NCBI Conserved Domain Search

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...

442-621

2.81e-80

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

Pssm-ID: 460175 Cd Length: 199 Bit Score: 264.06 E-value: 2.81e-80

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     442 TLQDLIAYFQPPEEEMRHEDKQNKL---RSLKNRQNLFKEEGMLALVLNCIDRLN-VYNSVAHFAGIAREESGMAWKEIL 517
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     518 NLLYKLLAALIRGNRNNCAQFSNNLDWLISKLDRLESSSGILEVLHCILTESPE-ALNLIAEGHIKSIISLLDKHGRNHK 596
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180
                   ....*....|....*....|....*
gi 2696015     597 VLDILCSLCLCNGVAVRANQNLICD 621
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICR 185

SPRY2_RyR

cd12878

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...

1073-1205

2.45e-78

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: 255.69 E-value: 2.45e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1073 RFFRVERSYPVRSGKWYFEFEVVTGGDMRVGWARPGCRPDVELGADDQAFVFEGNRGQRWHQGSGYFGRTWQPGDVVGCM 1152
Cdd:cd12878    1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 2696015  1153 INLDDASMIFTLNGELLITNKGSELAFADYEIENGFVPICCLGLSQIGRMNLG 1205
Cdd:cd12878   81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133

RYDR_ITPR

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...

2024-2234

1.65e-75

Pssm-ID: 460175 Cd Length: 199 Bit Score: 250.58 E-value: 1.65e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2024 QIRSLLSVRMGKEEELLMINGLGDIMNNKVFYQHPNLMRVLGMHETVMEVMvNVLGT-------------EKSQIAFPKM 2090
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlgEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2091 VASCCRFLCYFCRISRQNQKAMFEHLSYLLENssvgLASPSMRGSTpLDVAASSVMDNNELALsleepdlekvvTYLAGC 2170
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKEC 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2696015    2171 GLQSCPMLLAKGYPDvgwnpiegERYLSFLRFAVFVNSESVEENASVVVKLLIRRPECFGPALR 2234
Cdd:pfam01365  144 HIKSFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199

SPRY3_RyR

cd12879

SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...

1325-1463

8.46e-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: 237.97 E-value: 8.46e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1325 TTTQCYYAIRIFGGQDPSCVWVGWVTPDYHLYSEKFDLNKNCTVTVTLGDERGRVHESVKRSNCYMVWGGDIVASSQR-- 1402
Cdd:cd12879   11 LVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAGELLAEVGQds 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2696015  1403 SNRSNVDLEIGCLVDLAMGMLSFSANGKELGTCYQVEPNTKVFPAVFLQPTSTSLFQFELG 1463
Cdd:cd12879   91 SGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151

SPRY1_RyR

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...

641-793

1.89e-65

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: 219.88 E-value: 1.89e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   641 SIRPNIFLGVAEGSAQYKKWYFELIIDQVDPFlTAEPTHLRVGWASSSGYAPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 720
Cdd:cd12877    1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2696015   721 SGRIPRAVASINQHLLRSDDVgkllpgpRGC------PASHSASMGSPCRGCLENFNTDGLFFPVMSFSAGVKVRFLMG 793
Cdd:cd12877   80 TGGRSRRVTSGTQHLLKKGDV-------VGCcldlsvPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151

Ins145_P3_rec super family

cl48031

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...

14-212

1.93e-65

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

The actual alignment was detected with superfamily member pfam08709:

Pssm-ID: 462572 [Multi-domain] Cd Length: 212 Bit Score: 222.37 E-value: 1.93e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015      14 FLRTEDEVVLQCIATIhkeqrKFCLAAEGLGNRLCFLEPTSEAKYIPP-DLCVCNFVLEQSLSVRALQEML--ANTGENG 90
Cdd:pfam08709    4 FLHIGDIVSLSCEESV-----NGFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWsaGNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015      91 GEGAAQGG------GHRTLLYGHAVLLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATGEACWWTIHPASKQRSEGEK 164
Cdd:pfam08709   79 NSLTDALKhasnieGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDN 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2696015     165 VRIGDDLILVSVSSERYLHLSVS-----NGNIQVDASFMQTLWNVHPTCSGSS 212
Cdd:pfam08709  159 VCVGDEVILVPVSAPIFLHTTSSselrdNPGKEVNASFGQTSWKMEPFMSGCE 211

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

2599-2688

1.95e-45

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

Pssm-ID: 460419 Cd Length: 90 Bit Score: 159.98 E-value: 1.95e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2599 FDPKPINTMNFSLPEKLEYIVTKYAEHSHDKWACDKSQSGWKYGISLDENVKTHPLIRPFKTLTEKEKEIYRWPARESLK 2678
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2696015    2679 TMLAVGWTVE 2688
Cdd:pfam02026   81 TLLALGYTIE 90

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

964-1053

7.42e-41

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

Pssm-ID: 460419 Cd Length: 90 Bit Score: 146.88 E-value: 7.42e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     964 YKPAPLDLSDVKLLPPQEILVDKLAENAHNVWAKDRIKQGWTYGIQQDLKNKRNPRLVPYALLDERTKKSNRDSLREAVR 1043
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2696015    1044 TFVGYGYNIE 1053
Cdd:pfam02026   81 TLLALGYTIE 90

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

850-924

3.91e-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: 133.40 E-value: 3.91e-36

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2696015     850 FIPCPVDTSQVILPPHLEKIRDRLAENIHELWGMNKIELGWTFGKIRDDNKRQHPCLVEFSKLPETEKNYNLQMS 924
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPA 75

RIH_assoc

pfam08454

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...

3723-3840

2.25e-35

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

Pssm-ID: 462482 Cd Length: 98 Bit Score: 131.49 E-value: 2.25e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    3723 QNDEFTRDLFRFLQLLCEGHNSDFQNFLRTQMGNTTTVNVIISTVDYLLRLQESISdfywyysgkdiidesgQHNFSKAl 3802
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN----------------EKNIELI- 63

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2696015    3803 avtKQIFNSLTEYIQGPCIGNQQSLAHSRLWDAVVGFL 3840
Cdd:pfam08454   64 ---IQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98

Ion_trans

pfam00520

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...

4617-4777

3.02e-25

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: 107.74 E-value: 3.02e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4617 SFLYLAWYTTMSVLG-HYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKS 4695
Cdd:pfam00520   79 SLISLVLSSVGSLSGlRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTW 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4696 EDDDEPDMKCDDMMTCYLFHMYVgvRAGGGIGDEIEDPAGDPYEMYRIVFDITFFFFVIVILLAIIQGLIIDAFGELRDQ 4775
Cdd:pfam00520  159 ENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTER 236


                   ..
gi 2696015    4776 QE 4777
Cdd:pfam00520  237 TE 238

RyR super family

cl03409

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

2717-2796

3.99e-25

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

The actual alignment was detected with superfamily member pfam02026:

Pssm-ID: 460419 Cd Length: 90 Bit Score: 102.20 E-value: 3.99e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2717 YSPAPLDLSNVVLSRELQGMVEVVAENYHNIWAKKKKLELESKGGG------SHPLLVPYDTLTAKEKFKDREKAQDLFK 2790
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*.
gi 2696015    2791 FLQVNG 2796
Cdd:pfam02026   81 TLLALG 86

EF-hand_7

pfam13499

EF-hand domain pair;

3924-3979

4.30e-04

EF-hand domain pair;

Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 41.47 E-value: 4.30e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2696015    3924 FKEYDPDGKGIISKKEFQKAM---EGQKQYTQSEIDFLLSCAEADENDMFNYVDFVDRF 3979
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLrklEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66

Name

Accession

Description

Interval

E-value

beta-trefoil_MIR_RyR3

cd23292

MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...

216-405

4.11e-132

Pssm-ID: 467763 [Multi-domain] Cd Length: 187 Bit Score: 412.38 E-value: 4.11e-132

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   216 GYLLGGHVVRLFHGHDECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYL 295
Cdd:cd23292    1 GYLLGGHVVRLFHGHDECLTIPSTDQSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   296 ALTEDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKTSR 375
Cdd:cd23292   81 ALTEDQGLILQDRAKSDTKSTAFCFRAS---KEKLESGPKRDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSR 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 2696015   376 LGPLKRKVILHQEGHMDDGLTLQRCQREES 405
Cdd:cd23292  158 LGPLKRRAILHQEGHMDDGLTLQRCQHEES 187

RR_TM4-6

pfam06459

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

4230-4500

6.49e-112

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: 358.63 E-value: 6.49e-112

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4230 DMPDPTQFGIHDDTMEAERAEVMEPGITTELVHfIKGEKGDTDIMSDLFGLHPKKEGSLK----HGPEVGLGDLSEIIGK 4305
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLAD-AAGGEEEEDLLSDIFGLILKKEGGQYkvvpHDPEAGLGDLSETTAE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4306 DEPPTLEstvQKKRKAQAAEMKAANEAEGKVES-EKADMEDG-EKEDKDKEEEQAEYLW-TEVTKKKKRRCGQKVEKPEA 4382
Cdd:pfam06459   80 EPPPLLK---RKLQESEEAEDEEEEEEEPKPEPiEKADGENGeKEEKPKEEETESEAPEeEEMKKKQRKRHSKKKEEPEA 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4383 FTANFFKGLEIYQTKLLHYLARNFYNLRFLALFVAFAINFILLFYKV--------TEEPLEEETEDVANLWNSFNDEEEE 4454
Cdd:pfam06459  157 QGSAFWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVstsppdeeEEEGSGWGDSGSGSGGGSGEDEEEE 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2696015    4455 EAMVFFVLQESTGYMAPTLRALAIIHTIISLVCVVGYYCLKVPLVV 4500
Cdd:pfam06459  237 EGPVYFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282

RYDR_ITPR

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...

442-621

2.81e-80

Pssm-ID: 460175 Cd Length: 199 Bit Score: 264.06 E-value: 2.81e-80

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     442 TLQDLIAYFQPPEEEMRHEDKQNKL---RSLKNRQNLFKEEGMLALVLNCIDRLN-VYNSVAHFAGIAREESGMAWKEIL 517
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     518 NLLYKLLAALIRGNRNNCAQFSNNLDWLISKLDRLESSSGILEVLHCILTESPE-ALNLIAEGHIKSIISLLDKHGRNHK 596
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180
                   ....*....|....*....|....*
gi 2696015     597 VLDILCSLCLCNGVAVRANQNLICD 621
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICR 185

SPRY2_RyR

cd12878

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...

1073-1205

2.45e-78

Pssm-ID: 240458 Cd Length: 133 Bit Score: 255.69 E-value: 2.45e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1073 RFFRVERSYPVRSGKWYFEFEVVTGGDMRVGWARPGCRPDVELGADDQAFVFEGNRGQRWHQGSGYFGRTWQPGDVVGCM 1152
Cdd:cd12878    1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 2696015  1153 INLDDASMIFTLNGELLITNKGSELAFADYEIENGFVPICCLGLSQIGRMNLG 1205
Cdd:cd12878   81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133

MIR

pfam02815

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

216-397

8.27e-77

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

Pssm-ID: 397103 [Multi-domain] Cd Length: 185 Bit Score: 253.83 E-value: 8.27e-77

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     216 GYLLGGHVVRLFHGH-DECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRI-SWSGSNIRWGQAFRLRHLTTGH 293
Cdd:pfam02815    1 GYLKGGDVVRLFHSHqDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     294 YLALTEDQGLILQDRAKSDTKSTAFSFRASKELKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKT 373
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....
gi 2696015     374 SRLGPLKRKVILHQEGHMDDGLTL 397
Cdd:pfam02815  161 WGFGPEQQKVTCAKEGHMDDALTL 184

RYDR_ITPR

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...

2024-2234

1.65e-75

Pssm-ID: 460175 Cd Length: 199 Bit Score: 250.58 E-value: 1.65e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2024 QIRSLLSVRMGKEEELLMINGLGDIMNNKVFYQHPNLMRVLGMHETVMEVMvNVLGT-------------EKSQIAFPKM 2090
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlgEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2091 VASCCRFLCYFCRISRQNQKAMFEHLSYLLENssvgLASPSMRGSTpLDVAASSVMDNNELALsleepdlekvvTYLAGC 2170
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKEC 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2696015    2171 GLQSCPMLLAKGYPDvgwnpiegERYLSFLRFAVFVNSESVEENASVVVKLLIRRPECFGPALR 2234
Cdd:pfam01365  144 HIKSFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199

SPRY3_RyR

cd12879

SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...

1325-1463

8.46e-72

Pssm-ID: 293937 Cd Length: 151 Bit Score: 237.97 E-value: 8.46e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1325 TTTQCYYAIRIFGGQDPSCVWVGWVTPDYHLYSEKFDLNKNCTVTVTLGDERGRVHESVKRSNCYMVWGGDIVASSQR-- 1402
Cdd:cd12879   11 LVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAGELLAEVGQds 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2696015  1403 SNRSNVDLEIGCLVDLAMGMLSFSANGKELGTCYQVEPNTKVFPAVFLQPTSTSLFQFELG 1463
Cdd:cd12879   91 SGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151

SPRY1_RyR

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...

641-793

1.89e-65

Pssm-ID: 240457 Cd Length: 151 Bit Score: 219.88 E-value: 1.89e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   641 SIRPNIFLGVAEGSAQYKKWYFELIIDQVDPFlTAEPTHLRVGWASSSGYAPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 720
Cdd:cd12877    1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2696015   721 SGRIPRAVASINQHLLRSDDVgkllpgpRGC------PASHSASMGSPCRGCLENFNTDGLFFPVMSFSAGVKVRFLMG 793
Cdd:cd12877   80 TGGRSRRVTSGTQHLLKKGDV-------VGCcldlsvPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151

Ins145_P3_rec

pfam08709

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...

14-212

1.93e-65

Pssm-ID: 462572 [Multi-domain] Cd Length: 212 Bit Score: 222.37 E-value: 1.93e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015      14 FLRTEDEVVLQCIATIhkeqrKFCLAAEGLGNRLCFLEPTSEAKYIPP-DLCVCNFVLEQSLSVRALQEML--ANTGENG 90
Cdd:pfam08709    4 FLHIGDIVSLSCEESV-----NGFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWsaGNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015      91 GEGAAQGG------GHRTLLYGHAVLLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATGEACWWTIHPASKQRSEGEK 164
Cdd:pfam08709   79 NSLTDALKhasnieGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDN 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2696015     165 VRIGDDLILVSVSSERYLHLSVS-----NGNIQVDASFMQTLWNVHPTCSGSS 212
Cdd:pfam08709  159 VCVGDEVILVPVSAPIFLHTTSSselrdNPGKEVNASFGQTSWKMEPFMSGCE 211

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

2599-2688

1.95e-45

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

Pssm-ID: 460419 Cd Length: 90 Bit Score: 159.98 E-value: 1.95e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2599 FDPKPINTMNFSLPEKLEYIVTKYAEHSHDKWACDKSQSGWKYGISLDENVKTHPLIRPFKTLTEKEKEIYRWPARESLK 2678
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2696015    2679 TMLAVGWTVE 2688
Cdd:pfam02026   81 TLLALGYTIE 90

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

964-1053

7.42e-41

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

Pssm-ID: 460419 Cd Length: 90 Bit Score: 146.88 E-value: 7.42e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     964 YKPAPLDLSDVKLLPPQEILVDKLAENAHNVWAKDRIKQGWTYGIQQDLKNKRNPRLVPYALLDERTKKSNRDSLREAVR 1043
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2696015    1044 TFVGYGYNIE 1053
Cdd:pfam02026   81 TLLALGYTIE 90

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

850-924

3.91e-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: 133.40 E-value: 3.91e-36

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2696015     850 FIPCPVDTSQVILPPHLEKIRDRLAENIHELWGMNKIELGWTFGKIRDDNKRQHPCLVEFSKLPETEKNYNLQMS 924
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPA 75

RIH_assoc

pfam08454

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...

3723-3840

2.25e-35

Pssm-ID: 462482 Cd Length: 98 Bit Score: 131.49 E-value: 2.25e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    3723 QNDEFTRDLFRFLQLLCEGHNSDFQNFLRTQMGNTTTVNVIISTVDYLLRLQESISdfywyysgkdiidesgQHNFSKAl 3802
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN----------------EKNIELI- 63

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2696015    3803 avtKQIFNSLTEYIQGPCIGNQQSLAHSRLWDAVVGFL 3840
Cdd:pfam08454   64 ---IQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98

SPRY

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...

1085-1207

1.42e-31

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

Pssm-ID: 214669 Cd Length: 122 Bit Score: 121.63 E-value: 1.42e-31

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     1085 SGKWYFEFEVVTGGDMRVGWARPGCRPDVE--LGADDQAFVFEGNRGQRWHQGSG-YFGRTWQ-PGDVVGCMINLDDASM 1160
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNSTGpEYGLPLQePGDVIGCFLDLEAGTI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 2696015     1161 IFTLNGELLitnkgSELAFADYEIENGFVPICCLGLSQIGRMNLGTD 1207
Cdd:smart00449   81 SFYKNGKYL-----HGLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122

Ion_trans

pfam00520

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...

4617-4777

3.02e-25

Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 107.74 E-value: 3.02e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4617 SFLYLAWYTTMSVLG-HYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKS 4695
Cdd:pfam00520   79 SLISLVLSSVGSLSGlRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTW 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4696 EDDDEPDMKCDDMMTCYLFHMYVgvRAGGGIGDEIEDPAGDPYEMYRIVFDITFFFFVIVILLAIIQGLIIDAFGELRDQ 4775
Cdd:pfam00520  159 ENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTER 236


                   ..
gi 2696015    4776 QE 4777
Cdd:pfam00520  237 TE 238

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

2717-2796

3.99e-25

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

Pssm-ID: 460419 Cd Length: 90 Bit Score: 102.20 E-value: 3.99e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2717 YSPAPLDLSNVVLSRELQGMVEVVAENYHNIWAKKKKLELESKGGG------SHPLLVPYDTLTAKEKFKDREKAQDLFK 2790
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*.
gi 2696015    2791 FLQVNG 2796
Cdd:pfam02026   81 TLLALG 86

SPRY

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...

1087-1207

1.25e-21

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

Pssm-ID: 459877 Cd Length: 121 Bit Score: 93.18 E-value: 1.25e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    1087 KWYFEFEV--VTGGDMRVGWARPGCR--PDVELGADDQAFVFEGNRGQRWHQGSG--YFGRTWQPGDVVGCMINLDDASM 1160
Cdd:pfam00622    1 RHYFEVEIfgQDGGGWRVGWATKSVPrkGERFLGDESGSWGYDGWTGKKYWASTSplTGLPLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2696015    1161 IFTLNGELLITnkgselAFADYEIENGFVPICCLGLSQIGRMNLGTD 1207
Cdd:pfam00622   81 SFTKNGKSLGY------AFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121

SPRY

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...

1329-1464

6.22e-20

Pssm-ID: 459877 Cd Length: 121 Bit Score: 88.55 E-value: 6.22e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    1329 CYYAIRIFGgQDPSCVWVGWVTPDYHLYSEKFdlnknctvtvtLGDERGrvhesvkrSNCYMVWGGDIV-ASSQRSNRSN 1407
Cdd:pfam00622    2 HYFEVEIFG-QDGGGWRVGWATKSVPRKGERF-----------LGDESG--------SWGYDGWTGKKYwASTSPLTGLP 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2696015    1408 V---DLEIGCLVDLAMGMLSFSANGKELGTCYQVEPNT-KVFPAVFLQPTSTslFQFELGK 1464
Cdd:pfam00622   62 LfepGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSLGAGEG--LKFNFGL 120

SPRY

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...

1329-1465

3.62e-19

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

Pssm-ID: 214669 Cd Length: 122 Bit Score: 86.19 E-value: 3.62e-19

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     1329 CYYAIRIFggqDPSCVWVGWVTPDYHLYSEKfdlnknctvtvTLGDERG-RVHESVKRSNCYMVWGGDIVASSQRSNRsn 1407
Cdd:smart00449    4 HYFEVEIG---DGGHWRVGVATKSVPRGYFA-----------LLGEDKGsWGYDGDGGKKYHNSTGPEYGLPLQEPGD-- 67

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     1408 vdlEIGCLVDLAMGMLSFSANGKELG--TCYQVEPNTKVFPAVFLQPTSTSlfQFELGKL 1465
Cdd:smart00449   68 ---VIGCFLDLEAGTISFYKNGKYLHglAFFDVKFSGPLYPAFSLGSGNSV--RLNFGPL 122

SPRY

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...

659-795

7.90e-09

Pssm-ID: 459877 Cd Length: 121 Bit Score: 56.58 E-value: 7.90e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     659 KWYFELIIDQvdpfltAEPTHLRVGWAsssgYAPYPGGGEGWGGngvgDDLYSYGFDGlhlWSGRI--PRAVASINQHLL 736
Cdd:pfam00622    1 RHYFEVEIFG------QDGGGWRVGWA----TKSVPRKGERFLG----DESGSWGYDG---WTGKKywASTSPLTGLPLF 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2696015     737 RSDDVgkllpgpRGC---PASHSAS---MGSPCRGCLENFNTDGLFFPVMSFSAGVKVRFLMGGR 795
Cdd:pfam00622   64 EPGDV-------IGCfldYEAGTISftkNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121

MIR

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

275-368

8.52e-07

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

Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 48.88 E-value: 8.52e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015      275 GSNIRWGQAFRLRHLTTGHYLALTEDqglilqdraksdtkstafsfraskelKEKLDSSHKRDIEGMGVPEIKygdsvcf 354
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDE--------------------------KLPPWGDGQQEVTGYGNPAID------- 47

                            90
                    ....*....|....
gi 2696015      355 vqhiASGLWVTYKA 368
Cdd:smart00472   48 ----ANTLWLIEPV 57

MIR

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

100-155

1.25e-05

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

Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 45.41 E-value: 1.25e-05

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2696015      100 HRTLLYGHAVLLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATG-EACWWTIHPA 155
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57

SPRY

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...

659-794

2.41e-04

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: 43.82 E-value: 2.41e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015      659 KWYFELIIDqvdpfltaEPTHLRVGWASSSGYAPYpgggegwgGNGVGDDLYSYGFDGLHlwsgripravaSINQHLLRS 738
Cdd:smart00449    3 RHYFEVEIG--------DGGHWRVGVATKSVPRGY--------FALLGEDKGSWGYDGDG-----------GKKYHNSTG 55

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2696015      739 DDVGKLLPGPR---GC---PASHSAS---MGSPCRGC-LENFNTDGLFFPVMSFSAGVKVRFLMGG 794
Cdd:smart00449   56 PEYGLPLQEPGdviGCfldLEAGTISfykNGKYLHGLaFFDVKFSGPLYPAFSLGSGNSVRLNFGP 121

EF-hand_7

pfam13499

EF-hand domain pair;

3924-3979

4.30e-04

EF-hand domain pair;

Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 41.47 E-value: 4.30e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2696015    3924 FKEYDPDGKGIISKKEFQKAM---EGQKQYTQSEIDFLLSCAEADENDMFNYVDFVDRF 3979
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLrklEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66

Name

Accession

Description

Interval

E-value

beta-trefoil_MIR_RyR3

cd23292

MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...

216-405

4.11e-132

Pssm-ID: 467763 [Multi-domain] Cd Length: 187 Bit Score: 412.38 E-value: 4.11e-132

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   216 GYLLGGHVVRLFHGHDECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYL 295
Cdd:cd23292    1 GYLLGGHVVRLFHGHDECLTIPSTDQSDEQHRVVNYEAGGAGTRARSLWRLEPLRISWSGSHIRWGQTFRLRHLTTGHYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   296 ALTEDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKTSR 375
Cdd:cd23292   81 ALTEDQGLILQDRAKSDTKSTAFCFRAS---KEKLESGPKRDIDGMGIAEIKYGDSVCFVQHVASGLWLTYKAPDAKSSR 157

                        170       180       190
                 ....*....|....*....|....*....|
gi 2696015   376 LGPLKRKVILHQEGHMDDGLTLQRCQREES 405
Cdd:cd23292  158 LGPLKRRAILHQEGHMDDGLTLQRCQHEES 187

RR_TM4-6

pfam06459

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

4230-4500

6.49e-112

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: 358.63 E-value: 6.49e-112

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4230 DMPDPTQFGIHDDTMEAERAEVMEPGITTELVHfIKGEKGDTDIMSDLFGLHPKKEGSLK----HGPEVGLGDLSEIIGK 4305
Cdd:pfam06459    1 NMPDPTQDEVHGDVSEPEKDEEQEASGLPDLAD-AAGGEEEEDLLSDIFGLILKKEGGQYkvvpHDPEAGLGDLSETTAE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4306 DEPPTLEstvQKKRKAQAAEMKAANEAEGKVES-EKADMEDG-EKEDKDKEEEQAEYLW-TEVTKKKKRRCGQKVEKPEA 4382
Cdd:pfam06459   80 EPPPLLK---RKLQESEEAEDEEEEEEEPKPEPiEKADGENGeKEEKPKEEETESEAPEeEEMKKKQRKRHSKKKEEPEA 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4383 FTANFFKGLEIYQTKLLHYLARNFYNLRFLALFVAFAINFILLFYKV--------TEEPLEEETEDVANLWNSFNDEEEE 4454
Cdd:pfam06459  157 QGSAFWNELEVYQTKLLNYLARNFYNLRFLALFVAFAINFILLFYKVstsppdeeEEEGSGWGDSGSGSGGGSGEDEEEE 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2696015    4455 EAMVFFVLQESTGYMAPTLRALAIIHTIISLVCVVGYYCLKVPLVV 4500
Cdd:pfam06459  237 EGPVYFVLEESTGYMEPTLRFLAILHTIISFLCIIGYYCLKVPLVI 282

beta-trefoil_MIR_RyR

cd23278

MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...

220-401

1.05e-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: 327.73 E-value: 1.05e-102

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   220 GGHVVRLFHGH-DECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYLALT 298
Cdd:cd23278    1 GGDVLRLFHGHmDECLTIPAAGSKEDQHRTVIYEGGAVSTHARSLWRLELLRIKWSGSHIGWGQPFRLRHVTTGRYLALT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   299 EDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKTSRLGP 378
Cdd:cd23278   81 EDRGLVLVPKEKADVKATAFCFRQS---KDDKKVLDEKEDEGMGTPEIKYGDSLVFIQHVDTGLWLSYQAVETKKRVGGV 157

                        170       180
                 ....*....|....*....|...
gi 2696015   379 LKRKVILHQEGHMDDGLTLQRCQ 401
Cdd:cd23278  158 EERKAILHAEGHMDDGLSLSRAQ 180

beta-trefoil_MIR_RyR1

cd23290

MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...

211-405

2.16e-102

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

Pssm-ID: 467761 [Multi-domain] Cd Length: 192 Bit Score: 327.23 E-value: 2.16e-102

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   211 SSIEEGYLLGGHVVRLFHGH-DECLTIPSTDQNDsQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHL 289
Cdd:cd23290    1 SCCEEGYVTGGHVLRLFHGHmDECLTISAADSDD-QRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   290 TTGHYLALTEDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQ 369
Cdd:cd23290   80 TTGRYLALTEDQGLVVVDACKAHTKATSFCFRVS---KEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAP 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 2696015   370 DAKTSRLGPLKRKVILHQEGHMDDGLTLQRCQREES 405
Cdd:cd23290  157 DPKALRLGVLKKKAILHQEGHMDDALFLTRCQQEES 192

RYDR_ITPR

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...

442-621

2.81e-80

Pssm-ID: 460175 Cd Length: 199 Bit Score: 264.06 E-value: 2.81e-80

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     442 TLQDLIAYFQPPEEEMRHEDKQNKL---RSLKNRQNLFKEEGMLALVLNCIDRLN-VYNSVAHFAGIAREESGMAWKEIL 517
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLmnnKPLRQRQNLMREQGVLETVMEVIDLLGaPFTGALLFAEDLGEEKNAPWKKIV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     518 NLLYKLLAALIRGNRNNCAQFSNNLDWLISKLDRLESSSGILEVLHCILTESPE-ALNLIAEGHIKSIISLLDKHGRNHK 596
Cdd:pfam01365   81 RLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEGTLDVLTALLMDNPElLLNYIKECHIKSFISLLRKHGRDPR 160

                          170       180
                   ....*....|....*....|....*
gi 2696015     597 VLDILCSLCLCNGVAVRANQNLICD 621
Cdd:pfam01365  161 YLDFLSDLCVCNGEAVRENQNLICR 185

SPRY2_RyR

cd12878

SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ...

1073-1205

2.45e-78

Pssm-ID: 240458 Cd Length: 133 Bit Score: 255.69 E-value: 2.45e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1073 RFFRVERSYPVRSGKWYFEFEVVTGGDMRVGWARPGCRPDVELGADDQAFVFEGNRGQRWHQGSGYFGRTWQPGDVVGCM 1152
Cdd:cd12878    1 RTFRAEKTYAVTSGKWYFEFEVLTSGYMRVGWARPGFRPDLELGSDDLSYAFDGFLARKWHQGSESFGKQWQPGDVVGCM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 2696015  1153 INLDDASMIFTLNGELLITNKGSELAFADYEIENGFVPICCLGLSQIGRMNLG 1205
Cdd:cd12878   81 LDLVDRTISFTLNGELLIDSSGSEVAFKDIEIGEGFVPACSLGVGQKGRLNLG 133

beta-trefoil_MIR_RyR2

cd23291

MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...

220-405

4.45e-77

MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, also called RYR-2, or cardiac muscle ryanodine receptor-calcium release channel, or cardiac muscle ryanodine receptor, or type 2 ryanodine receptor, is a calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity of RYR-2 is modulated by formation of heterotetramers with RYR-3. RYR-2 is required for cellular calcium ion homeostasis. it plays an essential role in embryonic heart development. RYR-2 forms homotetramer and also forms heterotetramers with RYR-1 and RYR-3. RYR-2 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

Pssm-ID: 467762 [Multi-domain] Cd Length: 184 Bit Score: 254.58 E-value: 4.45e-77

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   220 GGHVVRLFHGH-DECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYLALT 298
Cdd:cd23291    1 GGDVLRLLHGHmDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   299 EDQGLILQDRAKSDTKSTAFSFRASkelKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKTSRLGP 378
Cdd:cd23291   81 EDKNLLLMDKEKADVKSTAFTFRSS---KEKLDVGVRKEVDGMGTSEIKYGDSVCYIQHVDTGLWLTYQSVDVKSVRMGS 157

                        170       180
                 ....*....|....*....|....*..
gi 2696015   379 LKRKVILHQEGHMDDGLTLQRCQREES 405
Cdd:cd23291  158 IQRKAIMHHEGHMDDGLNLSRSQHEES 184

MIR

pfam02815

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

216-397

8.27e-77

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

Pssm-ID: 397103 [Multi-domain] Cd Length: 185 Bit Score: 253.83 E-value: 8.27e-77

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     216 GYLLGGHVVRLFHGH-DECLTIPSTDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRI-SWSGSNIRWGQAFRLRHLTTGH 293
Cdd:pfam02815    1 GYLKGGDVVRLFHSHqDEYLTGSEQQQKQPFLRITLYPHGDANNSARSLWRIEVVRHdAWRGGLIKWGSPFRLRHLTTGR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     294 YLALTEDQGLILQDRAKSDTKSTAFSFRASKELKEKLDSSHKRDIEGMGVPEIKYGDSVCFVQHIASGLWVTYKAQDAKT 373
Cdd:pfam02815   81 YLHSHEEQKPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPK 160

                          170       180
                   ....*....|....*....|....
gi 2696015     374 SRLGPLKRKVILHQEGHMDDGLTL 397
Cdd:pfam02815  161 WGFGPEQQKVTCAKEGHMDDALTL 184

RYDR_ITPR

RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...

2024-2234

1.65e-75

Pssm-ID: 460175 Cd Length: 199 Bit Score: 250.58 E-value: 1.65e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2024 QIRSLLSVRMGKEEELLMINGLGDIMNNKVFYQHPNLMRVLGMHETVMEVMvNVLGT-------------EKSQIAFPKM 2090
Cdd:pfam01365    1 LLRDLIFFFAGPEEEELHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEVI-DLLGApftgallfaedlgEEKNAPWKKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2091 VASCCRFLCYFCRISRQNQKAMFEHLSYLLENssvgLASPSMRGSTpLDVAASSVMDNNELALsleepdlekvvTYLAGC 2170
Cdd:pfam01365   80 VRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQ----LGSPSLAEGT-LDVLTALLMDNPELLL-----------NYIKEC 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2696015    2171 GLQSCPMLLAKGYPDvgwnpiegERYLSFLRFAVFVNSESVEENASVVVKLLIRRPECFGPALR 2234
Cdd:pfam01365  144 HIKSFISLLRKHGRD--------PRYLDFLSDLCVCNGEAVRENQNLICRLLLPNPDLLLQTLL 199

SPRY3_RyR

cd12879

SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ...

1325-1463

8.46e-72

Pssm-ID: 293937 Cd Length: 151 Bit Score: 237.97 E-value: 8.46e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1325 TTTQCYYAIRIFGGQDPSCVWVGWVTPDYHLYSEKFDLNKNCTVTVTLGDERGRVHESVKRSNCYMVWGGDIVASSQR-- 1402
Cdd:cd12879   11 LVDEYYYSVRIFPGQDPSNVWVGWVTSDFHLYDPSFDPDKVRNVTVTMGDEKGGVYESIKRQNCYMVCAGELLAEVGQds 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2696015  1403 SNRSNVDLEIGCLVDLAMGMLSFSANGKELGTCYQVEPNTKVFPAVFLQPTSTSLFQFELG 1463
Cdd:cd12879   91 SGRASQGLLIGCLIDTATGLLTFTANGKETSTRFQVEPGTKLFPAVFVRPTSKEVLQFELG 151

SPRY1_RyR

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...

641-793

1.89e-65

Pssm-ID: 240457 Cd Length: 151 Bit Score: 219.88 E-value: 1.89e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   641 SIRPNIFLGVAEGSAQYKKWYFELIIDQVDPFlTAEPTHLRVGWASSSGYAPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 720
Cdd:cd12877    1 SIRPNIFVGVVEGSAQYKKWYFEVEVDHVEQF-THQPAHLRVGWANTSGYVPYPGGGEGWGGNGVGDDLYSYGFDGLHLW 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2696015   721 SGRIPRAVASINQHLLRSDDVgkllpgpRGC------PASHSASMGSPCRGCLENFNTDGLFFPVMSFSAGVKVRFLMG 793
Cdd:cd12877   80 TGGRSRRVTSGTQHLLKKGDV-------VGCcldlsvPSISFRVNGRPVQGMFENFNLDGMFFPVMSFSAGVSCRFLLG 151

Ins145_P3_rec

pfam08709

Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...

14-212

1.93e-65

Pssm-ID: 462572 [Multi-domain] Cd Length: 212 Bit Score: 222.37 E-value: 1.93e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015      14 FLRTEDEVVLQCIATIhkeqrKFCLAAEGLGNRLCFLEPTSEAKYIPP-DLCVCNFVLEQSLSVRALQEML--ANTGENG 90
Cdd:pfam08709    4 FLHIGDIVSLSCEESV-----NGFISALGLGNDRCFVENKAGDLNDPPkKFRDCVFKICPANSYAAQKELWsaGNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015      91 GEGAAQGG------GHRTLLYGHAVLLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATGEACWWTIHPASKQRSEGEK 164
Cdd:pfam08709   79 NSLTDALKhasnieGHQNLQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNGEGCWFIITPAYKQRSEGDN 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2696015     165 VRIGDDLILVSVSSERYLHLSVS-----NGNIQVDASFMQTLWNVHPTCSGSS 212
Cdd:pfam08709  159 VCVGDEVILVPVSAPIFLHTTSSselrdNPGKEVNASFGQTSWKMEPFMSGCE 211

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

2599-2688

1.95e-45

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

Pssm-ID: 460419 Cd Length: 90 Bit Score: 159.98 E-value: 1.95e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2599 FDPKPINTMNFSLPEKLEYIVTKYAEHSHDKWACDKSQSGWKYGISLDENVKTHPLIRPFKTLTEKEKEIYRWPARESLK 2678
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2696015    2679 TMLAVGWTVE 2688
Cdd:pfam02026   81 TLLALGYTIE 90

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

964-1053

7.42e-41

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

Pssm-ID: 460419 Cd Length: 90 Bit Score: 146.88 E-value: 7.42e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     964 YKPAPLDLSDVKLLPPQEILVDKLAENAHNVWAKDRIKQGWTYGIQQDLKNKRNPRLVPYALLDERTKKSNRDSLREAVR 1043
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPARETLK 80

                           90
                   ....*....|
gi 2696015    1044 TFVGYGYNIE 1053
Cdd:pfam02026   81 TLLALGYTIE 90

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

850-924

3.91e-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: 133.40 E-value: 3.91e-36

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2696015     850 FIPCPVDTSQVILPPHLEKIRDRLAENIHELWGMNKIELGWTFGKIRDDNKRQHPCLVEFSKLPETEKNYNLQMS 924
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVRDDAAKTHPCLVPYDLLTEKEKEYDREPA 75

RIH_assoc

pfam08454

RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...

3723-3840

2.25e-35

Pssm-ID: 462482 Cd Length: 98 Bit Score: 131.49 E-value: 2.25e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    3723 QNDEFTRDLFRFLQLLCEGHNSDFQNFLRTQMGNTTTVNVIISTVDYLLRLQESISdfywyysgkdiidesgQHNFSKAl 3802
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYNLVEETVDLLKAYCKSIN----------------EKNIELI- 63

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2696015    3803 avtKQIFNSLTEYIQGPCIGNQQSLAHSRLWDAVVGFL 3840
Cdd:pfam08454   64 ---IQCLDTLTEFIQGPCIENQIALCESKFLEIANDLL 98

SPRY

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...

1085-1207

1.42e-31

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

Pssm-ID: 214669 Cd Length: 122 Bit Score: 121.63 E-value: 1.42e-31

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     1085 SGKWYFEFEVVTGGDMRVGWARPGCRPDVE--LGADDQAFVFEGNRGQRWHQGSG-YFGRTWQ-PGDVVGCMINLDDASM 1160
Cdd:smart00449    1 SGRHYFEVEIGDGGHWRVGVATKSVPRGYFalLGEDKGSWGYDGDGGKKYHNSTGpEYGLPLQePGDVIGCFLDLEAGTI 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 2696015     1161 IFTLNGELLitnkgSELAFADYEIENGFVPICCLGLSQIGRMNLGTD 1207
Cdd:smart00449   81 SFYKNGKYL-----HGLAFFDVKFSGPLYPAFSLGSGNSVRLNFGPL 122

SPRY

cd11709

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...

1086-1203

7.26e-26

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

Pssm-ID: 293931 Cd Length: 118 Bit Score: 105.21 E-value: 7.26e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1086 GKWYFEFEVVT--GGDMRVGWARPGCRPDVE--LGADDQAFVFEGNRGQRWHQG-SGYFGRTWQPGDVVGCMINLDDASM 1160
Cdd:cd11709    1 GKWYWEVRVDSgnGGLIQVGWATKSFSLDGEggVGDDEESWGYDGSRLRKGHGGsSGPGGRPWKSGDVVGCLLDLDEGTL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 2696015  1161 IFTLNGELLITnkgselAFAD-YEIENGFVPICCLGLSQIGRMN 1203
Cdd:cd11709   81 SFSLNGKDLGV------AFTNlFLKGGGLYPAVSLGSGQGVTIN 118

Ion_trans

pfam00520

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...

4617-4777

3.02e-25

Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 107.74 E-value: 3.02e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4617 SFLYLAWYTTMSVLG-HYNNFFFAAHLLDIAMGFKTLRTILSSVTHNGKQLVLTVGLLAVVVYLYTVVAFNFFRKFYNKS 4695
Cdd:pfam00520   79 SLISLVLSSVGSLSGlRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTW 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    4696 EDDDEPDMKCDDMMTCYLFHMYVgvRAGGGIGDEIEDPAGDPYEMYRIVFDITFFFFVIVILLAIIQGLIIDAFGELRDQ 4775
Cdd:pfam00520  159 ENPDNGRTNFDNFPNAFLWLFQT--MTTEGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTER 236


                   ..
gi 2696015    4776 QE 4777
Cdd:pfam00520  237 TE 238

RyR

RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ...

2717-2796

3.99e-25

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

Pssm-ID: 460419 Cd Length: 90 Bit Score: 102.20 E-value: 3.99e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    2717 YSPAPLDLSNVVLSRELQGMVEVVAENYHNIWAKKKKLELESKGGG------SHPLLVPYDTLTAKEKFKDREKAQDLFK 2790
Cdd:pfam02026    1 YKPKPVDTSNVTLPEDLEALVEKLAENTHEVWAKEKIEQGWTYGEVrddaakTHPCLVPYDLLTEKEKEYDREPARETLK 80


                   ....*.
gi 2696015    2791 FLQVNG 2796
Cdd:pfam02026   81 TLLALG 86

SPRY

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...

1087-1207

1.25e-21

Pssm-ID: 459877 Cd Length: 121 Bit Score: 93.18 E-value: 1.25e-21

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    1087 KWYFEFEV--VTGGDMRVGWARPGCR--PDVELGADDQAFVFEGNRGQRWHQGSG--YFGRTWQPGDVVGCMINLDDASM 1160
Cdd:pfam00622    1 RHYFEVEIfgQDGGGWRVGWATKSVPrkGERFLGDESGSWGYDGWTGKKYWASTSplTGLPLFEPGDVIGCFLDYEAGTI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2696015    1161 IFTLNGELLITnkgselAFADYEIENGFVPICCLGLSQIGRMNLGTD 1207
Cdd:pfam00622   81 SFTKNGKSLGY------AFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121

SPRY

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...

1329-1464

6.22e-20

Pssm-ID: 459877 Cd Length: 121 Bit Score: 88.55 E-value: 6.22e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015    1329 CYYAIRIFGgQDPSCVWVGWVTPDYHLYSEKFdlnknctvtvtLGDERGrvhesvkrSNCYMVWGGDIV-ASSQRSNRSN 1407
Cdd:pfam00622    2 HYFEVEIFG-QDGGGWRVGWATKSVPRKGERF-----------LGDESG--------SWGYDGWTGKKYwASTSPLTGLP 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2696015    1408 V---DLEIGCLVDLAMGMLSFSANGKELGTCYQVEPNT-KVFPAVFLQPTSTslFQFELGK 1464
Cdd:pfam00622   62 LfepGDVIGCFLDYEAGTISFTKNGKSLGYAFRDVPFAgPLFPAVSLGAGEG--LKFNFGL 120

SPRY

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...

1329-1465

3.62e-19

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

Pssm-ID: 214669 Cd Length: 122 Bit Score: 86.19 E-value: 3.62e-19

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     1329 CYYAIRIFggqDPSCVWVGWVTPDYHLYSEKfdlnknctvtvTLGDERG-RVHESVKRSNCYMVWGGDIVASSQRSNRsn 1407
Cdd:smart00449    4 HYFEVEIG---DGGHWRVGVATKSVPRGYFA-----------LLGEDKGsWGYDGDGGKKYHNSTGPEYGLPLQEPGD-- 67

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     1408 vdlEIGCLVDLAMGMLSFSANGKELG--TCYQVEPNTKVFPAVFLQPTSTSlfQFELGKL 1465
Cdd:smart00449   68 ---VIGCFLDLEAGTISFYKNGKYLHglAFFDVKFSGPLYPAFSLGSGNSV--RLNFGPL 122

beta-trefoil_MIR_itr-1-like

cd23280

MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...

215-398

1.69e-18

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

Pssm-ID: 467751 [Multi-domain] Cd Length: 199 Bit Score: 87.06 E-value: 1.69e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   215 EGYLLGGHVVRLFH-------GHDECLTIPSTDQNDSQHRRIFYEAGGAG----TRARSLWRVEPLRISWSGSNIRWGQA 283
Cdd:cd23280    4 ENFLKGGDVVRLFHkeleaylSAEGSFVDEVLTEDVHLRVRPVDDRKPRTlfppTSGDTFWQIEKEDTPLKGGVIKWGDQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   284 FRLRHLTTGHYLALTEDQG---LILQDraKSDTKSTAFSFRASkeLKEKLDsshkrdiegmgvpEIKYGdSVCFVQHIAS 360
Cdd:cd23280   84 CRLRHLPTGKYLAVDDKTGngkVVLTS--DPSDPSTVFRLHPV--TKETSE-------------EVKFG-SYVRIEHVAT 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 2696015   361 GLWV-----TYKAQDAKTSRLGP----LKRKVILHQEGHMDDGLTLQ 398
Cdd:cd23280  146 GTWLhaetdEELRRSKKSPAGLSwdgaKLRKVSLSLERQDDDAFTIQ 192

SPRY_RNF123

cd12882

SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ...

1083-1166

4.32e-18

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

Pssm-ID: 293940 Cd Length: 128 Bit Score: 83.53 E-value: 4.32e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1083 VRSGKWYFEFEVVTGGDMRVGWARPGCRPDVELGADD--QAFVFEGNRGQRWHQGSGYFGRTWQPGDVVGCMINLDDASM 1160
Cdd:cd12882    8 VYKGKWMYEVTLGTKGIMQIGWATISCRFTQEEGVGDtrDSYAYDGNRVRKWNVSTQKYGEPWVAGDVIGCCIDLDKGTI 87


                 ....*.
gi 2696015  1161 IFTLNG 1166
Cdd:cd12882   88 SFYRNG 93

SPRY_Ash2

cd12872

SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ...

1080-1169

6.26e-17

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: 80.64 E-value: 6.26e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1080 SYPVRSGKWYFEFEVVTGGDM-----RVGWARPGCRPDVELGADDQAFVFEGNRGQRWHQGSG--YFGRTWQPGDVVGCM 1152
Cdd:cd12872   22 NHGVREGKWYFEVKILEGGGTetghvRVGWSRREASLQAPVGYDKYSYAIRDKDGSKFHQSRGkpYGEPGFKEGDVIGFL 101

                         90
                 ....*....|....*..
gi 2696015  1153 INLddASMIFTLNGELL 1169
Cdd:cd12872  102 ITL--PKIEFFKNGKSQ 116

beta-trefoil_MIR

cd23263

MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...

221-390

5.76e-15

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

Pssm-ID: 467746 [Multi-domain] Cd Length: 172 Bit Score: 75.88 E-value: 5.76e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   221 GHVVRLFHGH-DECLTIPS-TDQNDSQHRRIFYEAGGAGTRARSLWRVEPLRISWsGSNIRWGQAFRLRHLTTGHYLALT 298
Cdd:cd23263    1 GDVIWLKHSEtGKYLHSHRkNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQ-GGPVKWGDKIRLRHLSTGKYLSSE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   299 EDQG---------LILQDrakSDTKSTAFSFraskelkekldsshkrDIEGMGVPEIKY--GDSVCFVQHIASGLWVtyK 367
Cdd:cd23263   80 EGKKspksnhqevLCLTD---NPDKSSLFKF----------------EPIGSTKYKQKYvkKDSYFRLKHVNTNFWL--H 138

                        170       180
                 ....*....|....*....|...
gi 2696015   368 AQDAKTSRLGPLKRKVILHQEGH 390
Cdd:cd23263  139 SHEKKFNINNKTQQEVICHGERE 161

SPRY_RING

cd12883

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ...

1086-1166

1.07e-14

SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development.

Pssm-ID: 293941 Cd Length: 121 Bit Score: 73.54 E-value: 1.07e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1086 GKWYFEFEVVTGGDMRVGWARPGCRPDVE----LGADDQAFVFEGNRGQRWH--QGSGYFGRTWQPGDVVGCMINLDDAS 1159
Cdd:cd12883    1 GVWYYEVTVLTSGVMQIGWATKDSKFLNHegygIGDDEYSCAYDGCRQLIWYnaKSKPHTHPRWKPGDVLGCLLDLNKKQ 80


                 ....*..
gi 2696015  1160 MIFTLNG 1166
Cdd:cd12883   81 MIFSLNG 87

SPRY_RanBP_like

cd12885

SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ...

1073-1169

1.72e-12

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

Pssm-ID: 293943 Cd Length: 132 Bit Score: 67.30 E-value: 1.72e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1073 RFFRVERSYPVRSGKWYFEFEVV---TGGDMRVGWARPGCRPDVELGADDQAFVFEGNRGQRWHQGSGY--FGRTWQPGD 1147
Cdd:cd12885    1 GSVRADHPIPPKVPVFYFEVTILdlgEKGIVSIGFCTSGFPLNRMPGWEDGSYGYHGDDGRVYLGGGEGenYGPPFGTGD 80

                         90       100
                 ....*....|....*....|..
gi 2696015  1148 VVGCMINLDDASMIFTLNGELL 1169
Cdd:cd12885   81 VVGCGINFKTGEVFFTKNGELL 102

SPRY_DDX1

cd12873

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...

1085-1169

7.90e-12

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

Pssm-ID: 293933 Cd Length: 155 Bit Score: 66.44 E-value: 7.90e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1085 SGKWYFEFEVVTGGDMRVGWARPGCrpDVELGADDQAFVFeGNRGQRWH--QGSGYfGRTWQPGDVVGCMINLDDASMIF 1162
Cdd:cd12873   39 KGKYYYEVTVTDEGLCRVGWSTEDA--SLDLGTDKFGFGY-GGTGKKSHgrQFDDY-GEPFGLGDVIGCYLDLDNGTISF 114


                 ....*..
gi 2696015  1163 TLNGELL 1169
Cdd:cd12873  115 SKNGKDL 121

SPRY

cd11709

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...

1330-1450

3.27e-09

Pssm-ID: 293931 Cd Length: 118 Bit Score: 57.83 E-value: 3.27e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1330 YYAIRIFGGQdPSCVWVGWVTPDYHLYSEKfdlnknctvtvTLGDE---------RGRVHESVKRSNCYMVWG-GDIvas 1399
Cdd:cd11709    4 YWEVRVDSGN-GGLIQVGWATKSFSLDGEG-----------GVGDDeeswgydgsRLRKGHGGSSGPGGRPWKsGDV--- 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 2696015  1400 sqrsnrsnvdleIGCLVDLAMGMLSFSANGKELGTCYQVEPNTK--VFPAVFL 1450
Cdd:cd11709   69 ------------VGCLLDLDEGTLSFSLNGKDLGVAFTNLFLKGggLYPAVSL 109

beta-trefoil_MIR_ITPR

cd23277

MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...

215-364

4.35e-09

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

Pssm-ID: 467748 [Multi-domain] Cd Length: 204 Bit Score: 59.68 E-value: 4.35e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   215 EGYLLGGHVVRLFHGHDE-CLTipSTDQNDSQHrrIFYEAGG-----AGTRARSLWRVE-----PLRiswsGSNIRWGQA 283
Cdd:cd23277    8 EDVLKGGDVVRLFHAEQEkFLT--CDEYKKKQY--VFLRTTGrtsatSATSSKALWEVEvvqhdPCR----GGAGHWNSL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   284 FRLRHLTTGHYLAltedqglilqdrAKSDTKSTAFSFRaskelkEKLDSSHKRDIEGM-GVPE--------------IKY 348
Cdd:cd23277   80 FRFKHLATGQYLA------------AEVDPDPTPDPTR------SKLRGAPGKPVYCLvSVPHgndiasifeldpttLQR 141

                        170       180
                 ....*....|....*....|..
gi 2696015   349 GDSV----CFV--QHIASGLWV 364
Cdd:cd23277  142 GDSLvprsSYVrlRHLCTNTWV 163

SPRY

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...

659-795

7.90e-09

Pssm-ID: 459877 Cd Length: 121 Bit Score: 56.58 E-value: 7.90e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015     659 KWYFELIIDQvdpfltAEPTHLRVGWAsssgYAPYPGGGEGWGGngvgDDLYSYGFDGlhlWSGRI--PRAVASINQHLL 736
Cdd:pfam00622    1 RHYFEVEIFG------QDGGGWRVGWA----TKSVPRKGERFLG----DESGSWGYDG---WTGKKywASTSPLTGLPLF 63

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2696015     737 RSDDVgkllpgpRGC---PASHSAS---MGSPCRGCLENFNTDGLFFPVMSFSAGVKVRFLMGGR 795
Cdd:pfam00622   64 EPGDV-------IGCfldYEAGTISftkNGKSLGYAFRDVPFAGPLFPAVSLGAGEGLKFNFGLR 121

beta-trefoil_MIR_ITPR2

cd23288

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...

202-296

1.30e-08

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

Pssm-ID: 467759 [Multi-domain] Cd Length: 222 Bit Score: 58.51 E-value: 1.30e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   202 WNVHPTCSGSSIEEGYLLGGHVVRLFHGHDECLtIPSTDQNDSQH---RRIFYEAGGAGTRARSLWRVE-----PLRisw 273
Cdd:cd23288    1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKF-LTCDEYKKKQHiflRTTLRQSATSATSSKALWEIEvvhydPCR--- 76

                         90       100
                 ....*....|....*....|...
gi 2696015   274 sGSNIRWGQAFRLRHLTTGHYLA 296
Cdd:cd23288   77 -GGAGQWNSLFRFKHLATGNYLA 98

beta-trefoil_MIR_ITPR1

cd23287

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...

211-364

1.20e-07

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

Pssm-ID: 467758 [Multi-domain] Cd Length: 222 Bit Score: 55.85 E-value: 1.20e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   211 SSIEEGYLLGGHVVRLFHGHDECLtIPSTDQNDSQH---RRIFYEAGGAGTRARSLWRVE-----PLRiswsGSNIRWGQ 282
Cdd:cd23287    4 SDNKDDILKGGDVVRLFHAEQEKF-LTCDEHRKKQHvflRTTGRQSATSATSSKALWEVEvvqhdPCR----GGAGYWNS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   283 AFRLRHLTTGHYLA--LTEDQGLILQDRAKSDTKSTAFSFRASKELKEKLDSSHKRDIEGMGVPEI--------KYGDSV 352
Cdd:cd23287   79 LFRFKHLATGHYLAaeVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIfeldpttlRGGDSL 158

                        170
                 ....*....|....*...
gi 2696015   353 ------CFVQHIASGLWV 364
Cdd:cd23287  159 vprnsyVRLRHLCTNTWV 176

MIR

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

275-368

8.52e-07

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

Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 48.88 E-value: 8.52e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015      275 GSNIRWGQAFRLRHLTTGHYLALTEDqglilqdraksdtkstafsfraskelKEKLDSSHKRDIEGMGVPEIKygdsvcf 354
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDE--------------------------KLPPWGDGQQEVTGYGNPAID------- 47

                            90
                    ....*....|....
gi 2696015      355 vqhiASGLWVTYKA 368
Cdd:smart00472   48 ----ANTLWLIEPV 57

SPRY1_RyR

SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ...

1087-1194

2.68e-06

Pssm-ID: 240457 Cd Length: 151 Bit Score: 50.39 E-value: 2.68e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1087 KWYFEFEVvTGGD--------MRVGWAR-------PGCRPD---VELGADDQAFVFEG------NRGQRWHQGSGYFGRt 1142
Cdd:cd12877   19 KWYFEVEV-DHVEqfthqpahLRVGWANtsgyvpyPGGGEGwggNGVGDDLYSYGFDGlhlwtgGRSRRVTSGTQHLLK- 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 2696015  1143 wqPGDVVGCMINLDDASMIFTLNGELLitnKGSelaFADYEIENGFVPICCL 1194
Cdd:cd12877   97 --KGDVVGCCLDLSVPSISFRVNGRPV---QGM---FENFNLDGMFFPVMSF 140

beta-trefoil_MIR_ITPR3

cd23289

MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...

218-341

4.25e-06

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

Pssm-ID: 467760 [Multi-domain] Cd Length: 215 Bit Score: 51.20 E-value: 4.25e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   218 LLGGHVVRLFHGHDECLtIPSTDQNDSQH---RRIFYEAGGAGTRARSLWRVE-----PLRiswsGSNIRWGQAFRLRHL 289
Cdd:cd23289   11 LKGGDVVRLFHAEQEKF-LTCDEYKGKLQvflRTTLRQSATSATSSNALWEVEvvhhdPCR----GGAGHWNGLYRFKHL 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 2696015   290 TTGHYLAlTEDQGLILQDRAKSDTKSTAFSFRASK-----ELKEKLDS-SHKRDIEGM 341
Cdd:cd23289   86 ATGNYLA-AEENPSYKGDASDPKAAGMGAQSRTGRrnageKIKYCLVAvPHGNDIASL 142

SPRY_hnRNP

cd12884

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ...

1080-1169

4.27e-06

SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation.

Pssm-ID: 293942 Cd Length: 177 Bit Score: 50.28 E-value: 4.27e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1080 SYPVRSGKWYFEFEVV-------------TGGDMRVGWARPGCRpdVELGADDQAFVFEGNrGQRWHQG-SGYFGRTWQP 1145
Cdd:cd12884   39 TYGVTKGKVCFEVKVTenlpvkhlpteetDPHVVRVGWSVDSSS--LQLGEEEFSYGYGST-GKKSTNCkFEDYGEPFGE 115

                         90       100
                 ....*....|....*....|....*.
gi 2696015  1146 GDVVGCMINLD--DASMIFTLNGELL 1169
Cdd:cd12884  116 NDVIGCYLDFEsePVEISFSKNGKDL 141

SPRY_RanBP9_10

cd12909

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ...

1076-1169

1.09e-05

SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells.

Pssm-ID: 293966 Cd Length: 144 Bit Score: 48.29 E-value: 1.09e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1076 RVERSYPVRSGKWYFEFEVVTGGD---MRVGWarpgCRPDVEL----GADDQAFVFEGNRGQRWH-QGSGY-FGRTWQPG 1146
Cdd:cd12909   15 RANHPIPPQCGIYYFEVKIISKGRdgyIGIGF----STKDVNLnrlpGWEPHSWGYHGDDGHSFCsSGTGKpYGPTFTTG 90

                         90       100
                 ....*....|....*....|...
gi 2696015  1147 DVVGCMINLDDASMIFTLNGELL 1169
Cdd:cd12909   91 DVIGCGINFRDNTAFYTKNGVNL 113

MIR

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

100-155

1.25e-05

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

Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 45.41 E-value: 1.25e-05

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2696015      100 HRTLLYGHAVLLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATG-EACWWTIHPA 155
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57

SPRY_like

cd12886

SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ...

1086-1200

2.30e-04

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

Pssm-ID: 293944 Cd Length: 129 Bit Score: 44.03 E-value: 2.30e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015  1086 GKWYFEFEVVTGG---DMRVGWARPGCRPDVELG-ADDQA--FVFEGNRGQRWHQGSGY--FGRTWQPGDVVGCMINLDD 1157
Cdd:cd12886    1 GKWYWEVTVVSSAastYAGIGVANAAATGNNGLNgIELSSigYSLGVYSGNKLSNGSSVatYGAGFTAGDVIGVALDLDA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 2696015  1158 ASMIFTLNGELLitnKGSELAFADYEIENG--FVPICCLGLSQIG 1200
Cdd:cd12886   81 GKIWFYKNGVWQ---GGGDPAPGTNPAFAGtaMYPAVTGGSSTGG 122

SPRY

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...

659-794

2.41e-04

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: 43.82 E-value: 2.41e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015      659 KWYFELIIDqvdpfltaEPTHLRVGWASSSGYAPYpgggegwgGNGVGDDLYSYGFDGLHlwsgripravaSINQHLLRS 738
Cdd:smart00449    3 RHYFEVEIG--------DGGHWRVGVATKSVPRGY--------FALLGEDKGSWGYDGDG-----------GKKYHNSTG 55

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2696015      739 DDVGKLLPGPR---GC---PASHSAS---MGSPCRGC-LENFNTDGLFFPVMSFSAGVKVRFLMGG 794
Cdd:smart00449   56 PEYGLPLQEPGdviGCfldLEAGTISfykNGKYLHGLaFFDVKFSGPLYPAFSLGSGNSVRLNFGP 121

EF-hand_7

pfam13499

EF-hand domain pair;

3924-3979

4.30e-04

EF-hand domain pair;

Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 41.47 E-value: 4.30e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2696015    3924 FKEYDPDGKGIISKKEFQKAM---EGQKQYTQSEIDFLLSCAEADENDMFNYVDFVDRF 3979
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLrklEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66

SPRY_DDX1

cd12873

SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ...

1412-1451

7.08e-04

Pssm-ID: 293933 Cd Length: 155 Bit Score: 43.33 E-value: 7.08e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 2696015  1412 IGCLVDLAMGMLSFSANGKELGTCYQVEPNTK---VFPAVFLQ 1451
Cdd:cd12873  101 IGCYLDLDNGTISFSKNGKDLGKAFDIPPHLRnsaLFPAVCLK 143

SPRY

cd11709

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...

659-791

1.76e-03

Pssm-ID: 293931 Cd Length: 118 Bit Score: 41.26 E-value: 1.76e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2696015   659 KWYFELIIDqvdpflTAEPTHLRVGWASSSgyapypggGEGWGGNGVGDDLYSYGFDG--LHLWSGRIPRAvasiNQHLL 736
Cdd:cd11709    2 KWYWEVRVD------SGNGGLIQVGWATKS--------FSLDGEGGVGDDEESWGYDGsrLRKGHGGSSGP----GGRPW 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2696015   737 RSDDVGkllpgprGCPASHSASM------GSPCRGCLENFNTD-GLFFPVMSFSAGVKVRFL 791
Cdd:cd11709   64 KSGDVV-------GCLLDLDEGTlsfslnGKDLGVAFTNLFLKgGGLYPAVSLGSGQGVTIN 118

MIR

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

215-268

5.77e-03

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

Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 38.09 E-value: 5.77e-03

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2696015      215 EGYLLGGHVVRLFHGHDEC-LTIPSTD--QNDSQHRRIFYEaGGAGTRARSLWRVEP 268
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRyLHSHDEKlpPWGDGQQEVTGY-GNPAIDANTLWLIEP 56

MIR