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Conserved domains on  [gi|398366467|ref|NP_010593|]
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putative dolichyl-phosphate-mannose--protein mannosyltransferase [Saccharomyces cerevisiae S288C]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 292-488 4.06e-99

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: 301.66  E-value: 4.06e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 292 LYYGSTITLRHLDSMVGYLASHDISYPSDVDEQLVALSFEEFAADNEWLIEHPTLNLSFSevyHADQLIPVEFGQSIKLR 371
Cdd:cd23286    1 LLYGSTVTIRHLESLGGYLHSHDLTYPSGSNEQQVTLYDFEDDANNEWIIETKTKEQMDK---FPGQFREVRDGDVIRLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 372 HKSTGKLLRASTAKPPISEQDYDFQISCTKDSNYEGGMDERWDVLLIKDEINNDKKdnADDKYIKPLQSEIRFYNNGQRC 451
Cdd:cd23286   78 HVVTGKLLRASNARPPVSEQEYNNEVSCTGNANYSGDMDENWRIDVKGDESHAELK--LPNIKIKSTESVFQLYNRGTGC 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 398366467 452 GLLGHDLRLPEWGRFEQEVLCMEYPVIPRTTFLIDSV 488
Cdd:cd23286  156 TLLSHDTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
PMT_2 super family cl21590
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 104-253 3.33e-05

Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are not captured by pfam02366.


The actual alignment was detected with superfamily member pfam02366:

Pssm-ID: 473917 [Multi-domain]  Cd Length: 245  Bit Score: 45.76  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467  104 LRYVSLFLNSSTLGFLFLITRRINCSRLIS--ATGLLILSNweTFRNEGTIISFDSLewCLFSVV--IYSFISISIAKLG 179
Cdd:pfam02366  85 MRLFSALLGSLTVPLVYLTAKRLGFSKNTAllAALLVILEN--SFITLSRYILLDSP--LLFFTTlsMYCFWKFERKAPF 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366467  180 TTNWFANVITLSISLGLAISSKFIGIVTWAFVILSFVRQFDRLISDVKVTTIQIIKFVILCLLFVLIIPGSIFI 253
Cdd:pfam02366 161 SRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYL 234
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 292-488 4.06e-99

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: 301.66  E-value: 4.06e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 292 LYYGSTITLRHLDSMVGYLASHDISYPSDVDEQLVALSFEEFAADNEWLIEHPTLNLSFSevyHADQLIPVEFGQSIKLR 371
Cdd:cd23286    1 LLYGSTVTIRHLESLGGYLHSHDLTYPSGSNEQQVTLYDFEDDANNEWIIETKTKEQMDK---FPGQFREVRDGDVIRLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 372 HKSTGKLLRASTAKPPISEQDYDFQISCTKDSNYEGGMDERWDVLLIKDEINNDKKdnADDKYIKPLQSEIRFYNNGQRC 451
Cdd:cd23286   78 HVVTGKLLRASNARPPVSEQEYNNEVSCTGNANYSGDMDENWRIDVKGDESHAELK--LPNIKIKSTESVFQLYNRGTGC 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 398366467 452 GLLGHDLRLPEWGRFEQEVLCMEYPVIPRTTFLIDSV 488
Cdd:cd23286  156 TLLSHDTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
292-344 1.01e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.88  E-value: 1.01e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 398366467   292 LYYGSTITLRHLDSMvGYLASHDISYPSDVDEQLVALSFEEFA--ADNEWLIEHP 344
Cdd:smart00472   4 VRWGDVVRLRHVTTG-RYLHSHDEKLPPWGDGQQEVTGYGNPAidANTLWLIEPV 57
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 104-253 3.33e-05

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: 45.76  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467  104 LRYVSLFLNSSTLGFLFLITRRINCSRLIS--ATGLLILSNweTFRNEGTIISFDSLewCLFSVV--IYSFISISIAKLG 179
Cdd:pfam02366  85 MRLFSALLGSLTVPLVYLTAKRLGFSKNTAllAALLVILEN--SFITLSRYILLDSP--LLFFTTlsMYCFWKFERKAPF 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366467  180 TTNWFANVITLSISLGLAISSKFIGIVTWAFVILSFVRQFDRLISDVKVTTIQIIKFVILCLLFVLIIPGSIFI 253
Cdd:pfam02366 161 SRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYL 234
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 292-488 4.06e-99

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: 301.66  E-value: 4.06e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 292 LYYGSTITLRHLDSMVGYLASHDISYPSDVDEQLVALSFEEFAADNEWLIEHPTLNLSFSevyHADQLIPVEFGQSIKLR 371
Cdd:cd23286    1 LLYGSTVTIRHLESLGGYLHSHDLTYPSGSNEQQVTLYDFEDDANNEWIIETKTKEQMDK---FPGQFREVRDGDVIRLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 372 HKSTGKLLRASTAKPPISEQDYDFQISCTKDSNYEGGMDERWDVLLIKDEINNDKKdnADDKYIKPLQSEIRFYNNGQRC 451
Cdd:cd23286   78 HVVTGKLLRASNARPPVSEQEYNNEVSCTGNANYSGDMDENWRIDVKGDESHAELK--LPNIKIKSTESVFQLYNRGTGC 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 398366467 452 GLLGHDLRLPEWGRFEQEVLCMEYPVIPRTTFLIDSV 488
Cdd:cd23286  156 TLLSHDTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 292-486 1.46e-54

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: 184.46  E-value: 1.46e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 292 LYYGSTITLRHLDSMVGYLASHDISYPSDVDEQLVALsFEEFAADNEWLIEHPTLNLSFsevyHADQLIPVEFGQSIKLR 371
Cdd:cd23276    1 VAYGSQITLRNANSGGGYLHSHNHTYPDGSKQQQVTG-YGHKDENNWWQILKPRGDPSS----NPPDPEYVRDGDEVRLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 372 HKSTGKLLRASTAKPPISeqDYDFQISCTKDSNYEGGMDERWDVLLIKDEinndkkDNADDKYIKPLQSEIRFYNNGQRC 451
Cdd:cd23276   76 HKETNRYLRTHDAAAPVT--SKHKEVSAYPDENEDGDDNDLWVVEIVKDE------GKLEDKRIKPLTTRFRLRNKKTGC 147

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 398366467 452 GLLGHDLRLPEWGRFEQEVLCMEYP-VIPRTTFLID 486
Cdd:cd23276  148 YLTSSGVKLPEWGFRQGEVVCSKNKeSDPSTLWNVE 183
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 293-487 2.87e-31

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: 120.48  E-value: 2.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 293 YYGSTITLRHLDSMVGYLASHDISYPSDVDEQLVAL-SFEEfaADNEWLIEHPTLnlsfSEVYHADQLIPVEFGQSIKLR 371
Cdd:cd23283    2 AYGSTIRIRHLNTRGGYLHSHPHNYPAGSKQQQITLyPHRD--ENNDWLVELANA----PEEWSPTTFENLKDGDVVRLE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 372 HKSTGKLLRASTAKPPISEQDYDFQISCTKDSNYEGGMDERWDVLLIKDeinnDKKDNADDKYIKPLQSEIRFYNNGQRC 451
Cdd:cd23283   76 HVATGRRLHSHDHRPPVSDNDWQNEVSAYGYEGFEGDANDDWRVEILKD----DSRPGESKERVRAIDTKFRLVHVMTGC 151

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 398366467 452 GLLGHDLRLPEWGRFEQEVLCMEYPVIPRTTFLIDS 487
Cdd:cd23283  152 YLFSHGVKLPEWGFEQQEVTCAKSGLLELSLWYIET 187
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 294-473 1.57e-16

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: 78.13  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 294 YGSTITLRHLDSMVGYLASHDISYPSDVDEQLVA-LSFEEfaADNEWLIEHPTLNLSFSEvyHADQLIPVEFGQSIKLRH 372
Cdd:cd23284    6 YGSKVTIKNQGLGGGLLHSHVQTYPEGSNQQQVTcYGHKD--SNNEWIFERPRGLPSWDE--NDTDIEFIKDGDIVRLVH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 373 KSTGKLLRASTAKPPISEQDYdfQISC-----TKDSNyeggmdERWDVLLIKDeinndkKDNADDKYIKPLQSEIRFYNN 447
Cdd:cd23284   82 KQTGRNLHSHPVPAPISKSDY--EVSGygdltVGDEK------DNWVIEIVKQ------VGSEDPKKLHTLTTSFRLRHE 147

                        170       180
                 ....*....|....*....|....*.
gi 398366467 448 GQRCGLLGHDLRLPEWGRFEQEVLCM 473
Cdd:cd23284  148 VLGCYLAQTGVSLPEWGFKQGEVVCD 173
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 294-472 6.69e-15

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: 73.11  E-value: 6.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 294 YGSTITLRHLDSMVGYLASHDISYPSDV---DEQLVALSFEEfaADNEWLIEHPTLNLSFSEvyhadqliPVEF---GQS 367
Cdd:cd23282    3 YGSVITLKNHRTGGGYLHSHWHLYPEGVgarQQQVTTYSHKD--DNNLWLIKKHNQSSDLSD--------PVEYvrhGDL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 368 IKLRHKSTGKLLRASTAKPPISEQDYdfQISCTKDsNYEGGMDERWDVLLIKDEINNDkkdnaddkyIKPLQSEIRFYNN 447
Cdd:cd23282   73 IRLEHVNTKRNLHSHKEKAPLTKKHY--QVTGYGE-NGTGDANDVWRVEVVGGREGDP---------VKTVRSKFRLVHY 140

                        170       180
                 ....*....|....*....|....*
gi 398366467 448 GQRCGLLGHDLRLPEWGRFEQEVLC 472
Cdd:cd23282  141 NTGCALHSHGKQLPKWGWEQLEVTC 165
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 292-470 1.96e-11

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: 63.47  E-value: 1.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 292 LYYGSTITLRHLDSMVgYLASHDISYPSDVDE-------QLVALsFEEFAADNEWLIEhPTlnlsFSEVYHADQLIPVEF 364
Cdd:cd23285    1 VHYGDVITIKHRDTNA-FLHSHPERYPLRYEDgrissqgQQVTG-YPHKDANNQWQIL-PT----DPIDEHEGTGRPVRN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 365 GQSIKLRHKSTGKLLR----AS----------TAKPPISEQDYDfqisctkdsnyeggmDERWDVllikdEINNDKkdna 430
Cdd:cd23285   74 GDLIRLRHVSTDTYLLthdvASpltptnmeftTVSDDDTDERYN---------------ETLFRV-----EIEDTD---- 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 398366467 431 DDKYIKPLQSEIRFYNNGQRCGLLGHDLRLPEWGRFEQEV 470
Cdd:cd23285  130 EGDVLKTKSSHFRLIHVDTNVALWTHKKPLPDWGFGQQEV 169
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 292-470 3.96e-11

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: 62.71  E-value: 3.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 292 LYYGSTITLRHLDSMVGYLASHDISYP--------SDVDEQLVALSFEEfaADNEWLIEHPTLnlsfSEVYHADQLIPVE 363
Cdd:cd23281    1 VAYGSQVTLRNTHGSPCWLHSHKHRYPikypdgrgSSHQQQVTCYPFKD--VNNWWIIKDPGR----QDLAVDDPPRPVR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 364 FGQSIKLRHKSTGKLLRASTAKPPISEQDYdfQISCTKDSNYEGGMDERWDVllikdEINNdkkDNADDKYIKPLQSEIR 443
Cdd:cd23281   75 HGDIIQLVHGKTGRFLNSHDVAAPLSPTHQ--EVSCYIDYNISMPAQNLWRI-----EIVN---RDSEGDTWKAIKSQFR 144

                        170       180
                 ....*....|....*....|....*..
gi 398366467 444 FYNNGQRCGLLGHDLRLPEWGRFEQEV 470
Cdd:cd23281  145 LIHVNTSAALKLSGKQLPDWGFGQLEV 171
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 295-472 1.31e-09

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


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 57.78  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 295 GSTITLRHLDsMVGYLASHDISYPSDVDEQLVALSFEEFAAD--NEWLIEhptlnlsfSEVYHADQliPVEFGQSIKLRH 372
Cdd:cd23263    1 GDVIWLKHSE-TGKYLHSHRKNYPTGSGQQEVTFESSSRKGDtnGLWIIE--------SENGKQGG--PVKWGDKIRLRH 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 373 KSTGKLLraSTAKPPISEQDYDFQISCTKDSNYEGGMderWDVLLIKDEINNDKKDNADDKyikplqseIRFYNNGQRCG 452
Cdd:cd23263   70 LSTGKYL--SSEEGKKSPKSNHQEVLCLTDNPDKSSL---FKFEPIGSTKYKQKYVKKDSY--------FRLKHVNTNFW 136

                        170       180
                 ....*....|....*....|
gi 398366467 453 LLGHDLRLPEWGRFEQEVLC 472
Cdd:cd23263  137 LHSHEKKFNINNKTQQEVIC 156
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
292-344 1.01e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.88  E-value: 1.01e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 398366467   292 LYYGSTITLRHLDSMvGYLASHDISYPSDVDEQLVALSFEEFA--ADNEWLIEHP 344
Cdd:smart00472   4 VRWGDVVRLRHVTTG-RYLHSHDEKLPPWGDGQQEVTGYGNPAidANTLWLIEPV 57
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 294-429 2.53e-07

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: 51.15  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 294 YGSTITLRHLDSmvGY-LASHDISYPSDVDEQLVALSFEEFAADNEWLIeHPTLNLSFSEVyhADqliPVEFGQSIKLRH 372
Cdd:cd23279    1 YGSAIKLKHVNS--GYrLHSHEVSYGSGSGQQSVTAVPSADDANSLWTV-LPGLGEPCQEQ--GK---PVKCGDIIRLQH 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398366467 373 KSTGKLLRASTAKPPISEQdydFQISCTKDSNYEGGmDErWDVllikdEINNDKKDN 429
Cdd:cd23279   73 VNTRKNLHSHNHSSPLSGN---QEVSAFGGGDEDSG-DN-WIV-----ECEGKKAKF 119
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
440-488 1.17e-06

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: 1.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 398366467   440 SEIRFYNNGQRCGLLGHDLRLPEWGRFEQEVLCMEYPVI-PRTTFLIDSV 488
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 104-253 3.33e-05

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: 45.76  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467  104 LRYVSLFLNSSTLGFLFLITRRINCSRLIS--ATGLLILSNweTFRNEGTIISFDSLewCLFSVV--IYSFISISIAKLG 179
Cdd:pfam02366  85 MRLFSALLGSLTVPLVYLTAKRLGFSKNTAllAALLVILEN--SFITLSRYILLDSP--LLFFTTlsMYCFWKFERKAPF 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366467  180 TTNWFANVITLSISLGLAISSKFIGIVTWAFVILSFVRQFDRLISDVKVTTIQIIKFVILCLLFVLIIPGSIFI 253
Cdd:pfam02366 161 SRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYL 234
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
360-418 4.68e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.56  E-value: 4.68e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366467   360 IPVEFGQSIKLRHKSTGKLLRASTAKPPiSEQDYDFQISCTKDSnyEGGMDERWDVLLI 418
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEKLP-PWGDGQQEVTGYGNP--AIDANTLWLIEPV 57
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 295-404 2.47e-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: 39.20  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 295 GSTITLRHLDSMvGYLASHDISYPSDVDEQLVALSFEEFAADNEWLIEHPTLNLSFsevyhadqlipVEFGQSIKLRHKS 374
Cdd:cd23279   65 GDIIRLQHVNTR-KNLHSHNHSSPLSGNQEVSAFGGGDEDSGDNWIVECEGKKAKF-----------WKRGEPVRLKHVD 132

                         90       100       110
                 ....*....|....*....|....*....|....
gi 398366467 375 TGKLLRASTAK----PPISEQdydFQISCTKDSN 404
Cdd:cd23279  133 TGKYLSASKTHkftqQPIAGQ---LEVSAASSKD 163
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 294-399 2.94e-03

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: 39.28  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366467 294 YGSTITLRHlDSMVGYLASHDISYPSDVDEQLVAlSFEEFAADNE-WLIEhPTLNLSFSevyhadQLIPVEFGQSIKLRH 372
Cdd:cd23294    3 CGSVIKLQH-ERTKFRLHSHEVPYGSGSGQQSVT-GFPGVDDSNSyWIVK-PANGERCK------QGDVIKNGDVIRLQH 73

                         90       100
                 ....*....|....*....|....*..
gi 398366467 373 KSTGKLLRASTAKPPISEQDydfQISC 399
Cdd:cd23294   74 VSTRKWLHSHLHASPLSGNQ---EVSC 97
 
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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