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Conserved domains on  [gi|44888998|sp|P29993|]
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RecName: Full=Inositol 1,4,5-trisphosphate receptor; AltName: Full=InsP3 receptor; Short=IP3R; Short=InsP3R

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 ...
 231-460 1.03e-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: 1.03e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  231 MEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLY 310
Cdd:cd23277    1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  311 RFKHLATGHYLAAEAEIDVSAGAMSatsasghdlhlgdcskdsglscstmnSTINDKPKGKQYRLVSVPYSADIASVFVL 390
Cdd:cd23277   81 RFKHLATGQYLAAEVDPDPTPDPTR--------------------------SKLRGAPGKPVYCLVSVPHGNDIASIFEL 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  391 DATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSPVEV 460
Cdd:cd23277  135 DPTTLQRGDSLVPRSSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 8-236 1.69e-85

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: 279.00  E-value: 1.69e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998      8 SASFLHLGDIVSLYAEGSVCGFLSTLGLVDDRTVVCPEAGDLSCPPKKFRDCLIKICPMNRYSAQKQFWKAakQSASSNT 87
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSA--GNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998     88 DPnLLKRLHHAAEIEKKQNetenkkllgtsIQYGRaVVQLLHLKSNKYLTVNKRLPSLLEKNAMRVYLDANGN-EGSWFY 166
Cdd:pfam08709   79 NS-LTDALKHASNIEGHQN-----------LQYGS-AILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWFI 145

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    167 IKPFYKLRSIGDyVVVVGDKVILSPVNAdQQNLHVAANYELPDNPGcKEVNVLNSSTSWKISLFMEHKEN 236
Cdd:pfam08709  146 ITPAYKQRSEGD-NVCVGDEVILVPVSA-PIFLHTTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 496-697 6.93e-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: 6.93e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    496 LLQDIVYFIAGMENEQ-NKTKALEFTIKNPIRDRQKLLREQYILKQLFK---ILQGPFQehtagdGPFLRLDELSDPKNS 571
Cdd:pfam01365    1 LLRDLIFFFAGPEEEElHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT------GALLFAEDLGEEKNA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    572 PYKNIFRLCYRILRLSQQDYRKNQEYIAKHFGLMQKQIGYDILAE---DTITALLHNNRKLLEKHITAAEIETFVGLVRK 648
Cdd:pfam01365   75 PWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRK 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 44888998    649 nmHNWDSRFLDYLSDLCVSNRKAIAVTQELICKSVLSdkNKDILIETQV 697
Cdd:pfam01365  155 --HGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 2039-2148 1.49e-30

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: 117.24  E-value: 1.49e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2039 NKVLVMQPILRFLQLLCENHNPDMQNLLRNQNNKTNNN-LVSETLMFLDCICGSttgglgllglyINEHNLALINQTLEA 2117
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYnLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 44888998   2118 LTEYCQGPCHENQNCIatHESNGLDIITALI 2148
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2373-2692 6.86e-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: 6.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2373 LFNCVVVINMIV-AFFYPFDNTVPELSSHISLLFWIITIFSLVivlalpresgirtFIGSVILRFIFllgpestlcllgv 2451
Cdd:pfam00520    3 YFELFILLLILLnTIFLALETYFQPEEPLTTVLEILDYVFTGI-------------FTLEMLLKIIA------------- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2452 vtvtlksvhivsiMGNKGTLEKQLIKIITDFQLLYHCIYIAFCFCGLI----FHPFFYSLLLFDVVYREETLVNVIRSVT 2527
Cdd:pfam00520   57 -------------AGFKKRYFRSPWNILDFVVVLPSLISLVLSSVGSLsglrVLRLLRLLRLLRLIRRLEGLRTLVNSLI 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2528 RNGRSIVLTAVLALILVYLFSIIGYMFFKDDFLVSVDfeeqdnapppsvpltlsvpvsgdscsapddlgncqaakevapp 2607
Cdd:pfam00520  124 RSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWEN------------------------------------------- 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2608 saggGEVKERSCDSLVMCIVTTLNqgLRNGGGIGDILRAPSSKEGLFVArVIYDLLFFFIVIIIVLNLIFGVIIDTFADL 2687
Cdd:pfam00520  161 ----PDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFLLLNLFIAVIIDNFQEL 233


                   ....*
gi 44888998   2688 RSEKQ 2692
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 ...
 1295-1414 1.04e-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: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   1295 SVVKPRKHEQRLLRNVGVHTVVL---DLLQNPYD----------EKDDELMKELMCLAHEFLQNFCLGNQQNQVLLHNHL 1361
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMeviDLLGAPFTgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 44888998   1362 DLFLNP--------GILEakTVCAIFKDN--LALcNEVTDKVVQHFVHCIEIHGRHVAYLQFL 1414
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 ...
 231-460 1.03e-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: 1.03e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  231 MEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLY 310
Cdd:cd23277    1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  311 RFKHLATGHYLAAEAEIDVSAGAMSatsasghdlhlgdcskdsglscstmnSTINDKPKGKQYRLVSVPYSADIASVFVL 390
Cdd:cd23277   81 RFKHLATGQYLAAEVDPDPTPDPTR--------------------------SKLRGAPGKPVYCLVSVPHGNDIASIFEL 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  391 DATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSPVEV 460
Cdd:cd23277  135 DPTTLQRGDSLVPRSSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 8-236 1.69e-85

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: 279.00  E-value: 1.69e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998      8 SASFLHLGDIVSLYAEGSVCGFLSTLGLVDDRTVVCPEAGDLSCPPKKFRDCLIKICPMNRYSAQKQFWKAakQSASSNT 87
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSA--GNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998     88 DPnLLKRLHHAAEIEKKQNetenkkllgtsIQYGRaVVQLLHLKSNKYLTVNKRLPSLLEKNAMRVYLDANGN-EGSWFY 166
Cdd:pfam08709   79 NS-LTDALKHASNIEGHQN-----------LQYGS-AILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWFI 145

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    167 IKPFYKLRSIGDyVVVVGDKVILSPVNAdQQNLHVAANYELPDNPGcKEVNVLNSSTSWKISLFMEHKEN 236
Cdd:pfam08709  146 ITPAYKQRSEGD-NVCVGDEVILVPVSA-PIFLHTTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 496-697 6.93e-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: 6.93e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    496 LLQDIVYFIAGMENEQ-NKTKALEFTIKNPIRDRQKLLREQYILKQLFK---ILQGPFQehtagdGPFLRLDELSDPKNS 571
Cdd:pfam01365    1 LLRDLIFFFAGPEEEElHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT------GALLFAEDLGEEKNA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    572 PYKNIFRLCYRILRLSQQDYRKNQEYIAKHFGLMQKQIGYDILAE---DTITALLHNNRKLLEKHITAAEIETFVGLVRK 648
Cdd:pfam01365   75 PWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRK 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 44888998    649 nmHNWDSRFLDYLSDLCVSNRKAIAVTQELICKSVLSdkNKDILIETQV 697
Cdd:pfam01365  155 --HGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 239-453 1.49e-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: 1.49e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    239 HILKGGDVVRLFHAEQEKFLTMDEYKKQYHvFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLYRFKHLATG 318
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    319 HYLAAEAEIdvsagamsatsasghdlhlgdcskdsglsCSTMNSTINDKPKGKQYRLVSVPYSADIASVFVLDATTMARP 398
Cdd:pfam02815   80 RYLHSHEEQ-----------------------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGS 130

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 44888998    399 DSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALI 453
Cdd:pfam02815  131 DRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 2039-2148 1.49e-30

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: 117.24  E-value: 1.49e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2039 NKVLVMQPILRFLQLLCENHNPDMQNLLRNQNNKTNNN-LVSETLMFLDCICGSttgglgllglyINEHNLALINQTLEA 2117
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYnLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 44888998   2118 LTEYCQGPCHENQNCIatHESNGLDIITALI 2148
Cdd:pfam08454   70 LTEFIQGPCIENQIAL--CESKFLEIANDLL 98
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2373-2692 6.86e-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: 6.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2373 LFNCVVVINMIV-AFFYPFDNTVPELSSHISLLFWIITIFSLVivlalpresgirtFIGSVILRFIFllgpestlcllgv 2451
Cdd:pfam00520    3 YFELFILLLILLnTIFLALETYFQPEEPLTTVLEILDYVFTGI-------------FTLEMLLKIIA------------- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2452 vtvtlksvhivsiMGNKGTLEKQLIKIITDFQLLYHCIYIAFCFCGLI----FHPFFYSLLLFDVVYREETLVNVIRSVT 2527
Cdd:pfam00520   57 -------------AGFKKRYFRSPWNILDFVVVLPSLISLVLSSVGSLsglrVLRLLRLLRLLRLIRRLEGLRTLVNSLI 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2528 RNGRSIVLTAVLALILVYLFSIIGYMFFKDDFLVSVDfeeqdnapppsvpltlsvpvsgdscsapddlgncqaakevapp 2607
Cdd:pfam00520  124 RSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWEN------------------------------------------- 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2608 saggGEVKERSCDSLVMCIVTTLNqgLRNGGGIGDILRAPSSKEGLFVArVIYDLLFFFIVIIIVLNLIFGVIIDTFADL 2687
Cdd:pfam00520  161 ----PDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFLLLNLFIAVIIDNFQEL 233


                   ....*
gi 44888998   2688 RSEKQ 2692
Cdd:pfam00520  234 TERTE 238
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1295-1414 1.04e-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: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   1295 SVVKPRKHEQRLLRNVGVHTVVL---DLLQNPYD----------EKDDELMKELMCLAHEFLQNFCLGNQQNQVLLHNHL 1361
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMeviDLLGAPFTgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 44888998   1362 DLFLNP--------GILEakTVCAIFKDN--LALcNEVTDKVVQHFVHCIEIHGRHVAYLQFL 1414
Cdd:pfam01365  106 DWLQSQlgspslaeGTLD--VLTALLMDNpeLLL-NYIKECHIKSFISLLRKHGRDPRYLDFL 165
glyco_rpt_poly TIGR04370
oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic ...
 2358-2547 8.48e-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: 8.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2358 LLFWISSYMSLWsnILFNCVVVINMIVAFFYPFDNTVPELSSHISLLFWIITIFSLVIVLAL---------PRESGIRTF 2428
Cdd:TIGR04370    1 SYKKKKDILSPI--ILFSLIWLLIFLLSLLLLSYLSFLYPLSDYTYLIIILGILIFIFGSLFlslslkskkRKTRKKKLS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2429 IGSVILRFIFLLGPESTLCLLGVVTVTLKSVHIVSIMGNKG----TLEKQLIKIITDFQLLYHCIYIAFCFCGLIFHPFF 2504
Cdd:TIGR04370   79 KISISLIILFLFFLILILLLLIILLLLLYIISLIGILGILSllgsALGYLALSGSTFLSGLIILLYILIILLLLLFLLLL 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 44888998   2505 Y-------SLLLFdvvyreetLVNVIRSVTRNGRSIVLTAVLALILVYLF 2547
Cdd:TIGR04370  159 LkkkrkklLLLLI--------LLALLISLLTGSRTGLILLILSLLFIYYL 200
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
178-230 3.08e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.79  E-value: 3.08e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 44888998     178 DYVVVVGDKVILSPVNADQqNLHVAANYELPDNPGCKEVN-----VLNSSTSWKISLF 230
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGR-YLHSHDEKLPPWGDGQQEVTgygnpAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
238-294 6.00e-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: 6.00e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 44888998     238 EHILKGGDVVRLFHAEQEKFLT-MDEY-----KKQYHVFLRTTGRTSATaatsskALWEIEVV 294
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 ...
 231-460 1.03e-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: 1.03e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  231 MEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLY 310
Cdd:cd23277    1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  311 RFKHLATGHYLAAEAEIDVSAGAMSatsasghdlhlgdcskdsglscstmnSTINDKPKGKQYRLVSVPYSADIASVFVL 390
Cdd:cd23277   81 RFKHLATGQYLAAEVDPDPTPDPTR--------------------------SKLRGAPGKPVYCLVSVPHGNDIASIFEL 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  391 DATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSPVEV 460
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) ...
 231-465 3.37e-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: 3.37e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  231 MEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLY 310
Cdd:cd23287    1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  311 RFKHLATGHYLAAEAEIDVSAGAmsatsasghdlhlGDCSKDSGLSCSTMNSTINDKPKGKQYRLVSVPYSADIASVFVL 390
Cdd:cd23287   81 RFKHLATGHYLAAEVDPDFEEEC-------------LEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFEL 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 44888998  391 DATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSPVEVRDLDF 465
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) ...
 225-460 9.62e-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: 9.62e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  225 WKISLFMEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAG 304
Cdd:cd23288    1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  305 DWNSLYRFKHLATGHYLAAEAEIDVsagamsatsasghdlhlgdcsKDSGLSCSTMNSTINDKPKGKQ-------YRLVS 377
Cdd:cd23288   81 QWNSLFRFKHLATGNYLAAEVNPDY---------------------RDAQNEGKAVNDGDSPTSKKKRqaaekimYTLVS 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  378 VPYSADIASVFVLDATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSP 457
Cdd:cd23288  140 VPHGNDIASLFELDATTLQRADCLVPRNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPL 219


                 ...
gi 44888998  458 VEV 460
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) ...
 231-460 7.13e-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: 7.13e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  231 MEHKENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHVFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLY 310
Cdd:cd23289    1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  311 RFKHLATGHYLAAEAEIDVSAGAMSATSASghdlhlgdcskdSGLSCSTMNSTINDKPKgkqYRLVSVPYSADIASVFVL 390
Cdd:cd23289   81 RFKHLATGNYLAAEENPSYKGDASDPKAAG------------MGAQSRTGRRNAGEKIK---YCLVAVPHGNDIASLFEL 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  391 DATTMARPDSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALIPVSPVEV 460
Cdd:cd23289  146 DPTTLQKTDSFVPRNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 8-236 1.69e-85

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: 279.00  E-value: 1.69e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998      8 SASFLHLGDIVSLYAEGSVCGFLSTLGLVDDRTVVCPEAGDLSCPPKKFRDCLIKICPMNRYSAQKQFWKAakQSASSNT 87
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVNGFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSA--GNRSPNG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998     88 DPnLLKRLHHAAEIEKKQNetenkkllgtsIQYGRaVVQLLHLKSNKYLTVNKRLPSLLEKNAMRVYLDANGN-EGSWFY 166
Cdd:pfam08709   79 NS-LTDALKHASNIEGHQN-----------LQYGS-AILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgEGCWFI 145

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    167 IKPFYKLRSIGDyVVVVGDKVILSPVNAdQQNLHVAANYELPDNPGcKEVNVLNSSTSWKISLFMEHKEN 236
Cdd:pfam08709  146 ITPAYKQRSEGD-NVCVGDEVILVPVSA-PIFLHTTSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCEN 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 496-697 6.93e-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: 6.93e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    496 LLQDIVYFIAGMENEQ-NKTKALEFTIKNPIRDRQKLLREQYILKQLFK---ILQGPFQehtagdGPFLRLDELSDPKNS 571
Cdd:pfam01365    1 LLRDLIFFFAGPEEEElHEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT------GALLFAEDLGEEKNA 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    572 PYKNIFRLCYRILRLSQQDYRKNQEYIAKHFGLMQKQIGYDILAE---DTITALLHNNRKLLEKHITAAEIETFVGLVRK 648
Cdd:pfam01365   75 PWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISLLRK 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 44888998    649 nmHNWDSRFLDYLSDLCVSNRKAIAVTQELICKSVLSdkNKDILIETQV 697
Cdd:pfam01365  155 --HGRDPRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 239-453 1.49e-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: 1.49e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    239 HILKGGDVVRLFHAEQEKFLTMDEYKKQYHvFLRTTGRTSATAATSSKALWEIEVVQHDSCRGGAGDWNSLYRFKHLATG 318
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998    319 HYLAAEAEIdvsagamsatsasghdlhlgdcskdsglsCSTMNSTINDKPKGKQYRLVSVPYSADIASVFVLDATTMARP 398
Cdd:pfam02815   80 RYLHSHEEQ-----------------------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGS 130

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 44888998    399 DSLVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSMVCCSPIKEDKEAFALI 453
Cdd:pfam02815  131 DRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 2039-2148 1.49e-30

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: 117.24  E-value: 1.49e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2039 NKVLVMQPILRFLQLLCENHNPDMQNLLRNQNNKTNNN-LVSETLMFLDCICGSttgglgllglyINEHNLALINQTLEA 2117
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNNKNSYnLVEETVDLLKAYCKS-----------INEKNIELIIQCLDT 69

                           90       100       110
                   ....*....|....*....|....*....|.
gi 44888998   2118 LTEYCQGPCHENQNCIatHESNGLDIITALI 2148
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 ...
 235-460 1.86e-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: 1.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  235 ENQEHILKGGDVVRLFHAEQEKFLTMD------EYKKQYHV---FLRTTGRTSATAATSSKALWEIEVVqHDSCRGGAGD 305
Cdd:cd23280    1 KENENFLKGGDVVRLFHKELEAYLSAEgsfvdeVLTEDVHLrvrPVDDRKPRTLFPPTSGDTFWQIEKE-DTPLKGGVIK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  306 WNSLYRFKHLATGHYLAAEaeidvsagamsatsasghdlhlgdcskdsglscstmnstindkPKGKQYRLVSVPYSADIA 385
Cdd:cd23280   80 WGDQCRLRHLPTGKYLAVD-------------------------------------------DKTGNGKVVLTSDPSDPS 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  386 SVFVLDATTMARPDSlVPQSSYVRLQHICSNTWVHATSIPIDADDDKPVMSM---------VCCSPIKEDKEAFALIPVS 456
Cdd:cd23280  117 TVFRLHPVTKETSEE-VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGLswdgaklrkVSLSLERQDDDAFTIQEVD 195


                 ....
gi 44888998  457 PVEV 460
Cdd:cd23280  196 PDLV 199
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 244-458 8.98e-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: 8.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  244 GDVVRLFHAEQEKFLTMDEY-----KKQYHVFLRTTGRTsataaTSSKALWEIEVVQHDScrGGAGDWNSLYRFKHLATG 318
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHRKnyptgSGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  319 HYLAaeaeidvsagamsatsasghdLHLGDCSkdsglscstmnstindkPKGKQYRLVSVPYSADIASVFVLDAT-TMAR 397
Cdd:cd23263   74 KYLS---------------------SEEGKKS-----------------PKSNHQEVLCLTDNPDKSSLFKFEPIgSTKY 115

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 44888998  398 PDSLVPQSSYVRLQHICSNTWVHatSIPIDADDDKPVMSMVCCSpiKEDKEAFALIPVSPV 458
Cdd:cd23263  116 KQKYVKKDSYFRLKHVNTNFWLH--SHEKKFNINNKTQQEVICH--GEREEVFKLWKAELI 172
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2373-2692 6.86e-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: 6.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2373 LFNCVVVINMIV-AFFYPFDNTVPELSSHISLLFWIITIFSLVivlalpresgirtFIGSVILRFIFllgpestlcllgv 2451
Cdd:pfam00520    3 YFELFILLLILLnTIFLALETYFQPEEPLTTVLEILDYVFTGI-------------FTLEMLLKIIA------------- 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2452 vtvtlksvhivsiMGNKGTLEKQLIKIITDFQLLYHCIYIAFCFCGLI----FHPFFYSLLLFDVVYREETLVNVIRSVT 2527
Cdd:pfam00520   57 -------------AGFKKRYFRSPWNILDFVVVLPSLISLVLSSVGSLsglrVLRLLRLLRLLRLIRRLEGLRTLVNSLI 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2528 RNGRSIVLTAVLALILVYLFSIIGYMFFKDDFLVSVDfeeqdnapppsvpltlsvpvsgdscsapddlgncqaakevapp 2607
Cdd:pfam00520  124 RSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWEN------------------------------------------- 160

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2608 saggGEVKERSCDSLVMCIVTTLNqgLRNGGGIGDILRAPSSKEGLFVArVIYDLLFFFIVIIIVLNLIFGVIIDTFADL 2687
Cdd:pfam00520  161 ----PDNGRTNFDNFPNAFLWLFQ--TMTTEGWGDIMYDTIDGKGEFWA-YIYFVSFIILGGFLLLNLFIAVIIDNFQEL 233


                   ....*
gi 44888998   2688 RSEKQ 2692
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, ...
 241-322 4.70e-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: 4.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  241 LKGGDVVRLFHAEQEKfLTMDEYKkQYHVFLRTTGRTSATAATSSKALWEIEVVQhDSCRGGAGDWNSLYRFKHLATGHY 320
Cdd:cd23292    3 LLGGHVVRLFHGHDEC-LTIPSTD-QSDEQHRVVNYEAGGAGTRARSLWRLEPLR-ISWSGSHIRWGQTFRLRHLTTGHY 79


                 ..
gi 44888998  321 LA 322
Cdd:cd23292   80 LA 81
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1295-1414 1.04e-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: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   1295 SVVKPRKHEQRLLRNVGVHTVVL---DLLQNPYD----------EKDDELMKELMCLAHEFLQNFCLGNQQNQVLLHNHL 1361
Cdd:pfam01365   26 MNNKPLRQRQNLMREQGVLETVMeviDLLGAPFTgallfaedlgEEKNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHL 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 44888998   1362 DLFLNP--------GILEakTVCAIFKDN--LALcNEVTDKVVQHFVHCIEIHGRHVAYLQFL 1414
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, ...
 235-326 4.03e-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: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  235 ENQEHILKGGDVVRLFHAEQEKFLTMDEYKKQYHvfLRTTGRTSATAATSSKALWEIEVVQhDSCRGGAGDWNSLYRFKH 314
Cdd:cd23290    2 CCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQ--RRLVYYEGGAVCTHARSLWRLEPLR-ISWSGSHLRWGQPLRIRH 78

                         90
                 ....*....|..
gi 44888998  315 LATGHYLAAEAE 326
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 ...
 243-329 4.29e-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: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  243 GGDVVRLFHAEQEKFLTMDE--YKKQYHvflRTTGRTSATAATSSKALWEIEVVQHDSCrGGAGDWNSLYRFKHLATGHY 320
Cdd:cd23278    1 GGDVLRLFHGHMDECLTIPAagSKEDQH---RTVIYEGGAVSTHARSLWRLELLRIKWS-GSHIGWGQPFRLRHVTTGRY 76


                 ....*....
gi 44888998  321 LAAEAEIDV 329
Cdd:cd23278   77 LALTEDRGL 85
glyco_rpt_poly TIGR04370
oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic ...
 2358-2547 8.48e-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: 8.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2358 LLFWISSYMSLWsnILFNCVVVINMIVAFFYPFDNTVPELSSHISLLFWIITIFSLVIVLAL---------PRESGIRTF 2428
Cdd:TIGR04370    1 SYKKKKDILSPI--ILFSLIWLLIFLLSLLLLSYLSFLYPLSDYTYLIIILGILIFIFGSLFlslslkskkRKTRKKKLS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998   2429 IGSVILRFIFLLGPESTLCLLGVVTVTLKSVHIVSIMGNKG----TLEKQLIKIITDFQLLYHCIYIAFCFCGLIFHPFF 2504
Cdd:TIGR04370   79 KISISLIILFLFFLILILLLLIILLLLLYIISLIGILGILSllgsALGYLALSGSTFLSGLIILLYILIILLLLLFLLLL 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 44888998   2505 Y-------SLLLFdvvyreetLVNVIRSVTRNGRSIVLTAVLALILVYLF 2547
Cdd:TIGR04370  159 LkkkrkklLLLLI--------LLALLISLLTGSRTGLILLILSLLFIYYL 200
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
178-230 3.08e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 40.79  E-value: 3.08e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 44888998     178 DYVVVVGDKVILSPVNADQqNLHVAANYELPDNPGCKEVN-----VLNSSTSWKISLF 230
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 ...
 244-321 4.37e-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: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44888998  244 GDVVRLFHAEQEKFLTMDEYK---KQYHvfLRTTGRTSATAATSSKALWEIEVVQhDSCRGGAGDWNSL---YRFKHLAT 317
Cdd:cd23276   69 GDEVRLLHKETNRYLRTHDAAapvTSKH--KEVSAYPDENEDGDDNDLWVVEIVK-DEGKLEDKRIKPLttrFRLRNKKT 145


                 ....
gi 44888998  318 GHYL 321
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, ...
 276-342 4.73e-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: 4.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 44888998  276 RTSATAATSSKALWEIEVVQhdscrggagdwNSLYRFKHLATGHYLAAEAEID-VSAGAMSATSASGH 342
Cdd:cd23432   22 KYGTPPEDDTSAQWIIEDVG-----------DGYVRIKNRATGHYLHIENNTGyLESGPIPPGWWSAQ 78
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
238-294 6.00e-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: 6.00e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 44888998     238 EHILKGGDVVRLFHAEQEKFLT-MDEY-----KKQYHVFLRTTGRTSATaatsskALWEIEVV 294
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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