NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1173335|sp|P16960|]
View 

RecName: Full=Ryanodine receptor 1; Short=RYR-1; Short=RyR1; AltName: Full=Skeletal muscle calcium release channel; AltName: Full=Skeletal muscle ryanodine receptor; AltName: Full=Skeletal muscle-type ryanodine receptor; AltName: Full=Type 1 ryanodine receptor

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 207-398 1.86e-131

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: 410.43  E-value: 1.86e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   207 SGCEEGYVTGGHVLRLFHGHMDECLTISPADSDDQRRLVYYEGGSVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 286
Cdd:cd23290    1 SCCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   287 TGRYLALIEDQGLVVVDASKAHTKATSFCFRISKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 366
Cdd:cd23290   81 TGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 1173335   367 LRLGVLKKKAILHQEGHMDDALSLTRCQQEES 398
Cdd:cd23290  161 LRLGVLKKKAILHQEGHMDDALFLTRCQQEES 192
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1073-1205 1.18e-81

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: 265.32  E-value: 1.18e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1073 RIFRAEKSYAVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLGSELFGRPWQSGDVVGCM 1152
Cdd:cd12878    1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1173335  1153 IDLTENTIIFTLNGEVLMSDSGSETAFRDIEVGDGFLPVCSLGPGQVGHLNLG 1205
Cdd:cd12878   81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 444-637 1.40e-81

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


:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 267.91  E-value: 1.40e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     444 SLQDLIGYFEPPSEELQHEEKQSKL---RSLRNRQSLFQEEGMLSLVLNCIDRLN-VYTTAAHFAEFAGEEAAESWKEIV 519
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     520 NLLYEILASLIRGNRANCALFSNNLDWLVSKLDRLEASSGILEVLYCVLIESPE-VLNIIQENHIKSIISLLDKHGRNHK 598
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1173335     599 VLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNL 637
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 643-794 4.19e-79

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: 258.78  E-value: 4.19e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   643 SIRPNIFVGRAEGTTQYSKWYFEVMVDEVVPFlTAQATHLRVGWALTEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 722
Cdd:cd12877    1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173335   723 TGHVPRLVTSPGQHLLAPEDVVSCCLDLSVPSISFRINGCPVQGVFEAFNLNGLFFPVVSFSAGVKVRFLLG 794
Cdd:cd12877   80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4378-4668 9.48e-78

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: 260.40  E-value: 9.48e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4378 GMPDPTGDEVHGEQPAGPGGEADGEGAGEGAGEAWEGAGDEEVAVQEAGPGgadgavAVAEGGPFR---PEGAGGLGDMG 4454
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLADAAGGEEEEDLLSDIFGLI------LKKEGGQYKvvpHDPEAGLGDLS 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4455 DTTPAEPPtpegsPIIKRKLGVDGEEEELPPEPEPEPEPEPEKADAENGEKEEVPKPPPEPPKKTAPPPPPPKKEEG--- 4531
Cdd:pfam06459   75 ETTAEEPP-----PLLKRKLQESEEAEDEEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMKKKQRKRhsk 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4532 -----GSGGLEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDMEGSAAGDlsgagsggg 4606
Cdd:pfam06459  150 kkeepEAQGSAFWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGSGWGD--------- 220

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173335    4607 SGWGSGAGEEVEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVI 4668
Cdd:pfam06459  221 SGSGSGGGSGEDEEEEEGPVYFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1419-1567 1.25e-77

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: 254.54  E-value: 1.25e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1419 DDRDDPDIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMNFDLTKVRAVTVTMGDEQGNIHSSLKCSNCYMVWGG 1498
Cdd:cd12879    1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173335  1499 DFVSPGQQ--GRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVIQFELG 1567
Cdd:cd12879   81 ELLAEVGQdsSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
Ins145_P3_rec super family cl48031
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 11-210 1.61e-76

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: 253.96  E-value: 1.61e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335      11 VQFLRTDDEVVLQCNATVLkeqlkLCLAAEGFGNRLCFLEPTSNAQNVPP-DLAICCFVLEQSLSVRALQEMLAN----- 84
Cdd:pfam08709    2 SSFLHIGDIVSLSCEESVN-----GFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWSAgnrsp 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335      85 ----TVEAGVESSQGGGHRTLLYGHAILLRHAHSGMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTTHPASKQRSEG 160
Cdd:pfam08709   77 ngnsLTDALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1173335     161 EKVRVGDDLILVSVSSERYLHLST-----ASGELQVDASFMQTLWNMNPICSGCE 210
Cdd:pfam08709  157 DNVCVGDEVILVPVSAPIFLHTTSsselrDNPGKEVNASFGQTSWKMEPFMSGCE 211
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2162-2370 3.02e-71

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


:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 238.25  E-value: 3.02e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2162 QIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMvNVLGG------------GESKEIRFPKM 2229
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlGEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2230 VTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGiGLGMQGSTpLDVAAASVIDNNELALalqeqdlekvvSYLAGCGLQ 2309
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLG-SPSLAEGT-LDVLTALLMDNPELLL-----------NYIKECHIK 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173335    2310 SCPMLLAKGYPDigwnpcggERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALR 2370
Cdd:pfam01365  147 SFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 851-940 2.42e-45

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 159.59  E-value: 2.42e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     851 FVPCPVDTVQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVDFHSLPEPERNYNLQMSGETLK 930
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335     931 TLLALGCHVG 940
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2736-2825 1.27e-42

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 151.89  E-value: 1.27e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2736 FDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLK 2815
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335    2816 AMIAWEWTIE 2825
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 965-1054 2.97e-37

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 136.48  E-value: 2.97e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     965 YKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVR 1044
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335    1045 TLLGYGYNIE 1054
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2856-2939 1.82e-34

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 128.77  E-value: 1.82e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2856 YNPQPPDLSGVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGG------THPLLVPYDTLTAKEKARDREKAQELLK 2929
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335    2930 FLQMNGYAVT 2939
Cdd:pfam02026   81 TLLALGYTIE 90
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3872-3988 1.14e-31

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


:

Pssm-ID: 462482  Cd Length: 98  Bit Score: 121.09  E-value: 1.14e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    3872 DDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISdfywyysgkdvieeqgkrnfSKAMS 3951
Cdd:pfam08454    2 EVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN--------------------EKNIE 61

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1173335    3952 VAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFL 3988
Cdd:pfam08454   62 LIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4762-4946 8.64e-27

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


:

Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 111.98  E-value: 8.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4762 LLTWLMSIDVKYQIWKFGVI---FTDNSFLYLGWYMVMSLLG------------HYNNFFFAAHLLDIAMGVKTLRTILS 4826
Cdd:pfam00520   41 VFTGIFTLEMLLKIIAAGFKkryFRSPWNILDFVVVLPSLISlvlssvgslsglRVLRLLRLLRLLRLIRRLEGLRTLVN 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4827 SVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVgvRAGGGIGDEIEDPAGDE 4906
Cdd:pfam00520  121 SLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGK 198

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1173335    4907 YELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQE 4946
Cdd:pfam00520  199 GEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 207-398 1.86e-131

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: 410.43  E-value: 1.86e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   207 SGCEEGYVTGGHVLRLFHGHMDECLTISPADSDDQRRLVYYEGGSVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 286
Cdd:cd23290    1 SCCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   287 TGRYLALIEDQGLVVVDASKAHTKATSFCFRISKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 366
Cdd:cd23290   81 TGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 1173335   367 LRLGVLKKKAILHQEGHMDDALSLTRCQQEES 398
Cdd:cd23290  161 LRLGVLKKKAILHQEGHMDDALFLTRCQQEES 192
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1073-1205 1.18e-81

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: 265.32  E-value: 1.18e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1073 RIFRAEKSYAVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLGSELFGRPWQSGDVVGCM 1152
Cdd:cd12878    1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1173335  1153 IDLTENTIIFTLNGEVLMSDSGSETAFRDIEVGDGFLPVCSLGPGQVGHLNLG 1205
Cdd:cd12878   81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 444-637 1.40e-81

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


Pssm-ID: 460175  Cd Length: 199  Bit Score: 267.91  E-value: 1.40e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     444 SLQDLIGYFEPPSEELQHEEKQSKL---RSLRNRQSLFQEEGMLSLVLNCIDRLN-VYTTAAHFAEFAGEEAAESWKEIV 519
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     520 NLLYEILASLIRGNRANCALFSNNLDWLVSKLDRLEASSGILEVLYCVLIESPE-VLNIIQENHIKSIISLLDKHGRNHK 598
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1173335     599 VLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNL 637
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 643-794 4.19e-79

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: 258.78  E-value: 4.19e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   643 SIRPNIFVGRAEGTTQYSKWYFEVMVDEVVPFlTAQATHLRVGWALTEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 722
Cdd:cd12877    1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173335   723 TGHVPRLVTSPGQHLLAPEDVVSCCLDLSVPSISFRINGCPVQGVFEAFNLNGLFFPVVSFSAGVKVRFLLG 794
Cdd:cd12877   80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4378-4668 9.48e-78

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: 260.40  E-value: 9.48e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4378 GMPDPTGDEVHGEQPAGPGGEADGEGAGEGAGEAWEGAGDEEVAVQEAGPGgadgavAVAEGGPFR---PEGAGGLGDMG 4454
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLADAAGGEEEEDLLSDIFGLI------LKKEGGQYKvvpHDPEAGLGDLS 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4455 DTTPAEPPtpegsPIIKRKLGVDGEEEELPPEPEPEPEPEPEKADAENGEKEEVPKPPPEPPKKTAPPPPPPKKEEG--- 4531
Cdd:pfam06459   75 ETTAEEPP-----PLLKRKLQESEEAEDEEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMKKKQRKRhsk 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4532 -----GSGGLEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDMEGSAAGDlsgagsggg 4606
Cdd:pfam06459  150 kkeepEAQGSAFWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGSGWGD--------- 220

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173335    4607 SGWGSGAGEEVEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVI 4668
Cdd:pfam06459  221 SGSGSGGGSGEDEEEEEGPVYFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1419-1567 1.25e-77

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: 254.54  E-value: 1.25e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1419 DDRDDPDIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMNFDLTKVRAVTVTMGDEQGNIHSSLKCSNCYMVWGG 1498
Cdd:cd12879    1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173335  1499 DFVSPGQQ--GRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVIQFELG 1567
Cdd:cd12879   81 ELLAEVGQdsSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 11-210 1.61e-76

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: 253.96  E-value: 1.61e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335      11 VQFLRTDDEVVLQCNATVLkeqlkLCLAAEGFGNRLCFLEPTSNAQNVPP-DLAICCFVLEQSLSVRALQEMLAN----- 84
Cdd:pfam08709    2 SSFLHIGDIVSLSCEESVN-----GFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWSAgnrsp 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335      85 ----TVEAGVESSQGGGHRTLLYGHAILLRHAHSGMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTTHPASKQRSEG 160
Cdd:pfam08709   77 ngnsLTDALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1173335     161 EKVRVGDDLILVSVSSERYLHLST-----ASGELQVDASFMQTLWNMNPICSGCE 210
Cdd:pfam08709  157 DNVCVGDEVILVPVSAPIFLHTTSsselrDNPGKEVNASFGQTSWKMEPFMSGCE 211
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 212-390 6.23e-75

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 248.43  E-value: 6.23e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     212 GYVTGGHVLRLFHGHMDECLTISPADS-DDQRRLVYYEGGSVCTHARSLWRLEPLRI-SWSGSHLRWGQPLRIRHVTTGR 289
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQkQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     290 YLALIEDQGLVVVDASKAHTKATSFCFRIS---KEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 366
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFpgdNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....
gi 1173335     367 LRLGVLKKKAILHQEGHMDDALSL 390
Cdd:pfam02815  161 WGFGPEQQKVTCAKEGHMDDALTL 184
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2162-2370 3.02e-71

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


Pssm-ID: 460175  Cd Length: 199  Bit Score: 238.25  E-value: 3.02e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2162 QIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMvNVLGG------------GESKEIRFPKM 2229
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlGEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2230 VTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGiGLGMQGSTpLDVAAASVIDNNELALalqeqdlekvvSYLAGCGLQ 2309
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLG-SPSLAEGT-LDVLTALLMDNPELLL-----------NYIKECHIK 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173335    2310 SCPMLLAKGYPDigwnpcggERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALR 2370
Cdd:pfam01365  147 SFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 851-940 2.42e-45

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 159.59  E-value: 2.42e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     851 FVPCPVDTVQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVDFHSLPEPERNYNLQMSGETLK 930
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335     931 TLLALGCHVG 940
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2736-2825 1.27e-42

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 151.89  E-value: 1.27e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2736 FDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLK 2815
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335    2816 AMIAWEWTIE 2825
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 965-1054 2.97e-37

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 136.48  E-value: 2.97e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     965 YKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVR 1044
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335    1045 TLLGYGYNIE 1054
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2856-2939 1.82e-34

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 128.77  E-value: 1.82e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2856 YNPQPPDLSGVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGG------THPLLVPYDTLTAKEKARDREKAQELLK 2929
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335    2930 FLQMNGYAVT 2939
Cdd:pfam02026   81 TLLALGYTIE 90
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1085-1207 3.01e-33

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 126.64  E-value: 3.01e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     1085 SGRWYFEFEAVTTGEMRVGWARPELRPDVE--LGADELAYVFNGHRGQRWHLG-SELFGRPWQ-SGDVVGCMIDLTENTI 1160
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNStGPEYGLPLQePGDVIGCFLDLEAGTI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 1173335     1161 IFTLNGEVLMsdsgsETAFRDIEVGDGFLPVCSLGPGQVGHLNLGQD 1207
Cdd:smart00449   81 SFYKNGKYLH-----GLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3872-3988 1.14e-31

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


Pssm-ID: 462482  Cd Length: 98  Bit Score: 121.09  E-value: 1.14e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    3872 DDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISdfywyysgkdvieeqgkrnfSKAMS 3951
Cdd:pfam08454    2 EVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN--------------------EKNIE 61

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1173335    3952 VAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFL 3988
Cdd:pfam08454   62 LIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4762-4946 8.64e-27

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


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 111.98  E-value: 8.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4762 LLTWLMSIDVKYQIWKFGVI---FTDNSFLYLGWYMVMSLLG------------HYNNFFFAAHLLDIAMGVKTLRTILS 4826
Cdd:pfam00520   41 VFTGIFTLEMLLKIIAAGFKkryFRSPWNILDFVVVLPSLISlvlssvgslsglRVLRLLRLLRLLRLIRRLEGLRTLVN 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4827 SVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVgvRAGGGIGDEIEDPAGDE 4906
Cdd:pfam00520  121 SLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGK 198

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1173335    4907 YELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQE 4946
Cdd:pfam00520  199 GEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 661-796 4.79e-26

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 105.89  E-value: 4.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     661 KWYFEVMVDevvpflTAQATHLRVGWAlTEGYSPYPGGGEGwggngvgDDLYSYGFDGlhlWTGHVPRLVTSP--GQHLL 738
Cdd:pfam00622    1 RHYFEVEIF------GQDGGGWRVGWA-TKSVPRKGERFLG-------DESGSWGYDG---WTGKKYWASTSPltGLPLF 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1173335     739 APEDVVSCCLDLSVPSISFRINGCPVQGVFEAFNLNGLFFPVVSFSAGVKVRFLLGGR 796
Cdd:pfam00622   64 EPGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1432-1569 2.47e-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: 103.96  E-value: 2.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    1432 TYYYSVRVFaGQEPSCVWVGWVTPDYHQHDMNFDltkvravtvtmGDEQGnihsslkcSNCYMVWGGDFVSPGQQGRISH 1511
Cdd:pfam00622    1 RHYFEVEIF-GQDGGGWRVGWATKSVPRKGERFL-----------GDESG--------SWGYDGWTGKKYWASTSPLTGL 60

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173335    1512 ----TDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNT-KLFPAVFVlpTHQNVIQFELGKQ 1569
Cdd:pfam00622   61 plfePGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSL--GAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1087-1207 5.85e-24

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: 100.11  E-value: 5.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    1087 RWYFEFE--AVTTGEMRVGWARPE--LRPDVELGADELAYVFNGHRGQR-WHLGSELFGRP-WQSGDVVGCMIDLTENTI 1160
Cdd:pfam00622    1 RHYFEVEifGQDGGGWRVGWATKSvpRKGERFLGDESGSWGYDGWTGKKyWASTSPLTGLPlFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1173335    1161 IFTLNGEVLMsdsgseTAFRDIEVGDGFLPVCSLGPGQVGHLNLGQD 1207
Cdd:pfam00622   81 SFTKNGKSLG------YAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1431-1569 3.18e-23

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 97.75  E-value: 3.18e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     1431 TTYYYSVRVFagqEPSCVWVGWVTPDYHQHDMNfdltkvravtvTMGDEQGNI-HSSLKCSNCYMVWGGDFVSPGQQgri 1509
Cdd:smart00449    2 GRHYFEVEIG---DGGHWRVGVATKSVPRGYFA-----------LLGEDKGSWgYDGDGGKKYHNSTGPEYGLPLQE--- 64

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173335     1510 shTDLVIGCLVDLATGLMTFTANGKESN--TFFQVEPNTKLFPAVFVLPThqNVIQFELGKQ 1569
Cdd:smart00449   65 --PGDVIGCFLDLEAGTISFYKNGKYLHglAFFDVKFSGPLYPAFSLGSG--NSVRLNFGPL 122
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 661-795 3.78e-18

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 83.50  E-value: 3.78e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335      661 KWYFEVMVDEvvpfltaqATHLRVGWALTEGYSPYpgggegwgGNGVGDDLYSYGFDGLHL---WTGHVPRLVTSPGQHL 737
Cdd:smart00449    3 RHYFEVEIGD--------GGHWRVGVATKSVPRGY--------FALLGEDKGSWGYDGDGGkkyHNSTGPEYGLPLQEPG 66

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1173335      738 lapeDVVSCCLDLSVPSISFRINGCPVQGV-FEAFNLNGLFFPVVSFSAGVKVRFLLGG 795
Cdd:smart00449   67 ----DVIGCFLDLEAGTISFYKNGKYLHGLaFFDVKFSGPLYPAFSLGSGNSVRLNFGP 121
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
211-264 7.03e-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: 7.03e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1173335      211 EGYVTGGHVLRLFHGHMDECLTIS----PADSDDQRRLVYYEGGsvCTHARSLWRLEP 264
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHdeklPPWGDGQQEVTGYGNP--AIDANTLWLIEP 56
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
98-153 7.78e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 7.78e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1173335       98 HRTLLYGHAILLRHAHSGMYLSCLTTSRSMTDKLAFDVGLQEDATG-EACWWTTHPA 153
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 44-240 9.16e-06

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: 49.69  E-value: 9.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    44 NRLCFLEPTSNAQNVPPDLAICCFVLEqslsvralqemlantveaGVESSQGGGhrTLLYGHAILLRHAHSGMYLsCLTt 123
Cdd:cd23280   41 LRVRPVDDRKPRTLFPPTSGDTFWQIE------------------KEDTPLKGG--VIKWGDQCRLRHLPTGKYL-AVD- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   124 srsmTDKLAFDVGLQEDATGEACWWTTHPASKQRSEGekVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMN 203
Cdd:cd23280   99 ----DKTGNGKVVLTSDPSDPSTVFRLHPVTKETSEE--VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGLSWDGA 172

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1173335   204 PIC--SGCEEgyvtgghvlrlfhGHMDECLTISPADSDD 240
Cdd:cd23280  173 KLRkvSLSLE-------------RQDDDAFTIQEVDPDL 198
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 207-398 1.86e-131

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: 410.43  E-value: 1.86e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   207 SGCEEGYVTGGHVLRLFHGHMDECLTISPADSDDQRRLVYYEGGSVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 286
Cdd:cd23290    1 SCCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   287 TGRYLALIEDQGLVVVDASKAHTKATSFCFRISKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 366
Cdd:cd23290   81 TGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 1173335   367 LRLGVLKKKAILHQEGHMDDALSLTRCQQEES 398
Cdd:cd23290  161 LRLGVLKKKAILHQEGHMDDALFLTRCQQEES 192
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 216-394 1.15e-108

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: 344.68  E-value: 1.15e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   216 GGHVLRLFHGHMDECLTISPADS-DDQRRLVYYEGGSVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALI 294
Cdd:cd23278    1 GGDVLRLFHGHMDECLTIPAAGSkEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   295 EDQGLVVVDASKAHTKATSFCFRISKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKK 374
Cdd:cd23278   81 EDRGLVLVPKEKADVKATAFCFRQSKDDKKVLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVETKKRVGGVEER 160

                        170       180
                 ....*....|....*....|
gi 1173335   375 KAILHQEGHMDDALSLTRCQ 394
Cdd:cd23278  161 KAILHAEGHMDDGLSLSRAQ 180
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 212-398 7.73e-102

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: 325.71  E-value: 7.73e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   212 GYVTGGHVLRLFHGHmDECLTISPAD-SDDQRRLVYYEGGSVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRY 290
Cdd:cd23292    1 GYLLGGHVVRLFHGH-DECLTIPSTDqSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   291 LALIEDQGLVVVDASKAHTKATSFCFRISKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLG 370
Cdd:cd23292   80 LALTEDQGLILQDRAKSDTKSTAFCFRASKEKLESGPKRDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSRLG 159

                        170       180
                 ....*....|....*....|....*...
gi 1173335   371 VLKKKAILHQEGHMDDALSLTRCQQEES 398
Cdd:cd23292  160 PLKRRAILHQEGHMDDGLTLQRCQHEES 187
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1073-1205 1.18e-81

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: 265.32  E-value: 1.18e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1073 RIFRAEKSYAVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLGSELFGRPWQSGDVVGCM 1152
Cdd:cd12878    1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1173335  1153 IDLTENTIIFTLNGEVLMSDSGSETAFRDIEVGDGFLPVCSLGPGQVGHLNLG 1205
Cdd:cd12878   81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 444-637 1.40e-81

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


Pssm-ID: 460175  Cd Length: 199  Bit Score: 267.91  E-value: 1.40e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     444 SLQDLIGYFEPPSEELQHEEKQSKL---RSLRNRQSLFQEEGMLSLVLNCIDRLN-VYTTAAHFAEFAGEEAAESWKEIV 519
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     520 NLLYEILASLIRGNRANCALFSNNLDWLVSKLDRLEASSGILEVLYCVLIESPE-VLNIIQENHIKSIISLLDKHGRNHK 598
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1173335     599 VLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNL 637
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 216-398 4.96e-81

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: 265.75  E-value: 4.96e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   216 GGHVLRLFHGHMDECLTISPAD-SDDQRRLVYYEGGSVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALI 294
Cdd:cd23291    1 GGDVLRLLHGHMDECLTVPSGEhGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   295 EDQGLVVVDASKAHTKATSFCFRISKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKK 374
Cdd:cd23291   81 EDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSIQR 160

                        170       180
                 ....*....|....*....|....
gi 1173335   375 KAILHQEGHMDDALSLTRCQQEES 398
Cdd:cd23291  161 KAIMHHEGHMDDGLNLSRSQHEES 184
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 643-794 4.19e-79

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: 258.78  E-value: 4.19e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   643 SIRPNIFVGRAEGTTQYSKWYFEVMVDEVVPFlTAQATHLRVGWALTEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 722
Cdd:cd12877    1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173335   723 TGHVPRLVTSPGQHLLAPEDVVSCCLDLSVPSISFRINGCPVQGVFEAFNLNGLFFPVVSFSAGVKVRFLLG 794
Cdd:cd12877   80 TGGRSRRVTSGTQHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4378-4668 9.48e-78

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: 260.40  E-value: 9.48e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4378 GMPDPTGDEVHGEQPAGPGGEADGEGAGEGAGEAWEGAGDEEVAVQEAGPGgadgavAVAEGGPFR---PEGAGGLGDMG 4454
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLADAAGGEEEEDLLSDIFGLI------LKKEGGQYKvvpHDPEAGLGDLS 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4455 DTTPAEPPtpegsPIIKRKLGVDGEEEELPPEPEPEPEPEPEKADAENGEKEEVPKPPPEPPKKTAPPPPPPKKEEG--- 4531
Cdd:pfam06459   75 ETTAEEPP-----PLLKRKLQESEEAEDEEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMKKKQRKRhsk 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4532 -----GSGGLEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDMEGSAAGDlsgagsggg 4606
Cdd:pfam06459  150 kkeepEAQGSAFWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGSGWGD--------- 220

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173335    4607 SGWGSGAGEEVEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVI 4668
Cdd:pfam06459  221 SGSGSGGGSGEDEEEEEGPVYFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1419-1567 1.25e-77

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: 254.54  E-value: 1.25e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1419 DDRDDPDIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMNFDLTKVRAVTVTMGDEQGNIHSSLKCSNCYMVWGG 1498
Cdd:cd12879    1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173335  1499 DFVSPGQQ--GRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVIQFELG 1567
Cdd:cd12879   81 ELLAEVGQdsSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 11-210 1.61e-76

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: 253.96  E-value: 1.61e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335      11 VQFLRTDDEVVLQCNATVLkeqlkLCLAAEGFGNRLCFLEPTSNAQNVPP-DLAICCFVLEQSLSVRALQEMLAN----- 84
Cdd:pfam08709    2 SSFLHIGDIVSLSCEESVN-----GFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWSAgnrsp 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335      85 ----TVEAGVESSQGGGHRTLLYGHAILLRHAHSGMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTTHPASKQRSEG 160
Cdd:pfam08709   77 ngnsLTDALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1173335     161 EKVRVGDDLILVSVSSERYLHLST-----ASGELQVDASFMQTLWNMNPICSGCE 210
Cdd:pfam08709  157 DNVCVGDEVILVPVSAPIFLHTTSsselrDNPGKEVNASFGQTSWKMEPFMSGCE 211
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 212-390 6.23e-75

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 248.43  E-value: 6.23e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     212 GYVTGGHVLRLFHGHMDECLTISPADS-DDQRRLVYYEGGSVCTHARSLWRLEPLRI-SWSGSHLRWGQPLRIRHVTTGR 289
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQkQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     290 YLALIEDQGLVVVDASKAHTKATSFCFRIS---KEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKA 366
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFpgdNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....
gi 1173335     367 LRLGVLKKKAILHQEGHMDDALSL 390
Cdd:pfam02815  161 WGFGPEQQKVTCAKEGHMDDALTL 184
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2162-2370 3.02e-71

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


Pssm-ID: 460175  Cd Length: 199  Bit Score: 238.25  E-value: 3.02e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2162 QIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMvNVLGG------------GESKEIRFPKM 2229
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlGEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2230 VTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGiGLGMQGSTpLDVAAASVIDNNELALalqeqdlekvvSYLAGCGLQ 2309
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLG-SPSLAEGT-LDVLTALLMDNPELLL-----------NYIKECHIK 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1173335    2310 SCPMLLAKGYPDigwnpcggERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALR 2370
Cdd:pfam01365  147 SFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 851-940 2.42e-45

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 159.59  E-value: 2.42e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     851 FVPCPVDTVQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVDFHSLPEPERNYNLQMSGETLK 930
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335     931 TLLALGCHVG 940
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2736-2825 1.27e-42

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 151.89  E-value: 1.27e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2736 FDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLK 2815
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335    2816 AMIAWEWTIE 2825
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 965-1054 2.97e-37

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 136.48  E-value: 2.97e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     965 YKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVR 1044
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335    1045 TLLGYGYNIE 1054
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2856-2939 1.82e-34

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 128.77  E-value: 1.82e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    2856 YNPQPPDLSGVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGG------THPLLVPYDTLTAKEKARDREKAQELLK 2929
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1173335    2930 FLQMNGYAVT 2939
Cdd:pfam02026   81 TLLALGYTIE 90
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1085-1207 3.01e-33

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 126.64  E-value: 3.01e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     1085 SGRWYFEFEAVTTGEMRVGWARPELRPDVE--LGADELAYVFNGHRGQRWHLG-SELFGRPWQ-SGDVVGCMIDLTENTI 1160
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNStGPEYGLPLQePGDVIGCFLDLEAGTI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 1173335     1161 IFTLNGEVLMsdsgsETAFRDIEVGDGFLPVCSLGPGQVGHLNLGQD 1207
Cdd:smart00449   81 SFYKNGKYLH-----GLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3872-3988 1.14e-31

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


Pssm-ID: 462482  Cd Length: 98  Bit Score: 121.09  E-value: 1.14e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    3872 DDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISdfywyysgkdvieeqgkrnfSKAMS 3951
Cdd:pfam08454    2 EVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN--------------------EKNIE 61

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1173335    3952 VAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFL 3988
Cdd:pfam08454   62 LIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1086-1203 3.95e-29

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


Pssm-ID: 293931  Cd Length: 118  Bit Score: 114.45  E-value: 3.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1086 GRWYFEFEAVTT--GEMRVGWARPELRPDVE--LGADELAYVFNGHRGQRWHLGSEL-FGRPWQSGDVVGCMIDLTENTI 1160
Cdd:cd11709    1 GKWYWEVRVDSGngGLIQVGWATKSFSLDGEggVGDDEESWGYDGSRLRKGHGGSSGpGGRPWKSGDVVGCLLDLDEGTL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 1173335  1161 IFTLNGEVLMsdsgseTAFRDI-EVGDGFLPVCSLGPGQVGHLN 1203
Cdd:cd11709   81 SFSLNGKDLG------VAFTNLfLKGGGLYPAVSLGSGQGVTIN 118
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4762-4946 8.64e-27

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


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 111.98  E-value: 8.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4762 LLTWLMSIDVKYQIWKFGVI---FTDNSFLYLGWYMVMSLLG------------HYNNFFFAAHLLDIAMGVKTLRTILS 4826
Cdd:pfam00520   41 VFTGIFTLEMLLKIIAAGFKkryFRSPWNILDFVVVLPSLISlvlssvgslsglRVLRLLRLLRLLRLIRRLEGLRTLVN 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    4827 SVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVgvRAGGGIGDEIEDPAGDE 4906
Cdd:pfam00520  121 SLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGK 198

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1173335    4907 YELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQE 4946
Cdd:pfam00520  199 GEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 661-796 4.79e-26

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 105.89  E-value: 4.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     661 KWYFEVMVDevvpflTAQATHLRVGWAlTEGYSPYPGGGEGwggngvgDDLYSYGFDGlhlWTGHVPRLVTSP--GQHLL 738
Cdd:pfam00622    1 RHYFEVEIF------GQDGGGWRVGWA-TKSVPRKGERFLG-------DESGSWGYDG---WTGKKYWASTSPltGLPLF 63

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1173335     739 APEDVVSCCLDLSVPSISFRINGCPVQGVFEAFNLNGLFFPVVSFSAGVKVRFLLGGR 796
Cdd:pfam00622   64 EPGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1432-1569 2.47e-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: 103.96  E-value: 2.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    1432 TYYYSVRVFaGQEPSCVWVGWVTPDYHQHDMNFDltkvravtvtmGDEQGnihsslkcSNCYMVWGGDFVSPGQQGRISH 1511
Cdd:pfam00622    1 RHYFEVEIF-GQDGGGWRVGWATKSVPRKGERFL-----------GDESG--------SWGYDGWTGKKYWASTSPLTGL 60

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173335    1512 ----TDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNT-KLFPAVFVlpTHQNVIQFELGKQ 1569
Cdd:pfam00622   61 plfePGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSL--GAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1087-1207 5.85e-24

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: 100.11  E-value: 5.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    1087 RWYFEFE--AVTTGEMRVGWARPE--LRPDVELGADELAYVFNGHRGQR-WHLGSELFGRP-WQSGDVVGCMIDLTENTI 1160
Cdd:pfam00622    1 RHYFEVEifGQDGGGWRVGWATKSvpRKGERFLGDESGSWGYDGWTGKKyWASTSPLTGLPlFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1173335    1161 IFTLNGEVLMsdsgseTAFRDIEVGDGFLPVCSLGPGQVGHLNLGQD 1207
Cdd:pfam00622   81 SFTKNGKSLG------YAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1431-1569 3.18e-23

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 97.75  E-value: 3.18e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335     1431 TTYYYSVRVFagqEPSCVWVGWVTPDYHQHDMNfdltkvravtvTMGDEQGNI-HSSLKCSNCYMVWGGDFVSPGQQgri 1509
Cdd:smart00449    2 GRHYFEVEIG---DGGHWRVGVATKSVPRGYFA-----------LLGEDKGSWgYDGDGGKKYHNSTGPEYGLPLQE--- 64

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173335     1510 shTDLVIGCLVDLATGLMTFTANGKESN--TFFQVEPNTKLFPAVFVLPThqNVIQFELGKQ 1569
Cdd:smart00449   65 --PGDVIGCFLDLEAGTISFYKNGKYLHglAFFDVKFSGPLYPAFSLGSG--NSVRLNFGPL 122
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 1082-1205 3.51e-23

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: 97.78  E-value: 3.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1082 AVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADEL--AYVFNGHRGQRWHLGSELFGRPWQSGDVVGCMIDLTENT 1159
Cdd:cd12882    7 CVYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDTrdSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDLDKGT 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 1173335  1160 IIFTLNGEVLmsdsgsETAFRDIEVGDG--FLPVCSLGPGQVGHLNLG 1205
Cdd:cd12882   87 ISFYRNGRSL------GVAFDNVRRGPGlaYFPAVSLSFGERLELNFG 128
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 661-792 2.00e-19

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


Pssm-ID: 293931  Cd Length: 118  Bit Score: 86.72  E-value: 2.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   661 KWYFEVMVDevvpflTAQATHLRVGWAlTEGYSPYPGGGEGwggngvgDDLYSYGFDGLHLWTGHVPRlvTSPGQHLLAP 740
Cdd:cd11709    2 KWYWEVRVD------SGNGGLIQVGWA-TKSFSLDGEGGVG-------DDEESWGYDGSRLRKGHGGS--SGPGGRPWKS 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 1173335   741 EDVVSCCLDLSVPSISFRINGCPVQGVFEAFNL-NGLFFPVVSFSAGVKVRFL 792
Cdd:cd11709   66 GDVVGCLLDLDEGTLSFSLNGKDLGVAFTNLFLkGGGLYPAVSLGSGQGVTIN 118
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 661-795 3.78e-18

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 83.50  E-value: 3.78e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335      661 KWYFEVMVDEvvpfltaqATHLRVGWALTEGYSPYpgggegwgGNGVGDDLYSYGFDGLHL---WTGHVPRLVTSPGQHL 737
Cdd:smart00449    3 RHYFEVEIGD--------GGHWRVGVATKSVPRGY--------FALLGEDKGSWGYDGDGGkkyHNSTGPEYGLPLQEPG 66

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1173335      738 lapeDVVSCCLDLSVPSISFRINGCPVQGV-FEAFNLNGLFFPVVSFSAGVKVRFLLGG 795
Cdd:smart00449   67 ----DVIGCFLDLEAGTISFYKNGKYLHGLaFFDVKFSGPLYPAFSLGSGNSVRLNFGP 121
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 211-357 3.40e-15

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: 77.43  E-value: 3.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   211 EGYVTGGHVLRLFHGHMD-----ECLTISPADSDDQRRLVYY------EGGSVCTHARSLWRLEPLRISWSGSHLRWGQP 279
Cdd:cd23280    4 ENFLKGGDVVRLFHKELEaylsaEGSFVDEVLTEDVHLRVRPvddrkpRTLFPPTSGDTFWQIEKEDTPLKGGVIKWGDQ 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173335   280 LRIRHVTTGRYLALIEDQGLVVVDA-SKAHTKATSFCFriskekldtapkRDVEGMGPPEIKYGeSLCFVQHVASGLWL 357
Cdd:cd23280   84 CRLRHLPTGKYLAVDDKTGNGKVVLtSDPSDPSTVFRL------------HPVTKETSEEVKFG-SYVRIEHVATGTWL 149
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 1080-1205 4.51e-15

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: 75.63  E-value: 4.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1080 SYAVQSGRWYFEFE-----AVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLG-SELFGRPW-QSGDVVGCM 1152
Cdd:cd12872   22 NHGVREGKWYFEVKileggGTETGHVRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFHQSrGKPYGEPGfKEGDVIGFL 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1173335  1153 IDLTEntIIFTLNGEVLMsdsgseTAFRDIEVGDGFLPVCSL-GPGQVgHLNLG 1205
Cdd:cd12872  102 ITLPK--IEFFKNGKSQG------VAFEDIYGTGGYYPAVSLyKGATV-TINFG 146
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 1086-1205 1.13e-12

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: 67.76  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1086 GRWYFEFEAVTTGEMRVGWARPELRPDVE----LGADELAYVFNGHRGQRWH-LGSELFGRP-WQSGDVVGCMIDLTENT 1159
Cdd:cd12883    1 GVWYYEVTVLTSGVMQIGWATKDSKFLNHegygIGDDEYSCAYDGCRQLIWYnAKSKPHTHPrWKPGDVLGCLLDLNKKQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 1173335  1160 IIFTLNGEVLMSDSGSETAFRdievgDGFLPVCSLGPGQVGHLNLG 1205
Cdd:cd12883   81 MIFSLNGNRLPPERQVFTSAK-----SGFFAAASFMSFQQCEFNFG 121
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 217-357 1.37e-11

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


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 66.25  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   217 GHVLRLFHGHMDECLTIS--PADSDDQRRLVYYEGGSVCTHARSLWRLEPLRISWsGSHLRWGQPLRIRHVTTGRYLALI 294
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHrkNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173335   295 E------DQGLVVVDASKAHTKATSFCFRISKEKLDTapkrdvegmgpPEIKYGESLCFVQHVASGLWL 357
Cdd:cd23263   80 EgkkspkSNHQEVLCLTDNPDKSSLFKFEPIGSTKYK-----------QKYVKKDSYFRLKHVNTNFWL 137
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 1066-1206 2.48e-11

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: 64.90  E-value: 2.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1066 QSRWDRV-RIFRAEKSyAVQSGRWYFEFEAVTTGEMRVGWArpELRPDVELGADELAYVFNGHrGQRWHLGS-ELFGRPW 1143
Cdd:cd12873   20 QSREEKGwQGCRATKG-VKGKGKYYYEVTVTDEGLCRVGWS--TEDASLDLGTDKFGFGYGGT-GKKSHGRQfDDYGEPF 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173335  1144 QSGDVVGCMIDLTENTIIFTLNGEVLmsdsgsETAFrDIEV---GDGFLPVCSLGPGQVGhLNLGQ 1206
Cdd:cd12873   96 GLGDVIGCYLDLDNGTISFSKNGKDL------GKAF-DIPPhlrNSALFPAVCLKNAEVE-FNFGD 153
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 1073-1205 7.41e-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: 62.68  E-value: 7.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1073 RIFRAEKSYAVQSGRWYFE---FEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQ--RWHLGSELFGRPWQSGD 1147
Cdd:cd12885    1 GSVRADHPIPPKVPVFYFEvtiLDLGEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRvyLGGGEGENYGPPFGTGD 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 1173335  1148 VVGCMIDLTENTIIFTLNGEVLmsdsgsETAFRDIEVGDgFLPVCSLG-PGQVGHLNLG 1205
Cdd:cd12885   81 VVGCGINFKTGEVFFTKNGELL------GTAFENVVKGR-LYPTVGLGsPGVKVRVNFG 132
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1433-1559 5.44e-09

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


Pssm-ID: 293931  Cd Length: 118  Bit Score: 57.06  E-value: 5.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1433 YYYSVRVFAGQePSCVWVGWVTPDyhqhdmnFDLTKVRAVtvtMGDEQG---NIHSSLKCSNCYmvwGGDFVSPGQQGri 1509
Cdd:cd11709    3 WYWEVRVDSGN-GGLIQVGWATKS-------FSLDGEGGV---GDDEESwgyDGSRLRKGHGGS---SGPGGRPWKSG-- 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1173335  1510 shtDlVIGCLVDLATGLMTFTANGKESNTFFQVEPNTK--LFPAVFVLPTHQ 1559
Cdd:cd11709   67 ---D-VVGCLLDLDEGTLSFSLNGKDLGVAFTNLFLKGggLYPAVSLGSGQG 114
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 1087-1197 9.66e-09

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: 57.32  E-value: 9.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1087 RWYFEF-----EAVTTGE--MRVGWA-----RPELRPD-----VELGADELAYVFNG------HRGQRWHLGSELFGRPw 1143
Cdd:cd12877   19 KWYFEVevdhvEQFTHQPahLRVGWAntsgyVPYPGGGegwggNGVGDDLYSYGFDGlhlwtgGRSRRVTSGTQHLLKK- 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1173335  1144 qsGDVVGCMIDLTENTIIFTLNGEVLmsdsgsETAFRDIEVGDGFLPVCSLGPG 1197
Cdd:cd12877   98 --GDVVGCCLDLSVPSISFRVNGRPV------QGMFENFNLDGMFFPVMSFSAG 143
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 1076-1206 4.14e-08

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: 55.22  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1076 RAEKSYAVQSGRWYFEFEAVTTGE---MRVGWARPelrpDVEL----GADELAYVFNGHRGqrwHL----GSEL-FGRPW 1143
Cdd:cd12909   15 RANHPIPPQCGIYYFEVKIISKGRdgyIGIGFSTK----DVNLnrlpGWEPHSWGYHGDDG---HSfcssGTGKpYGPTF 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173335  1144 QSGDVVGCMIDLTENTIIFTLNGEVLmsdsgsETAFRDIEVGDgFLPVCSL-GPGQVGHLNLGQ 1206
Cdd:cd12909   88 TTGDVIGCGINFRDNTAFYTKNGVNL------GIAFRDIKKGN-LYPTVGLrTPGEHVEANFGQ 144
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 643-791 1.49e-07

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: 53.68  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   643 SIRPNIFVgrAEGttqysKWYFEVMVDEVVPFLTAqatHLRVGWALTE-------GYspypgggegwggngvgdDLYSYG 715
Cdd:cd12872   18 MARANHGV--REG-----KWYFEVKILEGGGTETG---HVRVGWSRREaslqapvGY-----------------DKYSYA 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173335   716 FDGLHLWTGHVPRLvTSPGQHLLAPEDVVSCCLDLsvPSISFRINGCPvQGV-FEAFNLNGLFFPVVS--FSAGVKVRF 791
Cdd:cd12872   71 IRDKDGSKFHQSRG-KPYGEPGFKEGDVIGFLITL--PKIEFFKNGKS-QGVaFEDIYGTGGYYPAVSlyKGATVTINF 145
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 1076-1169 4.38e-07

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: 53.36  E-value: 4.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1076 RAekSYAVQSGRWYFE-------------FEAVTTGEMRVGWARPelRPDVELGADELAYVFNGhRGQRWHLG-SELFGR 1141
Cdd:cd12884   37 RA--TYGVTKGKVCFEvkvtenlpvkhlpTEETDPHVVRVGWSVD--SSSLQLGEEEFSYGYGS-TGKKSTNCkFEDYGE 111

                         90       100       110
                 ....*....|....*....|....*....|
gi 1173335  1142 PWQSGDVVGCMIDL--TENTIIFTLNGEVL 1169
Cdd:cd12884  112 PFGENDVIGCYLDFesEPVEISFSKNGKDL 141
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
211-264 7.03e-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: 7.03e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1173335      211 EGYVTGGHVLRLFHGHMDECLTIS----PADSDDQRRLVYYEGGsvCTHARSLWRLEP 264
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHdeklPPWGDGQQEVTGYGNP--AIDANTLWLIEP 56
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
271-359 3.12e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 47.34  E-value: 3.12e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335      271 GSHLRWGQPLRIRHVTTGRYLALiedqglvvvdaskaHTKatsfcfrisKEKLDTAPKRDVEGMGPPEIkygeslcfvqh 350
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHS--------------HDE---------KLPPWGDGQQEVTGYGNPAI----------- 46


                    ....*....
gi 1173335      351 VASGLWLTY 359
Cdd:smart00472   47 DANTLWLIE 55
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 652-794 3.24e-06

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: 49.61  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   652 RAEGTTQYS--KWYFEVmvdEVVpfltaQATHLRVGWALTEGYSPYPGGGegwggngvgDDLySYGFDGlHL---WTGHV 726
Cdd:cd12878    4 RAEKTYAVTsgKWYFEF---EVL-----TSGYMRVGWARPGFRPDLELGS---------DDL-SYAFDG-FLarkWHQGS 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1173335   727 prlvTSPGQHLlAPEDVVSCCLDLSVPSISFRING---CPVQG---VFEAFNLNGLFFPVVSFSAGVKVRFLLG 794
Cdd:cd12878   65 ----ESFGKQW-QPGDVVGCMLDLVDRTISFTLNGellIDSSGsevAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
98-153 7.78e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 7.78e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1173335       98 HRTLLYGHAILLRHAHSGMYLSCLTTSRSMTDKLAFDVGLQEDATG-EACWWTTHPA 153
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 44-240 9.16e-06

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: 49.69  E-value: 9.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335    44 NRLCFLEPTSNAQNVPPDLAICCFVLEqslsvralqemlantveaGVESSQGGGhrTLLYGHAILLRHAHSGMYLsCLTt 123
Cdd:cd23280   41 LRVRPVDDRKPRTLFPPTSGDTFWQIE------------------KEDTPLKGG--VIKWGDQCRLRHLPTGKYL-AVD- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   124 srsmTDKLAFDVGLQEDATGEACWWTTHPASKQRSEGekVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMN 203
Cdd:cd23280   99 ----DKTGNGKVVLTSDPSDPSTVFRLHPVTKETSEE--VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGLSWDGA 172

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 1173335   204 PIC--SGCEEgyvtgghvlrlfhGHMDECLTISPADSDD 240
Cdd:cd23280  173 KLRkvSLSLE-------------RQDDDAFTIQEVDPDL 198
SPRY_SSH4_like cd12910
SPRY domain in SSH4 and similar proteins; This family includes SPRY domain in SSH4 (suppressor ...
 1120-1207 1.95e-05

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


Pssm-ID: 293967  Cd Length: 192  Bit Score: 48.51  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1120 LAYVF-NGHR--GQRWhlGSELFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMS-DSGSETAFRD--IEVGDGFLPV-- 1191
Cdd:cd12910   96 LAVHSdDGHRyiNDPF--GGKDFTPPFREGDTIGIGYRFSSGTIFFTRNGKRLGGwDLGEELDAEDdgVTGLEGFHDLya 173

                         90
                 ....*....|....*....
gi 1173335  1192 ---CSLGPGQVgHLNLGQD 1207
Cdd:cd12910  174 aigVFGGECEV-HVNPGQW 191
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 662-794 8.06e-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: 45.42  E-value: 8.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   662 WYFEVMVdevvpfLTAQAthLRVGWALT-------EGYSpypgggegwggngVGDDLYSYGFDGLH--LWTGHVPRLVTS 732
Cdd:cd12883    3 WYYEVTV------LTSGV--MQIGWATKdskflnhEGYG-------------IGDDEYSCAYDGCRqlIWYNAKSKPHTH 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173335   733 PGQHllaPEDVVSCCLDLSVPSISFRINGCPVQGVFEAFN-LNGLFFPVVSFSAGVKVRFLLG 794
Cdd:cd12883   62 PRWK---PGDVLGCLLDLNKKQMIFSLNGNRLPPERQVFTsAKSGFFAAASFMSFQQCEFNFG 121
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 1086-1195 2.02e-04

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


Pssm-ID: 293944  Cd Length: 129  Bit Score: 44.42  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1086 GRWYFEFEAVTTGE---MRVGWARPELRPDVELGADELA---YVFNGHRGQRWHLGSE--LFGRPWQSGDVVGCMIDLTE 1157
Cdd:cd12886    1 GKWYWEVTVVSSAAstyAGIGVANAAATGNNGLNGIELSsigYSLGVYSGNKLSNGSSvaTYGAGFTAGDVIGVALDLDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 1173335  1158 NTIIFTLNGeVLMSDSGSETAFRDIEVGDGFLPVCSLG 1195
Cdd:cd12886   81 GKIWFYKNG-VWQGGGDPAPGTNPAFAGTAMYPAVTGG 117
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 211-357 2.79e-04

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: 45.42  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   211 EGYVTGGHVLRLFHGHMDECLTispADSDDQRRLVYYE--GGSVCTHARS---LWRLE-----PLRiswsGSHLRWGQPL 280
Cdd:cd23277    8 EDVLKGGDVVRLFHAEQEKFLT---CDEYKKKQYVFLRttGRTSATSATSskaLWEVEvvqhdPCR----GGAGHWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   281 RIRHVTTGRYLALIEDQglvvvDASKAHTKATSfcfRISKEK----LDTAPKR-DVEG---MGPPEIKYGESL----CFV 348
Cdd:cd23277   81 RFKHLATGQYLAAEVDP-----DPTPDPTRSKL---RGAPGKpvycLVSVPHGnDIASifeLDPTTLQRGDSLvprsSYV 152

                        170
                 ....*....|.
gi 1173335   349 --QHVASGLWL 357
Cdd:cd23277  153 rlRHLCTNTWV 163
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
160-205 2.83e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.56  E-value: 2.83e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1173335      160 GEKVRVGDDLILVSVSSERYLHLSTA------SGELQVDAS-----FMQTLWNMNPI 205
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEklppwgDGQQEVTGYgnpaiDANTLWLIEPV 57
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 1426-1552 6.78e-04

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: 43.04  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1426 IILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMnfdltkvravtvtMGDEQGNIhsSLKCSNCYMVWGGDfvSPGQ 1505
Cdd:cd12885    9 IPPKVPVFYFEVTILDLGEKGIVSIGFCTSGFPLNRM-------------PGWEDGSY--GYHGDDGRVYLGGG--EGEN 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 1173335  1506 QGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAV 1552
Cdd:cd12885   72 YGPPFGTGDVVGCGINFKTGEVFFTKNGELLGTAFENVVKGRLYPTV 118
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 1433-1552 7.12e-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: 7.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335  1433 YYYSVRVfagQEPSCVWVGWVTPDyhqhdMNFDLTKvravtvtmgDEQGnihsslkcsncymvWGgdFvspGQQGRISHT 1512
Cdd:cd12873   42 YYYEVTV---TDEGLCRVGWSTED-----ASLDLGT---------DKFG--------------FG--Y---GGTGKKSHG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 1173335  1513 DL------------VIGCLVDLATGLMTFTANGKESNTFFQVEPNTK---LFPAV 1552
Cdd:cd12873   86 RQfddygepfglgdVIGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRnsaLFPAV 140
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 709-786 4.31e-03

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


Pssm-ID: 293940  Cd Length: 128  Bit Score: 40.39  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173335   709 DDLYSYGFDGLHLWTGHVPrlVTSPGQHLLAPeDVVSCCLDLSVPSISFRINGCPVqGVfeAFN----LNGL-FFPVVSF 783
Cdd:cd12882   44 DTRDSYAYDGNRVRKWNVS--TQKYGEPWVAG-DVIGCCIDLDKGTISFYRNGRSL-GV--AFDnvrrGPGLaYFPAVSL 117


                 ...
gi 1173335   784 SAG 786
Cdd:cd12882  118 SFG 120
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH