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Conserved domains on  [gi|766431904|gb|AJR57025|]
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Pmt4p [Saccharomyces cerevisiae YJM981]

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_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 334-521 1.60e-103

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: 315.39  E-value: 1.60e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 334 VNYFDIITIKHQDTDAFLHSHLARYPQRYEDGRISSAGQQVTGYTHPDFNNQWEVLPPHGSD--VGKGQAVLLNQHIRLR 411
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDehEGTGRPVRNGDLIRLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 412 HVATDTYLLAHDVASPFYPTNEEITTVTLEEGDgELYPETLFAFQpLKKSDEGHVLKSKTVSFRLFHVDTSVALWTHNDE 491
Cdd:cd23285   81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVE-IEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKP 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 766431904 492 lLPDWGFQQQEINGNKKVIDPSNNWVVDEI 521
Cdd:cd23285  159 -LPDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 58-305 6.40e-84

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: 266.48  E-value: 6.40e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904   58 IVTLLAFAARFYKIWYPKEVVFDEVHFGKFASYYLERSYFFDVHPPFAKMMIAFIGWLCGYDGSFKFDEIGYSYETHPAP 137
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  138 YIAYRSFNAILGTLTVPIMFNTLKELNFRAITCAFASLLVAIDTAHVTETRLILLDAILIISIAATMYCYVRFYKcqlRQ 217
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER---KA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  218 PFTWSWYIWLHATGLSLSFVISTKYVGVMTYSAIGFAVVVNLWQLLDIKAGLSLRQFMrHFSKRLNGLVLIPFVIYLFWF 297
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWK-HLFARLFCLIVIPWALYLAQF 237


                  ....*...
gi 766431904  298 WVHFTVLN 305
Cdd:pfam02366 238 YVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 543-755 2.99e-71

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: 231.28  E-value: 2.99e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  543 KKWIETQKSMFEHNNKLSSEHPFASEPYSWPGSLSGVSFWTNGDEKKQIYFIGNIIGWWFQVISLAVFVGIIVADLITRH 622
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  623 RGYYAL-NKMTREKLYGPLMFFFVSWCCHYFPFFLMARQKFLHHYLPAHLIACLFSGALWEVIFSDCKSLDLEKDEDIsg 701
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLRKRV-- 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 766431904  702 asyernpkvyvkpYTVFLVCVSCAVAWFFVYFSPLVYGDVSLSpSEVVSREWFD 755
Cdd:pfam16192 159 -------------GYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 334-521 1.60e-103

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: 315.39  E-value: 1.60e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 334 VNYFDIITIKHQDTDAFLHSHLARYPQRYEDGRISSAGQQVTGYTHPDFNNQWEVLPPHGSD--VGKGQAVLLNQHIRLR 411
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDehEGTGRPVRNGDLIRLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 412 HVATDTYLLAHDVASPFYPTNEEITTVTLEEGDgELYPETLFAFQpLKKSDEGHVLKSKTVSFRLFHVDTSVALWTHNDE 491
Cdd:cd23285   81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVE-IEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKP 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 766431904 492 lLPDWGFQQQEINGNKKVIDPSNNWVVDEI 521
Cdd:cd23285  159 -LPDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 58-305 6.40e-84

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: 266.48  E-value: 6.40e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904   58 IVTLLAFAARFYKIWYPKEVVFDEVHFGKFASYYLERSYFFDVHPPFAKMMIAFIGWLCGYDGSFKFDEIGYSYETHPAP 137
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  138 YIAYRSFNAILGTLTVPIMFNTLKELNFRAITCAFASLLVAIDTAHVTETRLILLDAILIISIAATMYCYVRFYKcqlRQ 217
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER---KA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  218 PFTWSWYIWLHATGLSLSFVISTKYVGVMTYSAIGFAVVVNLWQLLDIKAGLSLRQFMrHFSKRLNGLVLIPFVIYLFWF 297
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWK-HLFARLFCLIVIPWALYLAQF 237


                  ....*...
gi 766431904  298 WVHFTVLN 305
Cdd:pfam02366 238 YVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 543-755 2.99e-71

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: 231.28  E-value: 2.99e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  543 KKWIETQKSMFEHNNKLSSEHPFASEPYSWPGSLSGVSFWTNGDEKKQIYFIGNIIGWWFQVISLAVFVGIIVADLITRH 622
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  623 RGYYAL-NKMTREKLYGPLMFFFVSWCCHYFPFFLMARQKFLHHYLPAHLIACLFSGALWEVIFSDCKSLDLEKDEDIsg 701
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLRKRV-- 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 766431904  702 asyernpkvyvkpYTVFLVCVSCAVAWFFVYFSPLVYGDVSLSpSEVVSREWFD 755
Cdd:pfam16192 159 -------------GYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 343-503 9.01e-23

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: 96.28  E-value: 9.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  343 KHQDTDAFLHSHLARYPQRYEDGRISSaGQQVTGYTHPDFNNQ----WEVLPPHgSDVGKGQAVLLNQHIRLRHVATDTY 418
Cdd:pfam02815   4 KGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSarslWRIEVVR-HDAWRGGLIKWGSPFRLRHLTTGRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  419 LLAHDVASPF-YPTNEEITTVTLEEGDGELYP---ETLFAFQPLKKSDEGHVlKSKTVSFRLFHVDTSVALWTHNDElLP 494
Cdd:pfam02815  82 LHSHEEQKPPlVEKEDWQKEVSAYGFRGFPGDndiVEIFEKKSTTGMGSDRI-KPGDSYFRLQHVCTGCWLFSHSVK-LP 159

                         170
                  ....*....|.
gi 766431904  495 DWGF--QQQEI 503
Cdd:pfam02815 160 KWGFgpEQQKV 170
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 35-301 8.50e-21

Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 96.50  E-value: 8.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  35 QVAEHWLLQPLPEPESRYSFWVTI-VTLLAFAARFYKIWYPKEVVFDEVHFGKFASYYLER---------SYFFDVHPPF 104
Cdd:COG1928    3 AALPPARLVPPMPGDRLRGWLGTLlVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 105 AKMMIAFIGWLCGYDGSFkfdeigysyethpapyiAYRSFNAILGTLTVPIMFNTLKELNFRAITCAFASLLVAIDTAHV 184
Cdd:COG1928   83 GKWLIALGEWLFGYVNPF-----------------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 185 TETRLILLDAILIISIAATMYCYVR----------------FYKCQLRQPFTWSWyiWLHATGLSLSFVISTKYVGVmtY 248
Cdd:COG1928  146 VLSRTALLDIFLMFFVLAAFGCLLLdrdqvrrrlaaavaagRAPSRWGPRLGFRW--WRLAAGVLLGLACGVKWSGL--Y 221

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 766431904 249 SAIGFAVVVNLWqllDIKA-----------GLSLRQFMRHFSkrlnGLVLIPFVIYLFWFWVHF 301
Cdd:COG1928  222 FLAAFGLLTVAW---DAGArraagvrrpwlGALLRDGIPAFF----ALVIVPLLTYLASWTGWF 278
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
333-391 6.02e-09

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 52.73  E-value: 6.02e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 766431904   333 TVNYFDIITIKHQDTDAFLHSHLARYPqryedgRISSAGQQVTGYTHP--DFNNQWEVLPP 391
Cdd:smart00472   3 FVRWGDVVRLRHVTTGRYLHSHDEKLP------PWGDGQQEVTGYGNPaiDANTLWLIEPV 57
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 545-755 5.72e-06

Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 49.51  E-value: 5.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 545 WIETQKSMFEHNNKLSSEHPFASEPYSWPGSLSGVSFWTNGDEK-----------KQIYFIGNIIGWWFQVISLAVFVGI 613
Cdd:COG1928  307 LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcgagkcvRAVLAIGNPALWWLGLPALLWLLWR 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 614 IVAdlitrhrgyyalnkmTREKLYGPLMfffVSWCCHYFPFFLMA-RQKFLHHYLPAHLIACL-FSGALWEVIFSdcksl 691
Cdd:COG1928  387 WIA---------------RRDWRAGAVL---VGYAAGWLPWFLYLdRTMFFFYAIPFVPFLVLaLALVLGLILGP----- 443

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 766431904 692 dlekdediSGASYERnpkvyvkpyTVFLVCVSC---AVAWFFVYFSPLVYGDVsLSPSEVVSREWFD 755
Cdd:COG1928  444 --------ARASERR---------RLGRLVVGLyvgLVVANFAFFYPILTGLP-IPYDEWQARMWFP 492
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 334-521 1.60e-103

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: 315.39  E-value: 1.60e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 334 VNYFDIITIKHQDTDAFLHSHLARYPQRYEDGRISSAGQQVTGYTHPDFNNQWEVLPPHGSD--VGKGQAVLLNQHIRLR 411
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDehEGTGRPVRNGDLIRLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 412 HVATDTYLLAHDVASPFYPTNEEITTVTLEEGDgELYPETLFAFQpLKKSDEGHVLKSKTVSFRLFHVDTSVALWTHNDE 491
Cdd:cd23285   81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVE-IEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKP 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 766431904 492 lLPDWGFQQQEINGNKKVIDPSNNWVVDEI 521
Cdd:cd23285  159 -LPDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 58-305 6.40e-84

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: 266.48  E-value: 6.40e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904   58 IVTLLAFAARFYKIWYPKEVVFDEVHFGKFASYYLERSYFFDVHPPFAKMMIAFIGWLCGYDGSFKFDEIGYSYETHPAP 137
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  138 YIAYRSFNAILGTLTVPIMFNTLKELNFRAITCAFASLLVAIDTAHVTETRLILLDAILIISIAATMYCYVRFYKcqlRQ 217
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFER---KA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  218 PFTWSWYIWLHATGLSLSFVISTKYVGVMTYSAIGFAVVVNLWQLLDIKAGLSLRQFMrHFSKRLNGLVLIPFVIYLFWF 297
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWK-HLFARLFCLIVIPWALYLAQF 237


                  ....*...
gi 766431904  298 WVHFTVLN 305
Cdd:pfam02366 238 YVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 543-755 2.99e-71

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: 231.28  E-value: 2.99e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  543 KKWIETQKSMFEHNNKLSSEHPFASEPYSWPGSLSGVSFWTNGDEKKQIYFIGNIIGWWFQVISLAVFVGIIVADLITRH 622
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  623 RGYYAL-NKMTREKLYGPLMFFFVSWCCHYFPFFLMARQKFLHHYLPAHLIACLFSGALWEVIFSDCKSLDLEKDEDIsg 701
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLRKRV-- 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 766431904  702 asyernpkvyvkpYTVFLVCVSCAVAWFFVYFSPLVYGDVSLSpSEVVSREWFD 755
Cdd:pfam16192 159 -------------GYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 334-520 1.33e-50

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: 175.21  E-value: 1.33e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 334 VNYFDIITIKHQD-TDAFLHSHLARYPQRyedgrisSAGQQVTGYTHPDFNNQWEVLPPHGSDV---GKGQAVLLNQHIR 409
Cdd:cd23276    1 VAYGSQITLRNANsGGGYLHSHNHTYPDG-------SKQQQVTGYGHKDENNWWQILKPRGDPSsnpPDPEYVRDGDEVR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 410 LRHVATDTYLLAHDVASPFYPTNEEITTVTLEEGDGElyPETLFAFQPLKKS--DEGHVLKSKTVSFRLFHVDTSVALWT 487
Cdd:cd23276   74 LLHKETNRYLRTHDAAAPVTSKHKEVSAYPDENEDGD--DNDLWVVEIVKDEgkLEDKRIKPLTTRFRLRNKKTGCYLTS 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 766431904 488 HNDElLPDWGFQQQEINGNKKVI-DPSNNWVVDE 520
Cdd:cd23276  152 SGVK-LPEWGFRQGEVVCSKNKEsDPSTLWNVEE 184
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 334-520 2.81e-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: 143.60  E-value: 2.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 334 VNYFDIITIKHQDT-DAFLHSHLARYPQRYEDGRISSAGQQVTGYTHPDFNNQWEVLPPHGSDVGKGQAVLLNQH---IR 409
Cdd:cd23281    1 VAYGSQVTLRNTHGsPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPVRHgdiIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 410 LRHVATDTYLLAHDVASPFYPTNEEITTVTleEGDGELYPETLFAFQPLKKSDEGHVLKSKTVSFRLFHVDTSVALWThN 489
Cdd:cd23281   81 LVHGKTGRFLNSHDVAAPLSPTHQEVSCYI--DYNISMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKL-S 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 766431904 490 DELLPDWGFQQQEINGNKKVIDPSNNWVVDE 520
Cdd:cd23281  158 GKQLPDWGFGQLEVATDRAGNQSSTVWNVEE 188
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 343-503 9.01e-23

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: 96.28  E-value: 9.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  343 KHQDTDAFLHSHLARYPQRYEDGRISSaGQQVTGYTHPDFNNQ----WEVLPPHgSDVGKGQAVLLNQHIRLRHVATDTY 418
Cdd:pfam02815   4 KGGDVVRLFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSarslWRIEVVR-HDAWRGGLIKWGSPFRLRHLTTGRY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  419 LLAHDVASPF-YPTNEEITTVTLEEGDGELYP---ETLFAFQPLKKSDEGHVlKSKTVSFRLFHVDTSVALWTHNDElLP 494
Cdd:pfam02815  82 LHSHEEQKPPlVEKEDWQKEVSAYGFRGFPGDndiVEIFEKKSTTGMGSDRI-KPGDSYFRLQHVCTGCWLFSHSVK-LP 159

                         170
                  ....*....|.
gi 766431904  495 DWGF--QQQEI 503
Cdd:pfam02815 160 KWGFgpEQQKV 170
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 334-520 7.49e-22

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: 93.90  E-value: 7.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 334 VNYFDIITIKHQDTDA-FLHSHLARYPQryedgriSSAGQQVTGYTHPDFNNQWEVLPPHGSDVGKGQAVLLNQH---IR 409
Cdd:cd23283    1 VAYGSTIRIRHLNTRGgYLHSHPHNYPA-------GSKQQQITLYPHRDENNDWLVELANAPEEWSPTTFENLKDgdvVR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 410 LRHVATDTYLLAHDVASPFyPTNEEITTVT-----LEEGDgelyPETLFAFQPLKK-----SDEGHV--LKSKtvsFRLF 477
Cdd:cd23283   74 LEHVATGRRLHSHDHRPPV-SDNDWQNEVSaygyeGFEGD----ANDDWRVEILKDdsrpgESKERVraIDTK---FRLV 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 766431904 478 HVDTSVALWTHNdELLPDWGFQQQEINGNKKVIDPSNNWVVDE 520
Cdd:cd23283  146 HVMTGCYLFSHG-VKLPEWGFEQQEVTCAKSGLLELSLWYIET 187
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 334-523 1.25e-21

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: 92.75  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 334 VNYFDIITIK-HQDTDAFLHSHLARYPQRYEdgrisSAGQQVTGYTHPDFNNQWEVLPPHGSDVGKGQAVLLnQH---IR 409
Cdd:cd23282    1 VAYGSVITLKnHRTGGGYLHSHWHLYPEGVG-----ARQQQVTTYSHKDDNNLWLIKKHNQSSDLSDPVEYV-RHgdlIR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 410 LRHVATDTYLLAHDVASPfyptneeITT----VTLEEGDGELYPETLFAFQpLKKSDEGHVLKSKTVSFRLFHVDTSVAL 485
Cdd:cd23282   75 LEHVNTKRNLHSHKEKAP-------LTKkhyqVTGYGENGTGDANDVWRVE-VVGGREGDPVKTVRSKFRLVHYNTGCAL 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 766431904 486 WTHNdELLPDWGFQQQEINGNKKVIDPSNNWVVDEIVN 523
Cdd:cd23282  147 HSHG-KQLPKWGWEQLEVTCNPNVRDKNSLWNVEDNRN 183
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 35-301 8.50e-21

Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 96.50  E-value: 8.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904  35 QVAEHWLLQPLPEPESRYSFWVTI-VTLLAFAARFYKIWYPKEVVFDEVHFGKFASYYLER---------SYFFDVHPPF 104
Cdd:COG1928    3 AALPPARLVPPMPGDRLRGWLGTLlVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 105 AKMMIAFIGWLCGYDGSFkfdeigysyethpapyiAYRSFNAILGTLTVPIMFNTLKELNFRAITCAFASLLVAIDTAHV 184
Cdd:COG1928   83 GKWLIALGEWLFGYVNPF-----------------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 185 TETRLILLDAILIISIAATMYCYVR----------------FYKCQLRQPFTWSWyiWLHATGLSLSFVISTKYVGVmtY 248
Cdd:COG1928  146 VLSRTALLDIFLMFFVLAAFGCLLLdrdqvrrrlaaavaagRAPSRWGPRLGFRW--WRLAAGVLLGLACGVKWSGL--Y 221

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 766431904 249 SAIGFAVVVNLWqllDIKA-----------GLSLRQFMRHFSkrlnGLVLIPFVIYLFWFWVHF 301
Cdd:COG1928  222 FLAAFGLLTVAW---DAGArraagvrrpwlGALLRDGIPAFF----ALVIVPLLTYLASWTGWF 278
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 334-523 1.92e-19

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: 86.99  E-value: 1.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 334 VNYFDIITIKHQD-TDAFLHSHlaryPQRYEDGrisSAGQQVTGYTHPDFNNQWEVLPPHG--------SDVGkgqAVLL 404
Cdd:cd23284    4 VAYGSKVTIKNQGlGGGLLHSH----VQTYPEG---SNQQQVTCYGHKDSNNEWIFERPRGlpswdendTDIE---FIKD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 405 NQHIRLRHVATDTYLLAHDVASPFYPTNEEITTvtleEGDGELY-PETLFAFQPLKksDEGHVLKSK----TVSFRLFHV 479
Cdd:cd23284   74 GDIVRLVHKQTGRNLHSHPVPAPISKSDYEVSG----YGDLTVGdEKDNWVIEIVK--QVGSEDPKKlhtlTTSFRLRHE 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 766431904 480 DTSVALWTHNDElLPDWGFQQQEI----NGNKKviDPSNNWVVDEIVN 523
Cdd:cd23284  148 VLGCYLAQTGVS-LPEWGFKQGEVvcdkSNFKR--DKRTWWNIETHTN 192
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 334-521 1.52e-18

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: 84.41  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 334 VNYFDIITIKHQDT-DAFLHSHLARYPqryedgrISSAGQQVTGYTH-PDFNNQWEVLPP----HGSDVGKGQAVLLNQH 407
Cdd:cd23286    1 LLYGSTVTIRHLESlGGYLHSHDLTYP-------SGSNEQQVTLYDFeDDANNEWIIETKtkeqMDKFPGQFREVRDGDV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 408 IRLRHVATDTYLLAHDVASPF----YptNEEITTvtleEGDGELYPETLFAFQPLKKSDEGHV--------LKSKTVSFR 475
Cdd:cd23286   74 IRLRHVVTGKLLRASNARPPVseqeY--NNEVSC----TGNANYSGDMDENWRIDVKGDESHAelklpnikIKSTESVFQ 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 766431904 476 LFHVDTSVALWTHnDELLPDWGFQQQEINGNKKVIDPSNNWVVDEI 521
Cdd:cd23286  148 LYNRGTGCTLLSH-DTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 339-520 1.05e-17

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: 81.19  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 339 IITIKHQDTDAFLHSHLARYpqryedgrISSAGQQ-VTGYTHP-DFNNQWEVLPPHGSDVGK-GQAVLLNQHIRLRHVAT 415
Cdd:cd23279    4 AIKLKHVNSGYRLHSHEVSY--------GSGSGQQsVTAVPSAdDANSLWTVLPGLGEPCQEqGKPVKCGDIIRLQHVNT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 416 DTYLLAHDVASPFYPtNEEITTVtleeGDGELYPETLFAFQPLKKSDEghVLKSKTVsFRLFHVDTSVALWTHndellPD 495
Cdd:cd23279   76 RKNLHSHNHSSPLSG-NQEVSAF----GGGDEDSGDNWIVECEGKKAK--FWKRGEP-VRLKHVDTGKYLSAS-----KT 142

                        170       180       190
                 ....*....|....*....|....*....|
gi 766431904 496 WGFQQQEINGNKKV-----IDPSNNWVVDE 520
Cdd:cd23279  143 HKFTQQPIAGQLEVsaassKDSDSQWKAVE 172
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 338-521 2.13e-17

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: 80.51  E-value: 2.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 338 DIITIKHQDTDAFLHSHLARYPQryedgriSSAGQQVTGYTH---PDFNNQWEVLPPHGSdvgKGQAVLLNQHIRLRHVA 414
Cdd:cd23263    2 DVIWLKHSETGKYLHSHRKNYPT-------GSGQQEVTFESSsrkGDTNGLWIIESENGK---QGGPVKWGDKIRLRHLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 415 TDTYLLAHDVASPFYPTNEEITTVTlEEGDgelyPETLFAFQPLK-KSDEGHVLKSKTVsFRLFHVDTSVALWTHNDElL 493
Cdd:cd23263   72 TGKYLSSEEGKKSPKSNHQEVLCLT-DNPD----KSSLFKFEPIGsTKYKQKYVKKDSY-FRLKHVNTNFWLHSHEKK-F 144

                        170       180
                 ....*....|....*....|....*...
gi 766431904 494 PDWGFQQQEINGNKKVIDPSNNWVVDEI 521
Cdd:cd23263  145 NINNKTQQEVICHGEREEVFKLWKAELI 172
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 334-489 3.01e-11

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: 62.78  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 334 VNYFDIITIKHQDTDAFLHSHLARYPqryedgriSSAGQQ-VTGYTHP-DFNNQWEVLPPHGSDVGKGQAVLLNQHIRLR 411
Cdd:cd23294    1 VTCGSVIKLQHERTKFRLHSHEVPYG--------SGSGQQsVTGFPGVdDSNSYWIVKPANGERCKQGDVIKNGDVIRLQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 412 HVATDTYLLAHDVASPFYPTNEeittVTLEEGDGElypetlfafqplkkSDEGHVLKSKTVS----------FRLFHVDT 481
Cdd:cd23294   73 HVSTRKWLHSHLHASPLSGNQE----VSCFGGDGN--------------SDTGDNWIVEIEGggkvwerdqkVRLKHVDT 134


                 ....*...
gi 766431904 482 SVALWTHN 489
Cdd:cd23294  135 GGYLHSHD 142
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 339-485 7.79e-11

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: 61.52  E-value: 7.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 339 IITIKHQDTDAFLHSHLARYpqryedGriSSAGQQ-VTGYTHP-DFNNQWEVLPPHGSDVGKGQAVLLNQHIRLRHVATD 416
Cdd:cd23293    6 VVKLLNTRHNVRLHSHDVKY------G--SGSGQQsVTGVESSdDSNSYWQIRGPTGADCERGTPIKCGQTIRLTHLNTG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 766431904 417 TYLLAHDVASPFYPtNEEITTVTlEEGDGelypetlfafqplkksDEGHVLK--------SKTVSFRLFHVDTSVAL 485
Cdd:cd23293   78 KNLHSHHFQSPLSG-NQEVSAFG-EDGEG----------------DTGDNWTvvcsgtywERDEAVRLKHVDTEVYL 136
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
333-391 6.02e-09

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 52.73  E-value: 6.02e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 766431904   333 TVNYFDIITIKHQDTDAFLHSHLARYPqryedgRISSAGQQVTGYTHP--DFNNQWEVLPP 391
Cdd:smart00472   3 FVRWGDVVRLRHVTTGRYLHSHDEKLP------PWGDGQQEVTGYGNPaiDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
464-521 1.12e-08

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 51.96  E-value: 1.12e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 766431904   464 GHVLKSKTVsFRLFHVDTSVALWTHnDELLPDWGFQQQEINGNK-KVIDPSNNWVVDEI 521
Cdd:smart00472   1 GGFVRWGDV-VRLRHVTTGRYLHSH-DEKLPPWGDGQQEVTGYGnPAIDANTLWLIEPV 57
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 338-425 1.87e-07

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: 51.61  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 338 DIITIKHQDTDAFLHSHLARYPQryedgrisSAGQQVTGY---THPDFNNQWEVLPPhgsdvGKGQAVLLNQHIRLRHVA 414
Cdd:cd23294   67 DVIRLQHVSTRKWLHSHLHASPL--------SGNQEVSCFggdGNSDTGDNWIVEIE-----GGGKVWERDQKVRLKHVD 133

                         90
                 ....*....|.
gi 766431904 415 TDTYLLAHDVA 425
Cdd:cd23294  134 TGGYLHSHDKK 144
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 317-427 1.44e-06

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: 49.22  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 317 EFQETLKDSPLSVDSKTVNYF---DIITIKHQDTDAFLHSHLARYPqryedgrISSAGQQ--VTGYTHPDF----NNQW- 386
Cdd:cd23283   46 DWLVELANAPEEWSPTTFENLkdgDVVRLEHVATGRRLHSHDHRPP-------VSDNDWQneVSAYGYEGFegdaNDDWr 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 766431904 387 -EVLPPHGSDVGKGQAVL-LNQHIRLRHVATDTYLLAHDVASP 427
Cdd:cd23283  119 vEILKDDSRPGESKERVRaIDTKFRLVHVMTGCYLFSHGVKLP 161
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
399-457 2.15e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.41  E-value: 2.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 766431904   399 GQAVLLNQHIRLRHVATDTYLLAHDVasPFYPTNEEITTVTLEEGDGELyPETLFAFQP 457
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDE--KLPPWGDGQQEVTGYGNPAID-ANTLWLIEP 56
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 545-755 5.72e-06

Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 49.51  E-value: 5.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 545 WIETQKSMFEHNNKLSSEHPFASEPYSWPGSLSGVSFWTNGDEK-----------KQIYFIGNIIGWWFQVISLAVFVGI 613
Cdd:COG1928  307 LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcgagkcvRAVLAIGNPALWWLGLPALLWLLWR 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 614 IVAdlitrhrgyyalnkmTREKLYGPLMfffVSWCCHYFPFFLMA-RQKFLHHYLPAHLIACL-FSGALWEVIFSdcksl 691
Cdd:COG1928  387 WIA---------------RRDWRAGAVL---VGYAAGWLPWFLYLdRTMFFFYAIPFVPFLVLaLALVLGLILGP----- 443

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 766431904 692 dlekdediSGASYERnpkvyvkpyTVFLVCVSC---AVAWFFVYFSPLVYGDVsLSPSEVVSREWFD 755
Cdd:COG1928  444 --------ARASERR---------RLGRLVVGLyvgLVVANFAFFYPILTGLP-IPYDEWQARMWFP 492
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 338-532 1.39e-05

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: 46.61  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 338 DIITIKHQDTDAFLHShlarypqrYEDGRISSAGQQVTGYTHP-DFNNQWEVLPPHGSDV----------GKGQAVLLNQ 406
Cdd:cd23280   11 DVVRLFHKELEAYLSA--------EGSFVDEVLTEDVHLRVRPvDDRKPRTLFPPTSGDTfwqiekedtpLKGGVIKWGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 407 HIRLRHVATDTYLLAHDVaspfyPTNEEITTvtleeGDGELYPETLFAFQPLKKSDEGHVLKSKTVsfRLFHVDTSvaLW 486
Cdd:cd23280   83 QCRLRHLPTGKYLAVDDK-----TGNGKVVL-----TSDPSDPSTVFRLHPVTKETSEEVKFGSYV--RIEHVATG--TW 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 766431904 487 THNDELLPDWGFQQQEINGNKKV-----IDPSNNWVVDEIVNLDEVRKVYV 532
Cdd:cd23280  149 LHAETDEELRRSKKSPAGLSWDGaklrkVSLSLERQDDDAFTIQEVDPDLV 199
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 338-419 1.88e-04

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: 42.67  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 338 DIITIKHQDTDAFLHSHLARYPqryedgriSSAGQQVTGYTHPDF--NNQW--EVLPPHGSDVGKGQAVllnqhiRLRHV 413
Cdd:cd23279   66 DIIRLQHVNTRKNLHSHNHSSP--------LSGNQEVSAFGGGDEdsGDNWivECEGKKAKFWKRGEPV------RLKHV 131


                 ....*.
gi 766431904 414 ATDTYL 419
Cdd:cd23279  132 DTGKYL 137
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 405-534 3.17e-03

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: 39.29  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431904 405 NQHIRLRHVATDTYLLAHDvasPFYPTNEEITTVTLEEGDGELYPETLFAFQPLKKSDEGHVLKSKTvsFRLFHVDTSVA 484
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHR---KNYPTGSGQQEVTFESSSRKGDTNGLWIIESENGKQGGPVKWGDK--IRLRHLSTGKY 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 766431904 485 LWTHNDELLPDwgFQQQEINGNKKVIDPSNNWVVdEIVNLDEVRKVYVPK 534
Cdd:cd23263   76 LSSEEGKKSPK--SNHQEVLCLTDNPDKSSLFKF-EPIGSTKYKQKYVKK 122
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 340-386 7.22e-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: 38.13  E-value: 7.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 766431904 340 ITIKHQDTDAFLHSHLARYpqryedGRISSAGQQVTGYTHPDFNNQW 386
Cdd:cd23294  127 VRLKHVDTGGYLHSHDKKY------GRPIPGQQEVCAVASKNSNTLW 167
 
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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