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Conserved domains on  [gi|1254045463|ref|NP_001343815|]
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Ryanodine receptor [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 222-401 5.06e-102

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: 325.80  E-value: 5.06e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  222 GNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYLGVL 300
Cdd:cd23278      1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  301 -DNSVQLYHKEKADFDLTAFVMCQNKDPKKqMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEvTKKGLGKVE 379
Cdd:cd23278     81 eDRGLVLVPKEKADVKATAFCFRQSKDDKK-VLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVE-TKKRVGGVE 158

                          170       180
                   ....*....|....*....|..
gi 1254045463  380 EKKAVALKDGHMDDCYTFFMAL 401
Cdd:cd23278    159 ERKAILHAEGHMDDGLSLSRAQ 180
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 650-797 1.65e-84

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: 274.19  E-value: 1.65e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  650 SMMPNVMLGVVEGSALFRKWYFEAEVEHIETMTKQTPYLRIGWANSVGFKPFPGSGDKMGCNGVGDDFYSYGFDGKSMYF 729
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTHQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLWT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254045463  730 GGKSRRVGH---KLLEKGDVIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSLSAKVSCRFILG 797
Cdd:cd12877     81 GGRSRRVTSgtqHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1076-1208 2.14e-83

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: 270.33  E-value: 2.14e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1076 RTYRAEATYAVCGGKWYFEFEILTAGYMKIGWMDIGSTPEIQLGADDRSYAFDGYLGRKWHQGAETYGKEWKIGDVVGCF 1155
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1254045463 1156 LDLNDRTISFSLNGELLLDPSGSEMAFDNVVCGDGLVPAMTLGSGQRGRLNFG 1208
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 449-644 1.24e-75

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


:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 250.96  E-value: 1.24e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  449 LMEDLIEYFAQPNDEQDFEEKQNHL---RALRSRQDLFQEEGVLNMILDTIDKFS-QMEALPDFAGLIGEETHVKWEQIS 524
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  525 TYLYLLVAAMIKGNHYNCAQFASAqrLDWLFGRLSNPQSAEGILDVLYCVLTESPE-ALNMINEGHIRSVISLLEKVGRD 603
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKH--LDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRD 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1254045463  604 PKVLDVLSSLCEGNGMAVRSSQNLITQYLLPGKDLLLQTSM 644
Cdd:pfam01365  159 PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1540-1690 4.10e-72

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


:

Pssm-ID: 293937  Cd Length: 151  Bit Score: 238.74  E-value: 4.10e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1540 DAHALVHHKDKVDEYYYGIRIFPGQDPSQVWVGWVTTQYHYYNVNFDGSQgVRKCRFSEADHHGTTVDSVQSQNCYMVNV 1619
Cdd:cd12879      1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDK-VRNVTVTMGDEKGGVYESIKRQNCYMVCA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254045463 1620 SELLA-TTPDVANTKVSGTLIGCIIDTSIGELSFQVGSTDTGIKFKLEPGAMLFPAAFVTPTATEILQFELG 1690
Cdd:cd12879     80 GELLAeVGQDSSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2242-2465 3.38e-65

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: 220.92  E-value: 3.38e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2242 QIRELLTVQFEHTEEAILKRGLWKLMNNRIFFQHPDLMRLLSVHENVMSImMNILTAQQGTVEHEGDELKEKAPIkDASE 2321
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEV-IDLLGAPFTGALLFAEDLGEEKNA-PWKK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2322 MVVACSRFLCYFCRTSRQNQKAMFEHLSFLLDNatmlLARPSLRGSVpLDVAYSSFMDNNELALalkeeeldkvaVYLSR 2401
Cdd:pfam01365   79 IVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKE 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254045463 2402 CGLQPNSELITKGYPDigwdpvegERYIDFLRF-CVwINGENVEENANLVIRLLIRRPECLGVAL 2465
Cdd:pfam01365  143 CHIKSFISLLRKHGRD--------PRYLDFLSDlCV-CNGEAVRENQNLICRLLLPNPDLLLQTL 198
Ins145_P3_rec super family cl48031
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 19-211 2.09e-59

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: 205.04  E-value: 2.09e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463   19 GDIVCLSCVASHNrdgvlgserVCLCTEGFGNRMCTLENVSDKDI--PPDIAMCMLYIDNALSMRALQEMMSADS----- 91
Cdd:pfam08709    8 GDIVSLSCEESVN---------GFISALGLGNDRCFVENKAGDLNdpPKKFRDCVFKICPANSYAAQKELWSAGNrspng 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463   92 -----DHKSASGAGGHKTLLYGHAVQLKHVQSEMYLACL-SSCSSNDKLAFDVGVQETNEGEACWWTIHPASKQRSEGEK 165
Cdd:pfam08709   79 nsltdALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLkSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDN 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1254045463  166 VRVGDDVILVSVATERYLHMAYS------KGYMVIASFHQTLWNIQSVSSGS 211
Cdd:pfam08709  159 VCVGDEVILVPVSAPIFLHTTSSselrdnPGKEVNASFGQTSWKMEPFMSGC 210
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 851-939 1.77e-36

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: 134.55  E-value: 1.77e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  851 FIPTPIDVSATQLNHHATEMHQKYAENLHELWAMRKIELGWSYGETRSETSRKHPCLTKFEYLPETEKKYNILLALTTMK 930
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 1254045463  931 TIEALGYHL 939
Cdd:pfam02026   81 TLLALGYTI 89
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3988-4105 1.20e-35

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


:

Pssm-ID: 462482  Cd Length: 98  Bit Score: 132.26  E-value: 1.20e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 3988 NDADFTCSLFRFLQLTCEGHNLEFQNYLRTQPGHTTSVNLINCTVDYLLRLQESvmdfywhysskevIDEggkeyflRAI 4067
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKS-------------INE-------KNI 60

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1254045463 4068 QVCSQVFNTLTESIQGPCVGNQMTLANSRLWDAINGFF 4105
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 963-1054 1.04e-33

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 126.46  E-value: 1.04e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  963 YKPGPLDTHEIQLPAELQPLTEALARNTHNIWAKEKIKRGWTFGlsEHVDATQKRSPHLVPYEQVDERIKQANRESAAEN 1042
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYG--EVRDDAAKTHPCLVPYDLLTEKEKEYDREPARET 78

                           90
                   ....*....|..
gi 1254045463 1043 IRALQLFGIFLE 1054
Cdd:pfam02026   79 LKTLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2835-2924 2.43e-32

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: 122.61  E-value: 2.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2835 WIPRTVDVSRCEINRDLEKMTELFAEHFHDSWASRKLEKGWVHGDLYSRANFTHPRLKPFALLKDFEKSFYKERCSECLK 2914
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1254045463 2915 ALMAWNYSFE 2924
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2948-3030 4.36e-26

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: 104.89  E-value: 4.36e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2948 FAPKPIDLSSMTLEKDMVNAAEKMAEHSHLIWAKKVMNDLNTKGGFMPIP------LVPWDLLTDFERRKDRFRASEILK 3021
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAakthpcLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 1254045463 3022 FLQYHGYHV 3030
Cdd:pfam02026   81 TLLALGYTI 89
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4836-4978 5.60e-13

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: 71.91  E-value: 5.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4836 FFYAFHLIDVVLSFPMLKAILQSVTHNLQQLILTIMMTLVVVYLYTVIAFNFFRKFYvQEGEEGEEPDRKCHNMLTCFIY 4915
Cdd:pfam00520   99 LLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL-KTWENPDNGRTNFDNFPNAFLW 177

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254045463 4916 HFYagVRAGGGIGDELESPYGDDLEYPRMFYDISFFFFVIIILLAIMQGLIIDAFGELRDQQE 4978
Cdd:pfam00520  178 LFQ--TMTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
RR_TM4-6 super family cl24183
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4529-4709 1.12e-12

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


The actual alignment was detected with superfamily member pfam06459:

Pssm-ID: 461918  Cd Length: 282  Bit Score: 72.04  E-value: 1.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4529 VPPERPETPETVLEEEKPLNQETSPPTSPTSPASKAPSIYES--IGAPQMVQLQSEADFQQGQYEPKIaESNSTKsrgsI 4606
Cdd:pfam06459   98 EEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMkkKQRKRHSKKKEEPEAQGSAFWNEL-EVYQTK----L 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4607 LNMLARNFKTIEKITLYLAFFINVILLFHRVDISHAENAEAAS---------------EGDDDEDALESifitgmqfpYV 4671
Cdd:pfam06459  173 LNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGsgwgdsgsgsgggsgEDEEEEEGPVY---------FV 243

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1254045463 4672 EYEITGWMlAQILYWISVLHLSTSFALLVSFYQLKIPL 4709
Cdd:pfam06459  244 LEESTGYM-EPTLRFLAILHTIISFLCIIGYYCLKVPL 280
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 4188-4242 1.70e-09

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


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 56.79  E-value: 1.70e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254045463 4188 AFQDFDTNQDGWISPKEFQRAMESQKMYTVEDITYLMMCT-DVNNDGKVDYMEFTE 4242
Cdd:cd00051      5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREvDKDGDGKIDFEEFLE 60
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 222-401 5.06e-102

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: 325.80  E-value: 5.06e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  222 GNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYLGVL 300
Cdd:cd23278      1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  301 -DNSVQLYHKEKADFDLTAFVMCQNKDPKKqMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEvTKKGLGKVE 379
Cdd:cd23278     81 eDRGLVLVPKEKADVKATAFCFRQSKDDKK-VLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVE-TKKRVGGVE 158

                          170       180
                   ....*....|....*....|..
gi 1254045463  380 EKKAVALKDGHMDDCYTFFMAL 401
Cdd:cd23278    159 ERKAILHAEGHMDDGLSLSRAQ 180
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 650-797 1.65e-84

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: 274.19  E-value: 1.65e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  650 SMMPNVMLGVVEGSALFRKWYFEAEVEHIETMTKQTPYLRIGWANSVGFKPFPGSGDKMGCNGVGDDFYSYGFDGKSMYF 729
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTHQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLWT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254045463  730 GGKSRRVGH---KLLEKGDVIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSLSAKVSCRFILG 797
Cdd:cd12877     81 GGRSRRVTSgtqHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1076-1208 2.14e-83

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: 270.33  E-value: 2.14e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1076 RTYRAEATYAVCGGKWYFEFEILTAGYMKIGWMDIGSTPEIQLGADDRSYAFDGYLGRKWHQGAETYGKEWKIGDVVGCF 1155
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1254045463 1156 LDLNDRTISFSLNGELLLDPSGSEMAFDNVVCGDGLVPAMTLGSGQRGRLNFG 1208
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 449-644 1.24e-75

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


Pssm-ID: 460175  Cd Length: 199  Bit Score: 250.96  E-value: 1.24e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  449 LMEDLIEYFAQPNDEQDFEEKQNHL---RALRSRQDLFQEEGVLNMILDTIDKFS-QMEALPDFAGLIGEETHVKWEQIS 524
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  525 TYLYLLVAAMIKGNHYNCAQFASAqrLDWLFGRLSNPQSAEGILDVLYCVLTESPE-ALNMINEGHIRSVISLLEKVGRD 603
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKH--LDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRD 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1254045463  604 PKVLDVLSSLCEGNGMAVRSSQNLITQYLLPGKDLLLQTSM 644
Cdd:pfam01365  159 PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1540-1690 4.10e-72

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


Pssm-ID: 293937  Cd Length: 151  Bit Score: 238.74  E-value: 4.10e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1540 DAHALVHHKDKVDEYYYGIRIFPGQDPSQVWVGWVTTQYHYYNVNFDGSQgVRKCRFSEADHHGTTVDSVQSQNCYMVNV 1619
Cdd:cd12879      1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDK-VRNVTVTMGDEKGGVYESIKRQNCYMVCA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254045463 1620 SELLA-TTPDVANTKVSGTLIGCIIDTSIGELSFQVGSTDTGIKFKLEPGAMLFPAAFVTPTATEILQFELG 1690
Cdd:cd12879     80 GELLAeVGQDSSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2242-2465 3.38e-65

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: 220.92  E-value: 3.38e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2242 QIRELLTVQFEHTEEAILKRGLWKLMNNRIFFQHPDLMRLLSVHENVMSImMNILTAQQGTVEHEGDELKEKAPIkDASE 2321
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEV-IDLLGAPFTGALLFAEDLGEEKNA-PWKK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2322 MVVACSRFLCYFCRTSRQNQKAMFEHLSFLLDNatmlLARPSLRGSVpLDVAYSSFMDNNELALalkeeeldkvaVYLSR 2401
Cdd:pfam01365   79 IVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKE 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254045463 2402 CGLQPNSELITKGYPDigwdpvegERYIDFLRF-CVwINGENVEENANLVIRLLIRRPECLGVAL 2465
Cdd:pfam01365  143 CHIKSFISLLRKHGRD--------PRYLDFLSDlCV-CNGEAVRENQNLICRLLLPNPDLLLQTL 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 218-397 4.41e-65

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: 220.31  E-value: 4.41e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  218 GFLFGNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRM-KWHGALVGWEQVFRIKHITSGR 295
Cdd:pfam02815    1 GYLKGGDVVRLFHSHqDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  296 YLGVLDN-SVQLYHKEKADFDLTAFVMCQNKDPK--KQMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEVTK 372
Cdd:pfam02815   81 YLHSHEEqKPPLVEKEDWQKEVSAYGFRGFPGDNdiVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....*
gi 1254045463  373 KGLGKvEEKKAVALKDGHMDDCYTF 397
Cdd:pfam02815  161 WGFGP-EQQKVTCAKEGHMDDALTL 184
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 19-211 2.09e-59

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: 205.04  E-value: 2.09e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463   19 GDIVCLSCVASHNrdgvlgserVCLCTEGFGNRMCTLENVSDKDI--PPDIAMCMLYIDNALSMRALQEMMSADS----- 91
Cdd:pfam08709    8 GDIVSLSCEESVN---------GFISALGLGNDRCFVENKAGDLNdpPKKFRDCVFKICPANSYAAQKELWSAGNrspng 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463   92 -----DHKSASGAGGHKTLLYGHAVQLKHVQSEMYLACL-SSCSSNDKLAFDVGVQETNEGEACWWTIHPASKQRSEGEK 165
Cdd:pfam08709   79 nsltdALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLkSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDN 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1254045463  166 VRVGDDVILVSVATERYLHMAYS------KGYMVIASFHQTLWNIQSVSSGS 211
Cdd:pfam08709  159 VCVGDEVILVPVSAPIFLHTTSSselrdnPGKEVNASFGQTSWKMEPFMSGC 210
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 851-939 1.77e-36

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: 134.55  E-value: 1.77e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  851 FIPTPIDVSATQLNHHATEMHQKYAENLHELWAMRKIELGWSYGETRSETSRKHPCLTKFEYLPETEKKYNILLALTTMK 930
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 1254045463  931 TIEALGYHL 939
Cdd:pfam02026   81 TLLALGYTI 89
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3988-4105 1.20e-35

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


Pssm-ID: 462482  Cd Length: 98  Bit Score: 132.26  E-value: 1.20e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 3988 NDADFTCSLFRFLQLTCEGHNLEFQNYLRTQPGHTTSVNLINCTVDYLLRLQESvmdfywhysskevIDEggkeyflRAI 4067
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKS-------------INE-------KNI 60

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1254045463 4068 QVCSQVFNTLTESIQGPCVGNQMTLANSRLWDAINGFF 4105
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 963-1054 1.04e-33

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 126.46  E-value: 1.04e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  963 YKPGPLDTHEIQLPAELQPLTEALARNTHNIWAKEKIKRGWTFGlsEHVDATQKRSPHLVPYEQVDERIKQANRESAAEN 1042
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYG--EVRDDAAKTHPCLVPYDLLTEKEKEYDREPARET 78

                           90
                   ....*....|..
gi 1254045463 1043 IRALQLFGIFLE 1054
Cdd:pfam02026   79 LKTLLALGYTIE 90
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1089-1210 1.33e-32

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: 124.71  E-value: 1.33e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  1089 GKWYFEFEILTAGYMKIGW--MDIGSTPEIQLGADDRSYAFDGYLGRKWHQG-AETYGKEWKI-GDVVGCFLDLNDRTIS 1164
Cdd:smart00449    2 GRHYFEVEIGDGGHWRVGVatKSVPRGYFALLGEDKGSWGYDGDGGKKYHNStGPEYGLPLQEpGDVIGCFLDLEAGTIS 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1254045463  1165 FSLNGELLldpsgSEMAFDNVVCGDGLVPAMTLGSGQRGRLNFGQQ 1210
Cdd:smart00449   82 FYKNGKYL-----HGLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2835-2924 2.43e-32

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: 122.61  E-value: 2.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2835 WIPRTVDVSRCEINRDLEKMTELFAEHFHDSWASRKLEKGWVHGDLYSRANFTHPRLKPFALLKDFEKSFYKERCSECLK 2914
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1254045463 2915 ALMAWNYSFE 2924
Cdd:pfam02026   81 TLLALGYTIE 90
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 668-799 8.49e-30

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 116.67  E-value: 8.49e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  668 KWYFEAEVEhietmTKQTPYLRIGWANsvgfKPFPGSGDKMgcngVGDDFYSYGFDG--KSMYFGGKSRRVGHKLLEKGD 745
Cdd:pfam00622    1 RHYFEVEIF-----GQDGGGWRVGWAT----KSVPRKGERF----LGDESGSWGYDGwtGKKYWASTSPLTGLPLFEPGD 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1254045463  746 VIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSLSAKVSCRFILGGN 799
Cdd:pfam00622   68 VIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 668-799 1.92e-27

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: 110.08  E-value: 1.92e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463   668 KWYFEAEVEHietmtkqTPYLRIGWANSvgfkpfpgSGDKMGCNGVGDDFYSYGFDG--KSMYFGGKSRRVGHKLLEKGD 745
Cdd:smart00449    3 RHYFEVEIGD-------GGHWRVGVATK--------SVPRGYFALLGEDKGSWGYDGdgGKKYHNSTGPEYGLPLQEPGD 67

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1254045463   746 VIGCSIDLTIPEIKFSVNGTYMSG-SFKKFNIDGYFFPVMSLSAKVSCRFILGGN 799
Cdd:smart00449   68 VIGCFLDLEAGTISFYKNGKYLHGlAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2948-3030 4.36e-26

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: 104.89  E-value: 4.36e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2948 FAPKPIDLSSMTLEKDMVNAAEKMAEHSHLIWAKKVMNDLNTKGGFMPIP------LVPWDLLTDFERRKDRFRASEILK 3021
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAakthpcLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 1254045463 3022 FLQYHGYHV 3030
Cdd:pfam02026   81 TLLALGYTI 89
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1090-1210 1.71e-23

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 98.57  E-value: 1.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1090 KWYFEFEILTA--GYMKIGW--MDIGSTPEIQLGADDRSYAFDGYLGRKWH--QGAETYGKEWKIGDVVGCFLDLNDRTI 1163
Cdd:pfam00622    1 RHYFEVEIFGQdgGGWRVGWatKSVPRKGERFLGDESGSWGYDGWTGKKYWasTSPLTGLPLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1254045463 1164 SFSLNGELLLDpsgsemAFDNVVCGDGLVPAMTLGSGQRGRLNFGQQ 1210
Cdd:pfam00622   81 SFTKNGKSLGY------AFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1554-1692 4.97e-18

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: 83.16  E-value: 4.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1554 YYYGIRIFpGQDPSQVWVGWVTTQYHYYNVNFDGsqgvrkcrfseadhhgTTVDSVQSQNCYMV--------NVSELLAT 1625
Cdd:pfam00622    2 HYFEVEIF-GQDGGGWRVGWATKSVPRKGERFLG----------------DESGSWGYDGWTGKkywastspLTGLPLFE 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254045463 1626 TPDVantkvsgtlIGCIIDTSIGELSFQVGSTDTGIKFKLEPGA-MLFPAAFVTPtaTEILQFELGRI 1692
Cdd:pfam00622   65 PGDV---------IGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSLGA--GEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1554-1692 2.47e-17

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 81.19  E-value: 2.47e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  1554 YYYGIRIFpgqDPSQVWVGWVTTQYHYYNVNFDGSqgvrkcrfseaDHHGTTVDSVQSQNCYMVNVSE---LLATTPDVa 1630
Cdd:smart00449    4 HYFEVEIG---DGGHWRVGVATKSVPRGYFALLGE-----------DKGSWGYDGDGGKKYHNSTGPEyglPLQEPGDV- 68

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1254045463  1631 ntkvsgtlIGCIIDTSIGELSFQVGSTDTGIK--FKLEPGAMLFPAAFVTPtaTEILQFELGRI 1692
Cdd:smart00449   69 --------IGCFLDLEAGTISFYKNGKYLHGLafFDVKFSGPLYPAFSLGS--GNSVRLNFGPL 122
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4836-4978 5.60e-13

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: 71.91  E-value: 5.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4836 FFYAFHLIDVVLSFPMLKAILQSVTHNLQQLILTIMMTLVVVYLYTVIAFNFFRKFYvQEGEEGEEPDRKCHNMLTCFIY 4915
Cdd:pfam00520   99 LLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL-KTWENPDNGRTNFDNFPNAFLW 177

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254045463 4916 HFYagVRAGGGIGDELESPYGDDLEYPRMFYDISFFFFVIIILLAIMQGLIIDAFGELRDQQE 4978
Cdd:pfam00520  178 LFQ--TMTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4529-4709 1.12e-12

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: 72.04  E-value: 1.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4529 VPPERPETPETVLEEEKPLNQETSPPTSPTSPASKAPSIYES--IGAPQMVQLQSEADFQQGQYEPKIaESNSTKsrgsI 4606
Cdd:pfam06459   98 EEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMkkKQRKRHSKKKEEPEAQGSAFWNEL-EVYQTK----L 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4607 LNMLARNFKTIEKITLYLAFFINVILLFHRVDISHAENAEAAS---------------EGDDDEDALESifitgmqfpYV 4671
Cdd:pfam06459  173 LNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGsgwgdsgsgsgggsgEDEEEEEGPVY---------FV 243

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1254045463 4672 EYEITGWMlAQILYWISVLHLSTSFALLVSFYQLKIPL 4709
Cdd:pfam06459  244 LEESTGYM-EPTLRFLAILHTIISFLCIIGYYCLKVPL 280
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 4188-4242 1.70e-09

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 56.79  E-value: 1.70e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254045463 4188 AFQDFDTNQDGWISPKEFQRAMESQKMYTVEDITYLMMCT-DVNNDGKVDYMEFTE 4242
Cdd:cd00051      5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREvDKDGDGKIDFEEFLE 60
EF-hand_7 pfam13499
EF-hand domain pair;
4187-4244 4.54e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.94  E-value: 4.54e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254045463 4187 QAFQDFDTNQDGWISPKEFQRAMESQKM---YTVEDITYLMMCTDVNNDGKVDYMEFTERF 4244
Cdd:pfam13499    6 EAFKLLDSDGDGYLDVEELKKLLRKLEEgepLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4187-4248 1.97e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.48  E-value: 1.97e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254045463 4187 QAFQDFDTNQDGWISPKEFQRAMESQKMyTVEDITYLMMCTDVNNDGKVDYMEFTE---RFHNPA 4248
Cdd:COG5126     73 AAFDLLDTDGDGKISADEFRRLLTALGV-SEEEADELFARLDTDGDGKISFEEFVAavrDYYTPD 136
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
217-271 1.31e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.71  E-value: 1.31e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045463   217 MGFLFGNDVLRLFHGNDEC-LTIPENW---SEHPQHNMVIYEGGAAVtqARSLWRVELI 271
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRyLHSHDEKlppWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 93-185 1.87e-04

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


Pssm-ID: 467751 [Multi-domain]  Cd Length: 199  Bit Score: 45.84  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463   93 HKSASGAGGhkTLLYGHAVQLKHVQSEMYLaclssCSSNDKLAFDVGVQETNEGEACWWTIHPASKQRSEGekVRVGDDV 172
Cdd:cd23280     68 KEDTPLKGG--VIKWGDQCRLRHLPTGKYL-----AVDDKTGNGKVVLTSDPSDPSTVFRLHPVTKETSEE--VKFGSYV 138

                           90
                   ....*....|...
gi 1254045463  173 ILVSVATERYLHM 185
Cdd:cd23280    139 RIEHVATGTWLHA 151
PTZ00183 PTZ00183
centrin; Provisional
 4187-4279 1.13e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.75  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4187 QAFQDFDTNQDGWISPKEFQRAM-----ESQKmytvEDITYLMMCTDVNNDGKVDYMEF----TERFHN--PARDI--GF 4253
Cdd:PTZ00183    21 EAFDLFDTDGSGTIDPKELKVAMrslgfEPKK----EEIKQMIADVDKDGSGKIDFEEFldimTKKLGErdPREEIlkAF 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1254045463 4254 NL-------AVLLVNLK-------EHITnDPRLEKIIEKA 4279
Cdd:PTZ00183    97 RLfdddktgKISLKNLKrvakelgETIT-DEELQEMIDEA 135
 
Name Accession Description Interval E-value
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 222-401 5.06e-102

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: 325.80  E-value: 5.06e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  222 GNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYLGVL 300
Cdd:cd23278      1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  301 -DNSVQLYHKEKADFDLTAFVMCQNKDPKKqMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEvTKKGLGKVE 379
Cdd:cd23278     81 eDRGLVLVPKEKADVKATAFCFRQSKDDKK-VLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVE-TKKRVGGVE 158

                          170       180
                   ....*....|....*....|..
gi 1254045463  380 EKKAVALKDGHMDDCYTFFMAL 401
Cdd:cd23278    159 ERKAILHAEGHMDDGLSLSRAQ 180
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 650-797 1.65e-84

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: 274.19  E-value: 1.65e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  650 SMMPNVMLGVVEGSALFRKWYFEAEVEHIETMTKQTPYLRIGWANSVGFKPFPGSGDKMGCNGVGDDFYSYGFDGKSMYF 729
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTHQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLWT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254045463  730 GGKSRRVGH---KLLEKGDVIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSLSAKVSCRFILG 797
Cdd:cd12877     81 GGRSRRVTSgtqHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 1076-1208 2.14e-83

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: 270.33  E-value: 2.14e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1076 RTYRAEATYAVCGGKWYFEFEILTAGYMKIGWMDIGSTPEIQLGADDRSYAFDGYLGRKWHQGAETYGKEWKIGDVVGCF 1155
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1254045463 1156 LDLNDRTISFSLNGELLLDPSGSEMAFDNVVCGDGLVPAMTLGSGQRGRLNFG 1208
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 449-644 1.24e-75

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


Pssm-ID: 460175  Cd Length: 199  Bit Score: 250.96  E-value: 1.24e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  449 LMEDLIEYFAQPNDEQDFEEKQNHL---RALRSRQDLFQEEGVLNMILDTIDKFS-QMEALPDFAGLIGEETHVKWEQIS 524
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  525 TYLYLLVAAMIKGNHYNCAQFASAqrLDWLFGRLSNPQSAEGILDVLYCVLTESPE-ALNMINEGHIRSVISLLEKVGRD 603
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKH--LDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRD 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1254045463  604 PKVLDVLSSLCEGNGMAVRSSQNLITQYLLPGKDLLLQTSM 644
Cdd:pfam01365  159 PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
 1540-1690 4.10e-72

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


Pssm-ID: 293937  Cd Length: 151  Bit Score: 238.74  E-value: 4.10e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1540 DAHALVHHKDKVDEYYYGIRIFPGQDPSQVWVGWVTTQYHYYNVNFDGSQgVRKCRFSEADHHGTTVDSVQSQNCYMVNV 1619
Cdd:cd12879      1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDK-VRNVTVTMGDEKGGVYESIKRQNCYMVCA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254045463 1620 SELLA-TTPDVANTKVSGTLIGCIIDTSIGELSFQVGSTDTGIKFKLEPGAMLFPAAFVTPTATEILQFELG 1690
Cdd:cd12879     80 GELLAeVGQDSSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 2242-2465 3.38e-65

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: 220.92  E-value: 3.38e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2242 QIRELLTVQFEHTEEAILKRGLWKLMNNRIFFQHPDLMRLLSVHENVMSImMNILTAQQGTVEHEGDELKEKAPIkDASE 2321
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEV-IDLLGAPFTGALLFAEDLGEEKNA-PWKK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2322 MVVACSRFLCYFCRTSRQNQKAMFEHLSFLLDNatmlLARPSLRGSVpLDVAYSSFMDNNELALalkeeeldkvaVYLSR 2401
Cdd:pfam01365   79 IVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKE 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254045463 2402 CGLQPNSELITKGYPDigwdpvegERYIDFLRF-CVwINGENVEENANLVIRLLIRRPECLGVAL 2465
Cdd:pfam01365  143 CHIKSFISLLRKHGRD--------PRYLDFLSDlCV-CNGEAVRENQNLICRLLLPNPDLLLQTL 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 218-397 4.41e-65

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: 220.31  E-value: 4.41e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  218 GFLFGNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRM-KWHGALVGWEQVFRIKHITSGR 295
Cdd:pfam02815    1 GYLKGGDVVRLFHSHqDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  296 YLGVLDN-SVQLYHKEKADFDLTAFVMCQNKDPK--KQMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEVTK 372
Cdd:pfam02815   81 YLHSHEEqKPPLVEKEDWQKEVSAYGFRGFPGDNdiVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....*
gi 1254045463  373 KGLGKvEEKKAVALKDGHMDDCYTF 397
Cdd:pfam02815  161 WGFGP-EQQKVTCAKEGHMDDALTL 184
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 19-211 2.09e-59

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: 205.04  E-value: 2.09e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463   19 GDIVCLSCVASHNrdgvlgserVCLCTEGFGNRMCTLENVSDKDI--PPDIAMCMLYIDNALSMRALQEMMSADS----- 91
Cdd:pfam08709    8 GDIVSLSCEESVN---------GFISALGLGNDRCFVENKAGDLNdpPKKFRDCVFKICPANSYAAQKELWSAGNrspng 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463   92 -----DHKSASGAGGHKTLLYGHAVQLKHVQSEMYLACL-SSCSSNDKLAFDVGVQETNEGEACWWTIHPASKQRSEGEK 165
Cdd:pfam08709   79 nsltdALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLkSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDN 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1254045463  166 VRVGDDVILVSVATERYLHMAYS------KGYMVIASFHQTLWNIQSVSSGS 211
Cdd:pfam08709  159 VCVGDEVILVPVSAPIFLHTTSSselrdnPGKEVNASFGQTSWKMEPFMSGC 210
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 218-405 1.36e-49

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: 175.87  E-value: 1.36e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  218 GFLFGNDVLRLFHGNDECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYL 297
Cdd:cd23292      1 GYLLGGHVVRLFHGHDECLTIPSTDQSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHYL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  298 GVL-DNSVQLYHKEKADFDLTAFVMCQNKDpKKQMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEVTKKGLG 376
Cdd:cd23292     81 ALTeDQGLILQDRAKSDTKSTAFCFRASKE-KLESGPKRDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSRLG 159

                          170       180
                   ....*....|....*....|....*....
gi 1254045463  377 KVeEKKAVALKDGHMDDCYTFFMALEEES 405
Cdd:cd23292    160 PL-KRRAILHQEGHMDDGLTLQRCQHEES 187
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 218-405 1.33e-45

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: 164.68  E-value: 1.33e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  218 GFLFGNDVLRLFHGN-DECLTIPENWSEHpQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRY 296
Cdd:cd23290      6 GYVTGGHVLRLFHGHmDECLTISAADSDD-QRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRY 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  297 LGVL-DNSVQLYHKEKADFDLTAFVMCQNKDpKKQMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEVTKKGL 375
Cdd:cd23290     85 LALTeDQGLVVVDACKAHTKATSFCFRVSKE-KLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRL 163

                          170       180       190
                   ....*....|....*....|....*....|
gi 1254045463  376 GKVeEKKAVALKDGHMDDCYTFFMALEEES 405
Cdd:cd23290    164 GVL-KKKAILHQEGHMDDALFLTRCQQEES 192
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 222-405 2.10e-42

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: 155.20  E-value: 2.10e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  222 GNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYLGVL 300
Cdd:cd23291      1 GGDVLRLLHGHmDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  301 DN-SVQLYHKEKADFDLTAFVMCQNKDpKKQMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEVTKKGLGKVe 379
Cdd:cd23291     81 EDkNLLLMDKEKADVKSTAFTFRSSKE-KLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSI- 158

                          170       180
                   ....*....|....*....|....*.
gi 1254045463  380 EKKAVALKDGHMDDCYTFFMALEEES 405
Cdd:cd23291    159 QRKAIMHHEGHMDDGLNLSRSQHEES 184
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 851-939 1.77e-36

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: 134.55  E-value: 1.77e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  851 FIPTPIDVSATQLNHHATEMHQKYAENLHELWAMRKIELGWSYGETRSETSRKHPCLTKFEYLPETEKKYNILLALTTMK 930
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 1254045463  931 TIEALGYHL 939
Cdd:pfam02026   81 TLLALGYTI 89
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 3988-4105 1.20e-35

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


Pssm-ID: 462482  Cd Length: 98  Bit Score: 132.26  E-value: 1.20e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 3988 NDADFTCSLFRFLQLTCEGHNLEFQNYLRTQPGHTTSVNLINCTVDYLLRLQESvmdfywhysskevIDEggkeyflRAI 4067
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKS-------------INE-------KNI 60

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1254045463 4068 QVCSQVFNTLTESIQGPCVGNQMTLANSRLWDAINGFF 4105
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 963-1054 1.04e-33

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 126.46  E-value: 1.04e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  963 YKPGPLDTHEIQLPAELQPLTEALARNTHNIWAKEKIKRGWTFGlsEHVDATQKRSPHLVPYEQVDERIKQANRESAAEN 1042
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYG--EVRDDAAKTHPCLVPYDLLTEKEKEYDREPARET 78

                           90
                   ....*....|..
gi 1254045463 1043 IRALQLFGIFLE 1054
Cdd:pfam02026   79 LKTLLALGYTIE 90
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1089-1210 1.33e-32

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: 124.71  E-value: 1.33e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  1089 GKWYFEFEILTAGYMKIGW--MDIGSTPEIQLGADDRSYAFDGYLGRKWHQG-AETYGKEWKI-GDVVGCFLDLNDRTIS 1164
Cdd:smart00449    2 GRHYFEVEIGDGGHWRVGVatKSVPRGYFALLGEDKGSWGYDGDGGKKYHNStGPEYGLPLQEpGDVIGCFLDLEAGTIS 81

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1254045463  1165 FSLNGELLldpsgSEMAFDNVVCGDGLVPAMTLGSGQRGRLNFGQQ 1210
Cdd:smart00449   82 FYKNGKYL-----HGLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2835-2924 2.43e-32

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: 122.61  E-value: 2.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2835 WIPRTVDVSRCEINRDLEKMTELFAEHFHDSWASRKLEKGWVHGDLYSRANFTHPRLKPFALLKDFEKSFYKERCSECLK 2914
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 1254045463 2915 ALMAWNYSFE 2924
Cdd:pfam02026   81 TLLALGYTIE 90
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 1082-1208 1.75e-31

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: 121.66  E-value: 1.75e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1082 ATYAVCGGKWYFEFEILTAGYMKIGWMDIGS--TPEIQLGADDRSYAFDGYLGRKWHQGAETYGKEWKIGDVVGCFLDLN 1159
Cdd:cd12882      4 ANACVYKGKWMYEVTLGTKGIMQIGWATISCrfTQEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDLD 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1254045463 1160 DRTISFSLNGELLldpsgsEMAFDNVVCGDGLV--PAMTLGSGQRGRLNFG 1208
Cdd:cd12882     84 KGTISFYRNGRSL------GVAFDNVRRGPGLAyfPAVSLSFGERLELNFG 128
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 668-799 8.49e-30

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 116.67  E-value: 8.49e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  668 KWYFEAEVEhietmTKQTPYLRIGWANsvgfKPFPGSGDKMgcngVGDDFYSYGFDG--KSMYFGGKSRRVGHKLLEKGD 745
Cdd:pfam00622    1 RHYFEVEIF-----GQDGGGWRVGWAT----KSVPRKGERF----LGDESGSWGYDGwtGKKYWASTSPLTGLPLFEPGD 67

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1254045463  746 VIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSLSAKVSCRFILGGN 799
Cdd:pfam00622   68 VIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1089-1206 6.71e-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: 114.06  E-value: 6.71e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1089 GKWYFEFEILTA--GYMKIGWM--DIGSTPEIQLGADDRSYAFDGYLGRKWHQGAETYG-KEWKIGDVVGCFLDLNDRTI 1163
Cdd:cd11709      1 GKWYWEVRVDSGngGLIQVGWAtkSFSLDGEGGVGDDEESWGYDGSRLRKGHGGSSGPGgRPWKSGDVVGCLLDLDEGTL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1254045463 1164 SFSLNGELLldpsGSemAFDNVVC-GDGLVPAMTLGSGQRGRLN 1206
Cdd:cd11709     81 SFSLNGKDL----GV--AFTNLFLkGGGLYPAVSLGSGQGVTIN 118
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 668-799 1.92e-27

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: 110.08  E-value: 1.92e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463   668 KWYFEAEVEHietmtkqTPYLRIGWANSvgfkpfpgSGDKMGCNGVGDDFYSYGFDG--KSMYFGGKSRRVGHKLLEKGD 745
Cdd:smart00449    3 RHYFEVEIGD-------GGHWRVGVATK--------SVPRGYFALLGEDKGSWGYDGdgGKKYHNSTGPEYGLPLQEPGD 67

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1254045463   746 VIGCSIDLTIPEIKFSVNGTYMSG-SFKKFNIDGYFFPVMSLSAKVSCRFILGGN 799
Cdd:smart00449   68 VIGCFLDLEAGTISFYKNGKYLHGlAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
 2948-3030 4.36e-26

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: 104.89  E-value: 4.36e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 2948 FAPKPIDLSSMTLEKDMVNAAEKMAEHSHLIWAKKVMNDLNTKGGFMPIP------LVPWDLLTDFERRKDRFRASEILK 3021
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAakthpcLVPYDLLTEKEKEYDREPARETLK 80


                   ....*....
gi 1254045463 3022 FLQYHGYHV 3030
Cdd:pfam02026   81 TLLALGYTI 89
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1090-1210 1.71e-23

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


Pssm-ID: 459877  Cd Length: 121  Bit Score: 98.57  E-value: 1.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1090 KWYFEFEILTA--GYMKIGW--MDIGSTPEIQLGADDRSYAFDGYLGRKWH--QGAETYGKEWKIGDVVGCFLDLNDRTI 1163
Cdd:pfam00622    1 RHYFEVEIFGQdgGGWRVGWatKSVPRKGERFLGDESGSWGYDGWTGKKYWasTSPLTGLPLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1254045463 1164 SFSLNGELLLDpsgsemAFDNVVCGDGLVPAMTLGSGQRGRLNFGQQ 1210
Cdd:pfam00622   81 SFTKNGKSLGY------AFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 1082-1211 1.13e-18

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: 86.09  E-value: 1.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1082 ATYAV-CGGKWYFEFEILTAGYMKIGWmdigSTPE--IQLGADDRSYAFDGyLGRKWHQGA-ETYGKEWKIGDVVGCFLD 1157
Cdd:cd12873     32 ATKGVkGKGKYYYEVTVTDEGLCRVGW----STEDasLDLGTDKFGFGYGG-TGKKSHGRQfDDYGEPFGLGDVIGCYLD 106

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254045463 1158 LNDRTISFSLNGELLldpsgsEMAFDNVVC--GDGLVPAMTLGSGqRGRLNFGQQS 1211
Cdd:cd12873    107 LDNGTISFSKNGKDL------GKAFDIPPHlrNSALFPAVCLKNA-EVEFNFGDKP 155
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 668-795 1.69e-18

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: 84.40  E-value: 1.69e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  668 KWYFEAEVEhietmTKQTPYLRIGWANSvgfkpfpgSGDKMGCNGVGDDFYSYGFDGKSMYFGGKSR-RVGHKLLEKGDV 746
Cdd:cd11709      2 KWYWEVRVD-----SGNGGLIQVGWATK--------SFSLDGEGGVGDDEESWGYDGSRLRKGHGGSsGPGGRPWKSGDV 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1254045463  747 IGCSIDLTIPEIKFSVNGTYMSGSFKKFN-IDGYFFPVMSLSAKVSCRFI 795
Cdd:cd11709     69 VGCLLDLDEGTLSFSLNGKDLGVAFTNLFlKGGGLYPAVSLGSGQGVTIN 118
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1554-1692 4.97e-18

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: 83.16  E-value: 4.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1554 YYYGIRIFpGQDPSQVWVGWVTTQYHYYNVNFDGsqgvrkcrfseadhhgTTVDSVQSQNCYMV--------NVSELLAT 1625
Cdd:pfam00622    2 HYFEVEIF-GQDGGGWRVGWATKSVPRKGERFLG----------------DESGSWGYDGWTGKkywastspLTGLPLFE 64

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254045463 1626 TPDVantkvsgtlIGCIIDTSIGELSFQVGSTDTGIKFKLEPGA-MLFPAAFVTPtaTEILQFELGRI 1692
Cdd:pfam00622   65 PGDV---------IGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSLGA--GEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1554-1692 2.47e-17

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


Pssm-ID: 214669  Cd Length: 122  Bit Score: 81.19  E-value: 2.47e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  1554 YYYGIRIFpgqDPSQVWVGWVTTQYHYYNVNFDGSqgvrkcrfseaDHHGTTVDSVQSQNCYMVNVSE---LLATTPDVa 1630
Cdd:smart00449    4 HYFEVEIG---DGGHWRVGVATKSVPRGYFALLGE-----------DKGSWGYDGDGGKKYHNSTGPEyglPLQEPGDV- 68

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1254045463  1631 ntkvsgtlIGCIIDTSIGELSFQVGSTDTGIK--FKLEPGAMLFPAAFVTPtaTEILQFELGRI 1692
Cdd:smart00449   69 --------IGCFLDLEAGTISFYKNGKYLHGLafFDVKFSGPLYPAFSLGS--GNSVRLNFGPL 122
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 1092-1208 2.96e-17

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: 81.17  E-value: 2.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1092 YFEFEILTAGYMK---IGWMDIGSTPEIQLGADDRSYAFDGYLGRKWHQGA--ETYGKEWKIGDVVGCFLDLNDRTISFS 1166
Cdd:cd12885     17 YFEVTILDLGEKGivsIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGegENYGPPFGTGDVVGCGINFKTGEVFFT 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1254045463 1167 LNGELLldpsgsEMAFDNVVCGDgLVPAMTLGS-GQRGRLNFG 1208
Cdd:cd12885     97 KNGELL------GTAFENVVKGR-LYPTVGLGSpGVKVRVNFG 132
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
 668-806 3.11e-17

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: 81.19  E-value: 3.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  668 KWYFEAEVehietMTkqTPYLRIGWAnSVGFKPfpgsgDKMgcngVGDDFYSYGFDGksmyFGGKSRRVGH----KLLEK 743
Cdd:cd12878     15 KWYFEFEV-----LT--SGYMRVGWA-RPGFRP-----DLE----LGSDDLSYAFDG----FLARKWHQGSesfgKQWQP 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045463  744 GDVIGCSIDLTIPEIKFSVNGTYM---SGS---FKKFNIDGYFFPVMSLSAkvscrfilgGNQGRLRYG 806
Cdd:cd12878     74 GDVVGCMLDLVDRTISFTLNGELLidsSGSevaFKDIEIGEGFVPACSLGV---------GQKGRLNLG 133
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 1089-1208 1.25e-16

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: 78.93  E-value: 1.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1089 GKWYFEFEILTAGYMKIGWMDIGS---TPE-IQLGADDRSYAFDGYLGRKWH--QGAETYGKEWKIGDVVGCFLDLNDRT 1162
Cdd:cd12883      1 GVWYYEVTVLTSGVMQIGWATKDSkflNHEgYGIGDDEYSCAYDGCRQLIWYnaKSKPHTHPRWKPGDVLGCLLDLNKKQ 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1254045463 1163 ISFSLNGELLldPSGSEMAFDNVvcgDGLVPAMTLGSGQRGRLNFG 1208
Cdd:cd12883     81 MIFSLNGNRL--PPERQVFTSAK---SGFFAAASFMSFQQCEFNFG 121
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 658-794 1.01e-14

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


Pssm-ID: 293932  Cd Length: 150  Bit Score: 74.48  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  658 GVVEGsalfrKWYFEAEVEHIETmtKQTPYLRIGWANSVGFKPFPgsgdkmgcngVGDDFYSYGF---DGKSmYFGGKSR 734
Cdd:cd12872     24 GVREG-----KWYFEVKILEGGG--TETGHVRVGWSRREASLQAP----------VGYDKYSYAIrdkDGSK-FHQSRGK 85

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254045463  735 RVGHKLLEKGDVIGCSIDLtiPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSL--SAKVSCRF 794
Cdd:cd12872     86 PYGEPGFKEGDVIGFLITL--PKIEFFKNGKSQGVAFEDIYGTGGYYPAVSLykGATVTINF 145
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 1080-1210 2.07e-14

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: 74.55  E-value: 2.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1080 AEATYAVCGGKWYFEFEIL------------TAGYM-KIGWmDIGSTPeIQLGADDRSYAFDGYlGRKWHQGAET-YGKE 1145
Cdd:cd12884     36 ARATYGVTKGKVCFEVKVTenlpvkhlpteeTDPHVvRVGW-SVDSSS-LQLGEEEFSYGYGST-GKKSTNCKFEdYGEP 112

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254045463 1146 WKIGDVVGCFLDLN--DRTISFSLNGELLldpsGSEMAFDNVVCGDG-LVPAMtLGSGQRGRLNFGQQ 1210
Cdd:cd12884    113 FGENDVIGCYLDFEsePVEISFSKNGKDL----GVAFKISKEELGGKaLFPHV-LTKNCAVEVNFGQK 175
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 4836-4978 5.60e-13

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: 71.91  E-value: 5.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4836 FFYAFHLIDVVLSFPMLKAILQSVTHNLQQLILTIMMTLVVVYLYTVIAFNFFRKFYvQEGEEGEEPDRKCHNMLTCFIY 4915
Cdd:pfam00520   99 LLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL-KTWENPDNGRTNFDNFPNAFLW 177

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254045463 4916 HFYagVRAGGGIGDELESPYGDDLEYPRMFYDISFFFFVIIILLAIMQGLIIDAFGELRDQQE 4978
Cdd:pfam00520  178 LFQ--TMTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
RR_TM4-6 pfam06459
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ...
 4529-4709 1.12e-12

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: 72.04  E-value: 1.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4529 VPPERPETPETVLEEEKPLNQETSPPTSPTSPASKAPSIYES--IGAPQMVQLQSEADFQQGQYEPKIaESNSTKsrgsI 4606
Cdd:pfam06459   98 EEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMkkKQRKRHSKKKEEPEAQGSAFWNEL-EVYQTK----L 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4607 LNMLARNFKTIEKITLYLAFFINVILLFHRVDISHAENAEAAS---------------EGDDDEDALESifitgmqfpYV 4671
Cdd:pfam06459  173 LNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGsgwgdsgsgsgggsgEDEEEEEGPVY---------FV 243

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1254045463 4672 EYEITGWMlAQILYWISVLHLSTSFALLVSFYQLKIPL 4709
Cdd:pfam06459  244 LEESTGYM-EPTLRFLAILHTIISFLCIIGYYCLKVPL 280
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
 669-797 2.35e-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: 66.60  E-value: 2.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  669 WYFEAEVEHIETMtkqtpylRIGWA-------NSVGFkpfpgsgdkmgcnGVGDDFYSYGFDG--KSMYFGGKSRRVGHK 739
Cdd:cd12883      3 WYYEVTVLTSGVM-------QIGWAtkdskflNHEGY-------------GIGDDEYSCAYDGcrQLIWYNAKSKPHTHP 62

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045463  740 LLEKGDVIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGY-FFPVMSLSAKVSCRFILG 797
Cdd:cd12883     63 RWKPGDVLGCLLDLNKKQMIFSLNGNRLPPERQVFTSAKSgFFAAASFMSFQQCEFNFG 121
SPRY_Ash2 cd12872
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...
 1078-1208 2.89e-12

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


Pssm-ID: 293932  Cd Length: 150  Bit Score: 67.54  E-value: 2.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1078 YR-AEATYAVCGGKWYFEFEILTAGYMK-----IGWmdigSTPE--IQ--LGADDRSYAFDGYLGRKWHQGA-ETYG-KE 1145
Cdd:cd12872     16 YRmARANHGVREGKWYFEVKILEGGGTEtghvrVGW----SRREasLQapVGYDKYSYAIRDKDGSKFHQSRgKPYGePG 91

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254045463 1146 WKIGDVVGCFLDLNdrTISFSLNGELLldpsGSemAFDNVVCGDGLVPAMTLGSGQRGRLNFG 1208
Cdd:cd12872     92 FKEGDVIGFLITLP--KIEFFKNGKSQ----GV--AFEDIYGTGGYYPAVSLYKGATVTINFG 146
SPRY_RanBP9_10 cd12909
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...
 1089-1209 2.20e-11

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: 64.85  E-value: 2.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1089 GKWYFEFEILTAGymKIGWMDIG-STPEIQL----GADDRSYAF---DGYLGRKWHQGAEtYGKEWKIGDVVGCFLDLND 1160
Cdd:cd12909     25 GIYYFEVKIISKG--RDGYIGIGfSTKDVNLnrlpGWEPHSWGYhgdDGHSFCSSGTGKP-YGPTFTTGDVIGCGINFRD 101

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1161 RTISFSLNGELLldpsgsEMAFDNVVCGDgLVPAMTLGS-GQRGRLNFGQ 1209
Cdd:cd12909    102 NTAFYTKNGVNL------GIAFRDIKKGN-LYPTVGLRTpGEHVEANFGQ 144
SPRY_RanBP_like cd12885
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...
 667-794 7.18e-11

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


Pssm-ID: 293943  Cd Length: 132  Bit Score: 63.07  E-value: 7.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  667 RKWYFEAEVEHIETMTKqtpylrigwaNSVGFKPFPGSGDKMgcngVGDDFYSYGF---DGKsMYFGGKSRRVGHKLLEK 743
Cdd:cd12885     14 PVFYFEVTILDLGEKGI----------VSIGFCTSGFPLNRM----PGWEDGSYGYhgdDGR-VYLGGGEGENYGPPFGT 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1254045463  744 GDVIGCSIDLTIPEIKFSVNGTYMsGSFKKFNIDGYFFPVMSLS---AKVSCRF 794
Cdd:cd12885     79 GDVVGCGINFKTGEVFFTKNGELL-GTAFENVVKGRLYPTVGLGspgVKVRVNF 131
SPRY_RNF123 cd12882
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...
 668-797 4.44e-10

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: 60.42  E-value: 4.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  668 KWYFEAeveHIETmtkqTPYLRIGWANSVGfkPFPGSgdkmgcNGVGDDFYSYGFDGKSMY-FGGKSRRVGHKLLEkGDV 746
Cdd:cd12882     12 KWMYEV---TLGT----KGIMQIGWATISC--RFTQE------EGVGDTRDSYAYDGNRVRkWNVSTQKYGEPWVA-GDV 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1254045463  747 IGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGY--FFPVMSLSAKVSCRFILG 797
Cdd:cd12882     76 IGCCIDLDKGTISFYRNGRSLGVAFDNVRRGPGlaYFPAVSLSFGERLELNFG 128
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 4188-4242 1.70e-09

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 56.79  E-value: 1.70e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254045463 4188 AFQDFDTNQDGWISPKEFQRAMESQKMYTVEDITYLMMCT-DVNNDGKVDYMEFTE 4242
Cdd:cd00051      5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREvDKDGDGKIDFEEFLE 60
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
 658-794 3.20e-09

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: 59.52  E-value: 3.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  658 GVVEGsalfrKWYFEAE------VEHIETMTKQTPYLRIGWanSVGFKPFPgsgdkmgcngVGDDFYSYGFDGK-SMYFG 730
Cdd:cd12884     41 GVTKG-----KVCFEVKvtenlpVKHLPTEETDPHVVRVGW--SVDSSSLQ----------LGEEEFSYGYGSTgKKSTN 103

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  731 GKSRRVGHKLLEkGDVIGCSIDL--TIPEIKFSVNGTYMSGSFKKFNIDGY---FFP-VMSLSAKVSCRF 794
Cdd:cd12884    104 CKFEDYGEPFGE-NDVIGCYLDFesEPVEISFSKNGKDLGVAFKISKEELGgkaLFPhVLTKNCAVEVNF 172
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 223-385 7.65e-09

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: 58.16  E-value: 7.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  223 NDVLRLFHG-NDECLTIPENwsEHP---QHNMVIYEGGAAVTQARSLWRVELIRMKWhGALVGWEQVFRIKHITSGRYLg 298
Cdd:cd23263      1 GDVIWLKHSeTGKYLHSHRK--NYPtgsGQQEVTFESSSRKGDTNGLWIIESENGKQ-GGPVKWGDKIRLRHLSTGKYL- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  299 vldnSVQLYHKEKADFDLtaFVMCQNKDPKKQMLDEKEEEGMGNATIRYGETNAF--IQHVKTQLWLSYQT--------- 367
Cdd:cd23263     77 ----SSEEGKKSPKSNHQ--EVLCLTDNPDKSSLFKFEPIGSTKYKQKYVKKDSYfrLKHVNTNFWLHSHEkkfninnkt 150

                          170
                   ....*....|....*....
gi 1254045463  368 -TEVTKKGLGKVEEKKAVA 385
Cdd:cd23263    151 qQEVICHGEREEVFKLWKA 169
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 262-397 1.34e-08

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: 58.17  E-value: 1.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  262 ARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYLgVLDNSVQLYH---KEKADFDLTAFVmcqnkdpKKQMLDEKEEE 338
Cdd:cd23280     60 GDTFWQIEKEDTPLKGGVIKWGDQCRLRHLPTGKYL-AVDDKTGNGKvvlTSDPSDPSTVFR-------LHPVTKETSEE 131

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1254045463  339 gmgnatIRYGeTNAFIQHVKTQLWLS-----YQTTEVTKKGLGKVEEKKA---VALKDGHMDDCYTF 397
Cdd:cd23280    132 ------VKFG-SYVRIEHVATGTWLHaetdeELRRSKKSPAGLSWDGAKLrkvSLSLERQDDDAFTI 191
SPRY_like cd12886
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...
 1089-1208 1.65e-07

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


Pssm-ID: 293944  Cd Length: 129  Bit Score: 53.28  E-value: 1.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1089 GKWYFEFEILTAG---YMKIGWMDIGSTPE-----IQLGADdrSYAFDGYLGRKW--HQGAETYGKEWKIGDVVGCFLDL 1158
Cdd:cd12886      1 GKWYWEVTVVSSAastYAGIGVANAAATGNnglngIELSSI--GYSLGVYSGNKLsnGSSVATYGAGFTAGDVIGVALDL 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1254045463 1159 NDRTISFSLNGELLLDPS---GSEMAFDnvvcGDGLVPAMTLGSGQRGR--LNFG 1208
Cdd:cd12886     79 DAGKIWFYKNGVWQGGGDpapGTNPAFA----GTAMYPAVTGGSSTGGSftANFG 129
EF-hand_7 pfam13499
EF-hand domain pair;
4187-4244 4.54e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.94  E-value: 4.54e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254045463 4187 QAFQDFDTNQDGWISPKEFQRAMESQKM---YTVEDITYLMMCTDVNNDGKVDYMEFTERF 4244
Cdd:pfam13499    6 EAFKLLDSDGDGYLDVEELKKLLRKLEEgepLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
 1090-1208 4.75e-07

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: 52.32  E-value: 4.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1090 KWYFEFEI-------LTAGYMKIGW-MDIGSTPEIQ---------LGADDRSYAFDG---YLGRKWHQGAETYGKEWKIG 1149
Cdd:cd12877     19 KWYFEVEVdhveqftHQPAHLRVGWaNTSGYVPYPGggegwggngVGDDLYSYGFDGlhlWTGGRSRRVTSGTQHLLKKG 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045463 1150 DVVGCFLDLNDRTISFSLNGELLldpSGSemaFDNVVCGDGLVPAMTLGSGQRGRLNFG 1208
Cdd:cd12877     99 DVVGCCLDLSVPSISFRVNGRPV---QGM---FENFNLDGMFFPVMSFSAGVSCRFLLG 151
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 220-389 4.34e-06

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


Pssm-ID: 467758 [Multi-domain]  Cd Length: 222  Bit Score: 51.22  E-value: 4.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  220 LFGNDVLRLFHGNDE-CLTIPENwsEHPQHNMVIYEGGAAVTQARS---LWRVELIRmkwHGALVG----WEQVFRIKHI 291
Cdd:cd23287     11 LKGGDVVRLFHAEQEkFLTCDEH--RKKQHVFLRTTGRQSATSATSskaLWEVEVVQ---HDPCRGgagyWNSLFRFKHL 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  292 TSGRYLGVLDNSVQlyhkEKADFDLTAFVMCQNKDPKKQMLDEKEE---------EG--------MGNATIRYGET---- 350
Cdd:cd23287     86 ATGHYLAAEVDPDF----EEECLEFQPSVDPDQDASRSRLRNAQEKmvyslvsvpEGndissifeLDPTTLRGGDSlvpr 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1254045463  351 NAFI--QHVKTQLWLSYQTTEVTKkglgkvEEKKAVALKDG 389
Cdd:cd23287    162 NSYVrlRHLCTNTWVHSTNIPIDK------EEEKPVMLKIG 196
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4187-4248 1.97e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.48  E-value: 1.97e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254045463 4187 QAFQDFDTNQDGWISPKEFQRAMESQKMyTVEDITYLMMCTDVNNDGKVDYMEFTE---RFHNPA 4248
Cdd:COG5126     73 AAFDLLDTDGDGKISADEFRRLLTALGV-SEEEADELFARLDTDGDGKISFEEFVAavrDYYTPD 136
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1554-1681 4.77e-05

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: 45.88  E-value: 4.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1554 YYYGIRIFPGQdPSQVWVGWVTTQYhyynvNFDGSQGVRKcrfseaDHHGTTVDSVQSQNCYMVN--VSELLATTPDVan 1631
Cdd:cd11709      3 WYWEVRVDSGN-GGLIQVGWATKSF-----SLDGEGGVGD------DEESWGYDGSRLRKGHGGSsgPGGRPWKSGDV-- 68

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1254045463 1632 tkvsgtlIGCIIDTSIGELSFQVGSTDTGIKFKLEPGAM--LFPAAFVTPTA 1681
Cdd:cd11709     69 -------VGCLLDLDEGTLSFSLNGKDLGVAFTNLFLKGggLYPAVSLGSGQ 113
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 220-297 5.80e-05

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


Pssm-ID: 467759 [Multi-domain]  Cd Length: 222  Bit Score: 47.73  E-value: 5.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  220 LFGNDVLRLFHGNDECLTIPENWsEHPQH---NMVIYEGGAAVTQARSLWRVELIRMK-WHGALVGWEQVFRIKHITSGR 295
Cdd:cd23288     17 LKGGDVVRLFHAEQEKFLTCDEY-KKKQHiflRTTLRQSATSATSSKALWEIEVVHYDpCRGGAGQWNSLFRFKHLATGN 95


                   ..
gi 1254045463  296 YL 297
Cdd:cd23288     96 YL 97
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
 668-794 6.05e-05

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: 46.41  E-value: 6.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  668 KWYFEAEVehietmtkQTPYL-RIGWANsvgfkpfpgsgdkMGCN-GVGDDFYSYGFDGKsmyfGGKS-RRVGHKLLE-- 742
Cdd:cd12873     41 KYYYEVTV--------TDEGLcRVGWST-------------EDASlDLGTDKFGFGYGGT----GKKShGRQFDDYGEpf 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254045463  743 -KGDVIGCSIDLTIPEIKFSVNGTYMSGSFK-KFNIDG-YFFPVMSL-SAKVSCRF 794
Cdd:cd12873     96 gLGDVIGCYLDLDNGTISFSKNGKDLGKAFDiPPHLRNsALFPAVCLkNAEVEFNF 151
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
217-271 1.31e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.71  E-value: 1.31e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045463   217 MGFLFGNDVLRLFHGNDEC-LTIPENW---SEHPQHNMVIYEGGAAVtqARSLWRVELI 271
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRyLHSHDEKlppWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 93-185 1.87e-04

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


Pssm-ID: 467751 [Multi-domain]  Cd Length: 199  Bit Score: 45.84  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463   93 HKSASGAGGhkTLLYGHAVQLKHVQSEMYLaclssCSSNDKLAFDVGVQETNEGEACWWTIHPASKQRSEGekVRVGDDV 172
Cdd:cd23280     68 KEDTPLKGG--VIKWGDQCRLRHLPTGKYL-----AVDDKTGNGKVVLTSDPSDPSTVFRLHPVTKETSEE--VKFGSYV 138

                           90
                   ....*....|...
gi 1254045463  173 ILVSVATERYLHM 185
Cdd:cd23280    139 RIEHVATGTWLHA 151
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 107-303 2.08e-04

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


Pssm-ID: 467750 [Multi-domain]  Cd Length: 173  Bit Score: 45.37  E-value: 2.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  107 YGHAVQLKHVQSEMYLaclsscsSNDKLAFDVG--------VQETNEGEAcWWTIHPA--SKQRSEGEKVRVGDDVILVS 176
Cdd:cd23279      1 YGSAIKLKHVNSGYRL-------HSHEVSYGSGsgqqsvtaVPSADDANS-LWTVLPGlgEPCQEQGKPVKCGDIIRLQH 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  177 VATERYLHmaySKgymviaSFHQTLWNIQSVSSGSmrtrnmgflfGNDVLRlfhGNDecltipenwsehpqhnmviyegg 256
Cdd:cd23279     73 VNTRKNLH---SH------NHSSPLSGNQEVSAFG----------GGDEDS---GDN----------------------- 107

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1254045463  257 aavtqarslWRVELIRMK---WHGalvgwEQVFRIKHITSGRYLGVLDNS 303
Cdd:cd23279    108 ---------WIVECEGKKakfWKR-----GEPVRLKHVDTGKYLSASKTH 143
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
277-303 5.24e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.79  E-value: 5.24e-04
                            10        20
                    ....*....|....*....|....*..
gi 1254045463   277 GALVGWEQVFRIKHITSGRYLGVLDNS 303
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEK 27
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 218-302 9.24e-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: 43.88  E-value: 9.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  218 GFLFGNDVLRLFHGNDE-CLTIPEnwSEHPQHNMVIYEG---GAAVTQARSLWRVELIRmkwHGALVG----WEQVFRIK 289
Cdd:cd23277      9 DVLKGGDVVRLFHAEQEkFLTCDE--YKKKQYVFLRTTGrtsATSATSSKALWEVEVVQ---HDPCRGgaghWNSLFRFK 83

                           90
                   ....*....|...
gi 1254045463  290 HITSGRYLGVLDN 302
Cdd:cd23277     84 HLATGQYLAAEVD 96
PTZ00183 PTZ00183
centrin; Provisional
 4187-4279 1.13e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.75  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 4187 QAFQDFDTNQDGWISPKEFQRAM-----ESQKmytvEDITYLMMCTDVNNDGKVDYMEF----TERFHN--PARDI--GF 4253
Cdd:PTZ00183    21 EAFDLFDTDGSGTIDPKELKVAMrslgfEPKK----EEIKQMIADVDKDGSGKIDFEEFldimTKKLGErdPREEIlkAF 96

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1254045463 4254 NL-------AVLLVNLK-------EHITnDPRLEKIIEKA 4279
Cdd:PTZ00183    97 RLfdddktgKISLKNLKrvakelgETIT-DEELQEMIDEA 135
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 220-302 1.16e-03

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


Pssm-ID: 467760 [Multi-domain]  Cd Length: 215  Bit Score: 43.88  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463  220 LFGNDVLRLFHGNDE-CLTIPENWSE-HPQHNMVIYEGGAAVTQARSLWRVELIRMK-WHGALVGWEQVFRIKHITSGRY 296
Cdd:cd23289     11 LKGGDVVRLFHAEQEkFLTCDEYKGKlQVFLRTTLRQSATSATSSNALWEVEVVHHDpCRGGAGHWNGLYRFKHLATGNY 90


                   ....*.
gi 1254045463  297 LGVLDN 302
Cdd:cd23289     91 LAAEEN 96
EF-hand_8 pfam13833
EF-hand domain pair;
4196-4240 3.08e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.84  E-value: 3.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1254045463 4196 QDGWISPKEFQRAME--SQKMYTVEDITYLMMCTDVNNDGKVDYMEF 4240
Cdd:pfam13833    1 EKGVITREELKRALAllGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
 1115-1197 8.06e-03

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


Pssm-ID: 293947  Cd Length: 172  Bit Score: 40.69  E-value: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045463 1115 EIQLGADDRSYA--FDGylGRKW--HQGAETYGKEWKI--GDVVGCFLDLNDRTISFSLNGEllldPSGsEMAFDNVvcg 1188
Cdd:cd12889     78 DKMLGKDDKGWSmyIDN--NRSWflHNNEHSNRTEGGItvGSVVGVLLDLDRHTLSFYVNDE----PQG-PIAFRNL--- 147

                           90
                   ....*....|
gi 1254045463 1189 DGLV-PAMTL 1197
Cdd:cd12889    148 PGVFyPAVSL 157
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 4193-4245 8.12e-03

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 41.66  E-value: 8.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1254045463 4193 DTNQDGWISPKEFQR-AMESQKMYTVEDITYLMMCTDVNNDGKVDYMEFTERFH 4245
Cdd:cd15899     45 DVDKDGFISAKELHSwILESFKRHAMEESKEQFRAVDPDEDGHVSWDEYKNDTY 98
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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