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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569167299   1 IRLQHVATKKNLHSHYFSSPLSGNQEVSCYgDGDGEGDSGDNWTVVCNNDYWRRDSPVKLKHV 63
Cdd:cd23293    69 IRLTHLNTGKNLHSHHFQSPLSGNQEVSAF-GEDGEGDTGDNWTVVCSGTYWERDEAVRLKHV 130

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569167299   1 IRLQHVATKKNLHSHYFSSPLSGNQEVSCYgDGDGEGDSGDNWTVVCNNDYWRRDSPVKLKHV 63
Cdd:cd23293    69 IRLTHLNTGKNLHSHHFQSPLSGNQEVSAF-GEDGEGDTGDNWTVVCSGTYWERDEAVRLKHV 130

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2569167299   1 IRLQHVATKKNLHSHYFSSP-----LSGNQEVSCY 30
Cdd:pfam02815  71 FRLRHLTTGRYLHSHEEQKPplvekEDWQKEVSAY 105

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569167299   1 IRLQHVATKKNLHSHYFSSPLSGNQEVSCYgDGDGEGDSGDNWTVVCNNDYWRRDSPVKLKHV 63
Cdd:cd23293    69 IRLTHLNTGKNLHSHHFQSPLSGNQEVSAF-GEDGEGDTGDNWTVVCSGTYWERDEAVRLKHV 130

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569167299   1 IRLQHVATKKNLHSHYFSSPLSGNQEVSCYgDGDGEGDSGDNWTVVCNN--DYWRRDSPVKLKHV 63
Cdd:cd23294    69 IRLQHVSTRKWLHSHLHASPLSGNQEVSCF-GGDGNSDTGDNWIVEIEGggKVWERDQKVRLKHV 132

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.

                          10        20        30
                  ....*....|....*....|....*....|.
gi 2569167299   1 IRLQHVATKKNLHSHYFSSPLSGN-QEVSCY 30
Cdd:cd23282    73 IRLEHVNTKRNLHSHKEKAPLTKKhYQVTGY 103

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.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 2569167299   1 IRLQHVATKKNLHSHYFSSPLSGN---QEVSCY 30
Cdd:cd23283    72 VRLEHVATGRRLHSHDHRPPVSDNdwqNEVSAY 104

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2569167299   1 IRLQHVATKKNLHSHYFSSPLS-GNQEVSCYgdgdgegdsgDNWTVVCNNDYWR 53
Cdd:cd23284    77 VRLVHKQTGRNLHSHPVPAPISkSDYEVSGY----------GDLTVGDEKDNWV 120

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2569167299   1 IRLQHVATKKNLHSHYFSSP-----LSGNQEVSCY 30
Cdd:pfam02815  71 FRLRHLTTGRYLHSHEEQKPplvekEDWQKEVSAY 105

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.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 2569167299   1 IRLQHVATKKNLHS--HYFSSPLSGNQEVSCY 30
Cdd:cd23293   125 VRLKHVDTEVYLHVtgEQYGRPIHGQREVSGM 156