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Conserved domains on  [gi|164423013|ref|XP_963926|]
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mannosyltransferase PMTI [Neurospora crassa OR74A]

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 ...
 336-521 2.37e-113

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: 341.20  E-value: 2.37e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 336 IDYYDTISIRHKETKAYLHSHPDKYPLRYDDGRVSSQGQQVTGYPFNDTNNYWQILPPGPDDQ--KLGHPIKNHDLVRLR 413
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDEheGTGRPVRNGDLIRLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 414 HIVTDTILLSHDVASPYYPTNQEFTTVSIGDAYgDRAADTLFEIRIEHGKANQEFKSISSHFKLIHNPSKVAMWTHSKPL 493
Cdd:cd23285   81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVEIEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKPL 159

                        170       180
                 ....*....|....*....|....*...
gi 164423013 494 PEWGHKQQEINGNKQLAQSSNVWLVEDI 521
Cdd:cd23285  160 PDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 57-307 9.58e-84

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


:

Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 266.48  E-value: 9.58e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013   57 ILITGLAFLTRFWGISHPDEVVFDEVHFGKFASYYLERTYFFDVHPPFGKLLFAFMGWLVGYDGHFHFENIGDSYIRNKV 136
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  137 PYVAFRSLPAILGALTVSVVYMIMWESGYSLPACLIAAGLVLLDNAHIGQTRLILLDATLVFAMACSLLCYIKFHklRHE 216
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  217 PFSRKWWKWLILTGFALSCDISTKYVGLFAFITIGSAVCIDLWDLLDIKrpggALTLPQFGKHFAARAFGLIIMPFIFYL 296
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDL----SLLLKSIWKHLFARLFCLIVIPWALYL 234

                         250
                  ....*....|.
gi 164423013  297 FWFQVHFSILT 307
Cdd:pfam02366 235 AQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 545-766 4.24e-79

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: 252.47  E-value: 4.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  545 RKWFELQRSMFWHNNQLTSSHPYASLPYQWPFLLRGVSFWTQNDTRQQIYFLGNPIGWWLASSVLAIYAGIILADQFSLR 624
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  625 RGLDAM-DRRTRSRLYNSTGFFFLAWATHYFPFFVMGRQLFLHHYLPAHLASALVTGSVVEFLFStdsaepeyqpsksgk 703
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLS--------------- 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423013  704 kvapttkrrlSARERLAGQSMAGAWIATAVIMVLVAFGWYFFLPLTYGYPGLTApEVNRRKWL 766
Cdd:pfam16192 146 ----------LFRRLPRSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSE-ECKKLKWL 197
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 336-521 2.37e-113

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: 341.20  E-value: 2.37e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 336 IDYYDTISIRHKETKAYLHSHPDKYPLRYDDGRVSSQGQQVTGYPFNDTNNYWQILPPGPDDQ--KLGHPIKNHDLVRLR 413
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDEheGTGRPVRNGDLIRLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 414 HIVTDTILLSHDVASPYYPTNQEFTTVSIGDAYgDRAADTLFEIRIEHGKANQEFKSISSHFKLIHNPSKVAMWTHSKPL 493
Cdd:cd23285   81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVEIEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKPL 159

                        170       180
                 ....*....|....*....|....*...
gi 164423013 494 PEWGHKQQEINGNKQLAQSSNVWLVEDI 521
Cdd:cd23285  160 PDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 57-307 9.58e-84

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 266.48  E-value: 9.58e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013   57 ILITGLAFLTRFWGISHPDEVVFDEVHFGKFASYYLERTYFFDVHPPFGKLLFAFMGWLVGYDGHFHFENIGDSYIRNKV 136
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  137 PYVAFRSLPAILGALTVSVVYMIMWESGYSLPACLIAAGLVLLDNAHIGQTRLILLDATLVFAMACSLLCYIKFHklRHE 216
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  217 PFSRKWWKWLILTGFALSCDISTKYVGLFAFITIGSAVCIDLWDLLDIKrpggALTLPQFGKHFAARAFGLIIMPFIFYL 296
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDL----SLLLKSIWKHLFARLFCLIVIPWALYL 234

                         250
                  ....*....|.
gi 164423013  297 FWFQVHFSILT 307
Cdd:pfam02366 235 AQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 545-766 4.24e-79

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: 252.47  E-value: 4.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  545 RKWFELQRSMFWHNNQLTSSHPYASLPYQWPFLLRGVSFWTQNDTRQQIYFLGNPIGWWLASSVLAIYAGIILADQFSLR 624
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  625 RGLDAM-DRRTRSRLYNSTGFFFLAWATHYFPFFVMGRQLFLHHYLPAHLASALVTGSVVEFLFStdsaepeyqpsksgk 703
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLS--------------- 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423013  704 kvapttkrrlSARERLAGQSMAGAWIATAVIMVLVAFGWYFFLPLTYGYPGLTApEVNRRKWL 766
Cdd:pfam16192 146 ----------LFRRLPRSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSE-ECKKLKWL 197
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 34-300 4.57e-26

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 112.68  E-value: 4.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  34 TDKVPDAVAPAKSGSELEYKLALILITGLAFLTRFWGISHPDEVVFDEVHFGKFASYYLER---------TYFFDVHPPF 104
Cdd:COG1928    3 AALPPARLVPPMPGDRLRGWLGTLLVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 105 GKLLFAFMGWLVGYDGHFhfenigdsyirnkvpyvAFRSLPAILGALTVSVVYMIMWESGYSLPACLIAAGLVLLDNAHI 184
Cdd:COG1928   83 GKWLIALGEWLFGYVNPF-----------------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 185 GQTRLILLDATLVF----AMACSLL-----------CYIKFHKLRHEPFSRKWWKWLILTGFALSCDISTKYVGLFAFIT 249
Cdd:COG1928  146 VLSRTALLDIFLMFfvlaAFGCLLLdrdqvrrrlaaAVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLYFLAA 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 250 IGsAVCIdLWDL-----LDIKRPGGALTLPQFGKHFaaraFGLIIMPFIFYLF----WFQ 300
Cdd:COG1928  226 FG-LLTV-AWDAgarraAGVRRPWLGALLRDGIPAF----FALVIVPLLTYLAswtgWFA 279
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 354-503 1.01e-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: 84.72  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  354 HSHPDKYPLRYDDGRVSSQgQQVTGYPFNDTNNY----WQILPPGPDDQKLGHpIKNHDLVRLRHIVTDTILLSHDV-AS 428
Cdd:pfam02815  13 HSHQDEYLTGSEQQQKQPF-LRITLYPHGDANNSarslWRIEVVRHDAWRGGL-IKWGSPFRLRHLTTGRYLHSHEEqKP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  429 PYYPTNQEFTTVSigdAYGDRAAD------TLFEIRIEHGKANQEFKSISSHFKLIHNPSKVAMWTHSKPLPEWGHK--Q 500
Cdd:pfam02815  91 PLVEKEDWQKEVS---AYGFRGFPgdndivEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpeQ 167


                  ...
gi 164423013  501 QEI 503
Cdd:pfam02815 168 QKV 170
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 528-766 3.96e-15

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 78.78  E-value: 3.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 528 HARREKPEKKVKTLP-FLRKWFELQRSMFWHNNQLTSSHPYASLPYQWPFLLRGVSFWTQNDTR-----------QQIYF 595
Cdd:COG1928  287 HWAAQNPGSGLGWVPdALRSLWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcgagkcvRAVLA 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 596 LGNPIGWWLAssVLAIYAGIILAdqfSLRRgldamDRRtrsrlynsTGFFFLAWATHYFP-FFVMGRQLFLHHYLPAH-- 672
Cdd:COG1928  367 IGNPALWWLG--LPALLWLLWRW---IARR-----DWR--------AGAVLVGYAAGWLPwFLYLDRTMFFFYAIPFVpf 428

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 673 --LASALVTGSVVeflfstdsaepeyqpsksgkkvapttkRRLSARERlagqSMAGAWIAtAVIMVLVAFGWYFFLPLTY 750
Cdd:COG1928  429 lvLALALVLGLIL---------------------------GPARASER----RRLGRLVV-GLYVGLVVANFAFFYPILT 476

                        250
                 ....*....|....*.
gi 164423013 751 GYPgLTAPEVNRRKWL 766
Cdd:COG1928  477 GLP-IPYDEWQARMWF 491
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
338-393 2.18e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.11  E-value: 2.18e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 164423013   338 YYDTISIRHKETKAYLHSHPDKYPlryddgRVSSQGQQVTGYPFN--DTNNYWQILPP 393
Cdd:smart00472   6 WGDVVRLRHVTTGRYLHSHDEKLP------PWGDGQQEVTGYGNPaiDANTLWLIEPV 57
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 336-521 2.37e-113

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: 341.20  E-value: 2.37e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 336 IDYYDTISIRHKETKAYLHSHPDKYPLRYDDGRVSSQGQQVTGYPFNDTNNYWQILPPGPDDQ--KLGHPIKNHDLVRLR 413
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPLRYEDGRISSQGQQVTGYPHKDANNQWQILPTDPIDEheGTGRPVRNGDLIRLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 414 HIVTDTILLSHDVASPYYPTNQEFTTVSIGDAYgDRAADTLFEIRIEHGKANQEFKSISSHFKLIHNPSKVAMWTHSKPL 493
Cdd:cd23285   81 HVSTDTYLLTHDVASPLTPTNMEFTTVSDDDTD-ERYNETLFRVEIEDTDEGDVLKTKSSHFRLIHVDTNVALWTHKKPL 159

                        170       180
                 ....*....|....*....|....*...
gi 164423013 494 PEWGHKQQEINGNKQLAQSSNVWLVEDI 521
Cdd:cd23285  160 PDWGFGQQEVNGNKNIKDKSNIWVVDDI 187
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 57-307 9.58e-84

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 266.48  E-value: 9.58e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013   57 ILITGLAFLTRFWGISHPDEVVFDEVHFGKFASYYLERTYFFDVHPPFGKLLFAFMGWLVGYDGHFHFENIGDSYIRNKV 136
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  137 PYVAFRSLPAILGALTVSVVYMIMWESGYSLPACLIAAGLVLLDNAHIGQTRLILLDATLVFAMACSLLCYIKFHklRHE 216
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE--RKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  217 PFSRKWWKWLILTGFALSCDISTKYVGLFAFITIGSAVCIDLWDLLDIKrpggALTLPQFGKHFAARAFGLIIMPFIFYL 296
Cdd:pfam02366 159 PFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDL----SLLLKSIWKHLFARLFCLIVIPWALYL 234

                         250
                  ....*....|.
gi 164423013  297 FWFQVHFSILT 307
Cdd:pfam02366 235 AQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 545-766 4.24e-79

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: 252.47  E-value: 4.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  545 RKWFELQRSMFWHNNQLTSSHPYASLPYQWPFLLRGVSFWTQNDTRQQIYFLGNPIGWWLASSVLAIYAGIILADQFSLR 624
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  625 RGLDAM-DRRTRSRLYNSTGFFFLAWATHYFPFFVMGRQLFLHHYLPAHLASALVTGSVVEFLFStdsaepeyqpsksgk 703
Cdd:pfam16192  81 RGYYDLsDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLS--------------- 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164423013  704 kvapttkrrlSARERLAGQSMAGAWIATAVIMVLVAFGWYFFLPLTYGYPGLTApEVNRRKWL 766
Cdd:pfam16192 146 ----------LFRRLPRSLRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSE-ECKKLKWL 197
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 342-520 1.47e-48

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: 169.80  E-value: 1.47e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 342 ISIRHKETK-AYLHSHPDKYPLRYDDGRVSSQGQQVTGYPFNDTNNYWQILPPGPDDQ---KLGHPIKNHDLVRLRHIVT 417
Cdd:cd23281    7 VTLRNTHGSpCWLHSHKHRYPIKYPDGRGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLavdDPPRPVRHGDIIQLVHGKT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 418 DTILLSHDVASPYYPTNQEfttVSIGDAYGDR-AADTLFEIRIEHGKANQEF-KSISSHFKLIHNPSKVAMWTHSKPLPE 495
Cdd:cd23281   87 GRFLNSHDVAAPLSPTHQE---VSCYIDYNISmPAQNLWRIEIVNRDSEGDTwKAIKSQFRLIHVNTSAALKLSGKQLPD 163

                        170       180
                 ....*....|....*....|....*
gi 164423013 496 WGHKQQEINGNKQLAQSSNVWLVED 520
Cdd:cd23281  164 WGFGQLEVATDRAGNQSSTVWNVEE 188
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 338-520 2.37e-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: 2.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 338 YYDTISIRH-KETKAYLHSHPDKYPLRyddgrvsSQGQQVTGYPFNDTNNYWQILPP-GPDDQKLGHP--IKNHDLVRLR 413
Cdd:cd23276    3 YGSQITLRNaNSGGGYLHSHNHTYPDG-------SKQQQVTGYGHKDENNWWQILKPrGDPSSNPPDPeyVRDGDEVRLL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 414 HIVTDTILLSHDVASPYYPTNQEFTTVSIGDAYGDraADTLFEIRIEHGKANQEF---KSISSHFKLIHNPSKVAMWTHS 490
Cdd:cd23276   76 HKETNRYLRTHDAAAPVTSKHKEVSAYPDENEDGD--DNDLWVVEIVKDEGKLEDkriKPLTTRFRLRNKKTGCYLTSSG 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 164423013 491 KPLPEWGHKQQEINGNKQLAQS-SNVWLVED 520
Cdd:cd23276  154 VKLPEWGFRQGEVVCSKNKESDpSTLWNVEE 184
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 341-520 6.15e-32

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: 122.79  E-value: 6.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 341 TISIRHKETKA-YLHSHPDKYPlryddgrVSSQGQQVTGYPFNDTNNYWQILP---PGPDDQKLGHPIKNHDLVRLRHIV 416
Cdd:cd23283    6 TIRIRHLNTRGgYLHSHPHNYP-------AGSKQQQITLYPHRDENNDWLVELanaPEEWSPTTFENLKDGDVVRLEHVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 417 TDTILLSHDVASPYypTNQEFTT-VSigdAYGDR--AADT--LFEIRI-----EHGKANQEFKSISSHFKLIHNPSKVAM 486
Cdd:cd23283   79 TGRRLHSHDHRPPV--SDNDWQNeVS---AYGYEgfEGDAndDWRVEIlkddsRPGESKERVRAIDTKFRLVHVMTGCYL 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 164423013 487 WTHSKPLPEWGHKQQEINGNKQLAQSSNVWLVED 520
Cdd:cd23283  154 FSHGVKLPEWGFEQQEVTCAKSGLLELSLWYIET 187
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 338-520 1.63e-28

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: 112.78  E-value: 1.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 338 YYDTISIR-HKETKAYLHSHPDKYPlrydDGrVSSQGQQVTGYPFNDTNNYWQILPPG--PDDQKLGHPIKNHDLVRLRH 414
Cdd:cd23282    3 YGSVITLKnHRTGGGYLHSHWHLYP----EG-VGARQQQVTTYSHKDDNNLWLIKKHNqsSDLSDPVEYVRHGDLIRLEH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 415 IVTDTILLSHDVASPYypTNQEFTTVSIG-DAYGDraADTLFEIRIEHGKANQEFKSISSHFKLIHNPSKVAMWTHSKPL 493
Cdd:cd23282   78 VNTKRNLHSHKEKAPL--TKKHYQVTGYGeNGTGD--ANDVWRVEVVGGREGDPVKTVRSKFRLVHYNTGCALHSHGKQL 153

                        170       180
                 ....*....|....*....|....*..
gi 164423013 494 PEWGHKQQEINGNKQLAQSSNVWLVED 520
Cdd:cd23282  154 PKWGWEQLEVTCNPNVRDKNSLWNVED 180
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 34-300 4.57e-26

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 112.68  E-value: 4.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  34 TDKVPDAVAPAKSGSELEYKLALILITGLAFLTRFWGISHPDEVVFDEVHFGKFASYYLER---------TYFFDVHPPF 104
Cdd:COG1928    3 AALPPARLVPPMPGDRLRGWLGTLLVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 105 GKLLFAFMGWLVGYDGHFhfenigdsyirnkvpyvAFRSLPAILGALTVSVVYMIMWESGYSLPACLIAAGLVLLDNAHI 184
Cdd:COG1928   83 GKWLIALGEWLFGYVNPF-----------------GWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 185 GQTRLILLDATLVF----AMACSLL-----------CYIKFHKLRHEPFSRKWWKWLILTGFALSCDISTKYVGLFAFIT 249
Cdd:COG1928  146 VLSRTALLDIFLMFfvlaAFGCLLLdrdqvrrrlaaAVAAGRAPSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLYFLAA 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 250 IGsAVCIdLWDL-----LDIKRPGGALTLPQFGKHFaaraFGLIIMPFIFYLF----WFQ 300
Cdd:COG1928  226 FG-LLTV-AWDAgarraAGVRRPWLGALLRDGIPAF----FALVIVPLLTYLAswtgWFA 279
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 338-521 2.22e-24

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: 100.97  E-value: 2.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 338 YYDTISIRHKET-KAYLHSHPDKYPLryddgrvSSQGQQVTGYPF-NDTNNYWQILPPG-------PDDQKlghPIKNHD 408
Cdd:cd23286    3 YGSTVTIRHLESlGGYLHSHDLTYPS-------GSNEQQVTLYDFeDDANNEWIIETKTkeqmdkfPGQFR---EVRDGD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 409 LVRLRHIVTDTILLSHDVASP-----YypTNQEFTTVSIGDAyGDraADTLFEIRIEHGKANQE-------FKSISSHFK 476
Cdd:cd23286   73 VIRLRHVVTGKLLRASNARPPvseqeY--NNEVSCTGNANYS-GD--MDENWRIDVKGDESHAElklpnikIKSTESVFQ 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 164423013 477 LIHNPSKVAMWTHSKPLPEWGHKQQEINGNKQLAQSSNVWLVEDI 521
Cdd:cd23286  148 LYNRGTGCTLLSHDTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 338-520 4.93e-22

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: 94.31  E-value: 4.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 338 YYDTISIR-HKETKAYLHSHPDKYPlrydDGrvsSQGQQVTGYPFNDTNNYWQILPP----GPDDQKLGHP-IKNHDLVR 411
Cdd:cd23284    6 YGSKVTIKnQGLGGGLLHSHVQTYP----EG---SNQQQVTCYGHKDSNNEWIFERPrglpSWDENDTDIEfIKDGDIVR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 412 LRHIVTDTILLSHDVASPYYPTNQEfttVSigdAYGD-RAADTLFEIRIE-----HGKANQEFKSISSHFKLIHNPSKVA 485
Cdd:cd23284   79 LVHKQTGRNLHSHPVPAPISKSDYE---VS---GYGDlTVGDEKDNWVIEivkqvGSEDPKKLHTLTTSFRLRHEVLGCY 152

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 164423013 486 MWTHSKPLPEWGHKQQEI----NGNKQlaQSSNVWLVED 520
Cdd:cd23284  153 LAQTGVSLPEWGFKQGEVvcdkSNFKR--DKRTWWNIET 189
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 340-521 1.04e-21

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: 92.83  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 340 DTISIRHKETKAYLHSHPDKYPLryddgrvSSQGQQVTGYPFN---DTNNYWQILPPgpdDQKLGHPIKNHDLVRLRHIV 416
Cdd:cd23263    2 DVIWLKHSETGKYLHSHRKNYPT-------GSGQQEVTFESSSrkgDTNGLWIIESE---NGKQGGPVKWGDKIRLRHLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 417 TDTILLSHDVASPYYPTNQEFTTVSIgdaygDRAADTLFEI-RIEHGKANQEFKSISSHFKLIHNPSKVAMWTHSKPLPE 495
Cdd:cd23263   72 TGKYLSSEEGKKSPKSNHQEVLCLTD-----NPDKSSLFKFePIGSTKYKQKYVKKDSYFRLKHVNTNFWLHSHEKKFNI 146

                        170       180
                 ....*....|....*....|....*.
gi 164423013 496 WGHKQQEINGNKQLAQSSNVWLVEDI 521
Cdd:cd23263  147 NNKTQQEVICHGEREEVFKLWKAELI 172
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 338-518 1.83e-21

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: 91.98  E-value: 1.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 338 YYDTISIRHKETKAYLHSHPDKYplryddgrVSSQGQQ-VTGYP-FNDTNNYWQILPP-GPDDQKLGHPIKNHDLVRLRH 414
Cdd:cd23279    1 YGSAIKLKHVNSGYRLHSHEVSY--------GSGSGQQsVTAVPsADDANSLWTVLPGlGEPCQEQGKPVKCGDIIRLQH 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 415 IVTDTILLSHDVASPYYPtNQEfttVSigdAYGDRAADTLFEIRIEHGKANQEFKSISSHFKLIHNPSKVAMWTHSK--- 491
Cdd:cd23279   73 VNTRKNLHSHNHSSPLSG-NQE---VS---AFGGGDEDSGDNWIVECEGKKAKFWKRGEPVRLKHVDTGKYLSASKThkf 145

                        170       180
                 ....*....|....*....|....*...
gi 164423013 492 -PLPEWGHkqQEINGNKQlAQSSNVWLV 518
Cdd:cd23279  146 tQQPIAGQ--LEVSAASS-KDSDSQWKA 170
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 354-503 1.01e-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: 84.72  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  354 HSHPDKYPLRYDDGRVSSQgQQVTGYPFNDTNNY----WQILPPGPDDQKLGHpIKNHDLVRLRHIVTDTILLSHDV-AS 428
Cdd:pfam02815  13 HSHQDEYLTGSEQQQKQPF-LRITLYPHGDANNSarslWRIEVVRHDAWRGGL-IKWGSPFRLRHLTTGRYLHSHEEqKP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  429 PYYPTNQEFTTVSigdAYGDRAAD------TLFEIRIEHGKANQEFKSISSHFKLIHNPSKVAMWTHSKPLPEWGHK--Q 500
Cdd:pfam02815  91 PLVEKEDWQKEVS---AYGFRGFPgdndivEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpeQ 167


                  ...
gi 164423013  501 QEI 503
Cdd:pfam02815 168 QKV 170
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 528-766 3.96e-15

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 78.78  E-value: 3.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 528 HARREKPEKKVKTLP-FLRKWFELQRSMFWHNNQLTSSHPYASLPYQWPFLLRGVSFWTQNDTR-----------QQIYF 595
Cdd:COG1928  287 HWAAQNPGSGLGWVPdALRSLWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcgagkcvRAVLA 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 596 LGNPIGWWLAssVLAIYAGIILAdqfSLRRgldamDRRtrsrlynsTGFFFLAWATHYFP-FFVMGRQLFLHHYLPAH-- 672
Cdd:COG1928  367 IGNPALWWLG--LPALLWLLWRW---IARR-----DWR--------AGAVLVGYAAGWLPwFLYLDRTMFFFYAIPFVpf 428

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 673 --LASALVTGSVVeflfstdsaepeyqpsksgkkvapttkRRLSARERlagqSMAGAWIAtAVIMVLVAFGWYFFLPLTY 750
Cdd:COG1928  429 lvLALALVLGLIL---------------------------GPARASER----RRLGRLVV-GLYVGLVVANFAFFYPILT 476

                        250
                 ....*....|....*.
gi 164423013 751 GYPgLTAPEVNRRKWL 766
Cdd:COG1928  477 GLP-IPYDEWQARMWF 491
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 336-448 4.78e-15

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: 73.95  E-value: 4.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 336 IDYYDTISIRHKETKAYLHSHPDKYplryddGRVSSQgQQVTGYP-FNDTNNYWQILPPGPDDQKLGHPIKNHDLVRLRH 414
Cdd:cd23294    1 VTCGSVIKLQHERTKFRLHSHEVPY------GSGSGQ-QSVTGFPgVDDSNSYWIVKPANGERCKQGDVIKNGDVIRLQH 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 164423013 415 IVTDTILLSHDVASPyYPTNQEfttVSigdAYGD 448
Cdd:cd23294   74 VSTRKWLHSHLHASP-LSGNQE---VS---CFGG 100
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 341-448 8.76e-14

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: 69.99  E-value: 8.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 341 TISIRHKETKAYLHSHPDKYplryddGrvSSQGQQ-VTGYP-FNDTNNYWQILPPGPDDQKLGHPIKNHDLVRLRHIVTD 418
Cdd:cd23293    6 VVKLLNTRHNVRLHSHDVKY------G--SGSGQQsVTGVEsSDDSNSYWQIRGPTGADCERGTPIKCGQTIRLTHLNTG 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 164423013 419 TILLSHDVASPYYPtNQEfttVSigdAYGD 448
Cdd:cd23293   78 KNLHSHHFQSPLSG-NQE---VS---AFGE 100
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 48-297 3.44e-10

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


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 61.95  E-value: 3.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  48 SELEYKLALILITGLAFLTRFWGISHPDEVVFDEVHF----------GKFASYYLERTYFFDvHPPFGKLLFAFMGWLVG 117
Cdd:COG1807    2 SKTLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYaeiaremlesGDWLTPTLAGEPYFD-KPPLIYWLIALSYKLFG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 118 ydghfhfenigdsyirnkVPYVAFRSLPAILGALTVSVVYMIMWESgYSLPACLIAAGLVLLDNAHIGQTRLILLDATLV 197
Cdd:COG1807   81 ------------------VSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPLLLLFGRLATPDALLL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 198 FAMACSLLCYIKFhklrhepFSRKWWKWLILTGFALSCDISTKYVGLFAFITIGSAVCI----DLWDLLDIKRPGGAL-- 271
Cdd:COG1807  142 LFWTLALYALLRA-------LERRRLRWLLLAGLALGLGFLTKGPVALLLPGLALLLYLlltrRWRRLRRLRLLLGLLla 214

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 164423013 272 -----------TLPQFGKHFAARAFGLIIMPFIFYLF 297
Cdd:COG1807  215 lllalpwyianDWATGPAFLEYFFGYENLVPLLFFSL 251
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 335-426 3.40e-09

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


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 56.62  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 335 TIDYYDTISIRHKETKAYLHSHPDKYPLryddgrvSSQGQQVTGYPFN-DTNNYWQILPPGPDDQKLGHpIKNHDLVRLR 413
Cdd:cd23263   58 PVKWGDKIRLRHLSTGKYLSSEEGKKSP-------KSNHQEVLCLTDNpDKSSLFKFEPIGSTKYKQKY-VKKDSYFRLK 129

                         90
                 ....*....|...
gi 164423013 414 HIVTDTILLSHDV 426
Cdd:cd23263  130 HVNTNFWLHSHEK 142
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
338-393 2.18e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.11  E-value: 2.18e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 164423013   338 YYDTISIRHKETKAYLHSHPDKYPlryddgRVSSQGQQVTGYPFN--DTNNYWQILPP 393
Cdd:smart00472   6 WGDVVRLRHVTTGRYLHSHDEKLP------PWGDGQQEVTGYGNPaiDANTLWLIEPV 57
Stt3 COG1287
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
 50-234 2.54e-04

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


Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 44.40  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  50 LEYKLALILITGLAFLTRFwgISHPDEVVFDEVHFGKFASYYLERTY-----------FFDV--HPPFGK------LLFA 110
Cdd:COG1287   14 LLHLPALLLILALALWIRL--LPYDNVFRDGGVYLGGNDPWYHLRQIeyilangpstlPFDPltWYPWGRdigqfgPLFD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 111 FMGWLVGYdghfhFENIGDSYirNKVPYVAFRSLPAILGALTVSVVYMIMWESGYSLPAcLIAAGLVLLDNAHIGQTRLI 190
Cdd:COG1287   92 QLIALLAL-----ILGLGSPS--QSSVYTVAAWFPPIFGALTVIPVYLLGRRLGGRKAG-LLAALLLALSPGQLSRSLLG 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164423013 191 LLDATL--VFAMACSLLCYIKFHK-----LRHEPFSRKWWKWLILTGFALS 234
Cdd:COG1287  164 FADHHVaeLFFSTLAVLFLVLALKrakreKRDLEALKRPLLYAVLAGVALG 214
beta-trefoil_MIR_itr-1-like cd23280
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ...
 340-487 8.68e-04

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: 41.22  E-value: 8.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 340 DTISIRHKETKAYLH--SHPDKYPLRYDDG---RVSSQGQQVTGYPFNDTNNYWQIlppgpddQKL-----GHPIKNHDL 409
Cdd:cd23280   11 DVVRLFHKELEAYLSaeGSFVDEVLTEDVHlrvRPVDDRKPRTLFPPTSGDTFWQI-------EKEdtplkGGVIKWGDQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 410 VRLRHIVTDTILLSHDVaspyyPTNQEFTTVSIgdaygDRAADTLFEI-----------------RIEHGK------ANQ 466
Cdd:cd23280   84 CRLRHLPTGKYLAVDDK-----TGNGKVVLTSD-----PSDPSTVFRLhpvtketseevkfgsyvRIEHVAtgtwlhAET 153

                        170       180
                 ....*....|....*....|.
gi 164423013 467 EFKSISSHFKLIHNPSKVAMW 487
Cdd:cd23280  154 DEELRRSKKSPAGLSWDGAKL 174
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
 101-248 2.59e-03

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


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 40.75  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013 101 HPPFGKLLFAFMGWLVGYDghfhfenigdsyirnkvpYVAFRsLPA-ILGALTVSVVYMIMWESGYSLPACLIAAGLVLL 179
Cdd:COG4346   79 HPPLGKYIIALSMLLLGDK------------------PLYWR-LPSiILGALIVILVFLTARRLSGNIVAGLIASLLLAL 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164423013 180 DNAHIGQTRLILLDATLVFAMACSLLCYIKFHKLrhepfsrkwwkwliLTGFALSCDISTKYVGLFAFI 248
Cdd:COG4346  140 DPLLRVMSSIAMLDIYVAFFTALALYFAVSGRLL--------------LSSIALGLAAASKYSGLFLLI 194
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
473-521 2.62e-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: 2.62e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 164423013   473 SHFKLIHNPSKVAMWTHSKPLPEWGHKQQEINGNKQLAQ-SSNVWLVEDI 521
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 335-443 4.22e-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: 38.88  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164423013  335 TIDYYDTISIRHKETKAYLHSHPDKYPLRYDdgrVSSQGQQVTGY---PFNDTNNYWQILPPGPDDQKLGHPIKNHD-LV 410
Cdd:pfam02815  64 LIKWGSPFRLRHLTTGRYLHSHEEQKPPLVE---KEDWQKEVSAYgfrGFPGDNDIVEIFEKKSTTGMGSDRIKPGDsYF 140

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 164423013  411 RLRHIVTDTILLSHDVASP---YYPTNQEFTTVSIG 443
Cdd:pfam02815 141 RLQHVCTGCWLFSHSVKLPkwgFGPEQQKVTCAKEG 176
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
408-459 4.78e-03

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 35.78  E-value: 4.78e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 164423013   408 DLVRLRHIVTDTILLSHDVasPYYPTNQEFTTVSiGDAYGDRAADTLFEIRI 459
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDE--KLPPWGDGQQEVT-GYGNPAIDANTLWLIEP 56
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 342-388 6.70e-03

MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor 2-like protein (AtSDF2) and similar proteins; AtSDF2, also called SDF2-like protein, acts as a crucial component of the unfolded protein response (UPR) in Arabidopsis thaliana. It is involved in the endoplasmic reticulum (ER) protein quality control and unfolded protein response. It may be involved in the quality control of glycoproteins. AtSDF2 forms a complex in the ER with ERDJ3B and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity. AtSDF2 contains a MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467765 [Multi-domain]  Cd Length: 176  Bit Score: 38.13  E-value: 6.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 164423013 342 ISIRHKETKAYLHSHPDKYplryddGRVSSQGQQVTGYPFNDTNNYW 388
Cdd:cd23294  127 VRLKHVDTGGYLHSHDKKY------GRPIPGQQEVCAVASKNSNTLW 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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