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Conserved domains on  [gi|27574053|pdb|1N4K|A]
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Chain A, Inositol 1,4,5-trisphosphate receptor type 1

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 1-222 9.07e-180

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: 498.05  E-value: 9.07e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80
Cdd:cd23287   1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160
Cdd:cd23287  81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1N4K_A      161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
Cdd:cd23287 161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 253-381 1.35e-53

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: 175.85  E-value: 1.35e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        253 LLEDLVYFVTGGTNS---GQDVLEVVFSKPNRERQKLMREQNILKQIFK---LLQAPFTdcgdGPMLRLEELGDQRHAPF 326
Cdd:pfam01365   1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
1N4K_A        327 RHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAE---DTITALLHNNRK 381
Cdd:pfam01365  77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPE 134
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 1-222 9.07e-180

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: 498.05  E-value: 9.07e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80
Cdd:cd23287   1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160
Cdd:cd23287  81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1N4K_A      161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
Cdd:cd23287 161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 9-210 3.46e-81

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: 246.51  E-value: 3.46e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A          9 DILKGGDVVRLFHAEQEKFLTCDEHRKKQHvFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATG 88
Cdd:pfam02815   1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A         89 HYLAAEVDPdfeeeclefqpsvdpdQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLR 168
Cdd:pfam02815  80 RYLHSHEEQ----------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQ 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
1N4K_A        169 HLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIV 210
Cdd:pfam02815 144 HVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 253-381 1.35e-53

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: 175.85  E-value: 1.35e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        253 LLEDLVYFVTGGTNS---GQDVLEVVFSKPNRERQKLMREQNILKQIFK---LLQAPFTdcgdGPMLRLEELGDQRHAPF 326
Cdd:pfam01365   1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
1N4K_A        327 RHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAE---DTITALLHNNRK 381
Cdd:pfam01365  77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPE 134
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
8-64 6.43e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.80  E-value: 6.43e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
1N4K_A           8 DDILKGGDVVRLFHAEQEKFLTCDEHR------KKQHVFLRTTGRQSATSatsskaLWEVEVV 64
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlppwgdGQQEVTGYGNPAIDANT------LWLIEPV 57
 
Name Accession Description Interval E-value
beta-trefoil_MIR_ITPR1 cd23287
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ...
 1-222 9.07e-180

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: 498.05  E-value: 9.07e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80
Cdd:cd23287   1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160
Cdd:cd23287  81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1N4K_A      161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
Cdd:cd23287 161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDF 222
beta-trefoil_MIR_ITPR cd23277
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ...
 1-217 8.66e-157

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: 439.10  E-value: 8.66e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80
Cdd:cd23277   1 MEYKENLEDVLKGGDVVRLFHAEQEKFLTCDEYKKKQYVFLRTTGRTSATSATSSKALWEVEVVQHDPCRGGAGHWNSLF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       81 RFKHLATGHYLAAEVDPdfeeeclefqpsvDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160
Cdd:cd23277  81 RFKHLATGQYLAAEVDP-------------DPTPDPTRSKLRGAPGKPVYCLVSVPHGNDIASIFELDPTTLQRGDSLVP 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
1N4K_A      161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEV 217
Cdd:cd23277 148 RSSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKVGTAPIKEDKEAFAIVPVSPSEV 204
beta-trefoil_MIR_ITPR2 cd23288
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ...
 1-217 6.22e-134

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: 382.08  E-value: 6.22e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80
Cdd:cd23288   7 MKFSDYREDILKGGDVVRLFHAEQEKFLTCDEYKKKQHIFLRTTLRQSATSATSSKALWEIEVVHYDPCRGGAGQWNSLF 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       81 RFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRlRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160
Cdd:cd23288  87 RFKHLATGNYLAAEVNPDYRDAQNEGKAVNDGDSPTSKKK-RQAAEKIMYTLVSVPHGNDIASLFELDATTLQRADCLVP 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
1N4K_A      161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEV 217
Cdd:cd23288 166 RNSYVRLRHLCTNTWVTSTSIPIDTEEERPVMLKIGTCQTKEDKEAFAIVSVPLSEV 222
beta-trefoil_MIR_ITPR3 cd23289
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ...
 1-217 1.38e-124

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: 357.82  E-value: 1.38e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        1 MKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLF 80
Cdd:cd23289   1 MQFRDHLEEVLKGGDVVRLFHAEQEKFLTCDEYKGKLQVFLRTTLRQSATSATSSNALWEVEVVHHDPCRGGAGHWNGLY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       81 RFKHLATGHYLAAEVDPDFEEECLEfqPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVP 160
Cdd:cd23289  81 RFKHLATGNYLAAEENPSYKGDASD--PKAAGMGAQSRTGRRNAGEKIKYCLVAVPHGNDIASLFELDPTTLQKTDSFVP 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
1N4K_A      161 RNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEV 217
Cdd:cd23289 159 RNSYVRLRHLCTNTWIQSTNVPIDIEEERPIRLMLGTCPTKEDKEAFAIVSVPVSEI 215
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 9-210 3.46e-81

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: 246.51  E-value: 3.46e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A          9 DILKGGDVVRLFHAEQEKFLTCDEHRKKQHvFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATG 88
Cdd:pfam02815   1 GYLKGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSARSLWRIEVVRHDAWRGGLIKWGSPFRLRHLTTG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A         89 HYLAAEVDPdfeeeclefqpsvdpdQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLR 168
Cdd:pfam02815  80 RYLHSHEEQ----------------KPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQ 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
1N4K_A        169 HLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIV 210
Cdd:pfam02815 144 HVCTGCWLFSHSVKLPKWGFGPEQQKVTCAKEGHMDDALTLP 185
RYDR_ITPR pfam01365
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ...
 253-381 1.35e-53

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: 175.85  E-value: 1.35e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        253 LLEDLVYFVTGGTNS---GQDVLEVVFSKPNRERQKLMREQNILKQIFK---LLQAPFTdcgdGPMLRLEELGDQRHAPF 326
Cdd:pfam01365   1 LLRDLIFFFAGPEEEelhEEDLLKLMNNKPLRQRQNLMREQGVLETVMEvidLLGAPFT----GALLFAEDLGEEKNAPW 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
1N4K_A        327 RHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAE---DTITALLHNNRK 381
Cdd:pfam01365  77 KKIVRLCYRLLAYSCRGNRKNQEAIAKHLDWLQSQLGSPSLAEgtlDVLTALLMDNPE 134
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 8-217 2.06e-33

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: 123.26  E-value: 2.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        8 DDILKGGDVVRLFHAEQEKFLTCDEH--------RKKQHV-FLRTTGRQSATSATSSKALWEVEVVqHDPCRGGAGYWNS 78
Cdd:cd23280   4 ENFLKGGDVVRLFHKELEAYLSAEGSfvdevlteDVHLRVrPVDDRKPRTLFPPTSGDTFWQIEKE-DTPLKGGVIKWGD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       79 LFRFKHLATGHYLAAEVDPDFEEECLEfqpsvdpdqdasrsrlrnaqekmvyslvsvPEGNDISSIFELDPTTLRGGDSl 158
Cdd:cd23280  83 QCRLRHLPTGKYLAVDDKTGNGKVVLT------------------------------SDPSDPSTVFRLHPVTKETSEE- 131

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1N4K_A      159 VPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVML---------KIGTSPLKEDKEAFAIVPVSPAEV 217
Cdd:cd23280 132 VKFGSYVRIEHVATGTWLHAETDEELRRSKKSPAGlswdgaklrKVSLSLERQDDDAFTIQEVDPDLV 199
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 14-188 3.12e-28

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: 108.62  E-value: 3.12e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       14 GDVVRLFHAEQEKFLTCDEHR-----KKQHVFLRTTGRQsatsaTSSKALWEVEVVQHDPcrGGAGYWNSLFRFKHLATG 88
Cdd:cd23263   1 GDVIWLKHSETGKYLHSHRKNyptgsGQQEVTFESSSRK-----GDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLSTG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       89 HYLAAEVDPdfeeeclefqpsvdpdqdasRSRLRNAQEKMVYSlvsvpEGNDISSIFELDPTTLRGG-DSLVPRNSYVRL 167
Cdd:cd23263  74 KYLSSEEGK--------------------KSPKSNHQEVLCLT-----DNPDKSSLFKFEPIGSTKYkQKYVKKDSYFRL 128

                       170       180
                ....*....|....*....|.
1N4K_A      168 RHLCTNTWVHSTNIPIDKEEE 188
Cdd:cd23263 129 KHVNTNFWLHSHEKKFNINNK 149
beta-trefoil_MIR_RyR3 cd23292
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ...
 11-176 2.90e-08

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: 53.38  E-value: 2.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       11 LKGGDVVRLFHAEQEKF-LTCDEHRKKQHvflRTTGRQSATSATSSKALWEVEvvqhdPCR----GGAGYWNSLFRFKHL 85
Cdd:cd23292   3 LLGGHVVRLFHGHDECLtIPSTDQSDEQH---RVVNYEAGGAGTRARSLWRLE-----PLRiswsGSHIRWGQTFRLRHL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       86 ATGHYLAAEvdpdfEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIfeldpttlRGGDSLvprnsyV 165
Cdd:cd23292  75 TTGHYLALT-----EDQGLILQDRAKSDTKSTAFCFRASKEKLESGPKRDIDGMGIAEI--------KYGDSV------C 135

                       170
                ....*....|.
1N4K_A      166 RLRHLCTNTWV 176
Cdd:cd23292 136 FVQHVASGLWL 146
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
8-64 6.43e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.80  E-value: 6.43e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
1N4K_A           8 DDILKGGDVVRLFHAEQEKFLTCDEHR------KKQHVFLRTTGRQSATSatsskaLWEVEVV 64
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlppwgdGQQEVTGYGNPAIDANT------LWLIEPV 57
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 14-91 3.65e-06

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: 46.94  E-value: 3.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       14 GDVVRLFHAEQEKFLTCDEHR---KKQHvfLRTTGRQSATSATSSKALWEVEVVQhDPCRGGAGYWNSL---FRFKHLAT 87
Cdd:cd23276  69 GDEVRLLHKETNRYLRTHDAAapvTSKH--KEVSAYPDENEDGDDNDLWVVEIVK-DEGKLEDKRIKPLttrFRLRNKKT 145


                ....
1N4K_A       88 GHYL 91
Cdd:cd23276 146 GCYL 149
beta-trefoil_MIR_RyR cd23278
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ...
 13-196 4.50e-06

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: 4.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       13 GGDVVRLFHAEQEKFLTCDE--HRKKQHvflRTTGRQSATSATSSKALWEVEVVQHDPCrGGAGYWNSLFRFKHLATGHY 90
Cdd:cd23278   1 GGDVLRLFHGHMDECLTIPAagSKEDQH---RTVIYEGGAVSTHARSLWRLELLRIKWS-GSHIGWGQPFRLRHVTTGRY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       91 LAAEVDPDfeeecLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGndissifeLDPTTLRGGDSLvprnsyVRLRHL 170
Cdd:cd23278  77 LALTEDRG-----LVLVPKEKADVKATAFCFRQSKDDKKVLDEKEDEG--------MGTPEIKYGDSL------VFIQHV 137

                       170       180       190
                ....*....|....*....|....*....|.
1N4K_A      171 CTNTW-----VHSTNIPIDKEEEKPVMLKIG 196
Cdd:cd23278 138 DTGLWlsyqaVETKKRVGGVEERKAILHAEG 168
beta-trefoil_MIR_RyR2 cd23291
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ...
 13-176 2.14e-05

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


Pssm-ID: 467762 [Multi-domain]  Cd Length: 184  Bit Score: 44.65  E-value: 2.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       13 GGDVVRLFHAEQEKFLTC--DEHRKKQHvflRTTGRQSATSATSSKALWEVEVVQHdPCRGGAGYWNSLFRFKHLATGHY 90
Cdd:cd23291   1 GGDVLRLLHGHMDECLTVpsGEHGEEQR---RTVHYEGGAVSVHARSLWRLETLRV-AWSGSHIRWGQPFRLRHVTTGKY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       91 LAAevdpdFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIfeldpttlRGGDSLvprnSYVrlRHL 170
Cdd:cd23291  77 LSL-----MEDKNLLLMDKEKADVKSTAFTFRSSKEKLDVGVRKEVDGMGTSEI--------KYGDSV----CYI--QHV 137


                ....*.
1N4K_A      171 CTNTWV 176
Cdd:cd23291 138 DTGLWL 143
beta-trefoil_MIR_RyR1 cd23290
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ...
 11-96 4.75e-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: 43.72  E-value: 4.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       11 LKGGDVVRLFHAEQEKFLTC-----DEHRkkqhvflRTTGRQSATSATSSKALWEVEvvqhdPCR----GGAGYWNSLFR 81
Cdd:cd23290   8 VTGGHVLRLFHGHMDECLTIsaadsDDQR-------RLVYYEGGAVCTHARSLWRLE-----PLRiswsGSHLRWGQPLR 75

                        90
                ....*....|....*
1N4K_A       82 FKHLATGHYLAAEVD 96
Cdd:cd23290  76 IRHVTTGRYLALTED 90
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 4-91 6.15e-05

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: 43.14  E-value: 6.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        4 SDNKDDILKGGDVVRLFHAEQEKFLTCDEH---RKKQHVFLRTTGRQSATSatsskALWEVEVVQHDPcrGGAGYW--NS 78
Cdd:cd23263  52 NGKQGGPVKWGDKIRLRHLSTGKYLSSEEGkksPKSNHQEVLCLTDNPDKS-----SLFKFEPIGSTK--YKQKYVkkDS 124

                        90
                ....*....|...
1N4K_A       79 LFRFKHLATGHYL 91
Cdd:cd23263 125 YFRLKHVNTNFWL 137
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
71-98 1.60e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 39.25  E-value: 1.60e-04
                           10        20
                   ....*....|....*....|....*...
1N4K_A          71 GGAGYWNSLFRFKHLATGHYLAAEVDPD 98
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKL 28
beta-trefoil_Ricin_EndoBetaGal-like cd23432
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1, ...
 48-124 1.79e-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: 40.79  E-value: 1.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       48 SATSATSSKALWEVEVVqhdpcrgGAGYwnslFRFKHLATGHYLAAEVDPDFeEECLEFQPSVDPDQ------DASRSRL 121
Cdd:cd23432  24 GTPPEDDTSAQWIIEDV-------GDGY----VRIKNRATGHYLHIENNTGY-LESGPIPPGWWSAQwtlepvGTGYVRI 91


                ...
1N4K_A      122 RNA 124
Cdd:cd23432  92 RNR 94
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 1-93 6.14e-03

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 2 (PMT2) and similar proteins; Dolichyl-phosphate-mannose-protein mannosyltransferases (EC 2.4.1.109), also called 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. In Saccharomyces cerevisiae, a family of protein mannosyltransferases coded for by seven genes (PMT1-7). The family includes PMT2, PMT3 and PMT6. PMT2 forms a heterodimeric complex with PMT1 and more rarely with PMT5. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. It is required for incorporation of proteins in the cell wall. PMT3 form a functional heterodimer with PMT5 and more rarely with PMT1. It may have redundant activity to PMT2. PMT6 may form a heterodimer with PMT4. 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: 467755 [Multi-domain]  Cd Length: 192  Bit Score: 37.68  E-value: 6.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A        1 MKWSDNKDDI--LKGGDVVRLFHAEQEKFLtcDEHRKKQHVflrtTGRQSATSA------TSSKALWEVEVVQHDpcrgG 72
Cdd:cd23284  59 PSWDENDTDIefIKDGDIVRLVHKQTGRNL--HSHPVPAPI----SKSDYEVSGygdltvGDEKDNWVIEIVKQV----G 128

                        90       100
                ....*....|....*....|....*..
1N4K_A       73 AGYWNSL------FRFKHLATGHYLAA 93
Cdd:cd23284 129 SEDPKKLhtlttsFRLRHEVLGCYLAQ 155
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 14-93 8.84e-03

MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The SDF-2 family includes mammalian SDF-2 and SDF2-like protein 1 (SDF2L1) as well as similar proteins from plant, such as Arabidopsis thaliana stromal cell-derived factor 2-like protein (AtSDF2). SDF-2 is a secretory protein involved in multiple endoplasmic reticulum (ER) functions, including the misfolded protein catabolic process, protein glycosylation, and ER protein quality control. SDF2L1, also called PWP1-interacting protein 8, is an endoplasmic reticulum (ER)-localized protein that plays a role in ER-associated degradation (ERAD) of misfolded proinsulin in pancreatic beta-cells. It is a component of the endoplasmic reticulum (ER) chaperone complex and interacts with alpha- and beta-defensins. SDF2L1 may also act as a tumor suppressor that play an important role in a variety of cancers, such as breast cancer and ovarian cancer. AtSDF2, also called SDF2-like protein, acts as crucial component of the unfolded protein response (UPR) in Arabidopsis thaliana. It is involved in the endoplasmic reticulum (ER) protein quality control and unfolded protein response. It may be involved in the quality control of glycoproteins. AtSDF2 forms a complex in the ER with ERDJ3B and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467750 [Multi-domain]  Cd Length: 173  Bit Score: 36.89  E-value: 8.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1N4K_A       14 GDVVRLFHAEQEKFLtcdeHrkkQHVFLRTTGRQSATSA-----TSSKALWEVEvvqhdpCRG-GAGYW--NSLFRFKHL 85
Cdd:cd23279  65 GDIIRLQHVNTRKNL----H---SHNHSSPLSGNQEVSAfgggdEDSGDNWIVE------CEGkKAKFWkrGEPVRLKHV 131


                ....*...
1N4K_A       86 ATGHYLAA 93
Cdd:cd23279 132 DTGKYLSA 139
 
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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