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Conserved domains on  [gi|50303519|ref|XP_451701|]
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uncharacterized protein KLLA0_B03762g [Kluyveromyces lactis]

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 ...
 343-530 5.67e-85

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: 267.24  E-value: 5.67e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 343 INYHDIITIKHKATDAFLHSHLAKYPVRYEDGRISSNGQQVTCYSHEDINNQWEILPPSG--SKFKKGAPVKLDADIRLR 420
Cdd:cd23285   1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPidEHEGTGRPVRNGDLIRLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 421 HVGTNTYLLAHDVASPYYPTNEEVTTVSEEEANgESYDFTLFRFQpILPKNSGRVAKTKNSAFRIFHVQTAVALWTHNDK 500
Cdd:cd23285  81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVE-IEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKP 158

                       170       180       190
                ....*....|....*....|....*....|
gi 50303519 501 lLPEWGFSQQEVNGNKKVQDPENNWFVDSI 530
Cdd:cd23285 159 -LPDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 67-314 9.00e-79

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: 253.39  E-value: 9.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519    67 LVTGLALVLRLWRISEPREVVFDEVHFGKFASYYLERTYFFDVHPPMAKMLIAAIGWLTGYNGSFKFDDIGYSYDTYYAP 146
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   147 FVAYRSLSAVLGVLTVSVVFQTMKELNFKAVTCFIAAFLIAVDNAHVTDTRLILLDAMLIFSIALSIYCYVRFYKLQlts 226
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKA--- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   227 PFSSEWYLWLYLTGFSLSMVMSTKYVGLLTYCTIGLAVVVNLWQLLDIRSGLSMRkVVKHTLVRINGLIIFPFVVYLFWF 306
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKS-IWKHLFARLFCLIVIPWALYLAQF 237


                  ....*...
gi 50303519   307 WCHFAILN 314
Cdd:pfam02366 238 YVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 554-765 2.37e-68

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: 223.58  E-value: 2.37e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   554 QKWYELQFLMFEHNNKLSSEHPFASNPQSWPLSLSGVSFWTKEEGRKQIFFTGNIVGWWFEIVSVALYLGLVVADLITRQ 633
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   634 RAVYAL-NKMARQKLYGPMAFLIFGWCIHYFPFFLMARQKFLHHYLPAHLILAMFSAALWEIVFTDNQSLDFDLDeedsk 712
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR----- 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 50303519   713 nphdaepkvyTIAYYLFCLSVIVNVGGCFIYFAPLVYGLSMTVDQIKARQWFD 765
Cdd:pfam16192 156 ----------KRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 343-530 5.67e-85

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: 267.24  E-value: 5.67e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 343 INYHDIITIKHKATDAFLHSHLAKYPVRYEDGRISSNGQQVTCYSHEDINNQWEILPPSG--SKFKKGAPVKLDADIRLR 420
Cdd:cd23285   1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPidEHEGTGRPVRNGDLIRLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 421 HVGTNTYLLAHDVASPYYPTNEEVTTVSEEEANgESYDFTLFRFQpILPKNSGRVAKTKNSAFRIFHVQTAVALWTHNDK 500
Cdd:cd23285  81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVE-IEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKP 158

                       170       180       190
                ....*....|....*....|....*....|
gi 50303519 501 lLPEWGFSQQEVNGNKKVQDPENNWFVDSI 530
Cdd:cd23285 159 -LPDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 67-314 9.00e-79

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: 253.39  E-value: 9.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519    67 LVTGLALVLRLWRISEPREVVFDEVHFGKFASYYLERTYFFDVHPPMAKMLIAAIGWLTGYNGSFKFDDIGYSYDTYYAP 146
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   147 FVAYRSLSAVLGVLTVSVVFQTMKELNFKAVTCFIAAFLIAVDNAHVTDTRLILLDAMLIFSIALSIYCYVRFYKLQlts 226
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKA--- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   227 PFSSEWYLWLYLTGFSLSMVMSTKYVGLLTYCTIGLAVVVNLWQLLDIRSGLSMRkVVKHTLVRINGLIIFPFVVYLFWF 306
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKS-IWKHLFARLFCLIVIPWALYLAQF 237


                  ....*...
gi 50303519   307 WCHFAILN 314
Cdd:pfam02366 238 YVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 554-765 2.37e-68

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: 223.58  E-value: 2.37e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   554 QKWYELQFLMFEHNNKLSSEHPFASNPQSWPLSLSGVSFWTKEEGRKQIFFTGNIVGWWFEIVSVALYLGLVVADLITRQ 633
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   634 RAVYAL-NKMARQKLYGPMAFLIFGWCIHYFPFFLMARQKFLHHYLPAHLILAMFSAALWEIVFTDNQSLDFDLDeedsk 712
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR----- 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 50303519   713 nphdaepkvyTIAYYLFCLSVIVNVGGCFIYFAPLVYGLSMTVDQIKARQWFD 765
Cdd:pfam16192 156 ----------KRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 67-311 6.17e-28

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 118.46  E-value: 6.17e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519  67 LVTGLALVLRLWRISEPREVVFDEVHFGKFASYYLER---------TYFFDVHPPMAKMLIAAIGWLTGYNGSFkfddig 137
Cdd:COG1928  27 LVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPLGKWLIALGEWLFGYVNPF------ 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 138 ysydtyyapfvAYRSLSAVLGVLTVSVVFQTMKELNFKAVTCFIAAFLIAVDNAHVTDTRLILLDAMLIFSIALSIYCYV 217
Cdd:COG1928 101 -----------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGCLL 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 218 --------RFYKLQLTSPFSSEW------YLWLYLTGFSLSMVMSTKYVGLLTYCTIGLAVVVNLWQLldiRSGLSMRKV 283
Cdd:COG1928 170 ldrdqvrrRLAAAVAAGRAPSRWgprlgfRWWRLAAGVLLGLACGVKWSGLYFLAAFGLLTVAWDAGA---RRAAGVRRP 246

                       250       260       270
                ....*....|....*....|....*....|....
gi 50303519 284 VKHTLVRiNGLIIF------PFVVYLFWFWCHFA 311
Cdd:COG1928 247 WLGALLR-DGIPAFfalvivPLLTYLASWTGWFA 279
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 359-527 5.02e-21

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: 91.27  E-value: 5.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   359 FLHSHLAKYPVRYEDGRISSnGQQVTCYSHEDINNQ----WEILPPSGSKFKkGAPVKLDADIRLRHVGTNTYLLAHDV- 433
Cdd:pfam02815  11 LFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSarslWRIEVVRHDAWR-GGLIKWGSPFRLRHLTTGRYLHSHEEq 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   434 ASPYYPTNEEVTTVSEEEANGESYD---FTLFRFQPILPKNSGRVaKTKNSAFRIFHVQTAVALWTHNDKlLPEWGF--S 508
Cdd:pfam02815  89 KPPLVEKEDWQKEVSAYGFRGFPGDndiVEIFEKKSTTGMGSDRI-KPGDSYFRLQHVCTGCWLFSHSVK-LPKWGFgpE 166

                         170
                  ....*....|....*....
gi 50303519   509 QQEVNGNKKVQDPENNWFV 527
Cdd:pfam02815 167 QQKVTCAKEGHMDDALTLP 185
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
343-400 2.29e-09

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 53.88  E-value: 2.29e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519    343 INYHDIITIKHKATDAFLHSHLAKYPvryedgRISSNGQQVTCYSH--EDINNQWEILPP 400
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLP------PWGDGQQEVTGYGNpaIDANTLWLIEPV 57
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 556-765 2.28e-07

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 54.13  E-value: 2.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 556 WYELQFLMFEHNNKLSSEHPFASNPQSWPLSLSGVSFW--TKEEG---------RKQIFFTGNIVGWWFEIVSvalyLGL 624
Cdd:COG1928 307 LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYyeTGQTGtlgcgagkcVRAVLAIGNPALWWLGLPA----LLW 382

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 625 VVADLITRQ--RAVYALnkmarqklygpmafliFGWCIHYFPFFLMA-RQKFLHHYLPA--HLILAmfsaalweIVFTDN 699
Cdd:COG1928 383 LLWRWIARRdwRAGAVL----------------VGYAAGWLPWFLYLdRTMFFFYAIPFvpFLVLA--------LALVLG 438

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50303519 700 QSLdfdldeedskNPHDAEPKVYTIAyyLFCLSVIVNVGGCFIYFAPLVYGLSMTVDQIKARQWFD 765
Cdd:COG1928 439 LIL----------GPARASERRRLGR--LVVGLYVGLVVANFAFFYPILTGLPIPYDEWQARMWFP 492
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 343-530 5.67e-85

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: 267.24  E-value: 5.67e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 343 INYHDIITIKHKATDAFLHSHLAKYPVRYEDGRISSNGQQVTCYSHEDINNQWEILPPSG--SKFKKGAPVKLDADIRLR 420
Cdd:cd23285   1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPidEHEGTGRPVRNGDLIRLR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 421 HVGTNTYLLAHDVASPYYPTNEEVTTVSEEEANgESYDFTLFRFQpILPKNSGRVAKTKNSAFRIFHVQTAVALWTHNDK 500
Cdd:cd23285  81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVE-IEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKP 158

                       170       180       190
                ....*....|....*....|....*....|
gi 50303519 501 lLPEWGFSQQEVNGNKKVQDPENNWFVDSI 530
Cdd:cd23285 159 -LPDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 67-314 9.00e-79

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: 253.39  E-value: 9.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519    67 LVTGLALVLRLWRISEPREVVFDEVHFGKFASYYLERTYFFDVHPPMAKMLIAAIGWLTGYNGSFKFDDIGYSYDTYYAP 146
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   147 FVAYRSLSAVLGVLTVSVVFQTMKELNFKAVTCFIAAFLIAVDNAHVTDTRLILLDAMLIFSIALSIYCYVRFYKLQlts 226
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKA--- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   227 PFSSEWYLWLYLTGFSLSMVMSTKYVGLLTYCTIGLAVVVNLWQLLDIRSGLSMRkVVKHTLVRINGLIIFPFVVYLFWF 306
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKS-IWKHLFARLFCLIVIPWALYLAQF 237


                  ....*...
gi 50303519   307 WCHFAILN 314
Cdd:pfam02366 238 YVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 554-765 2.37e-68

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: 223.58  E-value: 2.37e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   554 QKWYELQFLMFEHNNKLSSEHPFASNPQSWPLSLSGVSFWTKEEGRKQIFFTGNIVGWWFEIVSVALYLGLVVADLITRQ 633
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   634 RAVYAL-NKMARQKLYGPMAFLIFGWCIHYFPFFLMARQKFLHHYLPAHLILAMFSAALWEIVFTDNQSLDFDLDeedsk 712
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRSLR----- 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 50303519   713 nphdaepkvyTIAYYLFCLSVIVNVGGCFIYFAPLVYGLSMTVDQIKARQWFD 765
Cdd:pfam16192 156 ----------KRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 343-528 3.77e-37

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: 137.46  E-value: 3.77e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 343 INYHDIITIKH-KATDAFLHSHLAKYPvryeDGrisSNGQQVTCYSHEDINNQWEILPPSG-SKFKKGAPVKL-DAD-IR 418
Cdd:cd23276   1 VAYGSQITLRNaNSGGGYLHSHNHTYP----DG---SKQQQVTGYGHKDENNWWQILKPRGdPSSNPPDPEYVrDGDeVR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 419 LRHVGTNTYLLAHDVASPYYPTNeeVTTVSEEEANGESYDFTLFRFQpILPKNSG---RVAKTKNSAFRIFHVQTAVALW 495
Cdd:cd23276  74 LLHKETNRYLRTHDAAAPVTSKH--KEVSAYPDENEDGDDNDLWVVE-IVKDEGKledKRIKPLTTRFRLRNKKTGCYLT 150

                       170       180       190
                ....*....|....*....|....*....|....
gi 50303519 496 THNDKlLPEWGFSQQEVNGNKKV-QDPENNWFVD 528
Cdd:cd23276 151 SSGVK-LPEWGFRQGEVVCSKNKeSDPSTLWNVE 183
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 343-528 4.43e-37

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: 137.44  E-value: 4.43e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 343 INYHDIITIKHKAT-DAFLHSHLAKYPVRYEDGRISSNGQQVTCYSHEDINNQWEILPPSGSKFKKGAPVKL--DAD-IR 418
Cdd:cd23281   1 VAYGSQVTLRNTHGsPCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDPPRPvrHGDiIQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 419 LRHVGTNTYLLAHDVASPYYPTNEEVTTVSEEEANGESYDftLFRFQPILPKNSGRVAKTKNSAFRIFHVQTAVALWThN 498
Cdd:cd23281  81 LVHGKTGRFLNSHDVAAPLSPTHQEVSCYIDYNISMPAQN--LWRIEIVNRDSEGDTWKAIKSQFRLIHVNTSAALKL-S 157

                       170       180       190
                ....*....|....*....|....*....|
gi 50303519 499 DKLLPEWGFSQQEVNGNKKVQDPENNWFVD 528
Cdd:cd23281 158 GKQLPDWGFGQLEVATDRAGNQSSTVWNVE 187
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 67-311 6.17e-28

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 118.46  E-value: 6.17e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519  67 LVTGLALVLRLWRISEPREVVFDEVHFGKFASYYLER---------TYFFDVHPPMAKMLIAAIGWLTGYNGSFkfddig 137
Cdd:COG1928  27 LVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPLGKWLIALGEWLFGYVNPF------ 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 138 ysydtyyapfvAYRSLSAVLGVLTVSVVFQTMKELNFKAVTCFIAAFLIAVDNAHVTDTRLILLDAMLIFSIALSIYCYV 217
Cdd:COG1928 101 -----------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGCLL 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 218 --------RFYKLQLTSPFSSEW------YLWLYLTGFSLSMVMSTKYVGLLTYCTIGLAVVVNLWQLldiRSGLSMRKV 283
Cdd:COG1928 170 ldrdqvrrRLAAAVAAGRAPSRWgprlgfRWWRLAAGVLLGLACGVKWSGLYFLAAFGLLTVAWDAGA---RRAAGVRRP 246

                       250       260       270
                ....*....|....*....|....*....|....
gi 50303519 284 VKHTLVRiNGLIIF------PFVVYLFWFWCHFA 311
Cdd:COG1928 247 WLGALLR-DGIPAFfalvivPLLTYLASWTGWFA 279
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 345-529 8.42e-26

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: 105.07  E-value: 8.42e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 345 YHDIITIKHKATDA-FLHSHLAKYPVryedgriSSNGQQVTCYSHEDINNQWEILPP--SGSKFKKG-APVKLDADIRLR 420
Cdd:cd23283   3 YGSTIRIRHLNTRGgYLHSHPHNYPA-------GSKQQQITLYPHRDENNDWLVELAnaPEEWSPTTfENLKDGDVVRLE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 421 HVGTNTYLLAHDVASP------------Y-YPTNEevttvseeeanGESYDftLFRFQpILPKNS-GRVAK----TKNSA 482
Cdd:cd23283  76 HVATGRRLHSHDHRPPvsdndwqnevsaYgYEGFE-----------GDAND--DWRVE-ILKDDSrPGESKervrAIDTK 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 50303519 483 FRIFHVQTAVALWTHNDKlLPEWGFSQQEVNGNKKVQDPENNWFVDS 529
Cdd:cd23283 142 FRLVHVMTGCYLFSHGVK-LPEWGFEQQEVTCAKSGLLELSLWYIET 187
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 345-532 5.93e-24

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: 99.69  E-value: 5.93e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 345 YHDIITIK-HKATDAFLHSHLAKYPVRYEdgrisSNGQQVTCYSHEDINNQWEILPPSGSKFKKGaPVKL--DAD-IRLR 420
Cdd:cd23282   3 YGSVITLKnHRTGGGYLHSHWHLYPEGVG-----ARQQQVTTYSHKDDNNLWLIKKHNQSSDLSD-PVEYvrHGDlIRLE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 421 HVGTNTYLLAHDVASPY---------YPTNeevttvseeeANGESYDFtlFRFQpILPKNSGRVAKTKNSAFRIFHVQTA 491
Cdd:cd23282  77 HVNTKRNLHSHKEKAPLtkkhyqvtgYGEN----------GTGDANDV--WRVE-VVGGREGDPVKTVRSKFRLVHYNTG 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 50303519 492 VALWTHNdKLLPEWGFSQQEVNGNKKVQDPENNWFVDSIVN 532
Cdd:cd23282 144 CALHSHG-KQLPKWGWEQLEVTCNPNVRDKNSLWNVEDNRN 183
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 359-527 5.02e-21

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: 91.27  E-value: 5.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   359 FLHSHLAKYPVRYEDGRISSnGQQVTCYSHEDINNQ----WEILPPSGSKFKkGAPVKLDADIRLRHVGTNTYLLAHDV- 433
Cdd:pfam02815  11 LFHSHQDEYLTGSEQQQKQP-FLRITLYPHGDANNSarslWRIEVVRHDAWR-GGLIKWGSPFRLRHLTTGRYLHSHEEq 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   434 ASPYYPTNEEVTTVSEEEANGESYD---FTLFRFQPILPKNSGRVaKTKNSAFRIFHVQTAVALWTHNDKlLPEWGF--S 508
Cdd:pfam02815  89 KPPLVEKEDWQKEVSAYGFRGFPGDndiVEIFEKKSTTGMGSDRI-KPGDSYFRLQHVCTGCWLFSHSVK-LPKWGFgpE 166

                         170
                  ....*....|....*....
gi 50303519   509 QQEVNGNKKVQDPENNWFV 527
Cdd:pfam02815 167 QQKVTCAKEGHMDDALTLP 185
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 347-527 1.24e-20

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: 89.75  E-value: 1.24e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 347 DIITIKHKATDAFLHSHLAKYPVryedgriSSNGQQVTCYSHE---DINNQWEILPPSGskfKKGAPVKLDADIRLRHVG 423
Cdd:cd23263   2 DVIWLKHSETGKYLHSHRKNYPT-------GSGQQEVTFESSSrkgDTNGLWIIESENG---KQGGPVKWGDKIRLRHLS 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 424 TNTYLLAHdvaspYYPTNEEVTTVSEEEANGESYDFTLFRFQPILPKNSGRVAKTKNSAFRIFHVQTAVALWTHNDKlLP 503
Cdd:cd23263  72 TGKYLSSE-----EGKKSPKSNHQEVLCLTDNPDKSSLFKFEPIGSTKYKQKYVKKDSYFRLKHVNTNFWLHSHEKK-FN 145

                       170       180
                ....*....|....*....|....
gi 50303519 504 EWGFSQQEVNGNKKvQDPENNWFV 527
Cdd:cd23263 146 INNKTQQEVICHGE-REEVFKLWK 168
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 343-530 7.10e-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: 88.26  E-value: 7.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 343 INYHDIITIKHKAT-DAFLHSHLAKYPvryedgrISSNGQQVTCYSHE-DINNQWEILPP----SGSKFKKGAPVKLDAD 416
Cdd:cd23286   1 LLYGSTVTIRHLESlGGYLHSHDLTYP-------SGSNEQQVTLYDFEdDANNEWIIETKtkeqMDKFPGQFREVRDGDV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 417 IRLRHVGTNTYLLAHDVASPYYPTNEEVTTVSEEEAN--GESYDFTLFRFQPILPKNSGRVAKTK----NSAFRIFHVQT 490
Cdd:cd23286  74 IRLRHVVTGKLLRASNARPPVSEQEYNNEVSCTGNANysGDMDENWRIDVKGDESHAELKLPNIKikstESVFQLYNRGT 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 50303519 491 AVALWTHnDKLLPEWGFSQQEVNGNKKVQDPENNWFVDSI 530
Cdd:cd23286 154 GCTLLSH-DTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 342-532 8.02e-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: 85.06  E-value: 8.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 342 SINYHDIITIK-HKATDAFLHSHLAKYPvryeDGrisSNGQQVTCYSHEDINNQWEILPPSGSKFKKG-----APVKLDA 415
Cdd:cd23284   3 DVAYGSKVTIKnQGLGGGLLHSHVQTYP----EG---SNQQQVTCYGHKDSNNEWIFERPRGLPSWDEndtdiEFIKDGD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 416 DIRLRHVGTNTYLLAHDVASPYYPTNEEVTTVSEEEANGESYDFTLFRFQPILPKNSGRVaKTKNSAFRIFHVQTAVALW 495
Cdd:cd23284  76 IVRLVHKQTGRNLHSHPVPAPISKSDYEVSGYGDLTVGDEKDNWVIEIVKQVGSEDPKKL-HTLTTSFRLRHEVLGCYLA 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 50303519 496 THNDKlLPEWGFSQQEVngnkkVQDPENN-------WFVDSIVN 532
Cdd:cd23284 155 QTGVS-LPEWGFKQGEV-----VCDKSNFkrdkrtwWNIETHTN 192
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 345-436 8.38e-18

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: 81.58  E-value: 8.38e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 345 YHDIITIKHKATDAFLHSHlakyPVRYEDGrisSNGQQVTCYSH-EDINNQWEILPPSGSKFKK-GAPVKLDADIRLRHV 422
Cdd:cd23279   1 YGSAIKLKHVNSGYRLHSH----EVSYGSG---SGQQSVTAVPSaDDANSLWTVLPGLGEPCQEqGKPVKCGDIIRLQHV 73

                        90
                ....*....|....
gi 50303519 423 GTNTYLLAHDVASP 436
Cdd:cd23279  74 NTRKNLHSHNHSSP 87
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 343-534 1.37e-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: 69.71  E-value: 1.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 343 INYHDIITIKHKATDAFLHSHLAKYpvryedGRISsnGQQ-VTCY-SHEDINNQWEILPPSGSKFKKGAPVKLDADIRLR 420
Cdd:cd23294   1 VTCGSVIKLQHERTKFRLHSHEVPY------GSGS--GQQsVTGFpGVDDSNSYWIVKPANGERCKQGDVIKNGDVIRLQ 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 421 HVGTNTYLLAHDVASPYypTNEEVTTVSEEEANGESYDFTlfrfqpILPKNSGRVAKTKNSAFRIFHVQTAVALWTHNDK 500
Cdd:cd23294  73 HVSTRKWLHSHLHASPL--SGNQEVSCFGGDGNSDTGDNW------IVEIEGGGKVWERDQKVRLKHVDTGGYLHSHDKK 144

                       170       180       190
                ....*....|....*....|....*....|....*
gi 50303519 501 LL-PEWGfsQQEVNGNKKvQDPENNWFVDSIVNMP 534
Cdd:cd23294 145 YGrPIPG--QQEVCAVAS-KNSNTLWLAAEGVYFP 176
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 348-436 8.89e-13

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: 67.30  E-value: 8.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 348 IITIKHKATDAFLHSHLAKYpvryedGriSSNGQQ-VTCY-SHEDINNQWEILPPSGSKFKKGAPVKLDADIRLRHVGTN 425
Cdd:cd23293   6 VVKLLNTRHNVRLHSHDVKY------G--SGSGQQsVTGVeSSDDSNSYWQIRGPTGADCERGTPIKCGQTIRLTHLNTG 77

                        90
                ....*....|.
gi 50303519 426 TYLLAHDVASP 436
Cdd:cd23293  78 KNLHSHHFQSP 88
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 66-309 9.96e-13

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: 69.65  E-value: 9.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519  66 YLVTGLALVLRLWRIS--------EPR--EVVFDEVHFGKFASYYLERTYFFDvHPPMAKMLIAAIGWLTGYNgsfkfdd 135
Cdd:COG1807  11 LLLLLLALLLRLLGLGslplwdpdEARyaEIAREMLESGDWLTPTLAGEPYFD-KPPLIYWLIALSYKLFGVS------- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 136 igysydtyyapFVAYRSLSAVLGVLTVSVVFQTMKELnFKAVTCFIAAFLIAVDNAHVTDTRLILLDAMLIFSIALSIYC 215
Cdd:COG1807  83 -----------EFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALYA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 216 YVRFYKlqltspfsSEWYLWLYLTGFSLSMVMSTKYVGLLTYctIGLAVVVNLWQLLDIRSGLSMRKVVkhtlvrinGLI 295
Cdd:COG1807 151 LLRALE--------RRRLRWLLLAGLALGLGFLTKGPVALLL--PGLALLLYLLLTRRWRRLRRLRLLL--------GLL 212

                       250
                ....*....|....
gi 50303519 296 IFpFVVYLFWFWCH 309
Cdd:COG1807 213 LA-LLLALPWYIAN 225
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 325-440 3.37e-12

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: 65.78  E-value: 3.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 325 SDFQDTLLDAPGAVEIKSINY---HDIITIKHKATDAFLHSHLAKYPVRYEDgrissNGQQVTCYSHE----DINNQW-- 395
Cdd:cd23283  45 NDWLVELANAPEEWSPTTFENlkdGDVVRLEHVATGRRLHSHDHRPPVSDND-----WQNEVSAYGYEgfegDANDDWrv 119

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 50303519 396 EILP-PSGSKFKKGAPVKLDADIRLRHVGTNTYLLAHDVaspYYPT 440
Cdd:cd23283 120 EILKdDSRPGESKERVRAIDTKFRLVHVMTGCYLFSHGV---KLPE 162
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
343-400 2.29e-09

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 53.88  E-value: 2.29e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519    343 INYHDIITIKHKATDAFLHSHLAKYPvryedgRISSNGQQVTCYSH--EDINNQWEILPP 400
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLP------PWGDGQQEVTGYGNpaIDANTLWLIEPV 57
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 347-428 3.67e-09

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: 56.54  E-value: 3.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 347 DIITIKHKATDAFLHSHLAKYPVryedgrisSNGQQVTCY--SHEDINNQW--EILPPSGSKFKKGAPVkldadiRLRHV 422
Cdd:cd23279  66 DIIRLQHVNTRKNLHSHNHSSPL--------SGNQEVSAFggGDEDSGDNWivECEGKKAKFWKRGEPV------RLKHV 131


                ....*.
gi 50303519 423 GTNTYL 428
Cdd:cd23279 132 DTGKYL 137
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 556-765 2.28e-07

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 54.13  E-value: 2.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 556 WYELQFLMFEHNNKLSSEHPFASNPQSWPLSLSGVSFW--TKEEG---------RKQIFFTGNIVGWWFEIVSvalyLGL 624
Cdd:COG1928 307 LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYyeTGQTGtlgcgagkcVRAVLAIGNPALWWLGLPA----LLW 382

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 625 VVADLITRQ--RAVYALnkmarqklygpmafliFGWCIHYFPFFLMA-RQKFLHHYLPA--HLILAmfsaalweIVFTDN 699
Cdd:COG1928 383 LLWRWIARRdwRAGAVL----------------VGYAAGWLPWFLYLdRTMFFFYAIPFvpFLVLA--------LALVLG 438

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50303519 700 QSLdfdldeedskNPHDAEPKVYTIAyyLFCLSVIVNVGGCFIYFAPLVYGLSMTVDQIKARQWFD 765
Cdd:COG1928 439 LIL----------GPARASERRRLGR--LVVGLYVGLVVANFAFFYPILTGLPIPYDEWQARMWFP 492
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 109-270 2.84e-07

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


Pssm-ID: 433048 [Multi-domain]  Cd Length: 160  Bit Score: 50.72  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   109 VHPPMAKMLIAAIGWLTGYNGsfkfddigysydtyyapfVAYRSLSAVLGVLTVSVVFQTMKELnFKAVTCFIAAFLIAV 188
Cdd:pfam13231   1 DHPPLAAWLIALFTALFGDSE------------------WAVRLPSALAGVLTILLLYLLARRL-FGKRAALLAALLLAV 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   189 DNAHVTDTRLILLDAMLIFSIALSIYCYVRFYKLQLTSpfssewylWLYLTGFSLSMVMSTKYVGLLTYCTIGLAVVVNL 268
Cdd:pfam13231  62 VPLFVALSRLFTPDAPLLLFWALALYFLLRALEKGRLK--------WWLLAGAAAGLGFLSKYTAALLVLAALLYLLISP 133


                  ..
gi 50303519   269 WQ 270
Cdd:pfam13231 134 GR 135
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 345-433 3.06e-07

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: 50.84  E-value: 3.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 345 YHDIITIKHKATDAFLHSHlakypvrYEDGRISSNGQQVTCYS-HEDINNQWEILpPSGSKFKKGAPVKLDADIRLRHVG 423
Cdd:cd23263  61 WGDKIRLRHLSTGKYLSSE-------EGKKSPKSNHQEVLCLTdNPDKSSLFKFE-PIGSTKYKQKYVKKDSYFRLKHVN 132

                        90
                ....*....|
gi 50303519 424 TNTYLLAHDV 433
Cdd:cd23263 133 TNFWLHSHEK 142
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
480-527 7.82e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 43.87  E-value: 7.82e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 50303519    480 NSAFRIFHVQTAVALWTHNDKlLPEWGFSQQEVNGNK-KVQDPENNWFV 527
Cdd:smart00472   7 GDVVRLRHVTTGRYLHSHDEK-LPPWGDGQQEVTGYGnPAIDANTLWLI 54
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 347-428 9.09e-06

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: 46.88  E-value: 9.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 347 DIITIKHKATDAFLHSHLAKYPVryedgrisSNGQQVTCYSHE---DINNQWEILPpSGSKFKKgapvklDADIRLRHVG 423
Cdd:cd23293  67 QTIRLTHLNTGKNLHSHHFQSPL--------SGNQEVSAFGEDgegDTGDNWTVVC-SGTYWER------DEAVRLKHVD 131


                ....*
gi 50303519 424 TNTYL 428
Cdd:cd23293 132 TEVYL 136
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 341-436 4.80e-04

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: 42.04  E-value: 4.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 341 KSINYHDIITIKHKATDAFLHSHLAKYPVRYED--GRISSNGQqvTCYShEDINNQWEIL-----PPSGSKFKKGAPVKL 413
Cdd:cd23286  66 REVRDGDVIRLRHVVTGKLLRASNARPPVSEQEynNEVSCTGN--ANYS-GDMDENWRIDvkgdeSHAELKLPNIKIKST 142

                        90       100
                ....*....|....*....|...
gi 50303519 414 DADIRLRHVGTNTYLLAHDVASP 436
Cdd:cd23286 143 ESVFQLYNRGTGCTLLSHDTRLP 165
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
 67-272 5.41e-04

Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General function prediction only];


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 43.50  E-value: 5.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519  67 LVTGLALVLRLWRISEpREVVFDEVHFGKFASYYLER-TYFFD--VHPPMAKMLIAAIGWLTGYngsfkfDDigysydty 143
Cdd:COG4745  21 AITALALLLRLVGLGA-RPFHWDEARVAYWSLRLLETgAYEYRpiYHGPFLYHVTAALFGLFGA------SD-------- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 144 yapFVAyRSLSAVLGVLTVSVVFQTMKELNFKAVtcFIAAFLIAVDNAHVTDTRLILLDAMLIFSIALSIYCYVRFYKlq 223
Cdd:COG4745  86 ---FTA-RLPVALVGGLLPLLALLLRERLGDAEV--LALALLLAFSPVLVYYSRFMRNDVLLAAFTLLALGAAVRAID-- 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 50303519 224 ltspFSSEWylWLYLTGFSLSMVMSTKYVGLLTYCTIGLAVVVNLWQLL 272
Cdd:COG4745 158 ----TRRRR--YLYLAAVALALAFATKENAVLYLLCWLGALLLLLDHRL 200
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 347-436 7.49e-04

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: 41.20  E-value: 7.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519   347 DIITIKHKATDAFLHSHLAKYPVRYEDgriSSNGQQVTCY---SHEDINNQWEILPPSGSKFKKGAPVK-LDADIRLRHV 422
Cdd:pfam02815  69 SPFRLRHLTTGRYLHSHEEQKPPLVEK---EDWQKEVSAYgfrGFPGDNDIVEIFEKKSTTGMGSDRIKpGDSYFRLQHV 145

                          90
                  ....*....|....
gi 50303519   423 GTNTYLLAHDVASP 436
Cdd:pfam02815 146 CTGCWLFSHSVKLP 159
COG5305 COG5305
Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT ...
 148-320 1.93e-03

Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT family [General function prediction only];


Pssm-ID: 444104 [Multi-domain]  Cd Length: 402  Bit Score: 41.17  E-value: 1.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 148 VAYRSLSAVLGVLTVSVVFQTMKELNFKAVTCFIAAFLIAVDNAHV---TDTRLIlldAMLIFSIALSIYCYVRFYKLQl 224
Cdd:COG5305 108 WALRSLSALFGLLAIPLIYWLGRELFRSRRVALLAAALMAVSPFHIyyaQEARMY---SLLTLLVLLSLLALLRALRRP- 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 225 tspfsSEWYLWLYltGFSLSMVMSTKYVGLLTYCTIGLAVVVNLWQLLDIRsglsmrkvvkhTLVRINGLIIFPFVVYLF 304
Cdd:COG5305 184 -----TRRLWLLY--ALANALGLYTHYFFALVLIAHGLYLLLLAWFRRDRK-----------TWLRYLLAAAAAVLLFLP 245

                       170
                ....*....|....*.
gi 50303519 305 WFWchfAILNQSGPGD 320
Cdd:COG5305 246 WLL---VLLTQLSRGN 258
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
 110-218 2.11e-03

Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 41.13  E-value: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 110 HPPMAKMLIAAIGWLTGYNgsfkfddigysydtyyaPFvAYRSLSAVLGVLTVSVVFQTMKELNFKAVTCFIAAFLIAVD 189
Cdd:COG4346  79 HPPLGKYIIALSMLLLGDK-----------------PL-YWRLPSIILGALIVILVFLTARRLSGNIVAGLIASLLLALD 140

                        90       100
                ....*....|....*....|....*....
gi 50303519 190 NAHVTDTRLILLDAMLIFSIALSIYCYVR 218
Cdd:COG4346 141 PLLRVMSSIAMLDIYVAFFTALALYFAVS 169
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
408-441 2.64e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 36.55  E-value: 2.64e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 50303519    408 GAPVKLDADIRLRHVGTNTYLLAHDVasPYYPTN 441
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDE--KLPPWG 32
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 347-538 4.37e-03

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: 39.29  E-value: 4.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 347 DIITIKHKATDAFLHSH-LAKYPVRYEDGRissngQQVTcysHEDINNQWEILPPSGSK--FK--------KGAPVKLDA 415
Cdd:cd23280  11 DVVRLFHKELEAYLSAEgSFVDEVLTEDVH-----LRVR---PVDDRKPRTLFPPTSGDtfWQiekedtplKGGVIKWGD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50303519 416 DIRLRHVGTNTYLLAHDVASPYYPTneevttvseeEANGESYDFTLFRFQPILPKNSGRVAKTknSAFRIFHVQTavALW 495
Cdd:cd23280  83 QCRLRHLPTGKYLAVDDKTGNGKVV----------LTSDPSDPSTVFRLHPVTKETSEEVKFG--SYVRIEHVAT--GTW 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 50303519 496 THNDKLLPEWGFSqqevNGNKKVQDPENNWF-VDSIVNMPENDS 538
Cdd:cd23280 149 LHAETDEELRRSK----KSPAGLSWDGAKLRkVSLSLERQDDDA 188
 
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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