putative dolichyl-phosphate-mannose--protein mannosyltransferase [Ustilago hordei]
Protein Classification
dolichyl-phosphate-mannose--protein mannosyltransferase( domain architecture ID 11449133)
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
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| beta-trefoil_MIR_PMT2-like | cd23284 | MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ... |
360-558 | 6.35e-103 | |||||
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: 314.64 E-value: 6.35e-103
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| PMT | pfam02366 | Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ... |
91-334 | 2.32e-68 | |||||
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families. : Pssm-ID: 396786 [Multi-domain] Cd Length: 245 Bit Score: 225.65 E-value: 2.32e-68
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| PMT_4TMC | pfam16192 | C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ... |
575-783 | 2.67e-63 | |||||
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes. : Pssm-ID: 465056 Cd Length: 198 Bit Score: 210.48 E-value: 2.67e-63
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| Name | Accession | Description | Interval | E-value | |||||
| beta-trefoil_MIR_PMT2-like | cd23284 | MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ... |
360-558 | 6.35e-103 | |||||
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: 314.64 E-value: 6.35e-103
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| PMT | pfam02366 | Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ... |
91-334 | 2.32e-68 | |||||
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families. Pssm-ID: 396786 [Multi-domain] Cd Length: 245 Bit Score: 225.65 E-value: 2.32e-68
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| PMT_4TMC | pfam16192 | C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ... |
575-783 | 2.67e-63 | |||||
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes. Pssm-ID: 465056 Cd Length: 198 Bit Score: 210.48 E-value: 2.67e-63
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| MIR | pfam02815 | MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ... |
380-549 | 4.38e-25 | |||||
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: 102.83 E-value: 4.38e-25
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| PMT1 | COG1928 | Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ... |
73-331 | 3.05e-15 | |||||
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441531 [Multi-domain] Cd Length: 495 Bit Score: 79.17 E-value: 3.05e-15
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| MIR | smart00472 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
498-554 | 1.72e-07 | |||||
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 48.49 E-value: 1.72e-07
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| PMT1 | COG1928 | Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ... |
574-725 | 1.34e-06 | |||||
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441531 [Multi-domain] Cd Length: 495 Bit Score: 51.82 E-value: 1.34e-06
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| TIGR03663 | TIGR03663 | TIGR03663 family protein; Members of this protein family, uncommon and rather sporadically ... |
87-265 | 1.51e-03 | |||||
TIGR03663 family protein; Members of this protein family, uncommon and rather sporadically distributed, are found almost always in the same genomes as members of family TIGR03662, and frequently as a nearby gene. Members show some N-terminal sequence similarity with pfam02366, dolichyl-phosphate-mannose-protein mannosyltransferase. The few invariant residues in this family, found toward the N-terminus, include a dipeptide DE, a tripeptide HGP, and two different Arg residues. Up to three members may be found in a genome. The function is unknown. Pssm-ID: 274709 Cd Length: 439 Bit Score: 41.65 E-value: 1.51e-03
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| Name | Accession | Description | Interval | E-value | |||||
| beta-trefoil_MIR_PMT2-like | cd23284 | MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ... |
360-558 | 6.35e-103 | |||||
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: 314.64 E-value: 6.35e-103
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| PMT | pfam02366 | Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ... |
91-334 | 2.32e-68 | |||||
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families. Pssm-ID: 396786 [Multi-domain] Cd Length: 245 Bit Score: 225.65 E-value: 2.32e-68
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| beta-trefoil_MIR_POMT2 | cd23282 | MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ... |
364-558 | 6.23e-68 | |||||
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: 222.18 E-value: 6.23e-68
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| beta-trefoil_MIR_PMT | cd23276 | MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ... |
364-556 | 6.72e-65 | |||||
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: 214.12 E-value: 6.72e-65
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| PMT_4TMC | pfam16192 | C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ... |
575-783 | 2.67e-63 | |||||
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes. Pssm-ID: 465056 Cd Length: 198 Bit Score: 210.48 E-value: 2.67e-63
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| beta-trefoil_MIR_PMT1-like | cd23283 | MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ... |
364-555 | 2.99e-59 | |||||
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: 199.06 E-value: 2.99e-59
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| beta-trefoil_MIR_POMT1 | cd23281 | MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ... |
364-556 | 1.05e-39 | |||||
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: 145.14 E-value: 1.05e-39
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| beta-trefoil_MIR_PMT7-like | cd23286 | MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ... |
365-554 | 3.02e-32 | |||||
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: 123.70 E-value: 3.02e-32
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| beta-trefoil_MIR_PMT4-like | cd23285 | MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ... |
365-554 | 1.33e-30 | |||||
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: 118.94 E-value: 1.33e-30
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| beta-trefoil_MIR_SDF2-like | cd23279 | MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ... |
365-544 | 6.94e-28 | |||||
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: 110.47 E-value: 6.94e-28
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| beta-trefoil_MIR_AtSDF2-like | cd23294 | MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ... |
366-551 | 1.29e-27 | |||||
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: 109.77 E-value: 1.29e-27
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| MIR | pfam02815 | MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ... |
380-549 | 4.38e-25 | |||||
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: 102.83 E-value: 4.38e-25
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| beta-trefoil_MIR | cd23263 | MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ... |
366-555 | 2.85e-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: 97.45 E-value: 2.85e-23
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| beta-trefoil_MIR_SDF2_meta | cd23293 | MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ... |
366-519 | 1.26e-18 | |||||
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: 84.25 E-value: 1.26e-18
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| PMT1 | COG1928 | Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ... |
73-331 | 3.05e-15 | |||||
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441531 [Multi-domain] Cd Length: 495 Bit Score: 79.17 E-value: 3.05e-15
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| beta-trefoil_MIR | cd23263 | MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ... |
437-556 | 1.16e-14 | |||||
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: 72.42 E-value: 1.16e-14
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| ArnT | COG1807 | PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ... |
90-330 | 4.34e-10 | |||||
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441412 [Multi-domain] Cd Length: 309 Bit Score: 61.56 E-value: 4.34e-10
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| MIR | smart00472 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
498-554 | 1.72e-07 | |||||
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 48.49 E-value: 1.72e-07
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| PMT1 | COG1928 | Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ... |
574-725 | 1.34e-06 | |||||
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441531 [Multi-domain] Cd Length: 495 Bit Score: 51.82 E-value: 1.34e-06
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| PMT | COG4745 | Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ... |
93-346 | 1.20e-05 | |||||
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General function prediction only]; Pssm-ID: 443779 [Multi-domain] Cd Length: 550 Bit Score: 48.89 E-value: 1.20e-05
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| MIR | smart00472 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
434-487 | 1.75e-05 | |||||
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 42.71 E-value: 1.75e-05
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| MIR | smart00472 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
364-414 | 2.70e-05 | |||||
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 42.33 E-value: 2.70e-05
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| TIGR03663 | TIGR03663 | TIGR03663 family protein; Members of this protein family, uncommon and rather sporadically ... |
87-265 | 1.51e-03 | |||||
TIGR03663 family protein; Members of this protein family, uncommon and rather sporadically distributed, are found almost always in the same genomes as members of family TIGR03662, and frequently as a nearby gene. Members show some N-terminal sequence similarity with pfam02366, dolichyl-phosphate-mannose-protein mannosyltransferase. The few invariant residues in this family, found toward the N-terminus, include a dipeptide DE, a tripeptide HGP, and two different Arg residues. Up to three members may be found in a genome. The function is unknown. Pssm-ID: 274709 Cd Length: 439 Bit Score: 41.65 E-value: 1.51e-03
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