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Conserved domains on  [gi|351065007|emb|CCD63766|]
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Inositol 1,4,5-trisphosphate receptor itr-1 [Caenorhabditis elegans]

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
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 33-271 1.15e-90

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: 294.02  E-value: 1.15e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007    33 NNGNLHIGDIISLYTESSSNqeqrGFLSTLGLVDDRCIVELKDGRPESPPKKFRDCLFKVCPVNRYAAQKHLWTEQKRFQ 112
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVN----GFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   113 TGDSMFDDdlmnkLKVAADKEREENesefqktlgnvIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKVYLDRAGN-E 191
Cdd:pfam08709   77 NGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgE 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   192 GSWFIIEPAYKHYAIGDNVSAGNKISLIPNSVSTTqaghvksqLHL-SSFNLLDHQSaAEVNCLNEPTEWQVFMFLLFDE 270
Cdd:pfam08709  141 GCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIF--------LHTtSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCE 211


                   .
gi 351065007   271 N 271
Cdd:pfam08709  212 N 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 547-746 2.68e-64

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: 217.84  E-value: 2.68e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   547 LLIDCILFVTNSSD---HLADPLKISDFSPSRDRQKLLREQEVLNQVF---LLLKAPFLprqgttelGPLLSsPSELSDS 620
Cdd:pfam01365    1 LLRDLIFFFAGPEEeelHEEDLLKLMNNKPLRQRQNLMREQGVLETVMeviDLLGAPFT--------GALLF-AEDLGEE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   621 RNEIFKTMFQLCYCLLKYSQVSYRKNQEFLAEKFGEIQEQIGFDLMAE---DTMTAVLHNNPKLLEKYVKTPHVERFVEL 697
Cdd:pfam01365   72 KNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISL 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 351065007   698 VRNNRQG-KFLDYLADLCVCRGEANKKIQELICTSVLSskHRDIFMDTKI 746
Cdd:pfam01365  152 LRKHGRDpRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 274-502 4.18e-57

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: 196.43  E-value: 4.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   274 NSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvvFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNKAYRFKH 353
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-----FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   354 LATDMYLSAEPSQvqvkpamngrrasliysktNNPMAMYSDGPNGVTNESTDTTQQNipsvwvlgptksefpeEDANLLF 433
Cdd:pfam02815   76 LTTGRYLHSHEEQ-------------------KPPLVEKEDWQKEVSAYGFRGFPGD----------------NDIVEIF 120

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351065007   434 QLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATNATEKQNlhyssKNEKGWVKVICEKNRVDKETFAL 502
Cdd:pfam02815  121 EKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW-----GFGPEQQKVTCAKEGHMDDALTL 184
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 2023-2129 1.41e-33

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: 125.72  E-value: 1.41e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2023 PEVALVEPILRVLQLLCENHNSLLQNFLRKQSD-RTNHNLVSETLSFLDTVCGStkgslgvfgeIGEHNFSLITQTLATL 2101
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNnKNSYNLVEETVDLLKAYCKS----------INEKNIELIIQCLDTL 70

                           90       100
                   ....*....|....*....|....*...
gi 351065007  2102 TEFCQGPCHENQNTMAmQENGLNIIISL 2129
Cdd:pfam08454   71 TEFIQGPCIENQIALC-ESKFLEIANDL 97
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2463-2718 4.10e-16

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: 80.39  E-value: 4.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2463 LLILASLCFLLLSSI--GVTLTLYIFGILQLVNKIVHVVAFvsnkgledrpIAEILACRN-LHYLLVYLFIC-------- 2531
Cdd:pfam00520   10 LLILLNTIFLALETYfqPEEPLTTVLEILDYVFTGIFTLEM----------LLKIIAAGFkKRYFRSPWNILdfvvvlps 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2532 -----------ILGLLVHPMIYCILLFDIIFTEETLQNVIASVTRNYQSIVWTGLLALILLYFFSILGFLYFRHDFYLEV 2600
Cdd:pfam00520   80 lislvlssvgsLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2601 DPVENDSSatissgipsetcpsegcpglqpsekddnddekkvksCETLWMCILqTGYQgLRNGGGIGDVLRNPAPwEDMF 2680
Cdd:pfam00520  160 NPDNGRTN------------------------------------FDNFPNAFL-WLFQ-TMTTEGWGDIMYDTID-GKGE 200

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 351065007  2681 IWRVAYDMTFFVVLIVIVLNLIFGVIIDTFGDLRAEKN 2718
Cdd:pfam00520  201 FWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
RYDR_ITPR super family cl03182
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1280-1427 2.09e-06

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: 51.05  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  1280 KPDTMNQQLLKNMRVYEVVLEFISV--------------PHDKKHDHdMMKLITLSHEFLRSFCKTNKENQSRLYKFISY 1345
Cdd:pfam01365   29 KPLRQRQNLMREQGVLETVMEVIDLlgapftgallfaedLGEEKNAP-WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDW 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  1346 EKDAKEGMLRVETIEEVGTlvAIFRNNRELASN-VPEELIAHIVGLIEHNSRNPIFLELLQALvCVYDKE-IESGQekva 1423
Cdd:pfam01365  108 LQSQLGSPSLAEGTLDVLT--ALLMDNPELLLNyIKECHIKSFISLLRKHGRDPRYLDFLSDL-CVCNGEaVRENQ---- 180


                   ....
gi 351065007  1424 NEIC 1427
Cdd:pfam01365  181 NLIC 184
 
Name Accession Description Interval E-value
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 33-271 1.15e-90

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: 294.02  E-value: 1.15e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007    33 NNGNLHIGDIISLYTESSSNqeqrGFLSTLGLVDDRCIVELKDGRPESPPKKFRDCLFKVCPVNRYAAQKHLWTEQKRFQ 112
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVN----GFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   113 TGDSMFDDdlmnkLKVAADKEREENesefqktlgnvIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKVYLDRAGN-E 191
Cdd:pfam08709   77 NGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgE 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   192 GSWFIIEPAYKHYAIGDNVSAGNKISLIPNSVSTTqaghvksqLHL-SSFNLLDHQSaAEVNCLNEPTEWQVFMFLLFDE 270
Cdd:pfam08709  141 GCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIF--------LHTtSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCE 211


                   .
gi 351065007   271 N 271
Cdd:pfam08709  212 N 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 547-746 2.68e-64

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: 217.84  E-value: 2.68e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   547 LLIDCILFVTNSSD---HLADPLKISDFSPSRDRQKLLREQEVLNQVF---LLLKAPFLprqgttelGPLLSsPSELSDS 620
Cdd:pfam01365    1 LLRDLIFFFAGPEEeelHEEDLLKLMNNKPLRQRQNLMREQGVLETVMeviDLLGAPFT--------GALLF-AEDLGEE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   621 RNEIFKTMFQLCYCLLKYSQVSYRKNQEFLAEKFGEIQEQIGFDLMAE---DTMTAVLHNNPKLLEKYVKTPHVERFVEL 697
Cdd:pfam01365   72 KNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISL 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 351065007   698 VRNNRQG-KFLDYLADLCVCRGEANKKIQELICTSVLSskHRDIFMDTKI 746
Cdd:pfam01365  152 LRKHGRDpRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 274-502 4.18e-57

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: 196.43  E-value: 4.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   274 NSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvvFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNKAYRFKH 353
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-----FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   354 LATDMYLSAEPSQvqvkpamngrrasliysktNNPMAMYSDGPNGVTNESTDTTQQNipsvwvlgptksefpeEDANLLF 433
Cdd:pfam02815   76 LTTGRYLHSHEEQ-------------------KPPLVEKEDWQKEVSAYGFRGFPGD----------------NDIVEIF 120

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351065007   434 QLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATNATEKQNlhyssKNEKGWVKVICEKNRVDKETFAL 502
Cdd:pfam02815  121 EKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW-----GFGPEQQKVTCAKEGHMDDALTL 184
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 268-510 5.85e-56

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: 194.11  E-value: 5.85e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  268 FDENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNpptdVVFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNK 347
Cdd:cd23277     3 YKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQ----YVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  348 AYRFKHLATDMYLSAEpsqvqvkpamngrrasLIYSKTNNPMAMYSDGPNGVTNESTDTTQQNipsvwvlgptksefpeE 427
Cdd:cd23277    79 LFRFKHLATGQYLAAE----------------VDPDPTPDPTRSKLRGAPGKPVYCLVSVPHG----------------N 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  428 DANLLFQLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATN-----ATEKQNLHyssknekgwvKVICEKNRVDKETFAL 502
Cdd:cd23277   127 DIASIFELDPTTLQRGDSLVPRSSYVRLRHLCTNTWVHSTNipidkEEEKPVML----------KVGTAPIKEDKEAFAI 196


                  ....*...
gi 351065007  503 LPVNPDEV 510
Cdd:cd23277   197 VPVSPSEV 204
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 2023-2129 1.41e-33

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: 125.72  E-value: 1.41e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2023 PEVALVEPILRVLQLLCENHNSLLQNFLRKQSD-RTNHNLVSETLSFLDTVCGStkgslgvfgeIGEHNFSLITQTLATL 2101
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNnKNSYNLVEETVDLLKAYCKS----------INEKNIELIIQCLDTL 70

                           90       100
                   ....*....|....*....|....*...
gi 351065007  2102 TEFCQGPCHENQNTMAmQENGLNIIISL 2129
Cdd:pfam08454   71 TEFIQGPCIENQIALC-ESKFLEIANDL 97
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2463-2718 4.10e-16

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: 80.39  E-value: 4.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2463 LLILASLCFLLLSSI--GVTLTLYIFGILQLVNKIVHVVAFvsnkgledrpIAEILACRN-LHYLLVYLFIC-------- 2531
Cdd:pfam00520   10 LLILLNTIFLALETYfqPEEPLTTVLEILDYVFTGIFTLEM----------LLKIIAAGFkKRYFRSPWNILdfvvvlps 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2532 -----------ILGLLVHPMIYCILLFDIIFTEETLQNVIASVTRNYQSIVWTGLLALILLYFFSILGFLYFRHDFYLEV 2600
Cdd:pfam00520   80 lislvlssvgsLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2601 DPVENDSSatissgipsetcpsegcpglqpsekddnddekkvksCETLWMCILqTGYQgLRNGGGIGDVLRNPAPwEDMF 2680
Cdd:pfam00520  160 NPDNGRTN------------------------------------FDNFPNAFL-WLFQ-TMTTEGWGDIMYDTID-GKGE 200

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 351065007  2681 IWRVAYDMTFFVVLIVIVLNLIFGVIIDTFGDLRAEKN 2718
Cdd:pfam00520  201 FWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 152-293 3.66e-09

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


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 58.55  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  152 GSMVQLLHVKSNKYITVQKNSPAKRERNAMkVYL---DRAGNEGSWFIIEPayKHYAIGDNVSAGNKISLIpnsvsttqa 228
Cdd:cd23263     1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQE-VTFessSRKGDTNGLWIIES--ENGKQGGPVKWGDKIRLR--------- 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351065007  229 gHVKSQLHLSSFNL-LDHQSAA-EVNCLNEP----TEWQvFMFLLFDENQQNSVKSGDVVRLFHADQQTFL 293
Cdd:cd23263    69 -HLSTGKYLSSEEGkKSPKSNHqEVLCLTDNpdksSLFK-FEPIGSTKYKQKYVKKDSYFRLKHVNTNFWL 137
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1280-1427 2.09e-06

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: 51.05  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  1280 KPDTMNQQLLKNMRVYEVVLEFISV--------------PHDKKHDHdMMKLITLSHEFLRSFCKTNKENQSRLYKFISY 1345
Cdd:pfam01365   29 KPLRQRQNLMREQGVLETVMEVIDLlgapftgallfaedLGEEKNAP-WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDW 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  1346 EKDAKEGMLRVETIEEVGTlvAIFRNNRELASN-VPEELIAHIVGLIEHNSRNPIFLELLQALvCVYDKE-IESGQekva 1423
Cdd:pfam01365  108 LQSQLGSPSLAEGTLDVLT--ALLMDNPELLLNyIKECHIKSFISLLRKHGRDPRYLDFLSDL-CVCNGEaVRENQ---- 180


                   ....
gi 351065007  1424 NEIC 1427
Cdd:pfam01365  181 NLIC 184
glyco_rpt_poly TIGR04370
oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic ...
 2406-2594 1.11e-04

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: 47.15  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2406 FHFAFIVNALVARYYPLPEHSNSSISLGNLYSWFAVFSSFLLA--------------------HYLRHDKIYLHKTSLLI 2465
Cdd:TIGR04370   15 FSLIWLLIFLLSLLLLSYLSFLYPLSDYTYLIIILGILIFIFGslflslslkskkrktrkkklSKISISLIILFLFFLIL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2466 LASLCFLLLSSIGVTLTLYIFGILQLVNKivhvvAFVSNKGLEDRPIAEILACRNLHYLLVYLFICILGLLVHPMIYCIL 2545
Cdd:TIGR04370   95 ILLLLIILLLLLYIISLIGILGILSLLGS-----ALGYLALSGSTFLSGLIILLYILIILLLLLFLLLLLKKKRKKLLLL 169

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 351065007  2546 LFdIIfteeTLQNVIASVTRnyqsivwTGLLALILLYFFsilGFLYFRH 2594
Cdd:TIGR04370  170 LI-LL----ALLISLLTGSR-------TGLILLILSLLF---IYYLFYK 203
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
146-200 5.74e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 37.32  E-value: 5.74e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 351065007    146 GNVIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKV--YLDRAGNEGSWFIIEPA 200
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVtgYGNPAIDANTLWLIEPV 57
 
Name Accession Description Interval E-value
Ins145_P3_rec pfam08709
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ...
 33-271 1.15e-90

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: 294.02  E-value: 1.15e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007    33 NNGNLHIGDIISLYTESSSNqeqrGFLSTLGLVDDRCIVELKDGRPESPPKKFRDCLFKVCPVNRYAAQKHLWTEQKRFQ 112
Cdd:pfam08709    1 MSSFLHIGDIVSLSCEESVN----GFISALGLGNDRCFVENKAGDLNDPPKKFRDCVFKICPANSYAAQKELWSAGNRSP 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   113 TGDSMFDDdlmnkLKVAADKEREENesefqktlgnvIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKVYLDRAGN-E 191
Cdd:pfam08709   77 NGNSLTDA-----LKHASNIEGHQN-----------LQYGSAILLLHVKSNMYLAVLKSSPSLRDKNAMRVVLDEAGNgE 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   192 GSWFIIEPAYKHYAIGDNVSAGNKISLIPNSVSTTqaghvksqLHL-SSFNLLDHQSaAEVNCLNEPTEWQVFMFLLFDE 270
Cdd:pfam08709  141 GCWFIITPAYKQRSEGDNVCVGDEVILVPVSAPIF--------LHTtSSSELRDNPG-KEVNASFGQTSWKMEPFMSGCE 211


                   .
gi 351065007   271 N 271
Cdd:pfam08709  212 N 212
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 547-746 2.68e-64

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: 217.84  E-value: 2.68e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   547 LLIDCILFVTNSSD---HLADPLKISDFSPSRDRQKLLREQEVLNQVF---LLLKAPFLprqgttelGPLLSsPSELSDS 620
Cdd:pfam01365    1 LLRDLIFFFAGPEEeelHEEDLLKLMNNKPLRQRQNLMREQGVLETVMeviDLLGAPFT--------GALLF-AEDLGEE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   621 RNEIFKTMFQLCYCLLKYSQVSYRKNQEFLAEKFGEIQEQIGFDLMAE---DTMTAVLHNNPKLLEKYVKTPHVERFVEL 697
Cdd:pfam01365   72 KNAPWKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPELLLNYIKECHIKSFISL 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 351065007   698 VRNNRQG-KFLDYLADLCVCRGEANKKIQELICTSVLSskHRDIFMDTKI 746
Cdd:pfam01365  152 LRKHGRDpRYLDFLSDLCVCNGEAVRENQNLICRLLLP--NPDLLLQTLL 199
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 274-502 4.18e-57

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: 196.43  E-value: 4.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   274 NSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvvFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNKAYRFKH 353
Cdd:pfam02815    1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-----FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007   354 LATDMYLSAEPSQvqvkpamngrrasliysktNNPMAMYSDGPNGVTNESTDTTQQNipsvwvlgptksefpeEDANLLF 433
Cdd:pfam02815   76 LTTGRYLHSHEEQ-------------------KPPLVEKEDWQKEVSAYGFRGFPGD----------------NDIVEIF 120

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 351065007   434 QLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATNATEKQNlhyssKNEKGWVKVICEKNRVDKETFAL 502
Cdd:pfam02815  121 EKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW-----GFGPEQQKVTCAKEGHMDDALTL 184
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 268-510 5.85e-56

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: 194.11  E-value: 5.85e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  268 FDENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNpptdVVFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNK 347
Cdd:cd23277     3 YKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQ----YVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  348 AYRFKHLATDMYLSAEpsqvqvkpamngrrasLIYSKTNNPMAMYSDGPNGVTNESTDTTQQNipsvwvlgptksefpeE 427
Cdd:cd23277    79 LFRFKHLATGQYLAAE----------------VDPDPTPDPTRSKLRGAPGKPVYCLVSVPHG----------------N 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  428 DANLLFQLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATN-----ATEKQNLHyssknekgwvKVICEKNRVDKETFAL 502
Cdd:cd23277   127 DIASIFELDPTTLQRGDSLVPRSSYVRLRHLCTNTWVHSTNipidkEEEKPVML----------KVGTAPIKEDKEAFAI 196


                  ....*...
gi 351065007  503 LPVNPDEV 510
Cdd:cd23277   197 VPVSPSEV 204
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 268-515 6.09e-50

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: 177.57  E-value: 6.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  268 FDENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvVFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKWNK 347
Cdd:cd23287     3 WSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQH----VFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  348 AYRFKHLATDMYLSAEPSQVQvkpamngrrasliySKTNNPMAMYSDGPNGVTNESTDTTQQNIPSVWVLGPTKSefpee 427
Cdd:cd23287    79 LFRFKHLATGHYLAAEVDPDF--------------EEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGN----- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  428 DANLLFQLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATNATekqnlhySSKNEKGWV--KVICEKNRVDKETFALLPV 505
Cdd:cd23287   140 DISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIP-------IDKEEEKPVmlKIGTSPLKEDKEAFAIVPV 212

                         250
                  ....*....|
gi 351065007  506 NPDEVRDLDF 515
Cdd:cd23287   213 SPAEVRDLDF 222
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 260-510 2.77e-44

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: 161.36  E-value: 2.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  260 WQVFMFLLFDENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvVFLRMTNRPSAADATSSRALWEVQVVQTNAYR 339
Cdd:cd23288     1 WKVTLFMKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQH----IFLRTTLRQSATSATSSKALWEIEVVHYDPCR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  340 GGTAKWNKAYRFKHLATDMYLSAEpsqvqVKPAmngrrasliYSKTNNPMAMYSDGpNGVTNESTDTTQQNIPSVWVLGP 419
Cdd:cd23288    77 GGAGQWNSLFRFKHLATGNYLAAE-----VNPD---------YRDAQNEGKAVNDG-DSPTSKKKRQAAEKIMYTLVSVP 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  420 TKSefpeeDANLLFQLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATnatekqNLHYSSKNEKG-WVKVICEKNRVDKE 498
Cdd:cd23288   142 HGN-----DIASLFELDATTLQRADCLVPRNSYVRLRHLCTNTWVTST------SIPIDTEEERPvMLKIGTCQTKEDKE 210

                         250
                  ....*....|..
gi 351065007  499 TFALLPVNPDEV 510
Cdd:cd23288   211 AFAIVSVPLSEV 222
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 270-510 2.16e-38

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: 143.29  E-value: 2.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  270 ENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNPPTDVV-----FLRMTNRPSAADATSSRALWEVQVVQTnAYRGGTAK 344
Cdd:cd23280     1 KENENFLKGGDVVRLFHKELEAYLSAEGSFVDEVLTEDVhlrvrPVDDRKPRTLFPPTSGDTFWQIEKEDT-PLKGGVIK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  345 WNKAYRFKHLATDMYLSAEPSqvqvkpamngrrasliysktnnpmamysdgpngvtnestdttqqNIPSVWVLGPTKSef 424
Cdd:cd23280    80 WGDQCRLRHLPTGKYLAVDDK--------------------------------------------TGNGKVVLTSDPS-- 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  425 peeDANLLFQLDPSTFMKSnKEVPRRSYVRLLHQSSDKWVHATNATEKQNLHYS----SKNEKGWVKVICEKNRVDKETF 500
Cdd:cd23280   114 ---DPSTVFRLHPVTKETS-EEVKFGSYVRIEHVATGTWLHAETDEELRRSKKSpaglSWDGAKLRKVSLSLERQDDDAF 189

                         250
                  ....*....|
gi 351065007  501 ALLPVNPDEV 510
Cdd:cd23280   190 TIQEVDPDLV 199
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 266-510 2.53e-38

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: 144.03  E-value: 2.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  266 LLFDENQQNSVKSGDVVRLFHADQQTFLTLDTIPKQNPptdvVFLRMTNRPSAADATSSRALWEVQVVQTNAYRGGTAKW 345
Cdd:cd23289     1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQ----VFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHW 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  346 NKAYRFKHLATDMYLSAEpsqvqVKPAMNGRrasliySKTNNPMAMYSDGPNGVTNestdtTQQNIPSVWVLGPTKSefp 425
Cdd:cd23289    77 NGLYRFKHLATGNYLAAE-----ENPSYKGD------ASDPKAAGMGAQSRTGRRN-----AGEKIKYCLVAVPHGN--- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  426 eeDANLLFQLDPSTFMKSNKEVPRRSYVRLLHQSSDKWVHATNATekqnlhySSKNEKGWVKVI---CeKNRVDKETFAL 502
Cdd:cd23289   138 --DIASLFELDPTTLQKTDSFVPRNSYVRLRHLCTNTWIQSTNVP-------IDIEEERPIRLMlgtC-PTKEDKEAFAI 207


                  ....*...
gi 351065007  503 LPVNPDEV 510
Cdd:cd23289   208 VSVPVSEI 215
RIH_assoc pfam08454
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ...
 2023-2129 1.41e-33

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: 125.72  E-value: 1.41e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2023 PEVALVEPILRVLQLLCENHNSLLQNFLRKQSD-RTNHNLVSETLSFLDTVCGStkgslgvfgeIGEHNFSLITQTLATL 2101
Cdd:pfam08454    1 QEVKIICRILRFLQLLCEGHNLDLQNYLRQQTNnKNSYNLVEETVDLLKAYCKS----------INEKNIELIIQCLDTL 70

                           90       100
                   ....*....|....*....|....*...
gi 351065007  2102 TEFCQGPCHENQNTMAmQENGLNIIISL 2129
Cdd:pfam08454   71 TEFIQGPCIENQIALC-ESKFLEIANDL 97
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 279-507 8.22e-22

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: 94.76  E-value: 8.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  279 GDVVRLFHADQQTFLTLDTIPKQ-NPPTDVVFLRMTNRPsaadaTSSRALWEVQVVQTNAyrGGTAKWNKAYRFKHLATD 357
Cdd:cd23263     1 GDVIWLKHSETGKYLHSHRKNYPtGSGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  358 MYLSAEPSQVQvkPAMNGRRasliysktnnpmamysdgpngvtnestdttqqnipsVWVLGptksefPEEDANLLFQLDP 437
Cdd:cd23263    74 KYLSSEEGKKS--PKSNHQE------------------------------------VLCLT------DNPDKSSLFKFEP 109

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351065007  438 STFMK-SNKEVPRRSYVRLLHQSSDKWVHATNATEKQnlhysskNEKGWVKVICEKNRvdKETFALLPVNP 507
Cdd:cd23263   110 IGSTKyKQKYVKKDSYFRLKHVNTNFWLHSHEKKFNI-------NNKTQQEVICHGER--EEVFKLWKAEL 171
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 2463-2718 4.10e-16

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: 80.39  E-value: 4.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2463 LLILASLCFLLLSSI--GVTLTLYIFGILQLVNKIVHVVAFvsnkgledrpIAEILACRN-LHYLLVYLFIC-------- 2531
Cdd:pfam00520   10 LLILLNTIFLALETYfqPEEPLTTVLEILDYVFTGIFTLEM----------LLKIIAAGFkKRYFRSPWNILdfvvvlps 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2532 -----------ILGLLVHPMIYCILLFDIIFTEETLQNVIASVTRNYQSIVWTGLLALILLYFFSILGFLYFRHDFYLEV 2600
Cdd:pfam00520   80 lislvlssvgsLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2601 DPVENDSSatissgipsetcpsegcpglqpsekddnddekkvksCETLWMCILqTGYQgLRNGGGIGDVLRNPAPwEDMF 2680
Cdd:pfam00520  160 NPDNGRTN------------------------------------FDNFPNAFL-WLFQ-TMTTEGWGDIMYDTID-GKGE 200

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 351065007  2681 IWRVAYDMTFFVVLIVIVLNLIFGVIIDTFGDLRAEKN 2718
Cdd:pfam00520  201 FWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 152-293 3.66e-09

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


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 58.55  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  152 GSMVQLLHVKSNKYITVQKNSPAKRERNAMkVYL---DRAGNEGSWFIIEPayKHYAIGDNVSAGNKISLIpnsvsttqa 228
Cdd:cd23263     1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQE-VTFessSRKGDTNGLWIIES--ENGKQGGPVKWGDKIRLR--------- 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 351065007  229 gHVKSQLHLSSFNL-LDHQSAA-EVNCLNEP----TEWQvFMFLLFDENQQNSVKSGDVVRLFHADQQTFL 293
Cdd:cd23263    69 -HLSTGKYLSSEEGkKSPKSNHqEVLCLTDNpdksSLFK-FEPIGSTKYKQKYVKKDSYFRLKHVNTNFWL 137
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 1280-1427 2.09e-06

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: 51.05  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  1280 KPDTMNQQLLKNMRVYEVVLEFISV--------------PHDKKHDHdMMKLITLSHEFLRSFCKTNKENQSRLYKFISY 1345
Cdd:pfam01365   29 KPLRQRQNLMREQGVLETVMEVIDLlgapftgallfaedLGEEKNAP-WKKIVRLCYRLLAYSCRGNRKNQEAIAKHLDW 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  1346 EKDAKEGMLRVETIEEVGTlvAIFRNNRELASN-VPEELIAHIVGLIEHNSRNPIFLELLQALvCVYDKE-IESGQekva 1423
Cdd:pfam01365  108 LQSQLGSPSLAEGTLDVLT--ALLMDNPELLLNyIKECHIKSFISLLRKHGRDPRYLDFLSDL-CVCNGEaVRENQ---- 180


                   ....
gi 351065007  1424 NEIC 1427
Cdd:pfam01365  181 NLIC 184
glyco_rpt_poly TIGR04370
oligosaccharide repeat unit polymerase; Members of this subfamily of highly hydrophobic ...
 2406-2594 1.11e-04

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: 47.15  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2406 FHFAFIVNALVARYYPLPEHSNSSISLGNLYSWFAVFSSFLLA--------------------HYLRHDKIYLHKTSLLI 2465
Cdd:TIGR04370   15 FSLIWLLIFLLSLLLLSYLSFLYPLSDYTYLIIILGILIFIFGslflslslkskkrktrkkklSKISISLIILFLFFLIL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  2466 LASLCFLLLSSIGVTLTLYIFGILQLVNKivhvvAFVSNKGLEDRPIAEILACRNLHYLLVYLFICILGLLVHPMIYCIL 2545
Cdd:TIGR04370   95 ILLLLIILLLLLYIISLIGILGILSLLGS-----ALGYLALSGSTFLSGLIILLYILIILLLLLFLLLLLKKKRKKLLLL 169

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 351065007  2546 LFdIIfteeTLQNVIASVTRnyqsivwTGLLALILLYFFsilGFLYFRH 2594
Cdd:TIGR04370  170 LI-LL----ALLISLLTGSR-------TGLILLILSLLF---IYYLFYK 203
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 276-366 2.86e-04

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: 44.49  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  276 VKSGDVVRLFHADQQTFLTLDTIPKQNPptdvvfLRMTNRPSAADATSSRALWEVQVVQTnAYRGGTAKWNKAYRFKHLA 355
Cdd:cd23290     8 VTGGHVLRLFHGHMDECLTISAADSDDQ------RRLVYYEGGAVCTHARSLWRLEPLRI-SWSGSHLRWGQPLRIRHVT 80

                          90
                  ....*....|.
gi 351065007  356 TDMYLSAEPSQ 366
Cdd:cd23290    81 TGRYLALTEDQ 91
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 279-366 3.73e-04

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: 44.13  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  279 GDVVRLFHADQQTFltldTIPKQNPpTDVVFlRMTNRPSAADATSSRALWEVQVVQTnAYRGGTAKWNKAYRFKHLATDM 358
Cdd:cd23292     6 GHVVRLFHGHDECL----TIPSTDQ-SDEQH-RVVNYEAGGAGTRARSLWRLEPLRI-SWSGSHIRWGQTFRLRHLTTGH 78


                  ....*...
gi 351065007  359 YLSAEPSQ 366
Cdd:cd23292    79 YLALTEDQ 86
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 279-366 3.96e-03

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: 40.75  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351065007  279 GDVVRLFHADQQTFLtldTIP----KQNPPTDVVFlrmtnrPSAADATSSRALWEVQVVQTnAYRGGTAKWNKAYRFKHL 354
Cdd:cd23278     2 GDVLRLFHGHMDECL---TIPaagsKEDQHRTVIY------EGGAVSTHARSLWRLELLRI-KWSGSHIGWGQPFRLRHV 71

                          90
                  ....*....|..
gi 351065007  355 ATDMYLSAEPSQ 366
Cdd:cd23278    72 TTGRYLALTEDR 83
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
146-200 5.74e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 37.32  E-value: 5.74e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 351065007    146 GNVIQYGSMVQLLHVKSNKYITVQKNSPAKRERNAMKV--YLDRAGNEGSWFIIEPA 200
Cdd:smart00472    1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVtgYGNPAIDANTLWLIEPV 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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