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Conserved domains on  [gi|1254045448|ref|NP_001343811|]
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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 ...
224-403 4.82e-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: 4.82e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  224 GNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYLGVL 302
Cdd:cd23278      1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  303 -DNSVQLYHKEKADFDLTAFVMCQNKDPKKqMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEvTKKGLGKVE 381
Cdd:cd23278     81 eDRGLVLVPKEKADVKATAFCFRQSKDDKK-VLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVE-TKKRVGGVE 158
                          170       180
                   ....*....|....*....|..
gi 1254045448  382 EKKAVALKDGHMDDCYTFFMAL 403
Cdd:cd23278    159 ERKAILHAEGHMDDGLSLSRAQ 180
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
652-799 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 1254045448  652 SMMPNVMLGVVEGSALFRKWYFEAEVEHIETMTKQTPYLRIGWANSVGFKPFPGSGDKMGCNGVGDDFYSYGFDGKSMYF 731
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTHQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLWT 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254045448  732 GGKSRRVGH---KLLEKGDVIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSLSAKVSCRFILG 799
Cdd:cd12877     81 GGRSRRVTSgtqHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
1078-1210 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 1254045448 1078 RTYRAEATYAVCGGKWYFEFEILTAGYMKIGWMDIGSTPEIQLGADDRSYAFDGYLGRKWHQGAETYGKEWKIGDVVGCF 1157
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1254045448 1158 LDLNDRTISFSLNGELLLDPSGSEMAFDNVVCGDGLVPAMTLGSGQRGRLNFG 1210
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
451-646 1.10e-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: 1.10e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  451 LMEDLIEYFAQPNDEQDFEEKQNHL---RALRSRQDLFQEEGVLNMILDTIDKFS-QMEALPDFAGLIGEETHVKWEQIS 526
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  527 TYLYLLVAAMIKGNHYNCAQFASAqrLDWLFGRLSNPQSAEGILDVLYCVLTESPE-ALNMINEGHIRSVISLLEKVGRD 605
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKH--LDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRD 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1254045448  606 PKVLDVLSSLCEGNGMAVRSSQNLITQYLLPGKDLLLQTSM 646
Cdd:pfam01365  159 PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
1542-1692 4.11e-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: 4.11e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 1542 DAHALVHHKDKVDEYYYGIRIFPGQDPSQVWVGWVTTQYHYYNVNFDGSQgVRKCRFSEADHHGTTVDSVQSQNCYMVNV 1621
Cdd:cd12879      1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDK-VRNVTVTMGDEKGGVYESIKRQNCYMVCA 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254045448 1622 SELLA-TTPDVANTKVSGTLIGCIIDTSIGELSFQVGSTDTGIKFKLEPGAMLFPAAFVTPTATEILQFELG 1692
Cdd:cd12879     80 GELLAeVGQDSSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
2244-2467 3.10e-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: 221.30  E-value: 3.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2244 QIRELLTVQFEHTEEAILKRGLWKLMNNRIFFQHPDLMRLLSVHENVMSImMNILTAQQGTVEHEGDELKEKAPIkDASE 2323
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEV-IDLLGAPFTGALLFAEDLGEEKNA-PWKK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2324 MVVACSRFLCYFCRTSRQNQKAMFEHLSFLLDNatmlLARPSLRGSVpLDVAYSSFMDNNELALalkeeeldkvaVYLSR 2403
Cdd:pfam01365   79 IVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKE 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254045448 2404 CGLQPNSELITKGYPDigwdpvegERYIDFLRF-CVwINGENVEENANLVIRLLIRRPECLGVAL 2467
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 ...
14-213 5.54e-63

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: 215.44  E-value: 5.54e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448   14 DVSFLRTGDIVCLSCVASHNrdgvlgserVCLCTEGFGNRMCTLENVSDKDI--PPDIAMCMLYIDNALSMRALQEMMSA 91
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVN---------GFISALGLGNDRCFVENKAGDLNdpPKKFRDCVFKICPANSYAAQKELWSA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448   92 DS----------DHKSASGAGGHKTLLYGHAVQLKHVQSEMYLACL-SSCSSNDKLAFDVGVQETNEGEACWWTIHPASK 160
Cdd:pfam08709   72 GNrspngnsltdALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLkSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYK 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045448  161 QRSEGEKVRVGDDVILVSVATERYLHMAYS------KGYMVIASFHQTLWNIQSVSSGS 213
Cdd:pfam08709  152 QRSEGDNVCVGDEVILVPVSAPIFLHTTSSselrdnPGKEVNASFGQTSWKMEPFMSGC 210
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
853-941 1.49e-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: 1.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  853 FIPTPIDVSATQLNHHATEMHQKYAENLHELWAMRKIELGWSYGETRSETSRKHPCLTKFEYLPETEKKYNILLALTTMK 932
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                   ....*....
gi 1254045448  933 TIEALGYHL 941
Cdd:pfam02026   81 TLLALGYTI 89
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
3991-4108 1.12e-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: 132.65  E-value: 1.12e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 3991 NDADFTCSLFRFLQLTCEGHNLEFQNYLRTQPGHTTSVNLINCTVDYLLRLQESvmdfywhysskevIDEggkeyflRAI 4070
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKS-------------INE-------KNI 60
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1254045448 4071 QVCSQVFNTLTESIQGPCVGNQMTLANSRLWDAINGFF 4108
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
965-1056 9.39e-34

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


:

Pssm-ID: 460419  Cd Length: 90  Bit Score: 126.85  E-value: 9.39e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  965 YKPGPLDTHEIQLPAELQPLTEALARNTHNIWAKEKIKRGWTFGlsEHVDATQKRSPHLVPYEQVDERIKQANRESAAEN 1044
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYG--EVRDDAAKTHPCLVPYDLLTEKEKEYDREPARET 78
                           90
                   ....*....|..
gi 1254045448 1045 IRALQLFGIFLE 1056
Cdd:pfam02026   79 LKTLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
2837-2926 2.04e-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: 123.00  E-value: 2.04e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2837 WIPRTVDVSRCEINRDLEKMTELFAEHFHDSWASRKLEKGWVHGDLYSRANFTHPRLKPFALLKDFEKSFYKERCSECLK 2916
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80
                           90
                   ....*....|
gi 1254045448 2917 ALMAWNYSFE 2926
Cdd:pfam02026   81 TLLALGYTIE 90
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
2950-3032 4.07e-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: 4.07e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2950 FAPKPIDLSSMTLEKDMVNAAEKMAEHSHLIWAKKVMNDLNTKGGFMPIP------LVPWDLLTDFERRKDRFRASEILK 3023
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAakthpcLVPYDLLTEKEKEYDREPARETLK 80

                   ....*....
gi 1254045448 3024 FLQYHGYHV 3032
Cdd:pfam02026   81 TLLALGYTI 89
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
4839-4981 5.15e-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: 5.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4839 FFYAFHLIDVVLSFPMLKAILQSVTHNLQQLILTIMMTLVVVYLYTVIAFNFFRKFYvQEGEEGEEPDRKCHNMLTCFIY 4918
Cdd:pfam00520   99 LLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL-KTWENPDNGRTNFDNFPNAFLW 177
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254045448 4919 HFYagVRAGGGIGDELESPYGDDLEYPRMFYDISFFFFVIIILLAIMQGLIIDAFGELRDQQE 4981
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 ...
4532-4712 1.05e-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: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4532 VPPERPETPETVLEEEKPLNQETSPPTSPTSPASKAPSIYES--IGAPQMVQLQSEADFQQGQYEPKIaESNSTKsrgsI 4609
Cdd:pfam06459   98 EEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMkkKQRKRHSKKKEEPEAQGSAFWNEL-EVYQTK----L 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4610 LNMLARNFKTIEKITLYLAFFINVILLFHRVDISHAENAEAAS---------------EGDDDEDALESifitgmqfpYV 4674
Cdd:pfam06459  173 LNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGsgwgdsgsgsgggsgEDEEEEEGPVY---------FV 243
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1254045448 4675 EYEITGWMlAQILYWISVLHLSTSFALLVSFYQLKIPL 4712
Cdd:pfam06459  244 LEESTGYM-EPTLRFLAILHTIISFLCIIGYYCLKVPL 280
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
4191-4245 1.61e-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: 1.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254045448 4191 AFQDFDTNQDGWISPKEFQRAMESQKMYTVEDITYLMMCT-DVNNDGKVDYMEFTE 4245
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 ...
224-403 4.82e-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: 4.82e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  224 GNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYLGVL 302
Cdd:cd23278      1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  303 -DNSVQLYHKEKADFDLTAFVMCQNKDPKKqMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEvTKKGLGKVE 381
Cdd:cd23278     81 eDRGLVLVPKEKADVKATAFCFRQSKDDKK-VLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVE-TKKRVGGVE 158
                          170       180
                   ....*....|....*....|..
gi 1254045448  382 EKKAVALKDGHMDDCYTFFMAL 403
Cdd:cd23278    159 ERKAILHAEGHMDDGLSLSRAQ 180
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
652-799 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 1254045448  652 SMMPNVMLGVVEGSALFRKWYFEAEVEHIETMTKQTPYLRIGWANSVGFKPFPGSGDKMGCNGVGDDFYSYGFDGKSMYF 731
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTHQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLWT 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254045448  732 GGKSRRVGH---KLLEKGDVIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSLSAKVSCRFILG 799
Cdd:cd12877     81 GGRSRRVTSgtqHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
1078-1210 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 1254045448 1078 RTYRAEATYAVCGGKWYFEFEILTAGYMKIGWMDIGSTPEIQLGADDRSYAFDGYLGRKWHQGAETYGKEWKIGDVVGCF 1157
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1254045448 1158 LDLNDRTISFSLNGELLLDPSGSEMAFDNVVCGDGLVPAMTLGSGQRGRLNFG 1210
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
451-646 1.10e-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: 1.10e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  451 LMEDLIEYFAQPNDEQDFEEKQNHL---RALRSRQDLFQEEGVLNMILDTIDKFS-QMEALPDFAGLIGEETHVKWEQIS 526
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  527 TYLYLLVAAMIKGNHYNCAQFASAqrLDWLFGRLSNPQSAEGILDVLYCVLTESPE-ALNMINEGHIRSVISLLEKVGRD 605
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKH--LDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRD 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1254045448  606 PKVLDVLSSLCEGNGMAVRSSQNLITQYLLPGKDLLLQTSM 646
Cdd:pfam01365  159 PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
1542-1692 4.11e-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: 4.11e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 1542 DAHALVHHKDKVDEYYYGIRIFPGQDPSQVWVGWVTTQYHYYNVNFDGSQgVRKCRFSEADHHGTTVDSVQSQNCYMVNV 1621
Cdd:cd12879      1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDK-VRNVTVTMGDEKGGVYESIKRQNCYMVCA 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254045448 1622 SELLA-TTPDVANTKVSGTLIGCIIDTSIGELSFQVGSTDTGIKFKLEPGAMLFPAAFVTPTATEILQFELG 1692
Cdd:cd12879     80 GELLAeVGQDSSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
2244-2467 3.10e-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: 221.30  E-value: 3.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2244 QIRELLTVQFEHTEEAILKRGLWKLMNNRIFFQHPDLMRLLSVHENVMSImMNILTAQQGTVEHEGDELKEKAPIkDASE 2323
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEV-IDLLGAPFTGALLFAEDLGEEKNA-PWKK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2324 MVVACSRFLCYFCRTSRQNQKAMFEHLSFLLDNatmlLARPSLRGSVpLDVAYSSFMDNNELALalkeeeldkvaVYLSR 2403
Cdd:pfam01365   79 IVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKE 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254045448 2404 CGLQPNSELITKGYPDigwdpvegERYIDFLRF-CVwINGENVEENANLVIRLLIRRPECLGVAL 2467
Cdd:pfam01365  143 CHIKSFISLLRKHGRD--------PRYLDFLSDlCV-CNGEAVRENQNLICRLLLPNPDLLLQTL 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
220-399 3.78e-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: 3.78e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  220 GFLFGNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRM-KWHGALVGWEQVFRIKHITSGR 297
Cdd:pfam02815    1 GYLKGGDVVRLFHSHqDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  298 YLGVLDN-SVQLYHKEKADFDLTAFVMCQNKDPK--KQMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEVTK 374
Cdd:pfam02815   81 YLHSHEEqKPPLVEKEDWQKEVSAYGFRGFPGDNdiVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160
                          170       180
                   ....*....|....*....|....*
gi 1254045448  375 KGLGKvEEKKAVALKDGHMDDCYTF 399
Cdd:pfam02815  161 WGFGP-EQQKVTCAKEGHMDDALTL 184
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
14-213 5.54e-63

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: 215.44  E-value: 5.54e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448   14 DVSFLRTGDIVCLSCVASHNrdgvlgserVCLCTEGFGNRMCTLENVSDKDI--PPDIAMCMLYIDNALSMRALQEMMSA 91
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVN---------GFISALGLGNDRCFVENKAGDLNdpPKKFRDCVFKICPANSYAAQKELWSA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448   92 DS----------DHKSASGAGGHKTLLYGHAVQLKHVQSEMYLACL-SSCSSNDKLAFDVGVQETNEGEACWWTIHPASK 160
Cdd:pfam08709   72 GNrspngnsltdALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLkSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYK 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045448  161 QRSEGEKVRVGDDVILVSVATERYLHMAYS------KGYMVIASFHQTLWNIQSVSSGS 213
Cdd:pfam08709  152 QRSEGDNVCVGDEVILVPVSAPIFLHTTSSselrdnPGKEVNASFGQTSWKMEPFMSGC 210
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
853-941 1.49e-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: 1.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  853 FIPTPIDVSATQLNHHATEMHQKYAENLHELWAMRKIELGWSYGETRSETSRKHPCLTKFEYLPETEKKYNILLALTTMK 932
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                   ....*....
gi 1254045448  933 TIEALGYHL 941
Cdd:pfam02026   81 TLLALGYTI 89
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
3991-4108 1.12e-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: 132.65  E-value: 1.12e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 3991 NDADFTCSLFRFLQLTCEGHNLEFQNYLRTQPGHTTSVNLINCTVDYLLRLQESvmdfywhysskevIDEggkeyflRAI 4070
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKS-------------INE-------KNI 60
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1254045448 4071 QVCSQVFNTLTESIQGPCVGNQMTLANSRLWDAINGFF 4108
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
965-1056 9.39e-34

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 126.85  E-value: 9.39e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  965 YKPGPLDTHEIQLPAELQPLTEALARNTHNIWAKEKIKRGWTFGlsEHVDATQKRSPHLVPYEQVDERIKQANRESAAEN 1044
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYG--EVRDDAAKTHPCLVPYDLLTEKEKEYDREPARET 78
                           90
                   ....*....|..
gi 1254045448 1045 IRALQLFGIFLE 1056
Cdd:pfam02026   79 LKTLLALGYTIE 90
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
1091-1212 1.34e-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: 1.34e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  1091 GKWYFEFEILTAGYMKIGW--MDIGSTPEIQLGADDRSYAFDGYLGRKWHQG-AETYGKEWKI-GDVVGCFLDLNDRTIS 1166
Cdd:smart00449    2 GRHYFEVEIGDGGHWRVGVatKSVPRGYFALLGEDKGSWGYDGDGGKKYHNStGPEYGLPLQEpGDVIGCFLDLEAGTIS 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1254045448  1167 FSLNGELLldpsgSEMAFDNVVCGDGLVPAMTLGSGQRGRLNFGQQ 1212
Cdd:smart00449   82 FYKNGKYL-----HGLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
2837-2926 2.04e-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: 123.00  E-value: 2.04e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2837 WIPRTVDVSRCEINRDLEKMTELFAEHFHDSWASRKLEKGWVHGDLYSRANFTHPRLKPFALLKDFEKSFYKERCSECLK 2916
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80
                           90
                   ....*....|
gi 1254045448 2917 ALMAWNYSFE 2926
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 ...
670-801 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 1254045448  670 KWYFEAEVEhietmTKQTPYLRIGWANsvgfKPFPGSGDKMgcngVGDDFYSYGFDG--KSMYFGGKSRRVGHKLLEKGD 747
Cdd:pfam00622    1 RHYFEVEIF-----GQDGGGWRVGWAT----KSVPRKGERF----LGDESGSWGYDGwtGKKYWASTSPLTGLPLFEPGD 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1254045448  748 VIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSLSAKVSCRFILGGN 801
Cdd:pfam00622   68 VIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
670-801 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 1254045448   670 KWYFEAEVEHietmtkqTPYLRIGWANSvgfkpfpgSGDKMGCNGVGDDFYSYGFDG--KSMYFGGKSRRVGHKLLEKGD 747
Cdd:smart00449    3 RHYFEVEIGD-------GGHWRVGVATK--------SVPRGYFALLGEDKGSWGYDGdgGKKYHNSTGPEYGLPLQEPGD 67
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1254045448   748 VIGCSIDLTIPEIKFSVNGTYMSG-SFKKFNIDGYFFPVMSLSAKVSCRFILGGN 801
Cdd:smart00449   68 VIGCFLDLEAGTISFYKNGKYLHGlAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
2950-3032 4.07e-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: 4.07e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2950 FAPKPIDLSSMTLEKDMVNAAEKMAEHSHLIWAKKVMNDLNTKGGFMPIP------LVPWDLLTDFERRKDRFRASEILK 3023
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAakthpcLVPYDLLTEKEKEYDREPARETLK 80

                   ....*....
gi 1254045448 3024 FLQYHGYHV 3032
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 ...
1092-1212 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 1254045448 1092 KWYFEFEILTA--GYMKIGW--MDIGSTPEIQLGADDRSYAFDGYLGRKWH--QGAETYGKEWKIGDVVGCFLDLNDRTI 1165
Cdd:pfam00622    1 RHYFEVEIFGQdgGGWRVGWatKSVPRKGERFLGDESGSWGYDGWTGKKYWasTSPLTGLPLFEPGDVIGCFLDYEAGTI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1254045448 1166 SFSLNGELLLDpsgsemAFDNVVCGDGLVPAMTLGSGQRGRLNFGQQ 1212
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 ...
1556-1694 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 1254045448 1556 YYYGIRIFpGQDPSQVWVGWVTTQYHYYNVNFDGsqgvrkcrfseadhhgTTVDSVQSQNCYMV--------NVSELLAT 1627
Cdd:pfam00622    2 HYFEVEIF-GQDGGGWRVGWATKSVPRKGERFLG----------------DESGSWGYDGWTGKkywastspLTGLPLFE 64
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254045448 1628 TPDVantkvsgtlIGCIIDTSIGELSFQVGSTDTGIKFKLEPGA-MLFPAAFVTPtaTEILQFELGRI 1694
Cdd:pfam00622   65 PGDV---------IGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSLGA--GEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
1556-1694 2.48e-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: 2.48e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  1556 YYYGIRIFpgqDPSQVWVGWVTTQYHYYNVNFDGSqgvrkcrfseaDHHGTTVDSVQSQNCYMVNVSE---LLATTPDVa 1632
Cdd:smart00449    4 HYFEVEIG---DGGHWRVGVATKSVPRGYFALLGE-----------DKGSWGYDGDGGKKYHNSTGPEyglPLQEPGDV- 68
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1254045448  1633 ntkvsgtlIGCIIDTSIGELSFQVGSTDTGIK--FKLEPGAMLFPAAFVTPtaTEILQFELGRI 1694
Cdd:smart00449   69 --------IGCFLDLEAGTISFYKNGKYLHGLafFDVKFSGPLYPAFSLGS--GNSVRLNFGPL 122
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
4839-4981 5.15e-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: 5.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4839 FFYAFHLIDVVLSFPMLKAILQSVTHNLQQLILTIMMTLVVVYLYTVIAFNFFRKFYvQEGEEGEEPDRKCHNMLTCFIY 4918
Cdd:pfam00520   99 LLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL-KTWENPDNGRTNFDNFPNAFLW 177
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254045448 4919 HFYagVRAGGGIGDELESPYGDDLEYPRMFYDISFFFFVIIILLAIMQGLIIDAFGELRDQQE 4981
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 ...
4532-4712 1.05e-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: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4532 VPPERPETPETVLEEEKPLNQETSPPTSPTSPASKAPSIYES--IGAPQMVQLQSEADFQQGQYEPKIaESNSTKsrgsI 4609
Cdd:pfam06459   98 EEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMkkKQRKRHSKKKEEPEAQGSAFWNEL-EVYQTK----L 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4610 LNMLARNFKTIEKITLYLAFFINVILLFHRVDISHAENAEAAS---------------EGDDDEDALESifitgmqfpYV 4674
Cdd:pfam06459  173 LNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGsgwgdsgsgsgggsgEDEEEEEGPVY---------FV 243
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1254045448 4675 EYEITGWMlAQILYWISVLHLSTSFALLVSFYQLKIPL 4712
Cdd:pfam06459  244 LEESTGYM-EPTLRFLAILHTIISFLCIIGYYCLKVPL 280
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
4191-4245 1.61e-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: 1.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254045448 4191 AFQDFDTNQDGWISPKEFQRAMESQKMYTVEDITYLMMCT-DVNNDGKVDYMEFTE 4245
Cdd:cd00051      5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREvDKDGDGKIDFEEFLE 60
EF-hand_7 pfam13499
EF-hand domain pair;
4190-4247 4.12e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.94  E-value: 4.12e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254045448 4190 QAFQDFDTNQDGWISPKEFQRAMESQKM---YTVEDITYLMMCTDVNNDGKVDYMEFTERF 4247
Cdd:pfam13499    6 EAFKLLDSDGDGYLDVEELKKLLRKLEEgepLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4190-4251 1.89e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.48  E-value: 1.89e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254045448 4190 QAFQDFDTNQDGWISPKEFQRAMESQKMyTVEDITYLMMCTDVNNDGKVDYMEFTE---RFHNPA 4251
Cdd:COG5126     73 AAFDLLDTDGDGKISADEFRRLLTALGV-SEEEADELFARLDTDGDGKISFEEFVAavrDYYTPD 136
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
12-187 1.06e-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: 46.61  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448   12 QDDVSFLRTGDIVCLSCvasHNRDGVLGservclCTEGFGNRMCTlENVSDKdippdiamcmLYIDNALSMRALQEMMSA 91
Cdd:cd23280      1 KENENFLKGGDVVRLFH---KELEAYLS------AEGSFVDEVLT-EDVHLR----------VRPVDDRKPRTLFPPTSG 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448   92 DS----DHKSASGAGGhkTLLYGHAVQLKHVQSEMYLaclssCSSNDKLAFDVGVQETNEGEACWWTIHPASKQRSEGek 167
Cdd:cd23280     61 DTfwqiEKEDTPLKGG--VIKWGDQCRLRHLPTGKYL-----AVDDKTGNGKVVLTSDPSDPSTVFRLHPVTKETSEE-- 131
                          170       180
                   ....*....|....*....|
gi 1254045448  168 VRVGDDVILVSVATERYLHM 187
Cdd:cd23280    132 VKFGSYVRIEHVATGTWLHA 151
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
219-273 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 1254045448   219 MGFLFGNDVLRLFHGNDEC-LTIPENW---SEHPQHNMVIYEGGAAVtqARSLWRVELI 273
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRyLHSHDEKlppWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
PTZ00183 PTZ00183
centrin; Provisional
4190-4282 1.00e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 43.14  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4190 QAFQDFDTNQDGWISPKEFQRAM-----ESQKmytvEDITYLMMCTDVNNDGKVDYMEF----TERFHN--PARDI--GF 4256
Cdd:PTZ00183    21 EAFDLFDTDGSGTIDPKELKVAMrslgfEPKK----EEIKQMIADVDKDGSGKIDFEEFldimTKKLGErdPREEIlkAF 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1254045448 4257 NL-------AVLLVNLK-------EHITnDPRLEKIIEKA 4282
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 ...
224-403 4.82e-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: 4.82e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  224 GNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYLGVL 302
Cdd:cd23278      1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  303 -DNSVQLYHKEKADFDLTAFVMCQNKDPKKqMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEvTKKGLGKVE 381
Cdd:cd23278     81 eDRGLVLVPKEKADVKATAFCFRQSKDDKK-VLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVE-TKKRVGGVE 158
                          170       180
                   ....*....|....*....|..
gi 1254045448  382 EKKAVALKDGHMDDCYTFFMAL 403
Cdd:cd23278    159 ERKAILHAEGHMDDGLSLSRAQ 180
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
652-799 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 1254045448  652 SMMPNVMLGVVEGSALFRKWYFEAEVEHIETMTKQTPYLRIGWANSVGFKPFPGSGDKMGCNGVGDDFYSYGFDGKSMYF 731
Cdd:cd12877      1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQFTHQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLWT 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254045448  732 GGKSRRVGH---KLLEKGDVIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSLSAKVSCRFILG 799
Cdd:cd12877     81 GGRSRRVTSgtqHLLKKGDVVGCCLDLSVPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151
SPRY2_RyR cd12878
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...
1078-1210 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 1254045448 1078 RTYRAEATYAVCGGKWYFEFEILTAGYMKIGWMDIGSTPEIQLGADDRSYAFDGYLGRKWHQGAETYGKEWKIGDVVGCF 1157
Cdd:cd12878      1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1254045448 1158 LDLNDRTISFSLNGELLLDPSGSEMAFDNVVCGDGLVPAMTLGSGQRGRLNFG 1210
Cdd:cd12878     81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
451-646 1.10e-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: 1.10e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  451 LMEDLIEYFAQPNDEQDFEEKQNHL---RALRSRQDLFQEEGVLNMILDTIDKFS-QMEALPDFAGLIGEETHVKWEQIS 526
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  527 TYLYLLVAAMIKGNHYNCAQFASAqrLDWLFGRLSNPQSAEGILDVLYCVLTESPE-ALNMINEGHIRSVISLLEKVGRD 605
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKH--LDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRD 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1254045448  606 PKVLDVLSSLCEGNGMAVRSSQNLITQYLLPGKDLLLQTSM 646
Cdd:pfam01365  159 PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199
SPRY3_RyR cd12879
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...
1542-1692 4.11e-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: 4.11e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 1542 DAHALVHHKDKVDEYYYGIRIFPGQDPSQVWVGWVTTQYHYYNVNFDGSQgVRKCRFSEADHHGTTVDSVQSQNCYMVNV 1621
Cdd:cd12879      1 DDRDDPSALDLVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDK-VRNVTVTMGDEKGGVYESIKRQNCYMVCA 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254045448 1622 SELLA-TTPDVANTKVSGTLIGCIIDTSIGELSFQVGSTDTGIKFKLEPGAMLFPAAFVTPTATEILQFELG 1692
Cdd:cd12879     80 GELLAeVGQDSSGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
2244-2467 3.10e-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: 221.30  E-value: 3.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2244 QIRELLTVQFEHTEEAILKRGLWKLMNNRIFFQHPDLMRLLSVHENVMSImMNILTAQQGTVEHEGDELKEKAPIkDASE 2323
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEV-IDLLGAPFTGALLFAEDLGEEKNA-PWKK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2324 MVVACSRFLCYFCRTSRQNQKAMFEHLSFLLDNatmlLARPSLRGSVpLDVAYSSFMDNNELALalkeeeldkvaVYLSR 2403
Cdd:pfam01365   79 IVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKE 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254045448 2404 CGLQPNSELITKGYPDigwdpvegERYIDFLRF-CVwINGENVEENANLVIRLLIRRPECLGVAL 2467
Cdd:pfam01365  143 CHIKSFISLLRKHGRD--------PRYLDFLSDlCV-CNGEAVRENQNLICRLLLPNPDLLLQTL 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
220-399 3.78e-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: 3.78e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  220 GFLFGNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRM-KWHGALVGWEQVFRIKHITSGR 297
Cdd:pfam02815    1 GYLKGGDVVRLFHSHqDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  298 YLGVLDN-SVQLYHKEKADFDLTAFVMCQNKDPK--KQMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEVTK 374
Cdd:pfam02815   81 YLHSHEEqKPPLVEKEDWQKEVSAYGFRGFPGDNdiVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160
                          170       180
                   ....*....|....*....|....*
gi 1254045448  375 KGLGKvEEKKAVALKDGHMDDCYTF 399
Cdd:pfam02815  161 WGFGP-EQQKVTCAKEGHMDDALTL 184
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
14-213 5.54e-63

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: 215.44  E-value: 5.54e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448   14 DVSFLRTGDIVCLSCVASHNrdgvlgserVCLCTEGFGNRMCTLENVSDKDI--PPDIAMCMLYIDNALSMRALQEMMSA 91
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVN---------GFISALGLGNDRCFVENKAGDLNdpPKKFRDCVFKICPANSYAAQKELWSA 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448   92 DS----------DHKSASGAGGHKTLLYGHAVQLKHVQSEMYLACL-SSCSSNDKLAFDVGVQETNEGEACWWTIHPASK 160
Cdd:pfam08709   72 GNrspngnsltdALKHASNIEGHQNLQYGSAILLLHVKSNMYLAVLkSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYK 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045448  161 QRSEGEKVRVGDDVILVSVATERYLHMAYS------KGYMVIASFHQTLWNIQSVSSGS 213
Cdd:pfam08709  152 QRSEGDNVCVGDEVILVPVSAPIFLHTTSSselrdnPGKEVNASFGQTSWKMEPFMSGC 210
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
220-407 1.32e-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: 1.32e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  220 GFLFGNDVLRLFHGNDECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYL 299
Cdd:cd23292      1 GYLLGGHVVRLFHGHDECLTIPSTDQSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHYL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  300 GVL-DNSVQLYHKEKADFDLTAFVMCQNKDpKKQMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEVTKKGLG 378
Cdd:cd23292     81 ALTeDQGLILQDRAKSDTKSTAFCFRASKE-KLESGPKRDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSRLG 159
                          170       180
                   ....*....|....*....|....*....
gi 1254045448  379 KVeEKKAVALKDGHMDDCYTFFMALEEES 407
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, ...
220-407 1.34e-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: 1.34e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  220 GFLFGNDVLRLFHGN-DECLTIPENWSEHpQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRY 298
Cdd:cd23290      6 GYVTGGHVLRLFHGHmDECLTISAADSDD-QRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  299 LGVL-DNSVQLYHKEKADFDLTAFVMCQNKDpKKQMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEVTKKGL 377
Cdd:cd23290     85 LALTeDQGLVVVDACKAHTKATSFCFRVSKE-KLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRL 163
                          170       180       190
                   ....*....|....*....|....*....|
gi 1254045448  378 GKVeEKKAVALKDGHMDDCYTFFMALEEES 407
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, ...
224-407 2.04e-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: 2.04e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  224 GNDVLRLFHGN-DECLTIPENWSEHPQHNMVIYEGGAAVTQARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYLGVL 302
Cdd:cd23291      1 GGDVLRLLHGHmDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  303 DN-SVQLYHKEKADFDLTAFVMCQNKDpKKQMLDEKEEEGMGNATIRYGETNAFIQHVKTQLWLSYQTTEVTKKGLGKVe 381
Cdd:cd23291     81 EDkNLLLMDKEKADVKSTAFTFRSSKE-KLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGSI- 158
                          170       180
                   ....*....|....*....|....*.
gi 1254045448  382 EKKAVALKDGHMDDCYTFFMALEEES 407
Cdd:cd23291    159 QRKAIMHHEGHMDDGLNLSRSQHEES 184
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
853-941 1.49e-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: 1.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  853 FIPTPIDVSATQLNHHATEMHQKYAENLHELWAMRKIELGWSYGETRSETSRKHPCLTKFEYLPETEKKYNILLALTTMK 932
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                   ....*....
gi 1254045448  933 TIEALGYHL 941
Cdd:pfam02026   81 TLLALGYTI 89
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
3991-4108 1.12e-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: 132.65  E-value: 1.12e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 3991 NDADFTCSLFRFLQLTCEGHNLEFQNYLRTQPGHTTSVNLINCTVDYLLRLQESvmdfywhysskevIDEggkeyflRAI 4070
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKS-------------INE-------KNI 60
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1254045448 4071 QVCSQVFNTLTESIQGPCVGNQMTLANSRLWDAINGFF 4108
Cdd:pfam08454   61 ELIIQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
965-1056 9.39e-34

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


Pssm-ID: 460419  Cd Length: 90  Bit Score: 126.85  E-value: 9.39e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  965 YKPGPLDTHEIQLPAELQPLTEALARNTHNIWAKEKIKRGWTFGlsEHVDATQKRSPHLVPYEQVDERIKQANRESAAEN 1044
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYG--EVRDDAAKTHPCLVPYDLLTEKEKEYDREPARET 78
                           90
                   ....*....|..
gi 1254045448 1045 IRALQLFGIFLE 1056
Cdd:pfam02026   79 LKTLLALGYTIE 90
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
1091-1212 1.34e-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: 1.34e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  1091 GKWYFEFEILTAGYMKIGW--MDIGSTPEIQLGADDRSYAFDGYLGRKWHQG-AETYGKEWKI-GDVVGCFLDLNDRTIS 1166
Cdd:smart00449    2 GRHYFEVEIGDGGHWRVGVatKSVPRGYFALLGEDKGSWGYDGDGGKKYHNStGPEYGLPLQEpGDVIGCFLDLEAGTIS 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1254045448  1167 FSLNGELLldpsgSEMAFDNVVCGDGLVPAMTLGSGQRGRLNFGQQ 1212
Cdd:smart00449   82 FYKNGKYL-----HGLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
2837-2926 2.04e-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: 123.00  E-value: 2.04e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2837 WIPRTVDVSRCEINRDLEKMTELFAEHFHDSWASRKLEKGWVHGDLYSRANFTHPRLKPFALLKDFEKSFYKERCSECLK 2916
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80
                           90
                   ....*....|
gi 1254045448 2917 ALMAWNYSFE 2926
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 ...
1084-1210 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 1254045448 1084 ATYAVCGGKWYFEFEILTAGYMKIGWMDIGS--TPEIQLGADDRSYAFDGYLGRKWHQGAETYGKEWKIGDVVGCFLDLN 1161
Cdd:cd12882      4 ANACVYKGKWMYEVTLGTKGIMQIGWATISCrfTQEEGVGDTRDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDLD 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1254045448 1162 DRTISFSLNGELLldpsgsEMAFDNVVCGDGLV--PAMTLGSGQRGRLNFG 1210
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 ...
670-801 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 1254045448  670 KWYFEAEVEhietmTKQTPYLRIGWANsvgfKPFPGSGDKMgcngVGDDFYSYGFDG--KSMYFGGKSRRVGHKLLEKGD 747
Cdd:pfam00622    1 RHYFEVEIF-----GQDGGGWRVGWAT----KSVPRKGERF----LGDESGSWGYDGwtGKKYWASTSPLTGLPLFEPGD 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1254045448  748 VIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSLSAKVSCRFILGGN 801
Cdd:pfam00622   68 VIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
1091-1208 6.72e-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: 6.72e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 1091 GKWYFEFEILTA--GYMKIGWM--DIGSTPEIQLGADDRSYAFDGYLGRKWHQGAETYG-KEWKIGDVVGCFLDLNDRTI 1165
Cdd:cd11709      1 GKWYWEVRVDSGngGLIQVGWAtkSFSLDGEGGVGDDEESWGYDGSRLRKGHGGSSGPGgRPWKSGDVVGCLLDLDEGTL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1254045448 1166 SFSLNGELLldpsGSemAFDNVVC-GDGLVPAMTLGSGQRGRLN 1208
Cdd:cd11709     81 SFSLNGKDL----GV--AFTNLFLkGGGLYPAVSLGSGQGVTIN 118
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
670-801 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 1254045448   670 KWYFEAEVEHietmtkqTPYLRIGWANSvgfkpfpgSGDKMGCNGVGDDFYSYGFDG--KSMYFGGKSRRVGHKLLEKGD 747
Cdd:smart00449    3 RHYFEVEIGD-------GGHWRVGVATK--------SVPRGYFALLGEDKGSWGYDGdgGKKYHNSTGPEYGLPLQEPGD 67
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1254045448   748 VIGCSIDLTIPEIKFSVNGTYMSG-SFKKFNIDGYFFPVMSLSAKVSCRFILGGN 801
Cdd:smart00449   68 VIGCFLDLEAGTISFYKNGKYLHGlAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122
RyR pfam02026
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...
2950-3032 4.07e-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: 4.07e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 2950 FAPKPIDLSSMTLEKDMVNAAEKMAEHSHLIWAKKVMNDLNTKGGFMPIP------LVPWDLLTDFERRKDRFRASEILK 3023
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAakthpcLVPYDLLTEKEKEYDREPARETLK 80

                   ....*....
gi 1254045448 3024 FLQYHGYHV 3032
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 ...
1092-1212 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 1254045448 1092 KWYFEFEILTA--GYMKIGW--MDIGSTPEIQLGADDRSYAFDGYLGRKWH--QGAETYGKEWKIGDVVGCFLDLNDRTI 1165
Cdd:pfam00622    1 RHYFEVEIFGQdgGGWRVGWatKSVPRKGERFLGDESGSWGYDGWTGKKYWasTSPLTGLPLFEPGDVIGCFLDYEAGTI 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1254045448 1166 SFSLNGELLLDpsgsemAFDNVVCGDGLVPAMTLGSGQRGRLNFGQQ 1212
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 ...
1084-1213 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 1254045448 1084 ATYAV-CGGKWYFEFEILTAGYMKIGWmdigSTPE--IQLGADDRSYAFDGyLGRKWHQGA-ETYGKEWKIGDVVGCFLD 1159
Cdd:cd12873     32 ATKGVkGKGKYYYEVTVTDEGLCRVGW----STEDasLDLGTDKFGFGYGG-TGKKSHGRQfDDYGEPFGLGDVIGCYLD 106
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254045448 1160 LNDRTISFSLNGELLldpsgsEMAFDNVVC--GDGLVPAMTLGSGqRGRLNFGQQS 1213
Cdd:cd12873    107 LDNGTISFSKNGKDL------GKAFDIPPHlrNSALFPAVCLKNA-EVEFNFGDKP 155
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
670-797 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 1254045448  670 KWYFEAEVEhietmTKQTPYLRIGWANSvgfkpfpgSGDKMGCNGVGDDFYSYGFDGKSMYFGGKSR-RVGHKLLEKGDV 748
Cdd:cd11709      2 KWYWEVRVD-----SGNGGLIQVGWATK--------SFSLDGEGGVGDDEESWGYDGSRLRKGHGGSsGPGGRPWKSGDV 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1254045448  749 IGCSIDLTIPEIKFSVNGTYMSGSFKKFN-IDGYFFPVMSLSAKVSCRFI 797
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 ...
1556-1694 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 1254045448 1556 YYYGIRIFpGQDPSQVWVGWVTTQYHYYNVNFDGsqgvrkcrfseadhhgTTVDSVQSQNCYMV--------NVSELLAT 1627
Cdd:pfam00622    2 HYFEVEIF-GQDGGGWRVGWATKSVPRKGERFLG----------------DESGSWGYDGWTGKkywastspLTGLPLFE 64
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254045448 1628 TPDVantkvsgtlIGCIIDTSIGELSFQVGSTDTGIKFKLEPGA-MLFPAAFVTPtaTEILQFELGRI 1694
Cdd:pfam00622   65 PGDV---------IGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSLGA--GEGLKFNFGLR 121
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
1556-1694 2.48e-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: 2.48e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  1556 YYYGIRIFpgqDPSQVWVGWVTTQYHYYNVNFDGSqgvrkcrfseaDHHGTTVDSVQSQNCYMVNVSE---LLATTPDVa 1632
Cdd:smart00449    4 HYFEVEIG---DGGHWRVGVATKSVPRGYFALLGE-----------DKGSWGYDGDGGKKYHNSTGPEyglPLQEPGDV- 68
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1254045448  1633 ntkvsgtlIGCIIDTSIGELSFQVGSTDTGIK--FKLEPGAMLFPAAFVTPtaTEILQFELGRI 1694
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 ...
1094-1210 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 1254045448 1094 YFEFEILTAGYMK---IGWMDIGSTPEIQLGADDRSYAFDGYLGRKWHQGA--ETYGKEWKIGDVVGCFLDLNDRTISFS 1168
Cdd:cd12885     17 YFEVTILDLGEKGivsIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGegENYGPPFGTGDVVGCGINFKTGEVFFT 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1254045448 1169 LNGELLldpsgsEMAFDNVVCGDgLVPAMTLGS-GQRGRLNFG 1210
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 ...
670-808 3.12e-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: 3.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  670 KWYFEAEVehietMTkqTPYLRIGWAnSVGFKPfpgsgDKMgcngVGDDFYSYGFDGksmyFGGKSRRVGH----KLLEK 745
Cdd:cd12878     15 KWYFEFEV-----LT--SGYMRVGWA-RPGFRP-----DLE----LGSDDLSYAFDG----FLARKWHQGSesfgKQWQP 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045448  746 GDVIGCSIDLTIPEIKFSVNGTYM---SGS---FKKFNIDGYFFPVMSLSAkvscrfilgGNQGRLRYG 808
Cdd:cd12878     74 GDVVGCMLDLVDRTISFTLNGELLidsSGSevaFKDIEIGEGFVPACSLGV---------GQKGRLNLG 133
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
1091-1210 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 1254045448 1091 GKWYFEFEILTAGYMKIGWMDIGS---TPE-IQLGADDRSYAFDGYLGRKWH--QGAETYGKEWKIGDVVGCFLDLNDRT 1164
Cdd:cd12883      1 GVWYYEVTVLTSGVMQIGWATKDSkflNHEgYGIGDDEYSCAYDGCRQLIWYnaKSKPHTHPRWKPGDVLGCLLDLNKKQ 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1254045448 1165 ISFSLNGELLldPSGSEMAFDNVvcgDGLVPAMTLGSGQRGRLNFG 1210
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 ...
660-796 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 1254045448  660 GVVEGsalfrKWYFEAEVEHIETmtKQTPYLRIGWANSVGFKPFPgsgdkmgcngVGDDFYSYGF---DGKSmYFGGKSR 736
Cdd:cd12872     24 GVREG-----KWYFEVKILEGGG--TETGHVRVGWSRREASLQAP----------VGYDKYSYAIrdkDGSK-FHQSRGK 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254045448  737 RVGHKLLEKGDVIGCSIDLtiPEIKFSVNGTYMSGSFKKFNIDGYFFPVMSL--SAKVSCRF 796
Cdd:cd12872     86 PYGEPGFKEGDVIGFLITL--PKIEFFKNGKSQGVAFEDIYGTGGYYPAVSLykGATVTINF 145
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
1082-1212 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 1254045448 1082 AEATYAVCGGKWYFEFEIL------------TAGYM-KIGWmDIGSTPeIQLGADDRSYAFDGYlGRKWHQGAET-YGKE 1147
Cdd:cd12884     36 ARATYGVTKGKVCFEVKVTenlpvkhlpteeTDPHVvRVGW-SVDSSS-LQLGEEEFSYGYGST-GKKSTNCKFEdYGEP 112
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254045448 1148 WKIGDVVGCFLDLN--DRTISFSLNGELLldpsGSEMAFDNVVCGDG-LVPAMtLGSGQRGRLNFGQQ 1212
Cdd:cd12884    113 FGENDVIGCYLDFEsePVEISFSKNGKDL----GVAFKISKEELGGKaLFPHV-LTKNCAVEVNFGQK 175
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
4839-4981 5.15e-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: 5.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4839 FFYAFHLIDVVLSFPMLKAILQSVTHNLQQLILTIMMTLVVVYLYTVIAFNFFRKFYvQEGEEGEEPDRKCHNMLTCFIY 4918
Cdd:pfam00520   99 LLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKL-KTWENPDNGRTNFDNFPNAFLW 177
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254045448 4919 HFYagVRAGGGIGDELESPYGDDLEYPRMFYDISFFFFVIIILLAIMQGLIIDAFGELRDQQE 4981
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 ...
4532-4712 1.05e-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: 1.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4532 VPPERPETPETVLEEEKPLNQETSPPTSPTSPASKAPSIYES--IGAPQMVQLQSEADFQQGQYEPKIaESNSTKsrgsI 4609
Cdd:pfam06459   98 EEEEEEEPKPEPIEKADGENGEKEEKPKEEETESEAPEEEEMkkKQRKRHSKKKEEPEAQGSAFWNEL-EVYQTK----L 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4610 LNMLARNFKTIEKITLYLAFFINVILLFHRVDISHAENAEAAS---------------EGDDDEDALESifitgmqfpYV 4674
Cdd:pfam06459  173 LNYLARNFYNLRFLALFVAFAINFILLFYKVSTSPPDEEEEEGsgwgdsgsgsgggsgEDEEEEEGPVY---------FV 243
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1254045448 4675 EYEITGWMlAQILYWISVLHLSTSFALLVSFYQLKIPL 4712
Cdd:pfam06459  244 LEESTGYM-EPTLRFLAILHTIISFLCIIGYYCLKVPL 280
SPRY_RING cd12883
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...
671-799 2.36e-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: 2.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  671 WYFEAEVEHIETMtkqtpylRIGWA-------NSVGFkpfpgsgdkmgcnGVGDDFYSYGFDG--KSMYFGGKSRRVGHK 741
Cdd:cd12883      3 WYYEVTVLTSGVM-------QIGWAtkdskflNHEGY-------------GIGDDEYSCAYDGcrQLIWYNAKSKPHTHP 62
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045448  742 LLEKGDVIGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGY-FFPVMSLSAKVSCRFILG 799
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 ...
1080-1210 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 1254045448 1080 YR-AEATYAVCGGKWYFEFEILTAGYMK-----IGWmdigSTPE--IQ--LGADDRSYAFDGYLGRKWHQGA-ETYG-KE 1147
Cdd:cd12872     16 YRmARANHGVREGKWYFEVKILEGGGTEtghvrVGW----SRREasLQapVGYDKYSYAIRDKDGSKFHQSRgKPYGePG 91
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254045448 1148 WKIGDVVGCFLDLNdrTISFSLNGELLldpsGSemAFDNVVCGDGLVPAMTLGSGQRGRLNFG 1210
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 ...
1091-1211 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 1254045448 1091 GKWYFEFEILTAGymKIGWMDIG-STPEIQL----GADDRSYAF---DGYLGRKWHQGAEtYGKEWKIGDVVGCFLDLND 1162
Cdd:cd12909     25 GIYYFEVKIISKG--RDGYIGIGfSTKDVNLnrlpGWEPHSWGYhgdDGHSFCSSGTGKP-YGPTFTTGDVIGCGINFRD 101
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1254045448 1163 RTISFSLNGELLldpsgsEMAFDNVVCGDgLVPAMTLGS-GQRGRLNFGQ 1211
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 ...
669-796 7.19e-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: 7.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  669 RKWYFEAEVEHIETMTKqtpylrigwaNSVGFKPFPGSGDKMgcngVGDDFYSYGF---DGKsMYFGGKSRRVGHKLLEK 745
Cdd:cd12885     14 PVFYFEVTILDLGEKGI----------VSIGFCTSGFPLNRM----PGWEDGSYGYhgdDGR-VYLGGGEGENYGPPFGT 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1254045448  746 GDVIGCSIDLTIPEIKFSVNGTYMsGSFKKFNIDGYFFPVMSLS---AKVSCRF 796
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 ...
670-799 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 1254045448  670 KWYFEAeveHIETmtkqTPYLRIGWANSVGfkPFPGSgdkmgcNGVGDDFYSYGFDGKSMY-FGGKSRRVGHKLLEkGDV 748
Cdd:cd12882     12 KWMYEV---TLGT----KGIMQIGWATISC--RFTQE------EGVGDTRDSYAYDGNRVRkWNVSTQKYGEPWVA-GDV 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1254045448  749 IGCSIDLTIPEIKFSVNGTYMSGSFKKFNIDGY--FFPVMSLSAKVSCRFILG 799
Cdd:cd12882     76 IGCCIDLDKGTISFYRNGRSLGVAFDNVRRGPGlaYFPAVSLSFGERLELNFG 128
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
4191-4245 1.61e-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: 1.61e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254045448 4191 AFQDFDTNQDGWISPKEFQRAMESQKMYTVEDITYLMMCT-DVNNDGKVDYMEFTE 4245
Cdd:cd00051      5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREvDKDGDGKIDFEEFLE 60
SPRY_hnRNP cd12884
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...
660-796 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 1254045448  660 GVVEGsalfrKWYFEAE------VEHIETMTKQTPYLRIGWanSVGFKPFPgsgdkmgcngVGDDFYSYGFDGK-SMYFG 732
Cdd:cd12884     41 GVTKG-----KVCFEVKvtenlpVKHLPTEETDPHVVRVGW--SVDSSSLQ----------LGEEEFSYGYGSTgKKSTN 103
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  733 GKSRRVGHKLLEkGDVIGCSIDL--TIPEIKFSVNGTYMSGSFKKFNIDGY---FFP-VMSLSAKVSCRF 796
Cdd:cd12884    104 CKFEDYGEPFGE-NDVIGCYLDFesEPVEISFSKNGKDLGVAFKISKEELGgkaLFPhVLTKNCAVEVNF 172
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
225-387 6.89e-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: 6.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  225 NDVLRLFHG-NDECLTIPENwsEHP---QHNMVIYEGGAAVTQARSLWRVELIRMKWhGALVGWEQVFRIKHITSGRYLg 300
Cdd:cd23263      1 GDVIWLKHSeTGKYLHSHRK--NYPtgsGQQEVTFESSSRKGDTNGLWIIESENGKQ-GGPVKWGDKIRLRHLSTGKYL- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  301 vldnSVQLYHKEKADFDLtaFVMCQNKDPKKQMLDEKEEEGMGNATIRYGETNAF--IQHVKTQLWLSYQT--------- 369
Cdd:cd23263     77 ----SSEEGKKSPKSNHQ--EVLCLTDNPDKSSLFKFEPIGSTKYKQKYVKKDSYfrLKHVNTNFWLHSHEkkfninnkt 150
                          170
                   ....*....|....*....
gi 1254045448  370 -TEVTKKGLGKVEEKKAVA 387
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 ...
264-399 1.26e-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: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  264 ARSLWRVELIRMKWHGALVGWEQVFRIKHITSGRYLgVLDNSVQLYH---KEKADFDLTAFVmcqnkdpKKQMLDEKEEE 340
Cdd:cd23280     60 GDTFWQIEKEDTPLKGGVIKWGDQCRLRHLPTGKYL-AVDDKTGNGKvvlTSDPSDPSTVFR-------LHPVTKETSEE 131
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1254045448  341 gmgnatIRYGeTNAFIQHVKTQLWLS-----YQTTEVTKKGLGKVEEKKA---VALKDGHMDDCYTF 399
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 ...
1091-1210 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 1254045448 1091 GKWYFEFEILTAG---YMKIGWMDIGSTPE-----IQLGADdrSYAFDGYLGRKW--HQGAETYGKEWKIGDVVGCFLDL 1160
Cdd:cd12886      1 GKWYWEVTVVSSAastYAGIGVANAAATGNnglngIELSSI--GYSLGVYSGNKLsnGSSVATYGAGFTAGDVIGVALDL 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1254045448 1161 NDRTISFSLNGELLLDPS---GSEMAFDnvvcGDGLVPAMTLGSGQRGR--LNFG 1210
Cdd:cd12886     79 DAGKIWFYKNGVWQGGGDpapGTNPAFA----GTAMYPAVTGGSSTGGSftANFG 129
EF-hand_7 pfam13499
EF-hand domain pair;
4190-4247 4.12e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.94  E-value: 4.12e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1254045448 4190 QAFQDFDTNQDGWISPKEFQRAMESQKM---YTVEDITYLMMCTDVNNDGKVDYMEFTERF 4247
Cdd:pfam13499    6 EAFKLLDSDGDGYLDVEELKKLLRKLEEgepLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
SPRY1_RyR cd12877
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...
1092-1210 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 1254045448 1092 KWYFEFEI-------LTAGYMKIGW-MDIGSTPEIQ---------LGADDRSYAFDG---YLGRKWHQGAETYGKEWKIG 1151
Cdd:cd12877     19 KWYFEVEVdhveqftHQPAHLRVGWaNTSGYVPYPGggegwggngVGDDLYSYGFDGlhlWTGGRSRRVTSGTQHLLKKG 98
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254045448 1152 DVVGCFLDLNDRTISFSLNGELLldpSGSemaFDNVVCGDGLVPAMTLGSGQRGRLNFG 1210
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) ...
222-391 4.35e-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: 4.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  222 LFGNDVLRLFHGNDE-CLTIPENwsEHPQHNMVIYEGGAAVTQARS---LWRVELIRmkwHGALVG----WEQVFRIKHI 293
Cdd:cd23287     11 LKGGDVVRLFHAEQEkFLTCDEH--RKKQHVFLRTTGRQSATSATSskaLWEVEVVQ---HDPCRGgagyWNSLFRFKHL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  294 TSGRYLGVLDNSVQlyhkEKADFDLTAFVMCQNKDPKKQMLDEKEE---------EG--------MGNATIRYGET---- 352
Cdd:cd23287     86 ATGHYLAAEVDPDF----EEECLEFQPSVDPDQDASRSRLRNAQEKmvyslvsvpEGndissifeLDPTTLRGGDSlvpr 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1254045448  353 NAFI--QHVKTQLWLSYQTTEVTKkglgkvEEKKAVALKDG 391
Cdd:cd23287    162 NSYVrlRHLCTNTWVHSTNIPIDK------EEEKPVMLKIG 196
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
4190-4251 1.89e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.48  E-value: 1.89e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1254045448 4190 QAFQDFDTNQDGWISPKEFQRAMESQKMyTVEDITYLMMCTDVNNDGKVDYMEFTE---RFHNPA 4251
Cdd:COG5126     73 AAFDLLDTDGDGKISADEFRRLLTALGV-SEEEADELFARLDTDGDGKISFEEFVAavrDYYTPD 136
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
1556-1683 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 1254045448 1556 YYYGIRIFPGQdPSQVWVGWVTTQYhyynvNFDGSQGVRKcrfseaDHHGTTVDSVQSQNCYMVN--VSELLATTPDVan 1633
Cdd:cd11709      3 WYWEVRVDSGN-GGLIQVGWATKSF-----SLDGEGGVGD------DEESWGYDGSRLRKGHGGSsgPGGRPWKSGDV-- 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1254045448 1634 tkvsgtlIGCIIDTSIGELSFQVGSTDTGIKFKLEPGAM--LFPAAFVTPTA 1683
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) ...
222-299 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 1254045448  222 LFGNDVLRLFHGNDECLTIPENWsEHPQH---NMVIYEGGAAVTQARSLWRVELIRMK-WHGALVGWEQVFRIKHITSGR 297
Cdd:cd23288     17 LKGGDVVRLFHAEQEKFLTCDEY-KKKQHiflRTTLRQSATSATSSKALWEIEVVHYDpCRGGAGQWNSLFRFKHLATGN 95

                   ..
gi 1254045448  298 YL 299
Cdd:cd23288     96 YL 97
SPRY_DDX1 cd12873
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...
670-796 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 1254045448  670 KWYFEAEVehietmtkQTPYL-RIGWANsvgfkpfpgsgdkMGCN-GVGDDFYSYGFDGKsmyfGGKS-RRVGHKLLE-- 744
Cdd:cd12873     41 KYYYEVTV--------TDEGLcRVGWST-------------EDASlDLGTDKFGFGYGGT----GKKShGRQFDDYGEpf 95
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1254045448  745 -KGDVIGCSIDLTIPEIKFSVNGTYMSGSFK-KFNIDG-YFFPVMSL-SAKVSCRF 796
Cdd:cd12873     96 gLGDVIGCYLDLDNGTISFSKNGKDLGKAFDiPPHLRNsALFPAVCLkNAEVEFNF 151
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
12-187 1.06e-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: 46.61  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448   12 QDDVSFLRTGDIVCLSCvasHNRDGVLGservclCTEGFGNRMCTlENVSDKdippdiamcmLYIDNALSMRALQEMMSA 91
Cdd:cd23280      1 KENENFLKGGDVVRLFH---KELEAYLS------AEGSFVDEVLT-EDVHLR----------VRPVDDRKPRTLFPPTSG 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448   92 DS----DHKSASGAGGhkTLLYGHAVQLKHVQSEMYLaclssCSSNDKLAFDVGVQETNEGEACWWTIHPASKQRSEGek 167
Cdd:cd23280     61 DTfwqiEKEDTPLKGG--VIKWGDQCRLRHLPTGKYL-----AVDDKTGNGKVVLTSDPSDPSTVFRLHPVTKETSEE-- 131
                          170       180
                   ....*....|....*....|
gi 1254045448  168 VRVGDDVILVSVATERYLHM 187
Cdd:cd23280    132 VKFGSYVRIEHVATGTWLHA 151
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
219-273 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 1254045448   219 MGFLFGNDVLRLFHGNDEC-LTIPENW---SEHPQHNMVIYEGGAAVtqARSLWRVELI 273
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRyLHSHDEKlppWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
109-305 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 1254045448  109 YGHAVQLKHVQSEMYLaclsscsSNDKLAFDVG--------VQETNEGEAcWWTIHPA--SKQRSEGEKVRVGDDVILVS 178
Cdd:cd23279      1 YGSAIKLKHVNSGYRL-------HSHEVSYGSGsgqqsvtaVPSADDANS-LWTVLPGlgEPCQEQGKPVKCGDIIRLQH 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  179 VATERYLHmaySKgymviaSFHQTLWNIQSVSSGSmrtrnmgflfGNDVLRlfhGNDecltipenwsehpqhnmviyegg 258
Cdd:cd23279     73 VNTRKNLH---SH------NHSSPLSGNQEVSAFG----------GGDEDS---GDN----------------------- 107
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1254045448  259 aavtqarslWRVELIRMK---WHGalvgwEQVFRIKHITSGRYLGVLDNS 305
Cdd:cd23279    108 ---------WIVECEGKKakfWKR-----GEPVRLKHVDTGKYLSASKTH 143
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
279-305 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 1254045448   279 GALVGWEQVFRIKHITSGRYLGVLDNS 305
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 ...
220-304 9.25e-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: 9.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448  220 GFLFGNDVLRLFHGNDE-CLTIPEnwSEHPQHNMVIYEG---GAAVTQARSLWRVELIRmkwHGALVG----WEQVFRIK 291
Cdd:cd23277      9 DVLKGGDVVRLFHAEQEkFLTCDE--YKKKQYVFLRTTGrtsATSATSSKALWEVEVVQ---HDPCRGgaghWNSLFRFK 83
                           90
                   ....*....|...
gi 1254045448  292 HITSGRYLGVLDN 304
Cdd:cd23277     84 HLATGQYLAAEVD 96
PTZ00183 PTZ00183
centrin; Provisional
4190-4282 1.00e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 43.14  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254045448 4190 QAFQDFDTNQDGWISPKEFQRAM-----ESQKmytvEDITYLMMCTDVNNDGKVDYMEF----TERFHN--PARDI--GF 4256
Cdd:PTZ00183    21 EAFDLFDTDGSGTIDPKELKVAMrslgfEPKK----EEIKQMIADVDKDGSGKIDFEEFldimTKKLGErdPREEIlkAF 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1254045448 4257 NL-------AVLLVNLK-------EHITnDPRLEKIIEKA 4282
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) ...
222-304 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 1254045448  222 LFGNDVLRLFHGNDE-CLTIPENWSE-HPQHNMVIYEGGAAVTQARSLWRVELIRMK-WHGALVGWEQVFRIKHITSGRY 298
Cdd:cd23289     11 LKGGDVVRLFHAEQEkFLTCDEYKGKlQVFLRTTLRQSATSATSSNALWEVEVVHHDpCRGGAGHWNGLYRFKHLATGNY 90

                   ....*.
gi 1254045448  299 LGVLDN 304
Cdd:cd23289     91 LAAEEN 96
EF-hand_8 pfam13833
EF-hand domain pair;
4199-4243 2.85e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.84  E-value: 2.85e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1254045448 4199 QDGWISPKEFQRAME--SQKMYTVEDITYLMMCTDVNNDGKVDYMEF 4243
Cdd:pfam13833    1 EKGVITREELKRALAllGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
4196-4248 7.57e-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: 7.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1254045448 4196 DTNQDGWISPKEFQR-AMESQKMYTVEDITYLMMCTDVNNDGKVDYMEFTERFH 4248
Cdd:cd15899     45 DVDKDGFISAKELHSwILESFKRHAMEESKEQFRAVDPDEDGHVSWDEYKNDTY 98
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
1117-1199 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 1254045448 1117 EIQLGADDRSYA--FDGylGRKW--HQGAETYGKEWKI--GDVVGCFLDLNDRTISFSLNGEllldPSGsEMAFDNVvcg 1190
Cdd:cd12889     78 DKMLGKDDKGWSmyIDN--NRSWflHNNEHSNRTEGGItvGSVVGVLLDLDRHTLSFYVNDE----PQG-PIAFRNL--- 147
                           90
                   ....*....|
gi 1254045448 1191 DGLV-PAMTL 1199
Cdd:cd12889    148 PGVFyPAVSL 157
 
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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