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Conserved domains on  [gi|389631735|ref|XP_003713520|]
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dolichyl-phosphate-mannose-protein mannosyltransferase 4 [Pyricularia oryzae 70-15]

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 ...
 336-520 1.41e-104

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: 318.47  E-value: 1.41e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 336 INYYDTITLRHKETKTYLHSHPDRYPLRYDDGRVSSQGQQVTGYPFNDTNNYWQILPMNDDKQE---GRVVRHQELVRLR 412
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDEHegtGRPVRNGDLIRLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 413 HLGTDTILLSHDVASPYYPTNQEFTTCSLTDAYgDRAKDTLFEVRFENGKPGQEFKSIASHFKLIHNPSKVAMWTHTTPL 492
Cdd:cd23285   81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVEIEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKPL 159

                        170       180
                 ....*....|....*....|....*...
gi 389631735 493 PEWGHKQQEINGNKQVTVSSNVWFVEDI 520
Cdd:cd23285  160 PDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 58-307 5.92e-83

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: 264.17  E-value: 5.92e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735   58 VITVLAFITRFWGISHPNEVVFDEVHFGKFASYYLQKTYFFDVHPPFGKLLFAFMGWLVGYDGHFHFDNIGDSYVVNKVP 137
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  138 YVAFRSLPALLGALTVSVVYLIMWESGYSVPACILAAGLVLFDNAHIGQTRLILLDATLVFAFACSLLCYIKFYkmRHEP 217
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  218 FSRKWWKWLILTGFALSCDISTKYVGVFAFISIGSAVVIDLWDLLDvkrkDGALSLPIWAKHFSARAFGLIIMPFIFYLF 297
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLG----DLSLLLKSIWKHLFARLFCLIVIPWALYLA 235

                         250
                  ....*....|
gi 389631735  298 WFQVHFAVLT 307
Cdd:pfam02366 236 QFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 544-766 2.87e-77

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: 247.46  E-value: 2.87e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  544 QKWFELQRSMFWHNSRLTSSHPYASLPYQWPFLLRGVSFWTQNDTRQQIYFLGNPIGWWLASSLLAVYIGILAADQFSLR 623
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  624 RGVDAL-DHRSRSRLYNSTGFFFLSWLTHYVPFYVMGRQLFLHHYLPSHLASCLVAGALIEFICNSDPMdgddvpatggk 702
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRR----------- 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389631735  703 kavavkpkrhitaaeRFAGKSLMVTWAVCMGILAIVIAGWYFFLPLTYGYPGLSvDQVLRRKWL 766
Cdd:pfam16192 150 ---------------LPRSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWL 197
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 336-520 1.41e-104

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: 318.47  E-value: 1.41e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 336 INYYDTITLRHKETKTYLHSHPDRYPLRYDDGRVSSQGQQVTGYPFNDTNNYWQILPMNDDKQE---GRVVRHQELVRLR 412
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDEHegtGRPVRNGDLIRLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 413 HLGTDTILLSHDVASPYYPTNQEFTTCSLTDAYgDRAKDTLFEVRFENGKPGQEFKSIASHFKLIHNPSKVAMWTHTTPL 492
Cdd:cd23285   81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVEIEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKPL 159

                        170       180
                 ....*....|....*....|....*...
gi 389631735 493 PEWGHKQQEINGNKQVTVSSNVWFVEDI 520
Cdd:cd23285  160 PDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 58-307 5.92e-83

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: 264.17  E-value: 5.92e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735   58 VITVLAFITRFWGISHPNEVVFDEVHFGKFASYYLQKTYFFDVHPPFGKLLFAFMGWLVGYDGHFHFDNIGDSYVVNKVP 137
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  138 YVAFRSLPALLGALTVSVVYLIMWESGYSVPACILAAGLVLFDNAHIGQTRLILLDATLVFAFACSLLCYIKFYkmRHEP 217
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  218 FSRKWWKWLILTGFALSCDISTKYVGVFAFISIGSAVVIDLWDLLDvkrkDGALSLPIWAKHFSARAFGLIIMPFIFYLF 297
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLG----DLSLLLKSIWKHLFARLFCLIVIPWALYLA 235

                         250
                  ....*....|
gi 389631735  298 WFQVHFAVLT 307
Cdd:pfam02366 236 QFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 544-766 2.87e-77

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: 247.46  E-value: 2.87e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  544 QKWFELQRSMFWHNSRLTSSHPYASLPYQWPFLLRGVSFWTQNDTRQQIYFLGNPIGWWLASSLLAVYIGILAADQFSLR 623
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  624 RGVDAL-DHRSRSRLYNSTGFFFLSWLTHYVPFYVMGRQLFLHHYLPSHLASCLVAGALIEFICNSDPMdgddvpatggk 702
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRR----------- 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389631735  703 kavavkpkrhitaaeRFAGKSLMVTWAVCMGILAIVIAGWYFFLPLTYGYPGLSvDQVLRRKWL 766
Cdd:pfam16192 150 ---------------LPRSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWL 197
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 58-300 7.44e-27

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 114.99  E-value: 7.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  58 VITVLAFITRFWGISHPNEVVFDEVHFGKFASYYLQ---------KTYFFDVHPPFGKLLFAFMGWLVGYDGHFhfdnig 128
Cdd:COG1928   27 LVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTngyernwpdPGPFFVVHPPLGKWLIALGEWLFGYVNPF------ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 129 dsyvvnkvpyvAFRSLPALLGALTVSVVYLIMWESGYSVPACILAAGLVLFDNAHIGQTRLILLDATLVF----AFACSL 204
Cdd:COG1928  101 -----------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFfvlaAFGCLL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 205 L-----------CYIKFYKMRHEPFSRKWWKWLILTGFALSCDISTKYVGVFAFISIGSAVVidLWDLLdvKRKDGALSL 273
Cdd:COG1928  170 LdrdqvrrrlaaAVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLYFLAAFGLLTV--AWDAG--ARRAAGVRR 245

                        250       260       270
                 ....*....|....*....|....*....|....
gi 389631735 274 PIWA---KHFSARAFGLIIMPFIFYLF----WFQ 300
Cdd:COG1928  246 PWLGallRDGIPAFFALVIVPLLTYLAswtgWFA 279
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 354-502 3.01e-18

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: 83.18  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  354 HSHPDRYPLRYDDGRVSSQgQQVTGYPFNDTNNY----WQILPMNDDKQEGRVVRHQELVRLRHLGTDTILLSHDV-ASP 428
Cdd:pfam02815  13 HSHQDEYLTGSEQQQKQPF-LRITLYPHGDANNSarslWRIEVVRHDAWRGGLIKWGSPFRLRHLTTGRYLHSHEEqKPP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  429 YYPTNQEFTTCSltdAYG------DRAKDTLFEVRFENGKPGQEFKSIASHFKLIHNPSKVAMWTHTTPLPEWGHK--QQ 500
Cdd:pfam02815  92 LVEKEDWQKEVS---AYGfrgfpgDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpeQQ 168


                  ..
gi 389631735  501 EI 502
Cdd:pfam02815 169 KV 170
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 546-766 7.50e-12

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 68.38  E-value: 7.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 546 WFELQRSMFWHNSRLTSSHPYASLPYQWPFLLRGVSFWTQNDTR-----------QQIYFLGNPIGWWLASSLLAVYIGI 614
Cdd:COG1928  307 LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcgagkcvRAVLAIGNPALWWLGLPALLWLLWR 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 615 LAAdqfslRRgvdalDHRSrsrlynstGFFFLSWLTHYVP-FYVMGRQLFLHHYLPSH----LASCLVAGALIeficnsd 689
Cdd:COG1928  387 WIA-----RR-----DWRA--------GAVLVGYAAGWLPwFLYLDRTMFFFYAIPFVpflvLALALVLGLIL------- 441

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 389631735 690 pmdgddvpatggkkavavkpkRHITAAERfagkSLMVTWAVCMgILAIVIAGWYFFLPLTYGYPgLSVDQVLRRKWL 766
Cdd:COG1928  442 ---------------------GPARASER----RRLGRLVVGL-YVGLVVANFAFFYPILTGLP-IPYDEWQARMWF 491
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
334-392 9.23e-09

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 51.96  E-value: 9.23e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 389631735   334 ITINYYDTITLRHKETKTYLHSHPDRYPlryddgRVSSQGQQVTGYPFN--DTNNYWQILP 392
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEKLP------PWGDGQQEVTGYGNPaiDANTLWLIEP 56
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 336-520 1.41e-104

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: 318.47  E-value: 1.41e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 336 INYYDTITLRHKETKTYLHSHPDRYPLRYDDGRVSSQGQQVTGYPFNDTNNYWQILPMNDDKQE---GRVVRHQELVRLR 412
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDEHegtGRPVRNGDLIRLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 413 HLGTDTILLSHDVASPYYPTNQEFTTCSLTDAYgDRAKDTLFEVRFENGKPGQEFKSIASHFKLIHNPSKVAMWTHTTPL 492
Cdd:cd23285   81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVEIEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKPL 159

                        170       180
                 ....*....|....*....|....*...
gi 389631735 493 PEWGHKQQEINGNKQVTVSSNVWFVEDI 520
Cdd:cd23285  160 PDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 58-307 5.92e-83

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: 264.17  E-value: 5.92e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735   58 VITVLAFITRFWGISHPNEVVFDEVHFGKFASYYLQKTYFFDVHPPFGKLLFAFMGWLVGYDGHFHFDNIGDSYVVNKVP 137
Cdd:pfam02366   2 ILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  138 YVAFRSLPALLGALTVSVVYLIMWESGYSVPACILAAGLVLFDNAHIGQTRLILLDATLVFAFACSLLCYIKFYkmRHEP 217
Cdd:pfam02366  82 YFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  218 FSRKWWKWLILTGFALSCDISTKYVGVFAFISIGSAVVIDLWDLLDvkrkDGALSLPIWAKHFSARAFGLIIMPFIFYLF 297
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLG----DLSLLLKSIWKHLFARLFCLIVIPWALYLA 235

                         250
                  ....*....|
gi 389631735  298 WFQVHFAVLT 307
Cdd:pfam02366 236 QFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 544-766 2.87e-77

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: 247.46  E-value: 2.87e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  544 QKWFELQRSMFWHNSRLTSSHPYASLPYQWPFLLRGVSFWTQNDTRQQIYFLGNPIGWWLASSLLAVYIGILAADQFSLR 623
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  624 RGVDAL-DHRSRSRLYNSTGFFFLSWLTHYVPFYVMGRQLFLHHYLPSHLASCLVAGALIEFICNSDPMdgddvpatggk 702
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRR----------- 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389631735  703 kavavkpkrhitaaeRFAGKSLMVTWAVCMGILAIVIAGWYFFLPLTYGYPGLSvDQVLRRKWL 766
Cdd:pfam16192 150 ---------------LPRSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWL 197
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 342-519 1.25e-46

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: 164.40  E-value: 1.25e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 342 ITLRHKETKT-YLHSHPDRYPLRYDDGRVSSQGQQVTGYPFNDTNNYWQILPMNDDKQ----EGRVVRHQELVRLRHLGT 416
Cdd:cd23281    7 VTLRNTHGSPcWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLavddPPRPVRHGDIIQLVHGKT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 417 DTILLSHDVASPYYPTNQEFTTcsLTDAYGDRAKDTLFEVRFEN-GKPGQEFKSIASHFKLIHNPSKVAMWTHTTPLPEW 495
Cdd:cd23281   87 GRFLNSHDVAAPLSPTHQEVSC--YIDYNISMPAQNLWRIEIVNrDSEGDTWKAIKSQFRLIHVNTSAALKLSGKQLPDW 164

                        170       180
                 ....*....|....*....|....
gi 389631735 496 GHKQQEINGNKQVTVSSNVWFVED 519
Cdd:cd23281  165 GFGQLEVATDRAGNQSSTVWNVEE 188
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 336-519 2.35e-39

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: 143.63  E-value: 2.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 336 INYYDTITLRHKETKT-YLHSHPDRYPLRyddgrvsSQGQQVTGYPFNDTNNYWQILPMNDD----KQEGRVVRHQELVR 410
Cdd:cd23276    1 VAYGSQITLRNANSGGgYLHSHNHTYPDG-------SKQQQVTGYGHKDENNWWQILKPRGDpssnPPDPEYVRDGDEVR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 411 LRHLGTDTILLSHDVASPYYPTNQEFTTCSLTDAYGDraKDTLFEVRFENGKPGQEF---KSIASHFKLIHNPSKVAMWT 487
Cdd:cd23276   74 LLHKETNRYLRTHDAAAPVTSKHKEVSAYPDENEDGD--DNDLWVVEIVKDEGKLEDkriKPLTTRFRLRNKKTGCYLTS 151

                        170       180       190
                 ....*....|....*....|....*....|...
gi 389631735 488 HTTPLPEWGHKQQEINGNKQVTVS-SNVWFVED 519
Cdd:cd23276  152 SGVKLPEWGFRQGEVVCSKNKESDpSTLWNVEE 184
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 338-519 2.23e-29

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: 115.09  E-value: 2.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 338 YYDTITLR-HKETKTYLHSHPDRYPlrydDGrVSSQGQQVTGYPFNDTNNYWQILPMN---DDKQEGRVVRHQELVRLRH 413
Cdd:cd23282    3 YGSVITLKnHRTGGGYLHSHWHLYP----EG-VGARQQQVTTYSHKDDNNLWLIKKHNqssDLSDPVEYVRHGDLIRLEH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 414 LGTDTILLSHDVASPYypTNQEF-TTCSLTDAYGDrAKDtLFEVRFENGKPGQEFKSIASHFKLIHNPSKVAMWTHTTPL 492
Cdd:cd23282   78 VNTKRNLHSHKEKAPL--TKKHYqVTGYGENGTGD-AND-VWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQL 153

                        170       180
                 ....*....|....*....|....*..
gi 389631735 493 PEWGHKQQEINGNKQVTVSSNVWFVED 519
Cdd:cd23282  154 PKWGWEQLEVTCNPNVRDKNSLWNVED 180
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 341-519 1.36e-27

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: 110.46  E-value: 1.36e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 341 TITLRHKETKT-YLHSHPDRYPlryddgrVSSQGQQVTGYPFNDTNNYWQILPM----NDDKQEGRVVRHQELVRLRHLG 415
Cdd:cd23283    6 TIRIRHLNTRGgYLHSHPHNYP-------AGSKQQQITLYPHRDENNDWLVELAnapeEWSPTTFENLKDGDVVRLEHVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 416 TDTILLSHDVASPYypTN----QEFTtcsltdAYGDR--AKDT--LFEVRFENGK----PGQEF-KSIASHFKLIHNPSK 482
Cdd:cd23283   79 TGRRLHSHDHRPPV--SDndwqNEVS------AYGYEgfEGDAndDWRVEILKDDsrpgESKERvRAIDTKFRLVHVMTG 150

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 389631735 483 VAMWTHTTPLPEWGHKQQEINGNKQVTVSSNVWFVED 519
Cdd:cd23283  151 CYLFSHGVKLPEWGFEQQEVTCAKSGLLELSLWYIET 187
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 58-300 7.44e-27

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 114.99  E-value: 7.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  58 VITVLAFITRFWGISHPNEVVFDEVHFGKFASYYLQ---------KTYFFDVHPPFGKLLFAFMGWLVGYDGHFhfdnig 128
Cdd:COG1928   27 LVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTngyernwpdPGPFFVVHPPLGKWLIALGEWLFGYVNPF------ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 129 dsyvvnkvpyvAFRSLPALLGALTVSVVYLIMWESGYSVPACILAAGLVLFDNAHIGQTRLILLDATLVF----AFACSL 204
Cdd:COG1928  101 -----------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFfvlaAFGCLL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 205 L-----------CYIKFYKMRHEPFSRKWWKWLILTGFALSCDISTKYVGVFAFISIGSAVVidLWDLLdvKRKDGALSL 273
Cdd:COG1928  170 LdrdqvrrrlaaAVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLYFLAAFGLLTV--AWDAG--ARRAAGVRR 245

                        250       260       270
                 ....*....|....*....|....*....|....
gi 389631735 274 PIWA---KHFSARAFGLIIMPFIFYLF----WFQ 300
Cdd:COG1928  246 PWLGallRDGIPAFFALVIVPLLTYLAswtgWFA 279
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 336-520 1.92e-21

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: 92.88  E-value: 1.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 336 INYYDTITLRHKET-KTYLHSHPDRYPLryddgrvSSQGQQVTGYPF-NDTNNYWQILP-----MNDDKQEGRVVRHQEL 408
Cdd:cd23286    1 LLYGSTVTIRHLESlGGYLHSHDLTYPS-------GSNEQQVTLYDFeDDANNEWIIETktkeqMDKFPGQFREVRDGDV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 409 VRLRHLGTDTILLSHDVASPYypTNQEFTT-CSLTdayGDRAK----DTLFEVRF-------ENGKPGQEFKSIASHFKL 476
Cdd:cd23286   74 IRLRHVVTGKLLRASNARPPV--SEQEYNNeVSCT---GNANYsgdmDENWRIDVkgdeshaELKLPNIKIKSTESVFQL 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 389631735 477 IHNPSKVAMWTHTTPLPEWGHKQQEINGNKQVTVSSNVWFVEDI 520
Cdd:cd23286  149 YNRGTGCTLLSHDTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 336-519 1.38e-20

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: 90.07  E-value: 1.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 336 INYYDTITLR-HKETKTYLHSHPDRYPlrydDGrvsSQGQQVTGYPFNDTNNYWQILP----MNDDKQEGRV--VRHQEL 408
Cdd:cd23284    4 VAYGSKVTIKnQGLGGGLLHSHVQTYP----EG---SNQQQVTCYGHKDSNNEWIFERprglPSWDENDTDIefIKDGDI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 409 VRLRHLGTDTILLSHDVASPYYPTNQEfTTCSLTDAYGDRAKDTLFE-VRFENGKPGQEFKSIASHFKLIHNPSKVAMWT 487
Cdd:cd23284   77 VRLVHKQTGRNLHSHPVPAPISKSDYE-VSGYGDLTVGDEKDNWVIEiVKQVGSEDPKKLHTLTTSFRLRHEVLGCYLAQ 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 389631735 488 HTTPLPEWGHKQQEINGNKQVTVSSN--VWFVED 519
Cdd:cd23284  156 TGVSLPEWGFKQGEVVCDKSNFKRDKrtWWNIET 189
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 354-502 3.01e-18

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: 83.18  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  354 HSHPDRYPLRYDDGRVSSQgQQVTGYPFNDTNNY----WQILPMNDDKQEGRVVRHQELVRLRHLGTDTILLSHDV-ASP 428
Cdd:pfam02815  13 HSHQDEYLTGSEQQQKQPF-LRITLYPHGDANNSarslWRIEVVRHDAWRGGLIKWGSPFRLRHLTTGRYLHSHEEqKPP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  429 YYPTNQEFTTCSltdAYG------DRAKDTLFEVRFENGKPGQEFKSIASHFKLIHNPSKVAMWTHTTPLPEWGHK--QQ 500
Cdd:pfam02815  92 LVEKEDWQKEVS---AYGfrgfpgDNDIVEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpeQQ 168


                  ..
gi 389631735  501 EI 502
Cdd:pfam02815 169 KV 170
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 340-520 5.79e-18

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: 82.05  E-value: 5.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 340 DTITLRHKETKTYLHSHPDRYPLryddgrvSSQGQQVTGYPFN---DTNNYWQILPMNDDKqeGRVVRHQELVRLRHLGT 416
Cdd:cd23263    2 DVIWLKHSETGKYLHSHRKNYPT-------GSGQQEVTFESSSrkgDTNGLWIIESENGKQ--GGPVKWGDKIRLRHLST 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 417 DTILLSHDvaSPYYPTNQEFTTCSLTDaygDRAKDTLFEVRF-ENGKPGQEFKSIASHFKLIHNPSKVAMWTHTTPLPEW 495
Cdd:cd23263   73 GKYLSSEE--GKKSPKSNHQEVLCLTD---NPDKSSLFKFEPiGSTKYKQKYVKKDSYFRLKHVNTNFWLHSHEKKFNIN 147

                        170       180
                 ....*....|....*....|....*
gi 389631735 496 GHKQQEINGNKQVTVSSNVWFVEDI 520
Cdd:cd23263  148 NKTQQEVICHGEREEVFKLWKAELI 172
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 338-517 8.56e-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: 8.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 338 YYDTITLRHKETKTYLHSHPDRYplryddgrVSSQGQQ-VTGYP-FNDTNNYWQILPMNDDKQE--GRVVRHQELVRLRH 413
Cdd:cd23279    1 YGSAIKLKHVNSGYRLHSHEVSY--------GSGSGQQsVTAVPsADDANSLWTVLPGLGEPCQeqGKPVKCGDIIRLQH 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 414 LGTDTILLSHDVASPYYPtNQEFTtcsltdAYGDRAKDTLFEVRFENGKPGQEFKSIASHFKLIHNPSKvaMWTHTTPlp 493
Cdd:cd23279   73 VNTRKNLHSHNHSSPLSG-NQEVS------AFGGGDEDSGDNWIVECEGKKAKFWKRGEPVRLKHVDTG--KYLSASK-- 141

                        170       180       190
                 ....*....|....*....|....*....|.
gi 389631735 494 ewGHK--QQEINGNKQVTVSSN-----VWFV 517
Cdd:cd23279  142 --THKftQQPIAGQLEVSAASSkdsdsQWKA 170
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 336-447 1.79e-12

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: 66.25  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 336 INYYDTITLRHKETKTYLHSHPDRYplryddGRVSSQgQQVTGYP-FNDTNNYWQILPMNDDK-QEGRVVRHQELVRLRH 413
Cdd:cd23294    1 VTCGSVIKLQHERTKFRLHSHEVPY------GSGSGQ-QSVTGFPgVDDSNSYWIVKPANGERcKQGDVIKNGDVIRLQH 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 389631735 414 LGTDTILLSHDVASPYypTNQEFTTCSLTDAYGD 447
Cdd:cd23294   74 VSTRKWLHSHLHASPL--SGNQEVSCFGGDGNSD 105
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 546-766 7.50e-12

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 68.38  E-value: 7.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 546 WFELQRSMFWHNSRLTSSHPYASLPYQWPFLLRGVSFWTQNDTR-----------QQIYFLGNPIGWWLASSLLAVYIGI 614
Cdd:COG1928  307 LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcgagkcvRAVLAIGNPALWWLGLPALLWLLWR 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 615 LAAdqfslRRgvdalDHRSrsrlynstGFFFLSWLTHYVP-FYVMGRQLFLHHYLPSH----LASCLVAGALIeficnsd 689
Cdd:COG1928  387 WIA-----RR-----DWRA--------GAVLVGYAAGWLPwFLYLDRTMFFFYAIPFVpflvLALALVLGLIL------- 441

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 389631735 690 pmdgddvpatggkkavavkpkRHITAAERfagkSLMVTWAVCMgILAIVIAGWYFFLPLTYGYPgLSVDQVLRRKWL 766
Cdd:COG1928  442 ---------------------GPARASER----RRLGRLVVGL-YVGLVVANFAFFYPILTGLP-IPYDEWQARMWF 491
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 48-302 1.38e-11

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: 66.19  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  48 PERDHQAAFTVITVLAFITRFWGISHPNEVVFDEVHF----------GKFASYYLQKTYFFDvHPPFGKLLFAFMGWLVG 117
Cdd:COG1807    2 SKTLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYaeiaremlesGDWLTPTLAGEPYFD-KPPLIYWLIALSYKLFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 118 ydghfhfdnigdsyvvnkVPYVAFRSLPALLGALTVSVVYLIMWESgYSVPACILAAGLVLFDNAHIGQTRLILLDATLV 197
Cdd:COG1807   81 ------------------VSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPLLLLFGRLATPDALLL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 198 FAFACSLLCYIKFYKmrhepfsRKWWKWLILTGFALSCDISTKYVGVFAFISIGSAVVIdlwdlldvkrkdgaLSLPIWA 277
Cdd:COG1807  142 LFWTLALYALLRALE-------RRRLRWLLLAGLALGLGFLTKGPVALLLPGLALLLYL--------------LLTRRWR 200

                        250       260
                 ....*....|....*....|....*
gi 389631735 278 KHFSARAFGLIIMPFIFYLFWFQVH 302
Cdd:COG1807  201 RLRRLRLLLGLLLALLLALPWYIAN 225
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 341-447 2.00e-10

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: 60.36  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 341 TITLRHKETKTYLHSHPDRYplryddGrvSSQGQQ-VTGYP-FNDTNNYWQIL-PMNDDKQEGRVVRHQELVRLRHLGTD 417
Cdd:cd23293    6 VVKLLNTRHNVRLHSHDVKY------G--SGSGQQsVTGVEsSDDSNSYWQIRgPTGADCERGTPIKCGQTIRLTHLNTG 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 389631735 418 TILLSHDVASPYYPtNQEFTtcsltdAYGD 447
Cdd:cd23293   78 KNLHSHHFQSPLSG-NQEVS------AFGE 100
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
334-392 9.23e-09

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 51.96  E-value: 9.23e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 389631735   334 ITINYYDTITLRHKETKTYLHSHPDRYPlryddgRVSSQGQQVTGYPFN--DTNNYWQILP 392
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEKLP------PWGDGQQEVTGYGNPaiDANTLWLIEP 56
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 340-426 2.96e-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: 45.44  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 340 DTITLRHKETKTYLHSHPDRYPLryddgrvsSQGQQVTGY---PFNDTNNYWQILPMNddkqEGRVVRHQELVRLRHLGT 416
Cdd:cd23294   67 DVIRLQHVSTRKWLHSHLHASPL--------SGNQEVSCFggdGNSDTGDNWIVEIEG----GGKVWERDQKVRLKHVDT 134

                         90
                 ....*....|
gi 389631735 417 DTILLSHDVA 426
Cdd:cd23294  135 GGYLHSHDKK 144
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 340-416 9.08e-05

MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate receptor Itr-1 and similar proteins; Itr-1, also called IP3 receptor, or IP3R, or InsP3R, or LET-23 fertility effector 1, is a receptor for inositol 1,4,5-trisphosphate, a second messenger that regulates intracellular calcium homeostasis. It binds in vitro to both inositol 1,4,5-trisphosphate (1,4,5-InsP3) and inositol 2,4,5-trisphosphate (2,4,5-InsP3) with high affinity. It can also bind inositol 1,3,4,5-tetrakisphosphate (1,3,4,5-InsP4) and inositol 4,5-bisphosphate (4,5-InsP2), but with lower affinity. Itr-1 acts as a timekeeper/rhythm generator via calcium signaling, affecting the defecation cycle and pharyngeal pumping. It affects normal hermaphrodite and male fertility as a participant in intracellular signaling by acting downstream of let-23/lin-3 which regulates ovulation, spermathecal valve dilation and male mating behavior. It plays an important role in early embryonic development. It controls epidermal cell migration and may also regulate filopodial protrusive activity during epithelial morphogenesis. Itr-1 functions as a component of inositol trisphosphate (IP3)-mediated downstream signaling pathways that controls amphid sensory neuronal (ASH)-mediated response to nose touch and benzaldehyde, but no other ASH-mediated responses. Itr-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467751 [Multi-domain]  Cd Length: 199  Bit Score: 44.30  E-value: 9.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 340 DTITLRHKETKTYLH--SHPDRYPLRYDDG---RVSSQGQQVTGYPFNDTNNYWQILpMNDDKQEGRVVRHQELVRLRHL 414
Cdd:cd23280   11 DVVRLFHKELEAYLSaeGSFVDEVLTEDVHlrvRPVDDRKPRTLFPPTSGDTFWQIE-KEDTPLKGGVIKWGDQCRLRHL 89


                 ..
gi 389631735 415 GT 416
Cdd:cd23280   90 PT 91
Stt3 COG1287
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
 58-296 1.01e-04

Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 45.94  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  58 VITVLAFITRFwgISHPNEVVFDEVHFGKFASYY--------LQKTYF---FDV--HPPFGK------LLFAFMGWLVGY 118
Cdd:COG1287   22 LILALALWIRL--LPYDNVFRDGGVYLGGNDPWYhlrqieyiLANGPStlpFDPltWYPWGRdigqfgPLFDQLIALLAL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 119 dghfhFDNIGDSyvVNKVPYVAFRSLPALLGALTVSVVYLIMWESGySVPACILAAGLVLFDNAHIGQTRLILLD---AT 195
Cdd:COG1287  100 -----ILGLGSP--SQSSVYTVAAWFPPIFGALTVIPVYLLGRRLG-GRKAGLLAALLLALSPGQLSRSLLGFADhhvAE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 196 LVFAFAcSLLCYIKFYK-----MRHEPFSRKWWKWLILTGFALSCDISTKYVGVFAFISIGSAVVIDLwdLLDVKRKDGA 270
Cdd:COG1287  172 LFFSTL-AVLFLVLALKrakreKRDLEALKRPLLYAVLAGVALGLYLLTWGGYVLFVGILALFALLQL--LLDLLRGRSP 248

                        250       260
                 ....*....|....*....|....*.
gi 389631735 271 LSLPIWAkhfsARAFGLIIMPFIFYL 296
Cdd:COG1287  249 EYLAIVG----AVSFAVAALLVLPFI 270
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
472-520 1.47e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 37.32  E-value: 1.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 389631735   472 SHFKLIHNPSKVAMWTHTTPLPEWGHKQQEINGNKQ-VTVSSNVWFVEDI 520
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNpAIDANTLWLIEPV 57
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
 101-296 4.75e-03

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


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 39.98  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 101 HPPFGKLLFAFMGWLvgydghfhfdnIGDSYVVNKVPYVafrslpaLLGALTVSVVYLIMWESGYSVPACILAAGLVLFD 180
Cdd:COG4346   79 HPPLGKYIIALSMLL-----------LGDKPLYWRLPSI-------ILGALIVILVFLTARRLSGNIVAGLIASLLLALD 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735 181 NAHIGQTRLILLDATLVFAFACSLLCYIKfykmrhepfsrkwwKWLILTGFALSCDISTKYVGVFAFISIgsavvidlwd 260
Cdd:COG4346  141 PLLRVMSSIAMLDIYVAFFTALALYFAVS--------------GRLLLSSIALGLAAASKYSGLFLLIPL---------- 196

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 389631735 261 lldvkrkdgALSLPIWAKHFSARAFGLIIMPFIFYL 296
Cdd:COG4346  197 ---------LLYLREIEKSPIKRFLYGILIPLAVFL 223
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 335-440 7.23e-03

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: 38.50  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389631735  335 TINYYDTITLRHKETKTYLHSHPDRYPLRYDdgrVSSQGQQVTGY---PFNDTNNYWQILPMNDDKQEG--RVVRHQELV 409
Cdd:pfam02815  64 LIKWGSPFRLRHLTTGRYLHSHEEQKPPLVE---KEDWQKEVSAYgfrGFPGDNDIVEIFEKKSTTGMGsdRIKPGDSYF 140

                          90       100       110
                  ....*....|....*....|....*....|....
gi 389631735  410 RLRHLGTDTILLSHDVASP---YYPTNQEFTTCS 440
Cdd:pfam02815 141 RLQHVCTGCWLFSHSVKLPkwgFGPEQQKVTCAK 174
 
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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