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Conserved domains on  [gi|6320107|ref|NP_010188|]
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dolichyl-phosphate-mannose-protein mannosyltransferase PMT1 [Saccharomyces cerevisiae S288C]

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_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 327-516 1.88e-121

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: 363.54  E-value: 1.88e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  327 VGIGSIISLRHLSTMGGYLHSHSHNYPAGSEQQQSTLYPHMDANNDWLLELYNAPGE-SLTTFQNLTDGTKVRLFHTVTR 405
Cdd:cd23283   1 VAYGSTIRIRHLNTRGGYLHSHPHNYPAGSKQQQITLYPHRDENNDWLVELANAPEEwSPTTFENLKDGDVVRLEHVATG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  406 CRLHSHDHKPPVSeSSDWQKEVSCYGYSGFDGDANDDWVVEIDKKNSAPGVAQERVIALDTKFRLRHAMTGCYLFSHEVK 485
Cdd:cd23283  81 RRLHSHDHRPPVS-DNDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGESKERVRAIDTKFRLVHVMTGCYLFSHGVK 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 6320107  486 LPAWGFEQQEVTCASSGRHDLTLWYVENNSN 516
Cdd:cd23283 160 LPEWGFEQQEVTCAKSGLLELSLWYIETNEH 190
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 54-297 1.20e-98

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: 306.54  E-value: 1.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107     54 ACLAVFTAVIRLHGLAWPDSVVFDEVHFGGFASQYIRGTYFMDVHPPLAKMLYAGVASLGGFQGDFDFENIG-DSFPSTT 132
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGgQYYPGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    133 PYVLMRFFSASLGALTVILMYMTLRYSGVRMWVALMSAICFAVENSYVTISRYILLDAPLMFFIAAAVYSFKKYEMYPAN 212
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    213 SLNAYKSLLATGIALGMASSSKWVGLFTVTWVGLLCIWRLWFMIGDLTKSSKSIFKVAFAKLAFLLGVPFALYLVFFYIH 292
Cdd:pfam02366 161 SRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVH 240


                  ....*
gi 6320107    293 FQSLT 297
Cdd:pfam02366 241 FWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 535-725 1.87e-83

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: 264.79  E-value: 1.87e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    535 SKFIESHKKMWHINKNLVEPHVYESQPTSWPFLLRGISYWGENNRN--VYLLGNAIVWWAVTAFIGIFGLIVITELFSWQ 612
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNaqIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    613 LGKPILKDSKVV-NFHVQVIHYLLGFAVHYAPSFLMQRQMFLHHYLPAYYFGILALGHALDIIVSYVFRSKR----QMGY 687
Cdd:pfam16192  81 RGYYDLSDDWTRsRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRslrkRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 6320107    688 AVVITFLAASVYFFKSFSPIIYGTPWTQELCQKSQWLS 725
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 327-516 1.88e-121

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: 363.54  E-value: 1.88e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  327 VGIGSIISLRHLSTMGGYLHSHSHNYPAGSEQQQSTLYPHMDANNDWLLELYNAPGE-SLTTFQNLTDGTKVRLFHTVTR 405
Cdd:cd23283   1 VAYGSTIRIRHLNTRGGYLHSHPHNYPAGSKQQQITLYPHRDENNDWLVELANAPEEwSPTTFENLKDGDVVRLEHVATG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  406 CRLHSHDHKPPVSeSSDWQKEVSCYGYSGFDGDANDDWVVEIDKKNSAPGVAQERVIALDTKFRLRHAMTGCYLFSHEVK 485
Cdd:cd23283  81 RRLHSHDHRPPVS-DNDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGESKERVRAIDTKFRLVHVMTGCYLFSHGVK 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 6320107  486 LPAWGFEQQEVTCASSGRHDLTLWYVENNSN 516
Cdd:cd23283 160 LPEWGFEQQEVTCAKSGLLELSLWYIETNEH 190
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 54-297 1.20e-98

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: 306.54  E-value: 1.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107     54 ACLAVFTAVIRLHGLAWPDSVVFDEVHFGGFASQYIRGTYFMDVHPPLAKMLYAGVASLGGFQGDFDFENIG-DSFPSTT 132
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGgQYYPGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    133 PYVLMRFFSASLGALTVILMYMTLRYSGVRMWVALMSAICFAVENSYVTISRYILLDAPLMFFIAAAVYSFKKYEMYPAN 212
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    213 SLNAYKSLLATGIALGMASSSKWVGLFTVTWVGLLCIWRLWFMIGDLTKSSKSIFKVAFAKLAFLLGVPFALYLVFFYIH 292
Cdd:pfam02366 161 SRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVH 240


                  ....*
gi 6320107    293 FQSLT 297
Cdd:pfam02366 241 FWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 535-725 1.87e-83

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: 264.79  E-value: 1.87e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    535 SKFIESHKKMWHINKNLVEPHVYESQPTSWPFLLRGISYWGENNRN--VYLLGNAIVWWAVTAFIGIFGLIVITELFSWQ 612
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNaqIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    613 LGKPILKDSKVV-NFHVQVIHYLLGFAVHYAPSFLMQRQMFLHHYLPAYYFGILALGHALDIIVSYVFRSKR----QMGY 687
Cdd:pfam16192  81 RGYYDLSDDWTRsRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRslrkRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 6320107    688 AVVITFLAASVYFFKSFSPIIYGTPWTQELCQKSQWLS 725
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 346-509 2.20e-60

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: 202.59  E-value: 2.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    346 HSHSHNYPAGSEQQQS------TLYPHMDANND----WLLELYNAPgesLTTFQNLTDGTKVRLFHTVTRCRLHSHDH-K 414
Cdd:pfam02815  13 HSHQDEYLTGSEQQQKqpflriTLYPHGDANNSarslWRIEVVRHD---AWRGGLIKWGSPFRLRHLTTGRYLHSHEEqK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    415 PPVSESSDWQKEVSCYGYSGFDGDaNDDwvVEIDKKNSAPGVAQERVIALDTKFRLRHAMTGCYLFSHEVKLPAWGFE-- 492
Cdd:pfam02815  90 PPLVEKEDWQKEVSAYGFRGFPGD-NDI--VEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpe 166

                         170
                  ....*....|....*..
gi 6320107    493 QQEVTCASSGRHDLTLW 509
Cdd:pfam02815 167 QQKVTCAKEGHMDDALT 183
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 56-727 1.11e-23

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 105.74  E-value: 1.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107   56 LAVFTAVIRLHGLAWPDSVVFDEVHFGGFASQYIR---------GTYFMDVHPPLAKMLYAGVASLGGFQGDFDFenigd 126
Cdd:COG1928  28 VTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTngyernwpdPGPFFVVHPPLGKWLIALGEWLFGYVNPFGW----- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  127 sfpsttpyvlmRFFSASLGALTV-ILMYMTLRYSGvRMWVALMSAICFAVENSYVTISRYILLDAPLMFFIAAAVYSF-- 203
Cdd:COG1928 103 -----------RFAAALAGTLSVlLVARIARRLTR-STLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGCLll 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  204 -------KKYEMYPANSLNAYKS--------LLATGIALGMASSSKWVGLftvtwvgllciwrlWFMIGdltkssksifk 268
Cdd:COG1928 171 drdqvrrRLAAAVAAGRAPSRWGprlgfrwwRLAAGVLLGLACGVKWSGL--------------YFLAA----------- 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  269 vafaklafllgvpFALYLVFFyihfqsltldgdgasffspefrstlknnkipqnvvaDVGIGSIISLRHlstmggylhsh 348
Cdd:COG1928 226 -------------FGLLTVAW------------------------------------DAGARRAAGVRR----------- 245

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  349 shnypagseqqqstlyphmdanndWLLelynapgeslttfqnltdGTKVRlfhtvtrcrlhshdhkppvsessdwqkevs 428
Cdd:COG1928 246 ------------------------PWL------------------GALLR------------------------------ 253

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  429 cygysgfdgdanddwvveidkkNSAPGVAQERVIALDTkfrlrhamtgcYLFSHevklpaWGFEQQEvtcASSGRHdltl 508
Cdd:COG1928 254 ----------------------DGIPAFFALVIVPLLT-----------YLASW------TGWFASD---TGYDRH---- 287

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  509 WYVENNSNPLlpedtkriSYKPASFISkFIESHKKMWHINKNLVEPHVYESQPTSWPFLLRGISYWGENNRN-------- 580
Cdd:COG1928 288 WAAQNPGSGL--------GWVPDALRS-LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcgag 358

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  581 -----VYLLGNAIVWWAvtAFIGIFGLIVITELF-SWQLGKPilkdskvvnfhvqvihyLLGFAVHYAPSFL-MQRQMFL 653
Cdd:COG1928 359 kcvraVLAIGNPALWWL--GLPALLWLLWRWIARrDWRAGAV-----------------LVGYAAGWLPWFLyLDRTMFF 419

                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320107  654 HHYLPAYYFGILALGHALD-IIVSYVFRSKRQMGYAVVITFLAASVYFFKSFSPIIYGTPWTQELCQKSQWLSGW 727
Cdd:COG1928 420 FYAIPFVPFLVLALALVLGlILGPARASERRRLGRLVVGLYVGLVVANFAFFYPILTGLPIPYDEWQARMWFPSW 494
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
459-512 1.22e-16

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 74.69  E-value: 1.22e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6320107     459 ERVIALDTKFRLRHAMTGCYLFSHEVKLPAWGFEQQEVTCASSGRHD-LTLWYVE 512
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDaNTLWLIE 55
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 44-306 2.05e-14

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: 75.04  E-value: 2.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107   44 MVTLKEKLLVACLAVFTAVIRLHGLAWPDSVVFDEVHF----------GGFASQYIRGTYFMDvHPPLAKMLYAGVASLG 113
Cdd:COG1807   1 MSKTLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYaeiaremlesGDWLTPTLAGEPYFD-KPPLIYWLIALSYKLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  114 GFqgdfdfenigdsfpsttPYVLMRFFSASLGALTVILMYMTLRYSGVRmWVALMSAICFAVENSYVTISRYILLDAPLM 193
Cdd:COG1807  80 GV-----------------SEFAARLPSALLGLLTVLLVYLLARRLFGR-RAALLAALLLLTSPLLLLFGRLATPDALLL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  194 FFIAAAVYSFKKYEMYpanslNAYKSLLATGIALGMASSSKWVGLFTVTWVGLLciwrLWFMIGDLTKSSKSIFKVAFAK 273
Cdd:COG1807 142 LFWTLALYALLRALER-----RRLRWLLLAGLALGLGFLTKGPVALLLPGLALL----LYLLLTRRWRRLRRLRLLLGLL 212

                       250       260       270
                ....*....|....*....|....*....|....
gi 6320107  274 LAFLLGVPFALYLVFFYI-HFQSLTLDGDGASFF 306
Cdd:COG1807 213 LALLLALPWYIANDWATGpAFLEYFFGYENLVPL 246
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 327-516 1.88e-121

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: 363.54  E-value: 1.88e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  327 VGIGSIISLRHLSTMGGYLHSHSHNYPAGSEQQQSTLYPHMDANNDWLLELYNAPGE-SLTTFQNLTDGTKVRLFHTVTR 405
Cdd:cd23283   1 VAYGSTIRIRHLNTRGGYLHSHPHNYPAGSKQQQITLYPHRDENNDWLVELANAPEEwSPTTFENLKDGDVVRLEHVATG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  406 CRLHSHDHKPPVSeSSDWQKEVSCYGYSGFDGDANDDWVVEIDKKNSAPGVAQERVIALDTKFRLRHAMTGCYLFSHEVK 485
Cdd:cd23283  81 RRLHSHDHRPPVS-DNDWQNEVSAYGYEGFEGDANDDWRVEILKDDSRPGESKERVRAIDTKFRLVHVMTGCYLFSHGVK 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 6320107  486 LPAWGFEQQEVTCASSGRHDLTLWYVENNSN 516
Cdd:cd23283 160 LPEWGFEQQEVTCAKSGLLELSLWYIETNEH 190
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 54-297 1.20e-98

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: 306.54  E-value: 1.20e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107     54 ACLAVFTAVIRLHGLAWPDSVVFDEVHFGGFASQYIRGTYFMDVHPPLAKMLYAGVASLGGFQGDFDFENIG-DSFPSTT 132
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGgQYYPGNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    133 PYVLMRFFSASLGALTVILMYMTLRYSGVRMWVALMSAICFAVENSYVTISRYILLDAPLMFFIAAAVYSFKKYEMYPAN 212
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    213 SLNAYKSLLATGIALGMASSSKWVGLFTVTWVGLLCIWRLWFMIGDLTKSSKSIFKVAFAKLAFLLGVPFALYLVFFYIH 292
Cdd:pfam02366 161 SRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVH 240


                  ....*
gi 6320107    293 FQSLT 297
Cdd:pfam02366 241 FWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 535-725 1.87e-83

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: 264.79  E-value: 1.87e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    535 SKFIESHKKMWHINKNLVEPHVYESQPTSWPFLLRGISYWGENNRN--VYLLGNAIVWWAVTAFIGIFGLIVITELFSWQ 612
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGWDDRNaqIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    613 LGKPILKDSKVV-NFHVQVIHYLLGFAVHYAPSFLMQRQMFLHHYLPAYYFGILALGHALDIIVSYVFRSKR----QMGY 687
Cdd:pfam16192  81 RGYYDLSDDWTRsRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRslrkRVGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 6320107    688 AVVITFLAASVYFFKSFSPIIYGTPWTQELCQKSQWLS 725
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 327-514 8.57e-76

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: 243.78  E-value: 8.57e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  327 VGIGSIISLRHLSTMGGYLHSHSHNYPAGSEQQQSTLYPHMDANNDWLLELYNAPGESLTTF-QNLTDGTKVRLFHTVTR 405
Cdd:cd23276   1 VAYGSQITLRNANSGGGYLHSHNHTYPDGSKQQQVTGYGHKDENNWWQILKPRGDPSSNPPDpEYVRDGDEVRLLHKETN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  406 CRLHSHDHKPPVsesSDWQKEVSCYGYSGFDGDANDDWVVEIDKKNSAPGVaqERVIALDTKFRLRHAMTGCYLFSHEVK 485
Cdd:cd23276  81 RYLRTHDAAAPV---TSKHKEVSAYPDENEDGDDNDLWVVEIVKDEGKLED--KRIKPLTTRFRLRNKKTGCYLTSSGVK 155

                       170       180       190
                ....*....|....*....|....*....|
gi 6320107  486 LPAWGFEQQEVTCASSGR-HDLTLWYVENN 514
Cdd:cd23276 156 LPEWGFRQGEVVCSKNKEsDPSTLWNVEEN 185
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 326-516 7.25e-62

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: 206.79  E-value: 7.25e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  326 DVGIGSIISLRHLSTMGGYLHSHSHNYPAGSEQQQSTLYPHMDANNDWLLEL---YNAPGESLTTFQNLTDGTKVRLFHT 402
Cdd:cd23284   3 DVAYGSKVTIKNQGLGGGLLHSHVQTYPEGSNQQQVTCYGHKDSNNEWIFERprgLPSWDENDTDIEFIKDGDIVRLVHK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  403 VTRCRLHSHDHKPPVSeSSDWqkEVSCYGySGFDGDANDDWVVEIDKKNSAPgvAQERVIALDTKFRLRHAMTGCYLFSH 482
Cdd:cd23284  83 QTGRNLHSHPVPAPIS-KSDY--EVSGYG-DLTVGDEKDNWVIEIVKQVGSE--DPKKLHTLTTSFRLRHEVLGCYLAQT 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6320107  483 EVKLPAWGFEQQEVTC--ASSGRHDLTLWYVENNSN 516
Cdd:cd23284 157 GVSLPEWGFKQGEVVCdkSNFKRDKRTWWNIETHTN 192
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 346-509 2.20e-60

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: 202.59  E-value: 2.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    346 HSHSHNYPAGSEQQQS------TLYPHMDANND----WLLELYNAPgesLTTFQNLTDGTKVRLFHTVTRCRLHSHDH-K 414
Cdd:pfam02815  13 HSHQDEYLTGSEQQQKqpflriTLYPHGDANNSarslWRIEVVRHD---AWRGGLIKWGSPFRLRHLTTGRYLHSHEEqK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    415 PPVSESSDWQKEVSCYGYSGFDGDaNDDwvVEIDKKNSAPGVAQERVIALDTKFRLRHAMTGCYLFSHEVKLPAWGFE-- 492
Cdd:pfam02815  90 PPLVEKEDWQKEVSAYGFRGFPGD-NDI--VEIFEKKSTTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKWGFGpe 166

                         170
                  ....*....|....*..
gi 6320107    493 QQEVTCASSGRHDLTLW 509
Cdd:pfam02815 167 QQKVTCAKEGHMDDALT 183
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 327-516 5.51e-58

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: 195.98  E-value: 5.51e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  327 VGIGSIISLRHLSTMGGYLHSHSHNYPAG--SEQQQSTLYPHMDANNDWLLELYNAPGESLTTFQNLTDGTKVRLFHTVT 404
Cdd:cd23282   1 VAYGSVITLKNHRTGGGYLHSHWHLYPEGvgARQQQVTTYSHKDDNNLWLIKKHNQSSDLSDPVEYVRHGDLIRLEHVNT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  405 RCRLHSHDHKPPVSESsdwQKEVSCYGYSGfDGDANDDWVVEIdkKNSAPGvaqERVIALDTKFRLRHAMTGCYLFSHEV 484
Cdd:cd23282  81 KRNLHSHKEKAPLTKK---HYQVTGYGENG-TGDANDVWRVEV--VGGREG---DPVKTVRSKFRLVHYNTGCALHSHGK 151

                       170       180       190
                ....*....|....*....|....*....|..
gi 6320107  485 KLPAWGFEQQEVTCASSGRHDLTLWYVENNSN 516
Cdd:cd23282 152 QLPKWGWEQLEVTCNPNVRDKNSLWNVEDNRN 183
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 330-514 1.74e-55

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: 189.18  E-value: 1.74e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  330 GSIISLRHLSTMGGYLHSHSHNYPAGSEQQQSTLYPHM-DANNDWLLE--LYNAPGESLTTFQNLTDGTKVRLFHTVTRC 406
Cdd:cd23286   4 GSTVTIRHLESLGGYLHSHDLTYPSGSNEQQVTLYDFEdDANNEWIIEtkTKEQMDKFPGQFREVRDGDVIRLRHVVTGK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  407 RLHSHDHKPPVSESsDWQKEVSCYGYSGFDGDANDDWVVEI--DKKNSAPGVAQERVIALDTKFRLRHAMTGCYLFSHEV 484
Cdd:cd23286  84 LLRASNARPPVSEQ-EYNNEVSCTGNANYSGDMDENWRIDVkgDESHAELKLPNIKIKSTESVFQLYNRGTGCTLLSHDT 162

                       170       180       190
                ....*....|....*....|....*....|
gi 6320107  485 KLPAWGFEQQEVTCASSGRHDLTLWYVENN 514
Cdd:cd23286 163 RLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 330-514 1.03e-40

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: 147.14  E-value: 1.03e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  330 GSIISLRHlSTMGGYLHSHSHNYPAGSEQQQSTLYPHM---DANNDWLLElynapGESLTTFQNLTDGTKVRLFHTVTRC 406
Cdd:cd23263   1 GDVIWLKH-SETGKYLHSHRKNYPTGSGQQEVTFESSSrkgDTNGLWIIE-----SENGKQGGPVKWGDKIRLRHLSTGK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  407 RLHSHDHKPpvsESSDWQKEVSCYGYsgfDGDANDDWVVEIDKKNSApgvaQERVIALDTKFRLRHAMTGCYLFSHEVKL 486
Cdd:cd23263  75 YLSSEEGKK---SPKSNHQEVLCLTD---NPDKSSLFKFEPIGSTKY----KQKYVKKDSYFRLKHVNTNFWLHSHEKKF 144

                       170       180
                ....*....|....*....|....*...
gi 6320107  487 PAWGFEQQEVTCASSGRHDLTLWYVENN 514
Cdd:cd23263 145 NINNKTQQEVICHGEREEVFKLWKAELI 172
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 330-509 1.01e-33

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: 127.49  E-value: 1.01e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  330 GSIISLRHLSTmGGYLHSHSHNYPAGSEQQQSTLYPHM-DANNDWLLElyNAPGESLTTFQNLTDGTKVRLFHTVTRCRL 408
Cdd:cd23294   4 GSVIKLQHERT-KFRLHSHEVPYGSGSGQQSVTGFPGVdDSNSYWIVK--PANGERCKQGDVIKNGDVIRLQHVSTRKWL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  409 HSHDHKPPVSEssdwQKEVSCYGYSGfDGDANDDWVVEIDKKNSapgvaqerVIALDTKFRLRHAMTGCYLFSHEVKL-- 486
Cdd:cd23294  81 HSHLHASPLSG----NQEVSCFGGDG-NSDTGDNWIVEIEGGGK--------VWERDQKVRLKHVDTGGYLHSHDKKYgr 147

                       170       180
                ....*....|....*....|...
gi 6320107  487 PAWGfeQQEVtCASSGRHDLTLW 509
Cdd:cd23294 148 PIPG--QQEV-CAVASKNSNTLW 167
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 330-516 3.53e-31

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: 120.88  E-value: 3.53e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  330 GSIISLRHLSTMGGYLHSHSHNYP-------AGSEQQQSTLYPHMDANNDWLLELYNAPGESLTT-FQNLTDGTKVRLFH 401
Cdd:cd23281   4 GSQVTLRNTHGSPCWLHSHKHRYPikypdgrGSSHQQQVTCYPFKDVNNWWIIKDPGRQDLAVDDpPRPVRHGDIIQLVH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  402 TVTRCRLHSHDHKPPVSESSdwqKEVSCYGYSGFDGDANDDWVVEIDKKNSaPGvaqERVIALDTKFRLRHAMTGCYL-F 480
Cdd:cd23281  84 GKTGRFLNSHDVAAPLSPTH---QEVSCYIDYNISMPAQNLWRIEIVNRDS-EG---DTWKAIKSQFRLIHVNTSAALkL 156

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 6320107  481 SHEvKLPAWGFEQQEVTCASSGRHDLTLWYVENNSN 516
Cdd:cd23281 157 SGK-QLPDWGFGQLEVATDRAGNQSSTVWNVEEHRY 191
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 330-511 1.17e-26

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: 107.00  E-value: 1.17e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  330 GSIISLRHLSTmGGYLHSHSHNYPAGSEQQQSTLYPH-MDANNDWLLELYNApgeslTTFQNLTD----GTKVRLFHTVT 404
Cdd:cd23279   2 GSAIKLKHVNS-GYRLHSHEVSYGSGSGQQSVTAVPSaDDANSLWTVLPGLG-----EPCQEQGKpvkcGDIIRLQHVNT 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  405 RCRLHSHDHKPPVSEssdwQKEVSCYGysGFDGDANDDWVVEIDKKNSapgvaqeRVIALDTKFRLRHAMTGCYLFSHEV 484
Cdd:cd23279  76 RKNLHSHNHSSPLSG----NQEVSAFG--GGDEDSGDNWIVECEGKKA-------KFWKRGEPVRLKHVDTGKYLSASKT 142

                       170       180       190
                ....*....|....*....|....*....|.
gi 6320107  485 KL----PAWGfeQQEVTCASSGRHDlTLWYV 511
Cdd:cd23279 143 HKftqqPIAG--QLEVSAASSKDSD-SQWKA 170
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 330-512 1.03e-25

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: 105.07  E-value: 1.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  330 GSIISLRHLSTmGGYLHSHSHNYP-------AGSEQQQSTLYPHMDANNDWLLELYNAPGESLTTFQNLTDGTKVRLFHT 402
Cdd:cd23285   4 GDVITIKHRDT-NAFLHSHPERYPlryedgrISSQGQQVTGYPHKDANNQWQILPTDPIDEHEGTGRPVRNGDLIRLRHV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  403 VTRCRLHSHDHKPPVSESSdwqKEVSCYGYSGFDGDANDD-WVVEIDKKNSaPGVAQERVialdTKFRLRHAMTGCYLFS 481
Cdd:cd23285  83 STDTYLLTHDVASPLTPTN---MEFTTVSDDDTDERYNETlFRVEIEDTDE-GDVLKTKS----SHFRLIHVDTNVALWT 154

                       170       180       190
                ....*....|....*....|....*....|.
gi 6320107  482 HEVKLPAWGFEQQEVTCASSGRHDLTLWYVE 512
Cdd:cd23285 155 HKKPLPDWGFGQQEVNGNKNIKDKSNIWVVD 185
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 56-727 1.11e-23

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 105.74  E-value: 1.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107   56 LAVFTAVIRLHGLAWPDSVVFDEVHFGGFASQYIR---------GTYFMDVHPPLAKMLYAGVASLGGFQGDFDFenigd 126
Cdd:COG1928  28 VTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTngyernwpdPGPFFVVHPPLGKWLIALGEWLFGYVNPFGW----- 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  127 sfpsttpyvlmRFFSASLGALTV-ILMYMTLRYSGvRMWVALMSAICFAVENSYVTISRYILLDAPLMFFIAAAVYSF-- 203
Cdd:COG1928 103 -----------RFAAALAGTLSVlLVARIARRLTR-STLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGCLll 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  204 -------KKYEMYPANSLNAYKS--------LLATGIALGMASSSKWVGLftvtwvgllciwrlWFMIGdltkssksifk 268
Cdd:COG1928 171 drdqvrrRLAAAVAAGRAPSRWGprlgfrwwRLAAGVLLGLACGVKWSGL--------------YFLAA----------- 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  269 vafaklafllgvpFALYLVFFyihfqsltldgdgasffspefrstlknnkipqnvvaDVGIGSIISLRHlstmggylhsh 348
Cdd:COG1928 226 -------------FGLLTVAW------------------------------------DAGARRAAGVRR----------- 245

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  349 shnypagseqqqstlyphmdanndWLLelynapgeslttfqnltdGTKVRlfhtvtrcrlhshdhkppvsessdwqkevs 428
Cdd:COG1928 246 ------------------------PWL------------------GALLR------------------------------ 253

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  429 cygysgfdgdanddwvveidkkNSAPGVAQERVIALDTkfrlrhamtgcYLFSHevklpaWGFEQQEvtcASSGRHdltl 508
Cdd:COG1928 254 ----------------------DGIPAFFALVIVPLLT-----------YLASW------TGWFASD---TGYDRH---- 287

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  509 WYVENNSNPLlpedtkriSYKPASFISkFIESHKKMWHINKNLVEPHVYESQPTSWPFLLRGISYWGENNRN-------- 580
Cdd:COG1928 288 WAAQNPGSGL--------GWVPDALRS-LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcgag 358

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  581 -----VYLLGNAIVWWAvtAFIGIFGLIVITELF-SWQLGKPilkdskvvnfhvqvihyLLGFAVHYAPSFL-MQRQMFL 653
Cdd:COG1928 359 kcvraVLAIGNPALWWL--GLPALLWLLWRWIARrDWRAGAV-----------------LVGYAAGWLPWFLyLDRTMFF 419

                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6320107  654 HHYLPAYYFGILALGHALD-IIVSYVFRSKRQMGYAVVITFLAASVYFFKSFSPIIYGTPWTQELCQKSQWLSGW 727
Cdd:COG1928 420 FYAIPFVPFLVLALALVLGlILGPARASERRRLGRLVVGLYVGLVVANFAFFYPILTGLPIPYDEWQARMWFPSW 494
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 330-509 2.15e-17

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: 80.39  E-value: 2.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  330 GSIISLRHLSTmGGYLHSHSHNYPAGSEQQQSTLYPH-MDANNDWllELYNAPGESLTTFQNLTDGTKVRLFHTVTRCRL 408
Cdd:cd23293   4 GSVVKLLNTRH-NVRLHSHDVKYGSGSGQQSVTGVESsDDSNSYW--QIRGPTGADCERGTPIKCGQTIRLTHLNTGKNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  409 HSHDHKPPVSESsdwqKEVSCYGYSGfDGDANDDWVVEIDkknsapGVAQERvialDTKFRLRHAMTGCYL------FSH 482
Cdd:cd23293  81 HSHHFQSPLSGN----QEVSAFGEDG-EGDTGDNWTVVCS------GTYWER----DEAVRLKHVDTEVYLhvtgeqYGR 145

                       170       180
                ....*....|....*....|....*..
gi 6320107  483 evklPAWGfeQQEVtCASSGRHDLTLW 509
Cdd:cd23293 146 ----PIHG--QREV-SGMSSPSQANYW 165
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
459-512 1.22e-16

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 74.69  E-value: 1.22e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6320107     459 ERVIALDTKFRLRHAMTGCYLFSHEVKLPAWGFEQQEVTCASSGRHD-LTLWYVE 512
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIDaNTLWLIE 55
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
391-447 3.92e-16

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 73.14  E-value: 3.92e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6320107     391 LTDGTKVRLFHTVTRCRLHSHDHKPPvsESSDWQKEVSCYGYSGfdGDANDDWVVEI 447
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLP--PWGDGQQEVTGYGNPA--IDANTLWLIEP 56
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 44-306 2.05e-14

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: 75.04  E-value: 2.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107   44 MVTLKEKLLVACLAVFTAVIRLHGLAWPDSVVFDEVHF----------GGFASQYIRGTYFMDvHPPLAKMLYAGVASLG 113
Cdd:COG1807   1 MSKTLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYaeiaremlesGDWLTPTLAGEPYFD-KPPLIYWLIALSYKLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  114 GFqgdfdfenigdsfpsttPYVLMRFFSASLGALTVILMYMTLRYSGVRmWVALMSAICFAVENSYVTISRYILLDAPLM 193
Cdd:COG1807  80 GV-----------------SEFAARLPSALLGLLTVLLVYLLARRLFGR-RAALLAALLLLTSPLLLLFGRLATPDALLL 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  194 FFIAAAVYSFKKYEMYpanslNAYKSLLATGIALGMASSSKWVGLFTVTWVGLLciwrLWFMIGDLTKSSKSIFKVAFAK 273
Cdd:COG1807 142 LFWTLALYALLRALER-----RRLRWLLLAGLALGLGFLTKGPVALLLPGLALL----LYLLLTRRWRRLRRLRLLLGLL 212

                       250       260       270
                ....*....|....*....|....*....|....
gi 6320107  274 LAFLLGVPFALYLVFFYI-HFQSLTLDGDGASFF 306
Cdd:COG1807 213 LALLLALPWYIANDWATGpAFLEYFFGYENLVPL 246
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
326-378 4.90e-11

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 58.51  E-value: 4.90e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 6320107     326 DVGIGSIISLRHLSTmGGYLHSHSHNYPA-GSEQQQSTLYPHM--DANNDWLLELY 378
Cdd:smart00472   3 FVRWGDVVRLRHVTT-GRYLHSHDEKLPPwGDGQQEVTGYGNPaiDANTLWLIEPV 57
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
 92-286 8.04e-08

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


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 55.39  E-value: 8.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107   92 TYFMDVHPPLAKMLYAGVASLGGFQgdfdfenigdsfpsttpYVLMRFFSASLGALTVILMYMTLRYSGVRMWVALMSAI 171
Cdd:COG4346  73 TYLNLEHPPLGKYIIALSMLLLGDK-----------------PLYWRLPSIILGALIVILVFLTARRLSGNIVAGLIASL 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  172 CFAVENSYVTISRYILLDAPLMFFIAAAVYsfkkyemypansLNAYKSLLATGIALGMASSSKWVGLFtvtwvGLLCiwr 251
Cdd:COG4346 136 LLALDPLLRVMSSIAMLDIYVAFFTALALY------------FAVSGRLLLSSIALGLAAASKYSGLF-----LLIP--- 195

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 6320107  252 LWFMIGDLTKS-SKSIFKVAFAKLAF--LLGVPFALYL 286
Cdd:COG4346 196 LLLYLREIEKSpIKRFLYGILIPLAVflIVSIPLIIYF 233
Stt3 COG1287
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
 35-310 7.73e-07

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


Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 52.87  E-value: 7.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107   35 SAELASLRTMVTLKEKLLVACLAVFTAVIRLhgLAWPDSVVFDEVHFGGF-------ASQYI--RGTYFM--DVH----- 98
Cdd:COG1287   2 SEKTSVLDKLKRLLHLPALLLILALALWIRL--LPYDNVFRDGGVYLGGNdpwyhlrQIEYIlaNGPSTLpfDPLtwypw 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107   99 -------PPLAKMLYAGVASLggfqgdfdfenIGDSFPST-TPYVLMRFFSASLGALTVILMYMTLRYSGVRmWVALMSA 170
Cdd:COG1287  80 grdigqfGPLFDQLIALLALI-----------LGLGSPSQsSVYTVAAWFPPIFGALTVIPVYLLGRRLGGR-KAGLLAA 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107  171 ICFAVenSYVTISRYIL--LD--APLMFFIAAAVYSF-------KKYEMYPANSLNAYKSLLATGIALGMASSSkWVGlF 239
Cdd:COG1287 148 LLLAL--SPGQLSRSLLgfADhhVAELFFSTLAVLFLvlalkraKREKRDLEALKRPLLYAVLAGVALGLYLLT-WGG-Y 223

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6320107  240 TVTWVGLLCIWRLWFMIGDLTKSSKSifkvafaKLAFLLGVPFALYLVFFYIHFQSLTLDGDGASFFSPEF 310
Cdd:COG1287 224 VLFVGILALFALLQLLLDLLRGRSPE-------YLAIVGAVSFAVAALLVLPFIPRLGFSGTGLSLLQPLL 287
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 97-285 1.17e-06

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


Pssm-ID: 433048 [Multi-domain]  Cd Length: 160  Bit Score: 49.18  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107     97 VHPPLAKMLYAGVASLGGFQGdfdfenigdsfpsttpyVLMRFFSASLGALTVILMYMTLRYSGVRmWVALMSAICFAVE 176
Cdd:pfam13231   1 DHPPLAAWLIALFTALFGDSE-----------------WAVRLPSALAGVLTILLLYLLARRLFGK-RAALLAALLLAVV 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320107    177 NSYVTISRYILLDAPLMFFIAAAVYSfkkyeMYPANSLNAYKSLLATGIALGMASSSKWvglftvtWVGLLCIWRLWFMI 256
Cdd:pfam13231  63 PLFVALSRLFTPDAPLLLFWALALYF-----LLRALEKGRLKWWLLAGAAAGLGFLSKY-------TAALLVLAALLYLL 130

                         170       180       190
                  ....*....|....*....|....*....|.
gi 6320107    257 GDLTKSS--KSIFKVAFAkLAFLLGVPFALY 285
Cdd:pfam13231 131 ISPGRRRlkSPKPYLGLL-LALLLFSPVLIW 160
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 468-512 2.60e-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: 39.67  E-value: 2.60e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6320107  468 FRLRHAMTGCYLFSHEVKLpAWGFEQQEVTCASSGRHDLTLWYVE 512
Cdd:cd23294   7 IKLQHERTKFRLHSHEVPY-GSGSGQQSVTGFPGVDDSNSYWIVK 50
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 469-517 3.32e-03

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: 39.20  E-value: 3.32e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6320107  469 RLRHAMTGCYLFSHEVKlpaWGF--EQQEVTCASSGRHDLTLWYV-ENNSNP 517
Cdd:cd23279   6 KLKHVNSGYRLHSHEVS---YGSgsGQQSVTAVPSADDANSLWTVlPGLGEP 54
 
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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