTWQPGDVVGCMINLDDAS 1158
Cdd:cd12882      7 CVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDtrDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDLDKGT 86


                   ....*..
gi 2462545459 1159 MIFTLNG 1165
Cdd:cd12882     87 ISFYRNG 93
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 659-793 3.99e-17

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 80.42  E-value: 3.99e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459   659 KWYFELIIDqvdpfltaEPTHLRVGWASSSGYAPYpgggegwgGNGVGDDLYSYGFDGLHLwSGRIPRAVASINQHLLRS 738
Cdd:smart00449    3 RHYFEVEIG--------DGGHWRVGVATKSVPRGY--------FALLGEDKGSWGYDGDGG-KKYHNSTGPEYGLPLQEP 65

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462545459   739 DDVVSCCLDLGVPSISFRINGQPVQGM-FENFNTDGLFFPVMSFSAGVKVRFLMGG 793
Cdd:smart00449   66 GDVIGCFLDLEAGTISFYKNGKYLHGLaFFDVKFSGPLYPAFSLGSGNSVRLNFGP 121
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 1079-1168 1.79e-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: 79.48  E-value: 1.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1079 SYAVRSGKWYFEFEVVTGGDM-----RVGWARPGCRPDVELGADDQAFVFEGNRGQRWHQGSG--YFGRTWQPGDVVGCM 1151
Cdd:cd12872     22 NHGVREGKWYFEVKILEGGGTetghvRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFHQSRGkpYGEPGFKEGDVIGFL 101

                           90
                   ....*....|....*..
gi 2462545459 1152 INLddASMIFTLNGELL 1168
Cdd:cd12872    102 ITL--PKIEFFKNGKSQ 116
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 221-390 4.33e-15

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: 76.27  E-value: 4.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  221 GHVVRLFHGH-DECLTIPS-TDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWsGSNIRWGQAFRLRHLTTGHYLALT 298
Cdd:cd23263      1 GDVIWLKHSEtGKYLHSHRkNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  299 EDQG---------LILQDrakSDTKSTAFSFraskelkekldsshkrDIEGMGVPEIKY--GDSVCFVQHIASGLWVtyK 367
Cdd:cd23263     80 EGKKspksnhqevLCLTD---NPDKSSLFKF----------------EPIGSTKYKQKYvkKDSYFRLKHVNTNFWL--H 138

                          170       180
                   ....*....|....*....|...
gi 2462545459  368 AQDAKTSRLGPLKRKVILHQEGH 390
Cdd:cd23263    139 SHEKKFNINNKTQQEVICHGERE 161
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 1085-1165 9.63e-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: 73.54  E-value: 9.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1085 GKWYFEFEVVTGGDMRVGWARPGCRPDVE----LGADDQAFVFEGNRGQRWH--QGSGYFGRTWQPGDVVGCMINLDDAS 1158
Cdd:cd12883      1 GVWYYEVTVLTSGVMQIGWATKDSKFLNHegygIGDDEYSCAYDGCRQLIWYnaKSKPHTHPRWKPGDVLGCLLDLNKKQ 80


                   ....*..
gi 2462545459 1159 MIFTLNG 1165
Cdd:cd12883     81 MIFSLNG 87
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 1084-1168 7.14e-12

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: 66.44  E-value: 7.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1084 SGKWYFEFEVVTGGDMRVGWARPGCrpDVELGADDQAFVFeGNRGQRWH--QGSGYfGRTWQPGDVVGCMINLDDASMIF 1161
Cdd:cd12873     39 KGKYYYEVTVTDEGLCRVGWSTEDA--SLDLGTDKFGFGY-GGTGKKSHgrQFDDY-GEPFGLGDVIGCYLDLDNGTISF 114


                   ....*..
gi 2462545459 1162 TLNGELL 1168
Cdd:cd12873    115 SKNGKDL 121
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 1072-1168 2.51e-11

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: 63.84  E-value: 2.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1072 RFFRVERSYAVRSGKWYFEFEVV---TGGDMRVGWARPGCRPDVELGADDQAFVFEGNRGQRWHQGSGY--FGRTWQPGD 1146
Cdd:cd12885      1 GSVRADHPIPPKVPVFYFEVTILdlgEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGenYGPPFGTGD 80

                           90       100
                   ....*....|....*....|..
gi 2462545459 1147 VVGCMINLDDASMIFTLNGELL 1168
Cdd:cd12885     81 VVGCGINFKTGEVFFTKNGELL 102
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1329-1449 6.68e-10

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: 59.37  E-value: 6.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1329 YYAIRIFAGQdPSCVWVGWVTPDYHLYSEKfdlnknctvtvTLGDE---------RGRVHESVKRSNCYMVWG-GDIvas 1398
Cdd:cd11709      4 YWEVRVDSGN-GGLIQVGWATKSFSLDGEG-----------GVGDDeeswgydgsRLRKGHGGSSGPGGRPWKsGDV--- 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462545459 1399 sqrsnrsnvdleIGCLVDLAMGMLSFSANGKELGTCYQVEPNTK--VFPAVFL 1449
Cdd:cd11709     69 ------------VGCLLDLDEGTLSFSLNGKDLGVAFTNLFLKGggLYPAVSL 109
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 215-364 3.92e-09

MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor (ITPR); Inositol 1,4,5 trisphosphate receptors (ITPRs) are a family of endoplasmic reticulum Ca2+ channels essential for the control of intracellular Ca2+ levels in virtually every mammalian cell type. Calcium-mediated signaling through ITPRs is essential for the regulation of numerous physiological processes, including fertilization, muscle contraction, apoptosis, secretion, and synaptic plasticity. The ITPR family includes three isoforms (ITPR1, ITPR2 and ITPR3), which can control different cellular processes due to their unique biophysical properties, subcellular localization, and tissue distribution. ITPRs contain an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467748 [Multi-domain]  Cd Length: 204  Bit Score: 59.68  E-value: 3.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  215 EGYLLGGHVVRLFHGHDE-CLTipSTDQNDSQHrrIFYEAGG-----AGTRARSLWRVE-----PLRiswsGSNIRWGQA 283
Cdd:cd23277      8 EDVLKGGDVVRLFHAEQEkFLT--CDEYKKKQY--VFLRTTGrtsatSATSSKALWEVEvvqhdPCR----GGAGHWNSL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  284 FRLRHLTTGHYLAltedqglilqdrAKSDTKSTAFSFRaskelkEKLDSSHKRDIEGM-GVPE--------------IKY 348
Cdd:cd23277     80 FRFKHLATGQYLA------------AEVDPDPTPDPTR------SKLRGAPGKPVYCLvSVPHgndiasifeldpttLQR 141

                          170       180
                   ....*....|....*....|..
gi 2462545459  349 GDSV----CFV--QHIASGLWV 364
Cdd:cd23277    142 GDSLvprsSYVrlRHLCTNTWV 163
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 649-789 4.81e-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: 57.91  E-value: 4.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  649 GVAEGsaqykKWYFELIIDQVDPFLTAeptHLRVGWasSSGYAPYpgggegwggngvgD-----DLYSYGF---DG--LH 718
Cdd:cd12872     24 GVREG-----KWYFEVKILEGGGTETG---HVRVGW--SRREASL-------------QapvgyDKYSYAIrdkDGskFH 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462545459  719 LwSGRIPRAVASINQhllrsDDVVSCCLDLgvPSISFRINGQPvQG-MFENFNTDGLFFPVMS--FSAGVKVRF 789
Cdd:cd12872     81 Q-SRGKPYGEPGFKE-----GDVIGFLITL--PKIEFFKNGKS-QGvAFEDIYGTGGYYPAVSlyKGATVTINF 145
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 202-296 1.17e-08

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) and similar proteins; ITPR2, also called IP3 receptor isoform 2 (IP3R 2), or InsP3R2, or type 2 inositol 1,4,5-trisphosphate receptor, or type 2 InsP3 receptor, is a key regulator for the activity of calcium ion transmembrane transportation, which plays a critical role in cell cycle and proliferation. It is a receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of cAMP-dependent protein kinase (PKA). ITPR2 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467759 [Multi-domain]  Cd Length: 222  Bit Score: 58.51  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  202 WNVHPTCSGSSIEEGYLLGGHVVRLFHGHDECLtIPSTDQNDSQH---RRIFYEAGGAGTRARSLWRVE-----PLRisw 273
Cdd:cd23288      1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKF-LTCDEYKKKQHiflRTTLRQSATSATSSKALWEIEvvhydPCR--- 76

                           90       100
                   ....*....|....*....|...
gi 2462545459  274 sGSNIRWGQAFRLRHLTTGHYLA 296
Cdd:cd23288     77 -GGAGQWNSLFRFKHLATGNYLA 98
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 659-792 3.97e-08

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


Pssm-ID: 240458  Cd Length: 133  Bit Score: 55.00  E-value: 3.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  659 KWYFELIIdqvdpfLTAEPthLRVGWASSSGYAPYPGGGegwggngvgDDLySYGFDGlhlWSGRIPRAVASINQHLLRS 738
Cdd:cd12878     15 KWYFEFEV------LTSGY--MRVGWARPGFRPDLELGS---------DDL-SYAFDG---FLARKWHQGSESFGKQWQP 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  739 DDVVSCCLDLGVPSISFRINGQPVQG------MFENFNTDGLFFPVMSFSAGVKVRFLMG 792
Cdd:cd12878     74 GDVVGCMLDLVDRTISFTLNGELLIDssgsevAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 211-364 1.09e-07

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) and similar proteins; ITPR1, also called IP3 receptor isoform 1 (IP3R 1), or InsP3R1, or type 1 inositol 1,4,5-trisphosphate receptor, or type 1 InsP3 receptor, is an intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. It is involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1. It plays a role in endoplasmic reticulum (ER) stress-induced apoptosis. ITPR1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467758 [Multi-domain]  Cd Length: 222  Bit Score: 55.85  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  211 SSIEEGYLLGGHVVRLFHGHDECLtIPSTDQNDSQH---RRIFYEAGGAGTRARSLWRVE-----PLRiswsGSNIRWGQ 282
Cdd:cd23287      4 SDNKDDILKGGDVVRLFHAEQEKF-LTCDEHRKKQHvflRTTGRQSATSATSSKALWEVEvvqhdPCR----GGAGYWNS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  283 AFRLRHLTTGHYLA--LTEDQGLILQDRAKSDTKSTAFSFRASKELKEKLDSSHKRDIEGMGVPEI--------KYGDSV 352
Cdd:cd23287     79 LFRFKHLATGHYLAaeVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIfeldpttlRGGDSL 158

                          170
                   ....*....|....*...
gi 2462545459  353 ------CFVQHIASGLWV 364
Cdd:cd23287    159 vprnsyVRLRHLCTNTWV 176
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
275-368 7.70e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.88  E-value: 7.70e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459   275 GSNIRWGQAFRLRHLTTGHYLALTEDqglilqdraksdtkstafsfraskelKEKLDSSHKRDIEGMGVPEIKygdsvcf 354
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDE--------------------------KLPPWGDGQQEVTGYGNPAID------- 47

                            90
                    ....*....|....
gi 2462545459   355 vqhiASGLWVTYKA 368
Cdd:smart00472   48 ----ANTLWLIEPV 57
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 1079-1168 1.63e-06

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: 51.44  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1079 SYAVRSGKWYFEFEVV-------------TGGDMRVGWARPGCRpdVELGADDQAFVFEGNrGQRWHQG-SGYFGRTWQP 1144
Cdd:cd12884     39 TYGVTKGKVCFEVKVTenlpvkhlpteetDPHVVRVGWSVDSSS--LQLGEEEFSYGYGST-GKKSTNCkFEDYGEPFGE 115

                           90       100
                   ....*....|....*....|....*.
gi 2462545459 1145 GDVVGCMINLD--DASMIFTLNGELL 1168
Cdd:cd12884    116 NDVIGCYLDFEsePVEISFSKNGKDL 141
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 1086-1193 2.42e-06

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: 50.39  E-value: 2.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1086 KWYFEFEVvTGGD--------MRVGWAR-------PGCRPD---VELGADDQAFVFEG------NRGQRWHQGSGYFGRt 1141
Cdd:cd12877     19 KWYFEVEV-DHVEqfthqpahLRVGWANtsgyvpyPGGGEGwggNGVGDDLYSYGFDGlhlwtgGRSRRVTSGTQHLLK- 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462545459 1142 wqPGDVVGCMINLDDASMIFTLNGELLitnKGSelaFADYEIENGFVPICCL 1193
Cdd:cd12877     97 --KGDVVGCCLDLSVPSISFRVNGRPV---QGM---FENFNLDGMFFPVMSF 140
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 218-341 3.84e-06

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) and similar proteins; ITPR3, also called IP3 receptor isoform 3 (IP3R 3), or InsP3R3, or type 3 inositol 1,4,5-trisphosphate receptor, or type 3 InsP3 receptor, acts as anti-oncogenic channel by propelling pro-apoptotic Ca2+ signals to mitochondria. It is the principal intracellular Ca2+ release channel in cholangiocytes and plays a particularly important role in cancer. ITPR3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467760 [Multi-domain]  Cd Length: 215  Bit Score: 51.20  E-value: 3.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  218 LLGGHVVRLFHGHDECLtIPSTDQNDSQH---RRIFYEAGGAGTRARSLWRVE-----PLRiswsGSNIRWGQAFRLRHL 289
Cdd:cd23289     11 LKGGDVVRLFHAEQEKF-LTCDEYKGKLQvflRTTLRQSATSATSSNALWEVEvvhhdPCR----GGAGHWNGLYRFKHL 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462545459  290 TTGHYLAlTEDQGLILQDRAKSDTKSTAFSFRASK-----ELKEKLDS-SHKRDIEGM 341
Cdd:cd23289     86 ATGNYLA-AEENPSYKGDASDPKAAGMGAQSRTGRrnageKIKYCLVAvPHGNDIASL 142
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
100-155 1.13e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.41  E-value: 1.13e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545459   100 HRTLLYGHAVLLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATG-EACWWTIHPA 155
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 660-800 2.48e-05

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: 46.57  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459  660 WYFELIIdqvdpfLTaePTHLRVGWASSS-------GYApypgggegwggngVGDDLYSYGFDGLH--LWSGRIPRAVAS 730
Cdd:cd12883      3 WYYEVTV------LT--SGVMQIGWATKDskflnheGYG-------------IGDDEYSCAYDGCRqlIWYNAKSKPHTH 61

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462545459  731 INqhlLRSDDVVSCCLDLGVPSISFRINGQPVQGMFENFN--TDGlFFPVMSFsagvkvrflMGGRHGEFKF 800
Cdd:cd12883     62 PR---WKPGDVLGCLLDLNKKQMIFSLNGNRLPPERQVFTsaKSG-FFAAASF---------MSFQQCEFNF 120
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 1081-1168 6.71e-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: 45.98  E-value: 6.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1081 AVRS--------GKWYFEFEVVTGGD---MRVGWarpgCRPDVEL----GADDQAFVFEGNRGQRWH-QGSGY-FGRTWQ 1143
Cdd:cd12909     13 AVRAnhpippqcGIYYFEVKIISKGRdgyIGIGF----STKDVNLnrlpGWEPHSWGYHGDDGHSFCsSGTGKpYGPTFT 88

                           90       100
                   ....*....|....*....|....*
gi 2462545459 1144 PGDVVGCMINLDDASMIFTLNGELL 1168
Cdd:cd12909     89 TGDVIGCGINFRDNTAFYTKNGVNL 113
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 1085-1199 2.08e-04

SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in bacterial and are mostly uncharacterized. SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 eukaryotic protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L).


Pssm-ID: 293944  Cd Length: 129  Bit Score: 44.03  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462545459 1085 GKWYFEFEVVTGG---DMRVGWARPGCRPDVELG-ADDQA--FVFEGNRGQRWHQGSGY--FGRTWQPGDVVGCMINLDD 1156
Cdd:cd12886      1 GKWYWEVTVVSSAastYAGIGVANAAATGNNGLNgIELSSigYSLGVYSGNKLSNGSSVatYGAGFTAGDVIGVALDLDA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2462545459 1157 ASMIFTLNGELLitnKGSELAFADYEIENG--FVPICCLGLSQIG 1199
Cdd:cd12886     81 GKIWFYKNGVWQ---GGGDPAPGTNPAFAGtaMYPAVTGGSSTGG 122
EF-hand_7 pfam13499
EF-hand domain pair;
3924-3979 3.13e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 3.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545459 3924 FKEYDPDGKGIISKKEFQKAM---EGQKQYTQSEIDFLLSCAEADENDMFNYVDFVDRF 3979
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLrklEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 1411-1450 6.39e-04

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


Pssm-ID: 293933  Cd Length: 155  Bit Score: 43.33  E-value: 6.39e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2462545459 1411 IGCLVDLAMGMLSFSANGKELGTCYQVEPNTK---VFPAVFLQ 1450
Cdd:cd12873    101 IGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRnsaLFPAVCLK 143
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
215-268 5.22e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 38.09  E-value: 5.22e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462545459   215 EGYLLGGHVVRLFHGHDEC-LTIPSTD--QNDSQHRRIFYEaGGAGTRARSLWRVEP 268
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRyLHSHDEKlpPWGDGQQEVTGY-GNPAIDANTLWLIEP 56
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
162-206 7.16e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 37.71  E-value: 7.16e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462545459   162 GEKVRIGDDLILVSVSSERYLHLS--------------VSNGNIQVDASfmqTLWNVHP 206
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHdeklppwgdgqqevTGYGNPAIDAN---TLWLIEP 56
 
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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