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Conserved domains on  [gi|17508635|ref|NP_491320|]
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MIR domain-containing protein [Caenorhabditis elegans]

Protein Classification

dolichyl-phosphate-mannose--protein mannosyltransferase( domain architecture ID 1001097)

dolichyl-phosphate-mannose--protein mannosyltransferase is a glycosyltransferase family 39 protein that transfers mannosyl residues to the hydroxyl group of serine or threonine residues, initiating the assembly of O-mannosyl glycans

EC:  2.4.1.109
Gene Ontology:  GO:0000030|GO:0016740|GO:0016757|GO:0005789
PubMed:  31285605|20378538|15809069

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 26-201 3.02e-111

MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 (SDF-2); The metazoan SDF-2 family includes SDF-2 and SDF2-like protein 1 (SDF2L1). 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. 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: 467764 [Multi-domain]  Cd Length: 175  Bit Score: 315.37  E-value: 3.02e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  26 VTCYSVLKFINANDGSRLHSHDVKYGSGSGQQSVTAVKNSDDINSHWQIFPALNAKCNRGDAIKCGDKIRLKHLTTGTFL 105
Cdd:cd23293   1 VTCGSVVKLLNTRHNVRLHSHDVKYGSGSGQQSVTGVESSDDSNSYWQIRGPTGADCERGTPIKCGQTIRLTHLNTGKNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635 106 HSHHFTAPLSkQHQEVSAFGSEAESDTGDDWTVICNGDEWLESEQFKLRHAVTGSYLSLSGQQFGRPIHGQREVVGTDSI 185
Cdd:cd23293  81 HSHHFQSPLS-GNQEVSAFGEDGEGDTGDNWTVVCSGTYWERDEAVRLKHVDTEVYLHVTGEQYGRPIHGQREVSGMSSP 159

                       170
                ....*....|....*.
gi 17508635 186 TGGSAWKVAEGIYIKH 201
Cdd:cd23293 160 SQANYWKAMEGIFIKP 175
 
Name Accession Description Interval E-value
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 26-201 3.02e-111

MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 (SDF-2); The metazoan SDF-2 family includes SDF-2 and SDF2-like protein 1 (SDF2L1). 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. 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: 467764 [Multi-domain]  Cd Length: 175  Bit Score: 315.37  E-value: 3.02e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  26 VTCYSVLKFINANDGSRLHSHDVKYGSGSGQQSVTAVKNSDDINSHWQIFPALNAKCNRGDAIKCGDKIRLKHLTTGTFL 105
Cdd:cd23293   1 VTCGSVVKLLNTRHNVRLHSHDVKYGSGSGQQSVTGVESSDDSNSYWQIRGPTGADCERGTPIKCGQTIRLTHLNTGKNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635 106 HSHHFTAPLSkQHQEVSAFGSEAESDTGDDWTVICNGDEWLESEQFKLRHAVTGSYLSLSGQQFGRPIHGQREVVGTDSI 185
Cdd:cd23293  81 HSHHFQSPLS-GNQEVSAFGEDGEGDTGDNWTVVCSGTYWERDEAVRLKHVDTEVYLHVTGEQYGRPIHGQREVSGMSSP 159

                       170
                ....*....|....*.
gi 17508635 186 TGGSAWKVAEGIYIKH 201
Cdd:cd23293 160 SQANYWKAMEGIFIKP 175
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 34-180 2.69e-14

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: 68.16  E-value: 2.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635    34 FINANDGSRL-HSHDVKYGSGSGQQ------SVTAVKNSDDIN---SHWQIFPALNAKCnRGDAIKCGDKIRLKHLTTGT 103
Cdd:pfam02815   2 YLKGGDVVRLfHSHQDEYLTGSEQQqkqpflRITLYPHGDANNsarSLWRIEVVRHDAW-RGGLIKWGSPFRLRHLTTGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635   104 FLHSH-HFTAPLS---KQHQEVSAFGSEAESDTGDDWTVICNGDEWLESEQ--------FKLRHAVTGSYLSLSGQQF-- 169
Cdd:pfam02815  81 YLHSHeEQKPPLVekeDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDrikpgdsyFRLQHVCTGCWLFSHSVKLpk 160

                         170
                  ....*....|.
gi 17508635   170 GRPIHGQREVV 180
Cdd:pfam02815 161 WGFGPEQQKVT 171
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
85-141 1.44e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 57.35  E-value: 1.44e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 17508635     85 GDAIKCGDKIRLKHLTTGTFLHSHHFT-APLSKQHQEVSAFGSEAESDTgDDWTVICN 141
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAIDAN-TLWLIEPV 57
 
Name Accession Description Interval E-value
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 26-201 3.02e-111

MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 (SDF-2); The metazoan SDF-2 family includes SDF-2 and SDF2-like protein 1 (SDF2L1). 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. 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: 467764 [Multi-domain]  Cd Length: 175  Bit Score: 315.37  E-value: 3.02e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  26 VTCYSVLKFINANDGSRLHSHDVKYGSGSGQQSVTAVKNSDDINSHWQIFPALNAKCNRGDAIKCGDKIRLKHLTTGTFL 105
Cdd:cd23293   1 VTCGSVVKLLNTRHNVRLHSHDVKYGSGSGQQSVTGVESSDDSNSYWQIRGPTGADCERGTPIKCGQTIRLTHLNTGKNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635 106 HSHHFTAPLSkQHQEVSAFGSEAESDTGDDWTVICNGDEWLESEQFKLRHAVTGSYLSLSGQQFGRPIHGQREVVGTDSI 185
Cdd:cd23293  81 HSHHFQSPLS-GNQEVSAFGEDGEGDTGDNWTVVCSGTYWERDEAVRLKHVDTEVYLHVTGEQYGRPIHGQREVSGMSSP 159

                       170
                ....*....|....*.
gi 17508635 186 TGGSAWKVAEGIYIKH 201
Cdd:cd23293 160 SQANYWKAMEGIFIKP 175
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 28-196 8.24e-75

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: 222.94  E-value: 8.24e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  28 CYSVLKFINANDGSRLHSHDVKYGSGSGQQSVTAVKNSDDINSHWQIFPALNAKCN-RGDAIKCGDKIRLKHLTTGTFLH 106
Cdd:cd23279   1 YGSAIKLKHVNSGYRLHSHEVSYGSGSGQQSVTAVPSADDANSLWTVLPGLGEPCQeQGKPVKCGDIIRLQHVNTRKNLH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635 107 SHHFTAPLSKQhQEVSAFGSEAEsDTGDDWTVICNGDE---WLESEQFKLRHAVTGSYLSLSGQQFGR--PIHGQREVVG 181
Cdd:cd23279  81 SHNHSSPLSGN-QEVSAFGGGDE-DSGDNWIVECEGKKakfWKRGEPVRLKHVDTGKYLSASKTHKFTqqPIAGQLEVSA 158

                       170
                ....*....|....*
gi 17508635 182 TDSITGGSAWKVAEG 196
Cdd:cd23279 159 ASSKDSDSQWKAVEG 173
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 26-198 4.54e-62

MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor 2-like protein (AtSDF2) and similar proteins; AtSDF2, also called SDF2-like protein, acts as a 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. AtSDF2 contains 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: 467765 [Multi-domain]  Cd Length: 176  Bit Score: 190.66  E-value: 4.54e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  26 VTCYSVLKFINANDGSRLHSHDVKYGSGSGQQSVTAVKNSDDINSHWQIFPALNAKCNRGDAIKCGDKIRLKHLTTGTFL 105
Cdd:cd23294   1 VTCGSVIKLQHERTKFRLHSHEVPYGSGSGQQSVTGFPGVDDSNSYWIVKPANGERCKQGDVIKNGDVIRLQHVSTRKWL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635 106 HSHHFTAPLSKQhQEVSAFGSEAESDTGDDWTVICNG--DEWLESEQFKLRHAVTGSYLSLSGQQFGRPIHGQREVVGTD 183
Cdd:cd23294  81 HSHLHASPLSGN-QEVSCFGGDGNSDTGDNWIVEIEGggKVWERDQKVRLKHVDTGGYLHSHDKKYGRPIPGQQEVCAVA 159

                       170
                ....*....|....*
gi 17508635 184 SITGGSAWKVAEGIY 198
Cdd:cd23294 160 SKNSNTLWLAAEGVY 174
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 39-179 2.61e-26

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 1 (PMT1) 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 PMT1 and PMT5. PMT1 forms a heterodimeric complex with PMT2 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. PMT5 form a functional heterodimer with PMT3 and more rarely with PMT1. 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: 467754 [Multi-domain]  Cd Length: 190  Bit Score: 99.68  E-value: 2.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  39 DGSRLHSHDVKYGSGSGQQSVTAVKNSDDiNSHWQIFPALNAKCNRGDA---IKCGDKIRLKHLTTGTFLHSHHFTAPLS 115
Cdd:cd23283  15 RGGYLHSHPHNYPAGSKQQQITLYPHRDE-NNDWLVELANAPEEWSPTTfenLKDGDVVRLEHVATGRRLHSHDHRPPVS 93

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17508635 116 KQ--HQEVSAFGSEA-ESDTGDDWTV-ICNGD----------EWLESeQFKLRHAVTGSYLSLSGQQFGRPIHGQREV 179
Cdd:cd23283  94 DNdwQNEVSAYGYEGfEGDANDDWRVeILKDDsrpgeskervRAIDT-KFRLVHVMTGCYLFSHGVKLPEWGFEQQEV 170
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 32-193 1.41e-24

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: 95.09  E-value: 1.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  32 LKFINANDGSrLHSHDVKYGSGSGQQSVTaVKNSDDINSHWQI-FPALNAKCNRGDA--IKCGDKIRLKHLTTGTFLHSH 108
Cdd:cd23276   9 LRNANSGGGY-LHSHNHTYPDGSKQQQVT-GYGHKDENNWWQIlKPRGDPSSNPPDPeyVRDGDEVRLLHKETNRYLRTH 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635 109 HFTAPLSKQHQEVSAFG-SEAESDTGDDWTV-ICNGDEWLESE-------QFKLRHAVTGSYLSLSGQQfgRPI--HGQR 177
Cdd:cd23276  87 DAAAPVTSKHKEVSAYPdENEDGDDNDLWVVeIVKDEGKLEDKrikplttRFRLRNKKTGCYLTSSGVK--LPEwgFRQG 164

                       170
                ....*....|....*...
gi 17508635 178 EVVGTDSIT--GGSAWKV 193
Cdd:cd23276 165 EVVCSKNKEsdPSTLWNV 182
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 37-166 6.36e-24

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: 93.54  E-value: 6.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  37 ANDGSRLHSHDVKYGSGSGQQSVTAVKNSDDiNSHWQIFPAL-------NAKCNRgdAIKCGDKIRLKHLTTGTFLHSHH 109
Cdd:cd23284  16 GLGGGLLHSHVQTYPEGSNQQQVTCYGHKDS-NNEWIFERPRglpswdeNDTDIE--FIKDGDIVRLVHKQTGRNLHSHP 92

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635 110 FTAPLSKQHQEVSAFGSEAESDTGDDWTVicngdEWLE-------------SEQFKLRHAVTGSYLSLSG 166
Cdd:cd23284  93 VPAPISKSDYEVSGYGDLTVGDEKDNWVI-----EIVKqvgsedpkklhtlTTSFRLRHEVLGCYLAQTG 157
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 40-195 2.15e-23

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: 91.68  E-value: 2.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  40 GSRLHSHDVKYGSGSGQQSVTAVKNSDDINSH--WQIFPALNAKcnrGDAIKCGDKIRLKHLTTGTFLHSHHFTAPLSKQ 117
Cdd:cd23263  12 GKYLHSHRKNYPTGSGQQEVTFESSSRKGDTNglWIIESENGKQ---GGPVKWGDKIRLRHLSTGKYLSSEEGKKSPKSN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635 118 HQEVSAFGseAESDTGDDWTVICNGDE-----WLESEQ-FKLRHAVTGSYLSLSGQQFGRPIHGQREVVGTDSITGGSAW 191
Cdd:cd23263  89 HQEVLCLT--DNPDKSSLFKFEPIGSTkykqkYVKKDSyFRLKHVNTNFWLHSHEKKFNINNKTQQEVICHGEREEVFKL 166


                ....
gi 17508635 192 KVAE 195
Cdd:cd23263 167 WKAE 170
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 40-179 1.81e-22

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar proteins; POMT2 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 2, is a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids. POMT2 transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins. POMT2 contains 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: 467753 [Multi-domain]  Cd Length: 183  Bit Score: 89.67  E-value: 1.81e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  40 GSRLHSHDVKY--GSGSGQQSVTAVKNSDDiNSHWQIFPAlNAKCNRGDAI---KCGDKIRLKHLTTGTFLHSHHFTAPL 114
Cdd:cd23282  16 GGYLHSHWHLYpeGVGARQQQVTTYSHKDD-NNLWLIKKH-NQSSDLSDPVeyvRHGDLIRLEHVNTKRNLHSHKEKAPL 93

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635 115 SKQHQEVSAFGSEAESDTGDDWTV-ICNG--DEWLES--EQFKLRHAVTGSYLSLSGQQFGRPIHGQREV 179
Cdd:cd23282  94 TKKHYQVTGYGENGTGDANDVWRVeVVGGreGDPVKTvrSKFRLVHYNTGCALHSHGKQLPKWGWEQLEV 163
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 43-198 5.77e-20

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar proteins; POMT1 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 1, belongs to the glycosyltransferase 39 family. It transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins, but not of cadherins and protocaherins. POMT1 contains 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: 467752 [Multi-domain]  Cd Length: 191  Bit Score: 83.13  E-value: 5.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  43 LHSHD----VKYGSG---SGQQSVTAVKNSDDINshWQIFPALNAK----CNRGDAIKCGDKIRLKHLTTGTFLHSHHFT 111
Cdd:cd23281  19 LHSHKhrypIKYPDGrgsSHQQQVTCYPFKDVNN--WWIIKDPGRQdlavDDPPRPVRHGDIIQLVHGKTGRFLNSHDVA 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635 112 APLSKQHQEVSAF-GSEAESDTGDDWTVICN-----GDEWLESE-QFKLRHAVTGSYLSLSGQQFGRPIHGQREVVGT-D 183
Cdd:cd23281  97 APLSPTHQEVSCYiDYNISMPAQNLWRIEIVnrdseGDTWKAIKsQFRLIHVNTSAALKLSGKQLPDWGFGQLEVATDrA 176

                       170
                ....*....|....*
gi 17508635 184 SITGGSAWKVAEGIY 198
Cdd:cd23281 177 GNQSSTVWNVEEHRY 191
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 29-195 2.31e-19

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 4 (PMT4) 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 PMT4. It forms a functional homodimer and may form a heterodimer with PMT6. PMT4 specifically acts on secretory proteins with an ER-luminally oriented Ser/Thr-rich region flanked by a membrane anchor such as FUS1, AXL2, GAS1, KEX2, MID2, WSC1, WSC2, OPY2, PRM5, RAX2, or YNL176. 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: 467756 [Multi-domain]  Cd Length: 187  Bit Score: 81.57  E-value: 2.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  29 YSVLKFINANDGSRLHSHDVKYG--------SGSGQQsVTAVKNsDDINSHWQIFPA--LNAKCNRGDAIKCGDKIRLKH 98
Cdd:cd23285   4 GDVITIKHRDTNAFLHSHPERYPlryedgriSSQGQQ-VTGYPH-KDANNQWQILPTdpIDEHEGTGRPVRNGDLIRLRH 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  99 LTTGTFLHSHHFTAPLSKQHQEVSaFGSEAESDTGDDWTV----ICNGDE----WLESEQFKLRHAVTGSYLSLSGQQFG 170
Cdd:cd23285  82 VSTDTYLLTHDVASPLTPTNMEFT-TVSDDDTDERYNETLfrveIEDTDEgdvlKTKSSHFRLIHVDTNVALWTHKKPLP 160

                       170       180
                ....*....|....*....|....*.
gi 17508635 171 RPIHGQREVVGTDSITGGSA-WKVAE 195
Cdd:cd23285 161 DWGFGQQEVNGNKNIKDKSNiWVVDD 186
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 40-162 1.39e-15

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 7 (PMT7) 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 PMT7. 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: 467757 [Multi-domain]  Cd Length: 192  Bit Score: 71.70  E-value: 1.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  40 GSRLHSHDVKYGSGSGQQSVTAVKNSDDINSHWQIFPALNA----KCNRGDAIKCGDKIRLKHLTTGTFLHSHHFTAPLS 115
Cdd:cd23286  16 GGYLHSHDLTYPSGSNEQQVTLYDFEDDANNEWIIETKTKEqmdkFPGQFREVRDGDVIRLRHVVTGKLLRASNARPPVS 95

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17508635 116 KQ--HQEVSAFGSEAES-DTGDDWTVICNGDEWLESEQ------------FKLRHAVTGSYL 162
Cdd:cd23286  96 EQeyNNEVSCTGNANYSgDMDENWRIDVKGDESHAELKlpnikikstesvFQLYNRGTGCTL 157
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 34-180 2.69e-14

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: 68.16  E-value: 2.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635    34 FINANDGSRL-HSHDVKYGSGSGQQ------SVTAVKNSDDIN---SHWQIFPALNAKCnRGDAIKCGDKIRLKHLTTGT 103
Cdd:pfam02815   2 YLKGGDVVRLfHSHQDEYLTGSEQQqkqpflRITLYPHGDANNsarSLWRIEVVRHDAW-RGGLIKWGSPFRLRHLTTGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635   104 FLHSH-HFTAPLS---KQHQEVSAFGSEAESDTGDDWTVICNGDEWLESEQ--------FKLRHAVTGSYLSLSGQQF-- 169
Cdd:pfam02815  81 YLHSHeEQKPPLVekeDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSDrikpgdsyFRLQHVCTGCWLFSHSVKLpk 160

                         170
                  ....*....|.
gi 17508635   170 GRPIHGQREVV 180
Cdd:pfam02815 161 WGFGPEQQKVT 171
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 91-193 2.69e-13

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: 65.10  E-value: 2.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  91 GDKIRLKHLTTGTFLHSHHFTAPLSKQHQEVSAFGSEAESDTGDDWTVICNGDEW---LESEQ-FKLRHAVTGSYLSLSG 166
Cdd:cd23263   1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQggpVKWGDkIRLRHLSTGKYLSSEE 80

                        90       100
                ....*....|....*....|....*..
gi 17508635 167 QQFGRPIHGQREVVGTDSITGGSAWKV 193
Cdd:cd23263  81 GKKSPKSNHQEVLCLTDNPDKSSLFKF 107
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
85-141 1.44e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 57.35  E-value: 1.44e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 17508635     85 GDAIKCGDKIRLKHLTTGTFLHSHHFT-APLSKQHQEVSAFGSEAESDTgDDWTVICN 141
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAIDAN-TLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
23-77 4.00e-09

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 50.80  E-value: 4.00e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 17508635     23 EDFVTCYSVLKFINANDGSRLHSHDVKYG-SGSGQQSVTAVKNSD-DINSHWQIFPA 77
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPpWGDGQQEVTGYGNPAiDANTLWLIEPV 57
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 91-165 1.04e-07

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 7 (PMT7) 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 PMT7. 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: 467757 [Multi-domain]  Cd Length: 192  Bit Score: 50.13  E-value: 1.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  91 GDKIRLKHL-TTGTFLHSHHFTAPLSKQHQEVsaFGSEAESDTGDDWTVICNGDEWLES--EQF---------KLRHAVT 158
Cdd:cd23286   4 GSTVTIRHLeSLGGYLHSHDLTYPSGSNEQQV--TLYDFEDDANNEWIIETKTKEQMDKfpGQFrevrdgdviRLRHVVT 81


                ....*..
gi 17508635 159 GSYLSLS 165
Cdd:cd23286  82 GKLLRAS 88
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 65-163 1.36e-07

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: 49.69  E-value: 1.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635  65 SDDINSHWQIfpALNAKCNRGDAIKCGDKIRLKHLTTGTFLHSHHFTAPLskqhqEVSafgseAESDTGDDWTVIC---- 140
Cdd:cd23280  57 PTSGDTFWQI--EKEDTPLKGGVIKWGDQCRLRHLPTGKYLAVDDKTGNG-----KVV-----LTSDPSDPSTVFRlhpv 124

                        90       100
                ....*....|....*....|....*.
gi 17508635 141 ---NGDEWLESEQFKLRHAVTGSYLS 163
Cdd:cd23280 125 tkeTSEEVKFGSYVRIEHVATGTWLH 150
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
143-195 1.88e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 43.48  E-value: 1.88e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 17508635    143 DEWLESEQ-FKLRHAVTGSYLSLSGQQFGRPIHGQREVVGTDSITG--GSAWKVAE 195
Cdd:smart00472   1 GGFVRWGDvVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdaNTLWLIEP 56
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 24-113 1.76e-04

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: 40.81  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508635    24 DFVTCYSVLKFINANDGSRLHSHDVK----YGSGSGQQSVTA--VKNSDDINSHWQIFPALNAKCNRGDAIKCGD-KIRL 96
Cdd:pfam02815  63 GLIKWGSPFRLRHLTTGRYLHSHEEQkpplVEKEDWQKEVSAygFRGFPGDNDIVEIFEKKSTTGMGSDRIKPGDsYFRL 142

                          90
                  ....*....|....*..
gi 17508635    97 KHLTTGTFLHSHHFTAP 113
Cdd:pfam02815 143 QHVCTGCWLFSHSVKLP 159
 
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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