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Conserved domains on  [gi|19113599|ref|NP_596807|]
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ER membrane O-mannosyltransferase Ogm4 [Schizosaccharomyces pombe]

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 ...
 339-529 4.72e-105

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: 320.01  E-value: 4.72e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 339 LNYYDIVTIKHMGTNAFLHSHPEKYPIPYDDGRISSGGQQVTGYQFDDENNYWMILPADHYDPPieAKLNVPVKNMDYIK 418
Cdd:cd23285   1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDEH--EGTGRPVRNGDLIR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 419 LHHVGTNTDLMTHDVASPYHPTNEEFTTVSVDESAgKKHEYTLFQVVMSDNTDPQRpLYTKASSFKLIHKLTHVAMWSDP 498
Cdd:cd23285  79 LRHVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVEIEDTDEGDV-LKTKSSHFRLIHVDTNVALWTHK 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 19113599 499 KPLPDWAFKQLEINGAKNIQTGSIFWTFDDI 529
Cdd:cd23285 157 KPLPDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 63-310 1.25e-76

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: 247.61  E-value: 1.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599    63 VLITVLSFITRFWNLNLPGEVVFDEVHFGKFASYYLQGKYFFDLHPPFAKLLLALVAKLAGYDGHYLFDNIGDNYKDNGV 142
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   143 PYVTIRAWPALLSSLVPPVVFLIMKESGYDLLACIVSSSLVLFDNAHVTEGRLILLDATLLFSMVCAIYCYVRFFklRHT 222
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   223 PFSRPWWAWLFFTGFFLSCTISTKYVGFFTFLSIGLSVCLELWYLWDIKTGLTVeRFFQHFLARFFCLIFFPFLFFLFWF 302
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLK-SIWKHLFARLFCLIVIPWALYLAQF 237


                  ....*...
gi 19113599   303 YMHFNILT 310
Cdd:pfam02366 238 YVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 551-768 1.70e-64

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: 213.56  E-value: 1.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   551 KKYLELQLTMFRQNNMLTEFHPYSSNPSDWFTLHHGIAFWAKSEENKQIYLLGNPIGWWIIAGTVLSTTVVAAAEILLRQ 630
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   631 RGIRTL-PETVRNHFYRSTMFFYMTYVFHYLPFFIMGRQLFLHHYLPAHLAGSLLVGAFIQLACRKSFRSPvsagvpipk 709
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLP--------- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113599   710 dvdekghskchRKYGHVIELICTLLLIFVVIYCFTFFAPMTYGDKSLSvDEWTRRKWLD 768
Cdd:pfam16192 152 -----------RSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 339-529 4.72e-105

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: 320.01  E-value: 4.72e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 339 LNYYDIVTIKHMGTNAFLHSHPEKYPIPYDDGRISSGGQQVTGYQFDDENNYWMILPADHYDPPieAKLNVPVKNMDYIK 418
Cdd:cd23285   1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDEH--EGTGRPVRNGDLIR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 419 LHHVGTNTDLMTHDVASPYHPTNEEFTTVSVDESAgKKHEYTLFQVVMSDNTDPQRpLYTKASSFKLIHKLTHVAMWSDP 498
Cdd:cd23285  79 LRHVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVEIEDTDEGDV-LKTKSSHFRLIHVDTNVALWTHK 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 19113599 499 KPLPDWAFKQLEINGAKNIQTGSIFWTFDDI 529
Cdd:cd23285 157 KPLPDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 63-310 1.25e-76

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: 247.61  E-value: 1.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599    63 VLITVLSFITRFWNLNLPGEVVFDEVHFGKFASYYLQGKYFFDLHPPFAKLLLALVAKLAGYDGHYLFDNIGDNYKDNGV 142
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   143 PYVTIRAWPALLSSLVPPVVFLIMKESGYDLLACIVSSSLVLFDNAHVTEGRLILLDATLLFSMVCAIYCYVRFFklRHT 222
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   223 PFSRPWWAWLFFTGFFLSCTISTKYVGFFTFLSIGLSVCLELWYLWDIKTGLTVeRFFQHFLARFFCLIFFPFLFFLFWF 302
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLK-SIWKHLFARLFCLIVIPWALYLAQF 237


                  ....*...
gi 19113599   303 YMHFNILT 310
Cdd:pfam02366 238 YVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 551-768 1.70e-64

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: 213.56  E-value: 1.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   551 KKYLELQLTMFRQNNMLTEFHPYSSNPSDWFTLHHGIAFWAKSEENKQIYLLGNPIGWWIIAGTVLSTTVVAAAEILLRQ 630
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   631 RGIRTL-PETVRNHFYRSTMFFYMTYVFHYLPFFIMGRQLFLHHYLPAHLAGSLLVGAFIQLACRKSFRSPvsagvpipk 709
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLP--------- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113599   710 dvdekghskchRKYGHVIELICTLLLIFVVIYCFTFFAPMTYGDKSLSvDEWTRRKWLD 768
Cdd:pfam16192 152 -----------RSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 60-271 1.36e-17

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 86.48  E-value: 1.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599  60 LAFVLITVLSFITRFWNLNLPGEVVFDEVHFGKFASYYLQGKY---------FFDLHPPFaklllalvaklagydGHYL- 129
Cdd:COG1928  23 LGTLLVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNGYernwpdpgpFFVVHPPL---------------GKWLi 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 130 ------FDNigdnykDNGVPYvtiRAWPALLSSLVPPVVFLIMKE-SGYDLLACIvSSSLVLFDNAHVTEGRLILLDATL 202
Cdd:COG1928  88 algewlFGY------VNPFGW---RFAAALAGTLSVLLVARIARRlTRSTLLGAI-AGLLLALDGLHLVLSRTALLDIFL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 203 LFSMVCAIYCYV------------RFFKLRHTPFSRP---WWAWLFFTGFFLSCTISTKYVGFFTFLSIGLsvcleLWYL 267
Cdd:COG1928 158 MFFVLAAFGCLLldrdqvrrrlaaAVAAGRAPSRWGPrlgFRWWRLAAGVLLGLACGVKWSGLYFLAAFGL-----LTVA 232


                ....
gi 19113599 268 WDIK 271
Cdd:COG1928 233 WDAG 236
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
337-396 8.22e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 57.74  E-value: 8.22e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113599    337 TILNYYDIVTIKHMGTNAFLHSHPEKYPipyddgRISSGGQQVTGYQFD--DENNYWMILPA 396
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEKLP------PWGDGQQEVTGYGNPaiDANTLWLIEPV 57
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 355-510 4.24e-09

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: 56.60  E-value: 4.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   355 FLHSHPEKYP-IPYDDGRisSGGQQVTGYQFDDENNY----WMILPADHYDPPIEAklnvpVKNMDYIKLHHVGTNTDLM 429
Cdd:pfam02815  11 LFHSHQDEYLtGSEQQQK--QPFLRITLYPHGDANNSarslWRIEVVRHDAWRGGL-----IKWGSPFRLRHLTTGRYLH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   430 THDV-ASPYHPTNEEFTTVSVDESAGKKHEYTLFQVVMSDNTDPQRP--LYTKASSFKLIHKLTHVAMWSDPKPLPDWAF 506
Cdd:pfam02815  84 SHEEqKPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSdrIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGF 163


                  ....
gi 19113599   507 KQLE 510
Cdd:pfam02815 164 GPEQ 167
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 567-771 1.07e-08

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 58.36  E-value: 1.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 567 LTEFHPYSSNPSDWFTLHHGIAFWAKSEEN-----------KQIYLLGNPIGWWiiagtvLSTTVVAAAEILLRQRgirt 635
Cdd:COG1928 321 LSSPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcgagkcvRAVLAIGNPALWW------LGLPALLWLLWRWIAR---- 390

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 636 lpetvrnhfyRSTMFFYMT--YVFHYLP-FFIMGRQLFLHHYLPAH----LAGSLLVGAFIQlacrksfrspvSAGVPip 708
Cdd:COG1928 391 ----------RDWRAGAVLvgYAAGWLPwFLYLDRTMFFFYAIPFVpflvLALALVLGLILG-----------PARAS-- 447

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113599 709 kdvdekghskchrkYGHVIELICTLLLIFVVIYCFTFFAPMTYGDkSLSVDEWTRRKWLDSWV 771
Cdd:COG1928 448 --------------ERRRLGRLVVGLYVGLVVANFAFFYPILTGL-PIPYDEWQARMWFPSWI 495
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 339-529 4.72e-105

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: 320.01  E-value: 4.72e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 339 LNYYDIVTIKHMGTNAFLHSHPEKYPIPYDDGRISSGGQQVTGYQFDDENNYWMILPADHYDPPieAKLNVPVKNMDYIK 418
Cdd:cd23285   1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDEH--EGTGRPVRNGDLIR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 419 LHHVGTNTDLMTHDVASPYHPTNEEFTTVSVDESAgKKHEYTLFQVVMSDNTDPQRpLYTKASSFKLIHKLTHVAMWSDP 498
Cdd:cd23285  79 LRHVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVEIEDTDEGDV-LKTKSSHFRLIHVDTNVALWTHK 156

                       170       180       190
                ....*....|....*....|....*....|.
gi 19113599 499 KPLPDWAFKQLEINGAKNIQTGSIFWTFDDI 529
Cdd:cd23285 157 KPLPDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 63-310 1.25e-76

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: 247.61  E-value: 1.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599    63 VLITVLSFITRFWNLNLPGEVVFDEVHFGKFASYYLQGKYFFDLHPPFAKLLLALVAKLAGYDGHYLFDNIGDNYKDNGV 142
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   143 PYVTIRAWPALLSSLVPPVVFLIMKESGYDLLACIVSSSLVLFDNAHVTEGRLILLDATLLFSMVCAIYCYVRFFklRHT 222
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   223 PFSRPWWAWLFFTGFFLSCTISTKYVGFFTFLSIGLSVCLELWYLWDIKTGLTVeRFFQHFLARFFCLIFFPFLFFLFWF 302
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLK-SIWKHLFARLFCLIVIPWALYLAQF 237


                  ....*...
gi 19113599   303 YMHFNILT 310
Cdd:pfam02366 238 YVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 551-768 1.70e-64

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: 213.56  E-value: 1.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   551 KKYLELQLTMFRQNNMLTEFHPYSSNPSDWFTLHHGIAFWAKSEENKQIYLLGNPIGWWIIAGTVLSTTVVAAAEILLRQ 630
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   631 RGIRTL-PETVRNHFYRSTMFFYMTYVFHYLPFFIMGRQLFLHHYLPAHLAGSLLVGAFIQLACRKSFRSPvsagvpipk 709
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLP--------- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113599   710 dvdekghskchRKYGHVIELICTLLLIFVVIYCFTFFAPMTYGDKSLSvDEWTRRKWLD 768
Cdd:pfam16192 152 -----------RSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 341-528 2.02e-41

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: 149.77  E-value: 2.02e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 341 YYDIVTIKH-MGTNAFLHSHPEKYPIPYDDGRISSGGQQVTGYQFDDENNYWMILPADHYDPPIEAKLnVPVKNMDYIKL 419
Cdd:cd23281   3 YGSQVTLRNtHGSPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPP-RPVRHGDIIQL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 420 HHVGTNTDLMTHDVASPYHPTNEEFTTVsVDESAgKKHEYTLFQVVMSDNTDPQRPLYTKASSFKLIHKLTHVAMWSDPK 499
Cdd:cd23281  82 VHGKTGRFLNSHDVAAPLSPTHQEVSCY-IDYNI-SMPAQNLWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKLSGK 159

                       170       180
                ....*....|....*....|....*....
gi 19113599 500 PLPDWAFKQLEINGAKNIQTGSIFWTFDD 528
Cdd:cd23281 160 QLPDWGFGQLEVATDRAGNQSSTVWNVEE 188
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 339-528 1.94e-32

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: 123.98  E-value: 1.94e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 339 LNYYDIVTIKHM-GTNAFLHSHPEKYPipydDGrisSGGQQVTGYQFDDENNYWMILP---ADHYDPPIEAklnvPVKNM 414
Cdd:cd23276   1 VAYGSQITLRNAnSGGGYLHSHNHTYP----DG---SKQQQVTGYGHKDENNWWQILKprgDPSSNPPDPE----YVRDG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 415 DYIKLHHVGTNTDLMTHDVASPYHPTNEEFTTVSVDESAGKkhEYTLFQVVMSDNTDPQRPLYTKA--SSFKLIHKLTHV 492
Cdd:cd23276  70 DEVRLLHKETNRYLRTHDAAAPVTSKHKEVSAYPDENEDGD--DNDLWVVEIVKDEGKLEDKRIKPltTRFRLRNKKTGC 147

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19113599 493 AMWSDPKPLPDWAFKQLEINGAKN-IQTGSIFWTFDD 528
Cdd:cd23276 148 YLTSSGVKLPEWGFRQGEVVCSKNkESDPSTLWNVEE 184
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 341-511 1.53e-24

MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae dolichyl-phosphate-mannose--protein mannosyltransferase 2 (PMT2) and similar proteins; Dolichyl-phosphate-mannose-protein mannosyltransferases (EC 2.4.1.109), also called PMTs, are responsible for O-linked glycosylation of proteins. They catalyze the transfer of mannose to seryl and threonyl residues of secretory proteins. Protein O-glycosylation is essential for cell wall rigidity and cell integrity. In Saccharomyces cerevisiae, a family of protein mannosyltransferases coded for by seven genes (PMT1-7). The family includes PMT2, PMT3 and PMT6. PMT2 forms a heterodimeric complex with PMT1 and more rarely with PMT5. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. It is required for incorporation of proteins in the cell wall. PMT3 form a functional heterodimer with PMT5 and more rarely with PMT1. It may have redundant activity to PMT2. PMT6 may form a heterodimer with PMT4. Members in this family contain a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467755 [Multi-domain]  Cd Length: 192  Bit Score: 101.63  E-value: 1.53e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 341 YYDIVTIKHMG-TNAFLHSHPEKYPipydDGrisSGGQQVTGYQFDDENNYWMI-LPADHYDPPIEAKLNVPVKNMDYIK 418
Cdd:cd23284   6 YGSKVTIKNQGlGGGLLHSHVQTYP----EG---SNQQQVTCYGHKDSNNEWIFeRPRGLPSWDENDTDIEFIKDGDIVR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 419 LHHVGTNTDLMTHDVASPYHPTNEEfttVSV--DESAGKKHEYTLFQVVMSDNTDPQRPLYTKASSFKLIHKLTHVAMWS 496
Cdd:cd23284  79 LVHKQTGRNLHSHPVPAPISKSDYE---VSGygDLTVGDEKDNWVIEIVKQVGSEDPKKLHTLTTSFRLRHEVLGCYLAQ 155

                       170
                ....*....|....*
gi 19113599 497 DPKPLPDWAFKQLEI 511
Cdd:cd23284 156 TGVSLPEWGFKQGEV 170
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 345-516 6.23e-23

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: 96.98  E-value: 6.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 345 VTIKHMGTNA-FLHSHPEKYPIpyddgriSSGGQQVTGYQFDDENNYWMILPADHYDP----PIEaklnvPVKNMDYIKL 419
Cdd:cd23283   7 IRIRHLNTRGgYLHSHPHNYPA-------GSKQQQITLYPHRDENNDWLVELANAPEEwsptTFE-----NLKDGDVVRL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 420 HHVGTNTDLMTHDVASPYhPTNEEFTTVSV--DES-AGKKHEYTLFQVVMSDNTDPQ-----RPLYTKassFKLIHKLTH 491
Cdd:cd23283  75 EHVATGRRLHSHDHRPPV-SDNDWQNEVSAygYEGfEGDANDDWRVEILKDDSRPGEskervRAIDTK---FRLVHVMTG 150

                       170       180
                ....*....|....*....|....*
gi 19113599 492 VAMWSDPKPLPDWAFKQLEINGAKN 516
Cdd:cd23283 151 CYLFSHGVKLPEWGFEQQEVTCAKS 175
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 339-528 1.90e-22

MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar proteins; POMT2 (EC 2.4.1.109), also called dolichyl-phosphate-mannose--protein mannosyltransferase 2, is a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids. POMT2 transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. It is essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins. POMT2 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467753 [Multi-domain]  Cd Length: 183  Bit Score: 95.45  E-value: 1.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 339 LNYYDIVTIK-HMGTNAFLHSHPEKYPipydDGrISSGGQQVTGYQFDDENNYWMILPAD-HYDPPIEAKLnvpVKNMDY 416
Cdd:cd23282   1 VAYGSVITLKnHRTGGGYLHSHWHLYP----EG-VGARQQQVTTYSHKDDNNLWLIKKHNqSSDLSDPVEY---VRHGDL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 417 IKLHHVGTNTDLMTHDVASPYHPTNEEFTTVSVDeSAGKKHEYTLFQVVMSDNTDPQRPLYTKassFKLIHKLTHVAMWS 496
Cdd:cd23282  73 IRLEHVNTKRNLHSHKEKAPLTKKHYQVTGYGEN-GTGDANDVWRVEVVGGREGDPVKTVRSK---FRLVHYNTGCALHS 148

                       170       180       190
                ....*....|....*....|....*....|..
gi 19113599 497 DPKPLPDWAFKQLEINGAKNIQTGSIFWTFDD 528
Cdd:cd23282 149 HGKQLPKWGWEQLEVTCNPNVRDKNSLWNVED 180
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 339-511 5.59e-20

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: 88.65  E-value: 5.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 339 LNYYDIVTIKHM-GTNAFLHSHPEKYPIpyddgriSSGGQQVTGYQF-DDENNYWMILPADHYDPPIEAKLNVPVKNMDY 416
Cdd:cd23286   1 LLYGSTVTIRHLeSLGGYLHSHDLTYPS-------GSNEQQVTLYDFeDDANNEWIIETKTKEQMDKFPGQFREVRDGDV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 417 IKLHHVGTNTDLMTHDVASP-----YHptNEEFTTVSVDESAGKKHEYTLFQVVMSDNTDPQRP---LYTKASSFKLIHK 488
Cdd:cd23286  74 IRLRHVVTGKLLRASNARPPvseqeYN--NEVSCTGNANYSGDMDENWRIDVKGDESHAELKLPnikIKSTESVFQLYNR 151

                       170       180
                ....*....|....*....|...
gi 19113599 489 LTHVAMWSDPKPLPDWAFKQLEI 511
Cdd:cd23286 152 GTGCTLLSHDTRLPDWAFHQQEV 174
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 60-271 1.36e-17

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 86.48  E-value: 1.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599  60 LAFVLITVLSFITRFWNLNLPGEVVFDEVHFGKFASYYLQGKY---------FFDLHPPFaklllalvaklagydGHYL- 129
Cdd:COG1928  23 LGTLLVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNGYernwpdpgpFFVVHPPL---------------GKWLi 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 130 ------FDNigdnykDNGVPYvtiRAWPALLSSLVPPVVFLIMKE-SGYDLLACIvSSSLVLFDNAHVTEGRLILLDATL 202
Cdd:COG1928  88 algewlFGY------VNPFGW---RFAAALAGTLSVLLVARIARRlTRSTLLGAI-AGLLLALDGLHLVLSRTALLDIFL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 203 LFSMVCAIYCYV------------RFFKLRHTPFSRP---WWAWLFFTGFFLSCTISTKYVGFFTFLSIGLsvcleLWYL 267
Cdd:COG1928 158 MFFVLAAFGCLLldrdqvrrrlaaAVAAGRAPSRWGPrlgFRWWRLAAGVLLGLACGVKWSGLYFLAAFGL-----LTVA 232


                ....
gi 19113599 268 WDIK 271
Cdd:COG1928 233 WDAG 236
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 346-436 6.22e-13

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: 67.79  E-value: 6.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 346 TIK--HMGTNAFLHSHPekypIPYDDGrisSGGQQVTGYQ-FDDENNYWMILPAdhydPPIEAKLNVPVKNMDYIKLHHV 422
Cdd:cd23294   6 VIKlqHERTKFRLHSHE----VPYGSG---SGQQSVTGFPgVDDSNSYWIVKPA----NGERCKQGDVIKNGDVIRLQHV 74

                        90
                ....*....|....
gi 19113599 423 GTNTDLMTHDVASP 436
Cdd:cd23294  75 STRKWLHSHLHASP 88
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 341-436 2.96e-12

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: 65.78  E-value: 2.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 341 YYDIVTIKHMGTNAFLHSHPEKYpipyddGRiSSGGQQVTGYQ-FDDENNYWMILPADhyDPPIEAKlNVPVKNMDYIKL 419
Cdd:cd23279   1 YGSAIKLKHVNSGYRLHSHEVSY------GS-GSGQQSVTAVPsADDANSLWTVLPGL--GEPCQEQ-GKPVKCGDIIRL 70

                        90
                ....*....|....*..
gi 19113599 420 HHVGTNTDLMTHDVASP 436
Cdd:cd23279  71 QHVNTRKNLHSHNHSSP 87
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 343-511 1.82e-11

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: 63.17  E-value: 1.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 343 DIVTIKHMGTNAFLHSHPEKYPipyddgrISSGGQQVTGYQFD---DENNYWMILPADHydppieaKLNVPVKNMDYIKL 419
Cdd:cd23263   2 DVIWLKHSETGKYLHSHRKNYP-------TGSGQQEVTFESSSrkgDTNGLWIIESENG-------KQGGPVKWGDKIRL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 420 HHVGTNTDLMTHDVASPyHPTNEEFTTVSVDEsagkKHEYTLFQVVMSDNTDPQRPLYTKASSFKLIHKLTHVAMWSDPK 499
Cdd:cd23263  68 RHLSTGKYLSSEEGKKS-PKSNHQEVLCLTDN----PDKSSLFKFEPIGSTKYKQKYVKKDSYFRLKHVNTNFWLHSHEK 142

                       170
                ....*....|..
gi 19113599 500 PLPDWAFKQLEI 511
Cdd:cd23263 143 KFNINNKTQQEV 154
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
337-396 8.22e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 57.74  E-value: 8.22e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113599    337 TILNYYDIVTIKHMGTNAFLHSHPEKYPipyddgRISSGGQQVTGYQFD--DENNYWMILPA 396
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEKLP------PWGDGQQEVTGYGNPaiDANTLWLIEPV 57
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 54-258 4.63e-10

PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 61.56  E-value: 4.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599  54 KAKKFKLAFVLITVLSFITRFWNLNLPGEVVFDEVHF----------GKFASYYLQGKYFFDlHPPFaklllalvaklag 123
Cdd:COG1807   2 SKTLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYaeiaremlesGDWLTPTLAGEPYFD-KPPL------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 124 ydgHYLFDNIGdnYKDNGVPYVTIRAWPALLSSLVPPVVFLIMKE---SGYDLLACIVSSSLVLFdnahVTEGRLILLDA 200
Cdd:COG1807  68 ---IYWLIALS--YKLFGVSEFAARLPSALLGLLTVLLVYLLARRlfgRRAALLAALLLLTSPLL----LLFGRLATPDA 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19113599 201 TLLFSMVCAIYCYVRFFKlrhtpfSRPWWAWLFFtGFFLSCTISTKYVGFFTFLSIGL 258
Cdd:COG1807 139 LLLLFWTLALYALLRALE------RRRLRWLLLA-GLALGLGFLTKGPVALLLPGLAL 189
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 355-510 4.24e-09

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: 56.60  E-value: 4.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   355 FLHSHPEKYP-IPYDDGRisSGGQQVTGYQFDDENNY----WMILPADHYDPPIEAklnvpVKNMDYIKLHHVGTNTDLM 429
Cdd:pfam02815  11 LFHSHQDEYLtGSEQQQK--QPFLRITLYPHGDANNSarslWRIEVVRHDAWRGGL-----IKWGSPFRLRHLTTGRYLH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599   430 THDV-ASPYHPTNEEFTTVSVDESAGKKHEYTLFQVVMSDNTDPQRP--LYTKASSFKLIHKLTHVAMWSDPKPLPDWAF 506
Cdd:pfam02815  84 SHEEqKPPLVEKEDWQKEVSAYGFRGFPGDNDIVEIFEKKSTTGMGSdrIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGF 163


                  ....
gi 19113599   507 KQLE 510
Cdd:pfam02815 164 GPEQ 167
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 567-771 1.07e-08

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 58.36  E-value: 1.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 567 LTEFHPYSSNPSDWFTLHHGIAFWAKSEEN-----------KQIYLLGNPIGWWiiagtvLSTTVVAAAEILLRQRgirt 635
Cdd:COG1928 321 LSSPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcgagkcvRAVLAIGNPALWW------LGLPALLWLLWRWIAR---- 390

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 636 lpetvrnhfyRSTMFFYMT--YVFHYLP-FFIMGRQLFLHHYLPAH----LAGSLLVGAFIQlacrksfrspvSAGVPip 708
Cdd:COG1928 391 ----------RDWRAGAVLvgYAAGWLPwFLYLDRTMFFFYAIPFVpflvLALALVLGLILG-----------PARAS-- 447

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113599 709 kdvdekghskchrkYGHVIELICTLLLIFVVIYCFTFFAPMTYGDkSLSVDEWTRRKWLDSWV 771
Cdd:COG1928 448 --------------ERRRLGRLVVGLYVGLVVANFAFFYPILTGL-PIPYDEWQARMWFPSWI 495
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 344-436 5.11e-08

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: 53.43  E-value: 5.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 344 IVTIKHMGTNAFLHSHPEKYpipyddgriSSG-GQQ-VTGY-QFDDENNYWMILPadhydpPIEAKLN--VPVKNMDYIK 418
Cdd:cd23293   6 VVKLLNTRHNVRLHSHDVKY---------GSGsGQQsVTGVeSSDDSNSYWQIRG------PTGADCErgTPIKCGQTIR 70

                        90
                ....*....|....*...
gi 19113599 419 LHHVGTNTDLMTHDVASP 436
Cdd:cd23293  71 LTHLNTGKNLHSHHFQSP 88
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 343-436 9.18e-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: 46.91  E-value: 9.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 343 DIVTIKHMGTNAFLHSHPEKYPIPYDDGRissggQQVTGYQFD----DENNYWM--ILPADHYDPpiEAKlnVPVKNMDY 416
Cdd:cd23283  70 DVVRLEHVATGRRLHSHDHRPPVSDNDWQ-----NEVSAYGYEgfegDANDDWRveILKDDSRPG--ESK--ERVRAIDT 140

                        90       100
                ....*....|....*....|.
gi 19113599 417 -IKLHHVGTNTDLMTHDVASP 436
Cdd:cd23283 141 kFRLVHVMTGCYLFSHGVKLP 161
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 343-434 5.92e-05

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: 44.29  E-value: 5.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 343 DIVTIKHMGTNAFLHSHPEKYPIpyddgrisSGGQQVTGYQFDDENNYwmilpADHYDPPIEAKLNVPVKNmDYIKLHHV 422
Cdd:cd23294  67 DVIRLQHVSTRKWLHSHLHASPL--------SGNQEVSCFGGDGNSDT-----GDNWIVEIEGGGKVWERD-QKVRLKHV 132

                        90
                ....*....|..
gi 19113599 423 GTNTDLMTHDVA 434
Cdd:cd23294 133 DTGGYLHSHDKK 144
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 345-391 6.44e-05

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: 44.29  E-value: 6.44e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 19113599 345 VTIKHMGTNAFLHSHPEKYpipyddGRISSGGQQVTGYQFDDENNYW 391
Cdd:cd23294 127 VRLKHVDTGGYLHSHDKKY------GRPIPGQQEVCAVASKNSNTLW 167
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 343-431 3.47e-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: 41.90  E-value: 3.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113599 343 DIVTIKHMGTNAFLHSHPEKYPIpyddgrisSGGQQVTGY--QFDDENNYWMILpadhydppIEAKLNVPVKNMDYIKLH 420
Cdd:cd23279  66 DIIRLQHVNTRKNLHSHNHSSPL--------SGNQEVSAFggGDEDSGDNWIVE--------CEGKKAKFWKRGEPVRLK 129

                        90
                ....*....|.
gi 19113599 421 HVGTNTDLMTH 431
Cdd:cd23279 130 HVDTGKYLSAS 140
 
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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