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Conserved domains on  [gi|24644261|ref|NP_730942|]
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inositol 1,4,5,-trisphosphate receptor, isoform A [Drosophila melanogaster]

Protein Classification

inositol 1,4,5-trisphosphate receptor( domain architecture ID 12096418)

inositol 1,4,5-trisphosphate receptor is an intracellular channel receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium

Gene Ontology:  GO:0005220|GO:0070679|GO:0070588
PubMed:  26830355|16102823|22453946
TCDB:  1.A.3

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 230-459 1.02e-130

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: 408.28  E-value: 1.02e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  230 MEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLY 309
Cdd:cd23277    1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  310 RFKHLATGHYLAAEAEIDVSAGAMSatsasghdlhlgdcskdsglscstmnSTINDKPKGKQYRLVSVPYSADIASVFVL 389
Cdd:cd23277   81 RFKHLATGQYLAAEVDPDPTPDPTR--------------------------SKLRGAPGKPVYCLVSVPHGNDIASIFEL 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  390 DATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSPVEV 459
Cdd:cd23277  135 DPTTLQRGDSLVPRSSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 8-235 1.70e-86

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


:

Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 282.08  E-value: 1.70e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261      8 SASFLHLGDIVSLYAEGSVCGFLSTLGLVDDRTVVCPEAGDLSCPPKKFRDCLIKICPMNRYSAQKQFWKAakQSASSNT 87
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSA--GNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261     88 DPnLLKRLHHAAEIEKKQNetenkkllgtsIQYGRaVVQLLHLKSNKYLTVNKRLPSLLEKNAMRVYLDANGN-EGSWFY 166
Cdd:pfam08709   79 NS-LTDALKHASNIEGHQN-----------LQYGS-AILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWFI 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24644261    167 IKPFYKLRSIGDYVVVGDKVILSPVNAdQQNLHVAANYELPDNPGcKEVNVLNSSTSWKISLFMEHKEN 235
Cdd:pfam08709  146 ITPAYKQRSEGDNVCVGDEVILVPVSA-PIFLHTTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 495-696 7.18e-78

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: 256.74  E-value: 7.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261    495 LLQDIVYFIAGMENEQ-NKTKALEFTIKNPIRDRQKLLREQYILKQLFK---ILQGPFQqhtagdGPFLRLDELSDPKNS 570
Cdd:pfam01365    1 LLRDLIFFFAGPEEEElHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT------GALLFAEDLGEEKNA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261    571 PYKNIFRLCYRILRLSQQDYRKNQEYIAKHFGLMQKQIGYDILAE---DTITALLHNNRKLLEKHITAAEIETFVGLVRK 647
Cdd:pfam01365   75 PWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRK 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 24644261    648 nmHNWDSRFLDYLSDLCVSNRKAIAVTQELICKSVLSdkNKDILIETQV 696
Cdd:pfam01365  155 --HGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 2029-2138 5.34e-31

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


:

Pssm-ID: 462482  Cd Length: 98  Bit Score: 118.40  E-value: 5.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2029 NKVLVMQPILRFLQLLCENHNPDMQNLLRNQNNKTNNN-LVSETLMFLDCICGSttgglgllglyINEHNVALINQTLEA 2107
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYnLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 24644261   2108 LTEYCQGPCHENQNCIatHESNGLDIITALI 2138
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2363-2682 7.65e-13

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


:

Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 70.76  E-value: 7.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2363 LFNCVVVINMIV-AFFYPFDNTVPELSSHISLLFWIITIFSLVivlalpresgirtFIGSVILRFIFllgpestlcllgv 2441
Cdd:pfam00520    3 YFELFILLLILLnTIFLALETYFQPEEPLTTVLEILDYVFTGI-------------FTLEMLLKIIA------------- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2442 vtvtlksvhivsiMGNKGTLEKQLIKIITDFQLLYHCIYIAFCFCGLI----FHPFFYSLLLFDVVYREETLVNVIRSVT 2517
Cdd:pfam00520   57 -------------AGFKKRYFRSPWNILDFVVVLPSLISLVLSSVGSLsglrVLRLLRLLRLLRLIRRLEGLRTLVNSLI 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2518 RNGRSIVLTAVLALILVYLFSIIGYMFFKDDFLVSVDfeeqdnapppsvpltlsvpvsgdscsapddlgncqaakevapp 2597
Cdd:pfam00520  124 RSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWEN------------------------------------------- 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2598 saggGEVKERSCDSLVMCIVTTLNqgLRNGGGIGDILRAPSSKEGLFVArVIYDLLFFFIVIIIVLNLIFGVIIDTFADL 2677
Cdd:pfam00520  161 ----PDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFLLLNLFIAVIIDNFQEL 233


                   ....*
gi 24644261   2678 RSEKQ 2682
Cdd:pfam00520  234 TERTE 238
RYDR_ITPR super family cl03182
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1285-1404 1.03e-05

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.


The actual alignment was detected with superfamily member pfam01365:

Pssm-ID: 460175  Cd Length: 199  Bit Score: 48.73  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   1285 SVVKPRKHEQRLLRNVGVHTVVL---DLLQNPYD----------EKDDELMKELMCLAHEFLQNFCLGNQQNQVLLHNHL 1351
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMeviDLLGAPFTgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644261   1352 DLFLNP--------GILEakTVCAIFKDN--LALcNEVTDKVVQHFVHCIEIHGRHVAYLQFL 1404
Cdd:pfam01365  106 DWLQSQlgspslaeGTLD--VLTALLMDNpeLLL-NYIKECHIKSFISLLRKHGRDPRYLDFL 165
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 230-459 1.02e-130

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: 408.28  E-value: 1.02e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  230 MEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLY 309
Cdd:cd23277    1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  310 RFKHLATGHYLAAEAEIDVSAGAMSatsasghdlhlgdcskdsglscstmnSTINDKPKGKQYRLVSVPYSADIASVFVL 389
Cdd:cd23277   81 RFKHLATGQYLAAEVDPDPTPDPTR--------------------------SKLRGAPGKPVYCLVSVPHGNDIASIFEL 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  390 DATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSPVEV 459
Cdd:cd23277  135 DPTTLQRGDSLVPRSSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 8-235 1.70e-86

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


Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 282.08  E-value: 1.70e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261      8 SASFLHLGDIVSLYAEGSVCGFLSTLGLVDDRTVVCPEAGDLSCPPKKFRDCLIKICPMNRYSAQKQFWKAakQSASSNT 87
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSA--GNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261     88 DPnLLKRLHHAAEIEKKQNetenkkllgtsIQYGRaVVQLLHLKSNKYLTVNKRLPSLLEKNAMRVYLDANGN-EGSWFY 166
Cdd:pfam08709   79 NS-LTDALKHASNIEGHQN-----------LQYGS-AILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWFI 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24644261    167 IKPFYKLRSIGDYVVVGDKVILSPVNAdQQNLHVAANYELPDNPGcKEVNVLNSSTSWKISLFMEHKEN 235
Cdd:pfam08709  146 ITPAYKQRSEGDNVCVGDEVILVPVSA-PIFLHTTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 495-696 7.18e-78

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: 256.74  E-value: 7.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261    495 LLQDIVYFIAGMENEQ-NKTKALEFTIKNPIRDRQKLLREQYILKQLFK---ILQGPFQqhtagdGPFLRLDELSDPKNS 570
Cdd:pfam01365    1 LLRDLIFFFAGPEEEElHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT------GALLFAEDLGEEKNA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261    571 PYKNIFRLCYRILRLSQQDYRKNQEYIAKHFGLMQKQIGYDILAE---DTITALLHNNRKLLEKHITAAEIETFVGLVRK 647
Cdd:pfam01365   75 PWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRK 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 24644261    648 nmHNWDSRFLDYLSDLCVSNRKAIAVTQELICKSVLSdkNKDILIETQV 696
Cdd:pfam01365  155 --HGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 238-452 1.60e-69

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: 232.25  E-value: 1.60e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261    238 HILKGGDVVRLFHAEQEKFLTMDEYKKQYHvFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLYRFKHLATG 317
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261    318 HYLAAEAEIdvsagamsatsasghdlhlgdcskdsglsCSTMNSTINDKPKGKQYRLVSVPYSADIASVFVLDATTMARP 397
Cdd:pfam02815   80 RYLHSHEEQ-----------------------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGS 130

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24644261    398 DSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALI 452
Cdd:pfam02815  131 DRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 2029-2138 5.34e-31

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


Pssm-ID: 462482  Cd Length: 98  Bit Score: 118.40  E-value: 5.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2029 NKVLVMQPILRFLQLLCENHNPDMQNLLRNQNNKTNNN-LVSETLMFLDCICGSttgglgllglyINEHNVALINQTLEA 2107
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYnLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 24644261   2108 LTEYCQGPCHENQNCIatHESNGLDIITALI 2138
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2363-2682 7.65e-13

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


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 70.76  E-value: 7.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2363 LFNCVVVINMIV-AFFYPFDNTVPELSSHISLLFWIITIFSLVivlalpresgirtFIGSVILRFIFllgpestlcllgv 2441
Cdd:pfam00520    3 YFELFILLLILLnTIFLALETYFQPEEPLTTVLEILDYVFTGI-------------FTLEMLLKIIA------------- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2442 vtvtlksvhivsiMGNKGTLEKQLIKIITDFQLLYHCIYIAFCFCGLI----FHPFFYSLLLFDVVYREETLVNVIRSVT 2517
Cdd:pfam00520   57 -------------AGFKKRYFRSPWNILDFVVVLPSLISLVLSSVGSLsglrVLRLLRLLRLLRLIRRLEGLRTLVNSLI 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2518 RNGRSIVLTAVLALILVYLFSIIGYMFFKDDFLVSVDfeeqdnapppsvpltlsvpvsgdscsapddlgncqaakevapp 2597
Cdd:pfam00520  124 RSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWEN------------------------------------------- 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2598 saggGEVKERSCDSLVMCIVTTLNqgLRNGGGIGDILRAPSSKEGLFVArVIYDLLFFFIVIIIVLNLIFGVIIDTFADL 2677
Cdd:pfam00520  161 ----PDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFLLLNLFIAVIIDNFQEL 233


                   ....*
gi 24644261   2678 RSEKQ 2682
Cdd:pfam00520  234 TERTE 238
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1285-1404 1.03e-05

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: 48.73  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   1285 SVVKPRKHEQRLLRNVGVHTVVL---DLLQNPYD----------EKDDELMKELMCLAHEFLQNFCLGNQQNQVLLHNHL 1351
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMeviDLLGAPFTgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644261   1352 DLFLNP--------GILEakTVCAIFKDN--LALcNEVTDKVVQHFVHCIEIHGRHVAYLQFL 1404
Cdd:pfam01365  106 DWLQSQlgspslaeGTLD--VLTALLMDNpeLLL-NYIKECHIKSFISLLRKHGRDPRYLDFL 165
glyco_rpt_poly TIGR04370
oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic ...
 2348-2537 9.14e-05

oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic proteins, with few highly conserved residues, all may act to polymerize the oligosaccharide repeat units of surface polysaccharides, including O-antigen in Gram-negative bacteria such as Leptospira (assign gene symbol wzy) and capsular polysaccharide in Gram-positive bacteria such as Streptococcus. O-antigen biosynthesis enzymes produce a repeat unit, usually an oligosaccharide, which itself is polymerized. O-antigen polymerase, usually designated Wzy. This family bears homology to the O-antigen ligase WaaL, but known examples of WaaL fall outside the bounds defined here. This model is much broader than pfam14296. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 275163 [Multi-domain]  Cd Length: 392  Bit Score: 47.54  E-value: 9.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2348 LLFWISSYMSLWsnILFNCVVVINMIVAFFYPFDNTVPELSSHISLLFWIITIFSLVIVLAL---------PRESGIRTF 2418
Cdd:TIGR04370    1 SYKKKKDILSPI--ILFSLIWLLIFLLSLLLLSYLSFLYPLSDYTYLIIILGILIFIFGSLFlslslkskkRKTRKKKLS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2419 IGSVILRFIFLLGPESTLCLLGVVTVTLKSVHIVSIMGNKG----TLEKQLIKIITDFQLLYHCIYIAFCFCGLIFHPFF 2494
Cdd:TIGR04370   79 KISISLIILFLFFLILILLLLIILLLLLYIISLIGILGILSllgsALGYLALSGSTFLSGLIILLYILIILLLLLFLLLL 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 24644261   2495 Y-------SLLLFdvvyreetLVNVIRSVTRNGRSIVLTAVLALILVYLF 2537
Cdd:TIGR04370  159 LkkkrkklLLLLI--------LLALLISLLTGSRTGLILLILSLLFIYYL 200
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
177-229 2.70e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.17  E-value: 2.70e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 24644261     177 GDYVVVGDKVILSPVNADQqNLHVAANYELPDNPGCKEVN-----VLNSSTSWKISLF 229
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGR-YLHSHDEKLPPWGDGQQEVTgygnpAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
237-293 5.98e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.02  E-value: 5.98e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644261     237 EHILKGGDVVRLFHAEQEKFLT-MDEY-----KKQYHVFLRTTGRTSATaatsskALWEIEVV 293
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHsHDEKlppwgDGQQEVTGYGNPAIDAN------TLWLIEPV 57
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 230-459 1.02e-130

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: 408.28  E-value: 1.02e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  230 MEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLY 309
Cdd:cd23277    1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  310 RFKHLATGHYLAAEAEIDVSAGAMSatsasghdlhlgdcskdsglscstmnSTINDKPKGKQYRLVSVPYSADIASVFVL 389
Cdd:cd23277   81 RFKHLATGQYLAAEVDPDPTPDPTR--------------------------SKLRGAPGKPVYCLVSVPHGNDIASIFEL 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  390 DATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSPVEV 459
Cdd:cd23277  135 DPTTLQRGDSLVPRSSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 230-464 3.36e-103

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: 330.11  E-value: 3.36e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  230 MEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLY 309
Cdd:cd23287    1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  310 RFKHLATGHYLAAEAEIDVSAGAmsatsasghdlhlGDCSKDSGLSCSTMNSTINDKPKGKQYRLVSVPYSADIASVFVL 389
Cdd:cd23287   81 RFKHLATGHYLAAEVDPDFEEEC-------------LEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFEL 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24644261  390 DATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSPVEVRDLDF 464
Cdd:cd23287  148 DPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 224-459 9.58e-95

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: 306.20  E-value: 9.58e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  224 WKISLFMEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAG 303
Cdd:cd23288    1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  304 DWNSLYRFKHLATGHYLAAEAEIDVsagamsatsasghdlhlgdcsKDSGLSCSTMNSTINDKPKGKQ-------YRLVS 376
Cdd:cd23288   81 QWNSLFRFKHLATGNYLAAEVNPDY---------------------RDAQNEGKAVNDGDSPTSKKKRqaaekimYTLVS 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  377 VPYSADIASVFVLDATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSP 456
Cdd:cd23288  140 VPHGNDIASLFELDATTLQRADCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPL 219


                 ...
gi 24644261  457 VEV 459
Cdd:cd23288  220 SEV 222
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 230-459 7.10e-89

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: 288.87  E-value: 7.10e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  230 MEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLY 309
Cdd:cd23289    1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  310 RFKHLATGHYLAAEAEIDVSAGAMSATSASghdlhlgdcskdSGLSCSTMNSTINDKPKgkqYRLVSVPYSADIASVFVL 389
Cdd:cd23289   81 RFKHLATGNYLAAEENPSYKGDASDPKAAG------------MGAQSRTGRRNAGEKIK---YCLVAVPHGNDIASLFEL 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  390 DATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSPVEV 459
Cdd:cd23289  146 DPTTLQKTDSFVPRNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 8-235 1.70e-86

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


Pssm-ID: 462572 [Multi-domain]  Cd Length: 212  Bit Score: 282.08  E-value: 1.70e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261      8 SASFLHLGDIVSLYAEGSVCGFLSTLGLVDDRTVVCPEAGDLSCPPKKFRDCLIKICPMNRYSAQKQFWKAakQSASSNT 87
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSA--GNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261     88 DPnLLKRLHHAAEIEKKQNetenkkllgtsIQYGRaVVQLLHLKSNKYLTVNKRLPSLLEKNAMRVYLDANGN-EGSWFY 166
Cdd:pfam08709   79 NS-LTDALKHASNIEGHQN-----------LQYGS-AILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWFI 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24644261    167 IKPFYKLRSIGDYVVVGDKVILSPVNAdQQNLHVAANYELPDNPGcKEVNVLNSSTSWKISLFMEHKEN 235
Cdd:pfam08709  146 ITPAYKQRSEGDNVCVGDEVILVPVSA-PIFLHTTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 495-696 7.18e-78

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: 256.74  E-value: 7.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261    495 LLQDIVYFIAGMENEQ-NKTKALEFTIKNPIRDRQKLLREQYILKQLFK---ILQGPFQqhtagdGPFLRLDELSDPKNS 570
Cdd:pfam01365    1 LLRDLIFFFAGPEEEElHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT------GALLFAEDLGEEKNA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261    571 PYKNIFRLCYRILRLSQQDYRKNQEYIAKHFGLMQKQIGYDILAE---DTITALLHNNRKLLEKHITAAEIETFVGLVRK 647
Cdd:pfam01365   75 PWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRK 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 24644261    648 nmHNWDSRFLDYLSDLCVSNRKAIAVTQELICKSVLSdkNKDILIETQV 696
Cdd:pfam01365  155 --HGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 238-452 1.60e-69

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: 232.25  E-value: 1.60e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261    238 HILKGGDVVRLFHAEQEKFLTMDEYKKQYHvFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLYRFKHLATG 317
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261    318 HYLAAEAEIdvsagamsatsasghdlhlgdcskdsglsCSTMNSTINDKPKGKQYRLVSVPYSADIASVFVLDATTMARP 397
Cdd:pfam02815   80 RYLHSHEEQ-----------------------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGS 130

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24644261    398 DSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALI 452
Cdd:pfam02815  131 DRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 2029-2138 5.34e-31

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


Pssm-ID: 462482  Cd Length: 98  Bit Score: 118.40  E-value: 5.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2029 NKVLVMQPILRFLQLLCENHNPDMQNLLRNQNNKTNNN-LVSETLMFLDCICGSttgglgllglyINEHNVALINQTLEA 2107
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYnLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 24644261   2108 LTEYCQGPCHENQNCIatHESNGLDIITALI 2138
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 234-459 2.14e-28

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: 114.79  E-value: 2.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  234 ENQEHILKGGDVVRLFHAEQEKFLTMD------EYKKQYHV---FLRTTGRTSATAATSSKALWEIEVVqHDSCRGGAGD 304
Cdd:cd23280    1 KENENFLKGGDVVRLFHKELEAYLSAEgsfvdeVLTEDVHLrvrPVDDRKPRTLFPPTSGDTFWQIEKE-DTPLKGGVIK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  305 WNSLYRFKHLATGHYLAAEaeidvsagamsatsasghdlhlgdcskdsglscstmnstindkPKGKQYRLVSVPYSADIA 384
Cdd:cd23280   80 WGDQCRLRHLPTGKYLAVD-------------------------------------------DKTGNGKVVLTSDPSDPS 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  385 SVFVLDATTMARPDSlVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSM---------VCCSPIKEDKEAFALIPVS 455
Cdd:cd23280  117 TVFRLHPVTKETSEE-VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGLswdgaklrkVSLSLERQDDDAFTIQEVD 195


                 ....
gi 24644261  456 PVEV 459
Cdd:cd23280  196 PDLV 199
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 243-457 9.95e-20

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: 88.98  E-value: 9.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  243 GDVVRLFHAEQEKFLTMDEY-----KKQYHVFLRTTGRTsataaTSSKALWEIEVVQHDScrGGAGDWNSLYRFKHLATG 317
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHRKnyptgSGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  318 HYLAaeaeidvsagamsatsasghdLHLGDCSkdsglscstmnstindkPKGKQYRLVSVPYSADIASVFVLDAT-TMAR 396
Cdd:cd23263   74 KYLS---------------------SEEGKKS-----------------PKSNHQEVLCLTDNPDKSSLFKFEPIgSTKY 115

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24644261  397 PDSLVPQSSYVRLQHICSNTWVHatSIPIDADDDKPVMSMVCCSpiKEDKEAFALIPVSPV 457
Cdd:cd23263  116 KQKYVKKDSYFRLKHVNTNFWLH--SHEKKFNINNKTQQEVICH--GEREEVFKLWKAELI 172
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2363-2682 7.65e-13

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


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 70.76  E-value: 7.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2363 LFNCVVVINMIV-AFFYPFDNTVPELSSHISLLFWIITIFSLVivlalpresgirtFIGSVILRFIFllgpestlcllgv 2441
Cdd:pfam00520    3 YFELFILLLILLnTIFLALETYFQPEEPLTTVLEILDYVFTGI-------------FTLEMLLKIIA------------- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2442 vtvtlksvhivsiMGNKGTLEKQLIKIITDFQLLYHCIYIAFCFCGLI----FHPFFYSLLLFDVVYREETLVNVIRSVT 2517
Cdd:pfam00520   57 -------------AGFKKRYFRSPWNILDFVVVLPSLISLVLSSVGSLsglrVLRLLRLLRLLRLIRRLEGLRTLVNSLI 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2518 RNGRSIVLTAVLALILVYLFSIIGYMFFKDDFLVSVDfeeqdnapppsvpltlsvpvsgdscsapddlgncqaakevapp 2597
Cdd:pfam00520  124 RSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWEN------------------------------------------- 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2598 saggGEVKERSCDSLVMCIVTTLNqgLRNGGGIGDILRAPSSKEGLFVArVIYDLLFFFIVIIIVLNLIFGVIIDTFADL 2677
Cdd:pfam00520  161 ----PDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFLLLNLFIAVIIDNFQEL 233


                   ....*
gi 24644261   2678 RSEKQ 2682
Cdd:pfam00520  234 TERTE 238
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 240-321 4.68e-06

MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, also called RYR-3, or brain ryanodine receptor-calcium release channel, or brain-type ryanodine receptor, or type 3 ryanodine receptor, is a calcium channel that plays a role in cellular calcium signaling. It mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. It also mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. RYR-3 forms homotetramer and also forms heterotetramer with RYR-2. RYR-3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467763 [Multi-domain]  Cd Length: 187  Bit Score: 49.52  E-value: 4.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  240 LKGGDVVRLFHAEQEKfLTMDEYKkQYHVFLRTTGRTSATAATSSKALWEIEVVQhDSCRGGAGDWNSLYRFKHLATGHY 319
Cdd:cd23292    3 LLGGHVVRLFHGHDEC-LTIPSTD-QSDEQHRVVNYEAGGAGTRARSLWRLEPLR-ISWSGSHIRWGQTFRLRHLTTGHY 79


                 ..
gi 24644261  320 LA 321
Cdd:cd23292   80 LA 81
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1285-1404 1.03e-05

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: 48.73  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   1285 SVVKPRKHEQRLLRNVGVHTVVL---DLLQNPYD----------EKDDELMKELMCLAHEFLQNFCLGNQQNQVLLHNHL 1351
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMeviDLLGAPFTgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644261   1352 DLFLNP--------GILEakTVCAIFKDN--LALcNEVTDKVVQHFVHCIEIHGRHVAYLQFL 1404
Cdd:pfam01365  106 DWLQSQlgspslaeGTLD--VLTALLMDNpeLLL-NYIKECHIKSFISLLRKHGRDPRYLDFL 165
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 234-325 4.02e-05

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: 47.19  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  234 ENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHvfLRTTGRTSATAATSSKALWEIEVVQhDSCRGGAGDWNSLYRFKH 313
Cdd:cd23290    2 CCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQ--RRLVYYEGGAVCTHARSLWRLEPLR-ISWSGSHLRWGQPLRIRH 78

                         90
                 ....*....|..
gi 24644261  314 LATGHYLAAEAE 325
Cdd:cd23290   79 VTTGRYLALTED 90
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 242-328 4.28e-05

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: 46.53  E-value: 4.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  242 GGDVVRLFHAEQEKFLTMDE--YKKQYHvflRTTGRTSATAATSSKALWEIEVVQHDSCrGGAGDWNSLYRFKHLATGHY 319
Cdd:cd23278    1 GGDVLRLFHGHMDECLTIPAagSKEDQH---RTVIYEGGAVSTHARSLWRLELLRIKWS-GSHIGWGQPFRLRHVTTGRY 76


                 ....*....
gi 24644261  320 LAAEAEIDV 328
Cdd:cd23278   77 LALTEDRGL 85
glyco_rpt_poly TIGR04370
oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic ...
 2348-2537 9.14e-05

oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic proteins, with few highly conserved residues, all may act to polymerize the oligosaccharide repeat units of surface polysaccharides, including O-antigen in Gram-negative bacteria such as Leptospira (assign gene symbol wzy) and capsular polysaccharide in Gram-positive bacteria such as Streptococcus. O-antigen biosynthesis enzymes produce a repeat unit, usually an oligosaccharide, which itself is polymerized. O-antigen polymerase, usually designated Wzy. This family bears homology to the O-antigen ligase WaaL, but known examples of WaaL fall outside the bounds defined here. This model is much broader than pfam14296. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 275163 [Multi-domain]  Cd Length: 392  Bit Score: 47.54  E-value: 9.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2348 LLFWISSYMSLWsnILFNCVVVINMIVAFFYPFDNTVPELSSHISLLFWIITIFSLVIVLAL---------PRESGIRTF 2418
Cdd:TIGR04370    1 SYKKKKDILSPI--ILFSLIWLLIFLLSLLLLSYLSFLYPLSDYTYLIIILGILIFIFGSLFlslslkskkRKTRKKKLS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261   2419 IGSVILRFIFLLGPESTLCLLGVVTVTLKSVHIVSIMGNKG----TLEKQLIKIITDFQLLYHCIYIAFCFCGLIFHPFF 2494
Cdd:TIGR04370   79 KISISLIILFLFFLILILLLLIILLLLLYIISLIGILGILSllgsALGYLALSGSTFLSGLIILLYILIILLLLLFLLLL 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 24644261   2495 Y-------SLLLFdvvyreetLVNVIRSVTRNGRSIVLTAVLALILVYLF 2537
Cdd:TIGR04370  159 LkkkrkklLLLLI--------LLALLISLLTGSRTGLILLILSLLFIYYL 200
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
177-229 2.70e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.17  E-value: 2.70e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 24644261     177 GDYVVVGDKVILSPVNADQqNLHVAANYELPDNPGCKEVN-----VLNSSTSWKISLF 229
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGR-YLHSHDEKLPPWGDGQQEVTgygnpAIDANTLWLIEPV 57
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 243-320 4.31e-04

MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein mannosyltransferase (PMT); The PMT (EC 2.4.1.109) family includes mammalian protein O-mannosyl-transferases (POMT1 and POMT2) and yeast PMT1-7. PMTs are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467747 [Multi-domain]  Cd Length: 185  Bit Score: 43.86  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24644261  243 GDVVRLFHAEQEKFLTMDEYK---KQYHvfLRTTGRTSATAATSSKALWEIEVVQhDSCRGGAGDWNSL---YRFKHLAT 316
Cdd:cd23276   69 GDEVRLLHKETNRYLRTHDAAapvTSKH--KEVSAYPDENEDGDDNDLWVVEIVK-DEGKLEDKRIKPLttrFRLRNKKT 145


                 ....
gi 24644261  317 GHYL 320
Cdd:cd23276  146 GCYL 149
beta-trefoil_Ricin_EndoBetaGal-like cd23432
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1, ...
 275-341 4.71e-04

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1,4-Gal-releasing endo-beta-galactosidase (Endo-beta-Gal(GnGa)) and similar proteins; Endo-beta-Gal(GnGa) can release disaccharide GlcNAc-alpha-1,4Gal from O-glycans expressed in the gastric gland mucous cell-type mucin. It contains a C-terminal ricin B-type lectin domain with a 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. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467310  Cd Length: 127  Bit Score: 42.33  E-value: 4.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24644261  275 RTSATAATSSKALWEIEVVQhdscrggagdwNSLYRFKHLATGHYLAAEAEID-VSAGAMSATSASGH 341
Cdd:cd23432   22 KYGTPPEDDTSAQWIIEDVG-----------DGYVRIKNRATGHYLHIENNTGyLESGPIPPGWWSAQ 78
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
237-293 5.98e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.02  E-value: 5.98e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24644261     237 EHILKGGDVVRLFHAEQEKFLT-MDEY-----KKQYHVFLRTTGRTSATaatsskALWEIEVV 293
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHsHDEKlppwgDGQQEVTGYGNPAIDAN------TLWLIEPV 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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