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Conserved domains on  [gi|149386124|gb|ABN65834|]
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dolichyl-phosphate-mannose-protein mannosyltransferase [Scheffersomyces stipitis CBS 6054]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 319-509 1.47e-91

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: 283.94  E-value: 1.47e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHN-NLEEYLHSHDHNYPGGSQEQQVSLYGFSPDENNEWIIETKNKAREGQLQKNFKAVLDGDTIRLFHKQ 397
Cdd:cd23286    1 LLYGSTVTIRHLeSLGGYLHSHDLTYPSGSNEQQVTLYDFEDDANNEWIIETKTKEQMDKFPGQFREVRDGDVIRLRHVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 398 TGKYLHVNDIRPPISEHDYSNEVSCSGSRELLGDINYEFKVRIMNKKPHSQNNLPMIKLRATESIFQLVHHGTKCVMMSH 477
Cdd:cd23286   81 TGKLLRASNARPPVSEQEYNNEVSCTGNANYSGDMDENWRIDVKGDESHAELKLPNIKIKSTESVFQLYNRGTGCTLLSH 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 149386124 478 SDKLPNWGFEQNEVLCVDEPTIPNTLWYIEEN 509
Cdd:cd23286  161 DTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 52-288 6.68e-67

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: 221.03  E-value: 6.68e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124   52 SVLVRLYKLPFPTRVVFDEVHFGGFAKDYFAGEFFLDVHPPLVKLIYYWIAVLFGWNGQFTFEEIG-NLYDKDVPYVIMR 130
Cdd:pfam02366   7 AFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGgQYYPGNVPYFGMR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  131 LFPALCGIFTVVLTFLTLRLTNCRSFVALFGAFLVLIENSLVTQSRFILLDSPLLFFMSISIYGLMKQRVCQPFTKQWFK 210
Cdd:pfam02366  87 LFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPFSRKWWL 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149386124  211 SLLLAGMGLGMTVSTKLTGLYTIAWVGLLTIVELWDYLGDLNVTMRQWYTHFAARFVALVCVPVTIYLSVFYLHFLSL 288
Cdd:pfam02366 167 WLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLL 244
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 532-728 1.70e-61

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: 204.70  E-value: 1.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  532 SKLWEYSKAMVRINSTFKSEHVYSSRPESWPFVMRGISFYSNenenkltDEQGSHVYLLGNMAIYWIGFFIITLGMAKLF 611
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGW-------DDRNAQIYLLGNPVIWWSSTAAILVFVLLLL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  612 FYYLKHLNPFVITGETLSSSVFYQFCFEFILGWLLHYFPAFYMKRQLFMHHYLPALYFSILLIAQFIEYQIS-------- 683
Cdd:pfam16192  74 AYLLRWQRGYYDLSDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSlfrrlprs 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 149386124  684 KRRLTGYLLMVATAAMAGYCFWAFVPIIYGTDWTRAQCNHAKWFS 728
Cdd:pfam16192 154 LRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 319-509 1.47e-91

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: 283.94  E-value: 1.47e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHN-NLEEYLHSHDHNYPGGSQEQQVSLYGFSPDENNEWIIETKNKAREGQLQKNFKAVLDGDTIRLFHKQ 397
Cdd:cd23286    1 LLYGSTVTIRHLeSLGGYLHSHDLTYPSGSNEQQVTLYDFEDDANNEWIIETKTKEQMDKFPGQFREVRDGDVIRLRHVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 398 TGKYLHVNDIRPPISEHDYSNEVSCSGSRELLGDINYEFKVRIMNKKPHSQNNLPMIKLRATESIFQLVHHGTKCVMMSH 477
Cdd:cd23286   81 TGKLLRASNARPPVSEQEYNNEVSCTGNANYSGDMDENWRIDVKGDESHAELKLPNIKIKSTESVFQLYNRGTGCTLLSH 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 149386124 478 SDKLPNWGFEQNEVLCVDEPTIPNTLWYIEEN 509
Cdd:cd23286  161 DTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 52-288 6.68e-67

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: 221.03  E-value: 6.68e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124   52 SVLVRLYKLPFPTRVVFDEVHFGGFAKDYFAGEFFLDVHPPLVKLIYYWIAVLFGWNGQFTFEEIG-NLYDKDVPYVIMR 130
Cdd:pfam02366   7 AFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGgQYYPGNVPYFGMR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  131 LFPALCGIFTVVLTFLTLRLTNCRSFVALFGAFLVLIENSLVTQSRFILLDSPLLFFMSISIYGLMKQRVCQPFTKQWFK 210
Cdd:pfam02366  87 LFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPFSRKWWL 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149386124  211 SLLLAGMGLGMTVSTKLTGLYTIAWVGLLTIVELWDYLGDLNVTMRQWYTHFAARFVALVCVPVTIYLSVFYLHFLSL 288
Cdd:pfam02366 167 WLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLL 244
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 532-728 1.70e-61

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: 204.70  E-value: 1.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  532 SKLWEYSKAMVRINSTFKSEHVYSSRPESWPFVMRGISFYSNenenkltDEQGSHVYLLGNMAIYWIGFFIITLGMAKLF 611
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGW-------DDRNAQIYLLGNPVIWWSSTAAILVFVLLLL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  612 FYYLKHLNPFVITGETLSSSVFYQFCFEFILGWLLHYFPAFYMKRQLFMHHYLPALYFSILLIAQFIEYQIS-------- 683
Cdd:pfam16192  74 AYLLRWQRGYYDLSDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSlfrrlprs 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 149386124  684 KRRLTGYLLMVATAAMAGYCFWAFVPIIYGTDWTRAQCNHAKWFS 728
Cdd:pfam16192 154 LRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 45-287 1.60e-21

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 98.81  E-value: 1.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  45 IAVLLSASVLvRLYKLPFPTRVVFDEVHF---------GGFAKDYFAGEFFLDVHPPLVKliyYWIAV---LFGWNGQFT 112
Cdd:COG1928   26 LLVTLLAGVL-RFWGLGRPNTLVFDETYYvkdawslltNGYERNWPDPGPFFVVHPPLGK---WLIALgewLFGYVNPFG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 113 FeeignlydkdvpyvimRLFPALCGIFTVVLTF-LTLRLTNcRSFVALFGAFLVLIENSLVTQSRFILLDSPLLFFMSIS 191
Cdd:COG1928  102 W----------------RFAAALAGTLSVLLVArIARRLTR-STLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 192 IYGL------MKQRVCQPFTKQWFKS-----------LLLAGMGLGMTVSTKLTGLYTIAWVGLLTIveLWDYLGDLNVT 254
Cdd:COG1928  165 FGCLlldrdqVRRRLAAAVAAGRAPSrwgprlgfrwwRLAAGVLLGLACGVKWSGLYFLAAFGLLTV--AWDAGARRAAG 242

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 149386124 255 MRQWYTHFAAR-----FVALVCVPVTIYLSVFYLHFLS 287
Cdd:COG1928  243 VRRPWLGALLRdgipaFFALVIVPLLTYLASWTGWFAS 280
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 337-504 9.00e-21

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 90.50  E-value: 9.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  337 HSHDHNYPGGSQEQQ------VSLYGfSPDENNE----WIIETKNKAREgqlqkNFKAVLDGDTIRLFHKQTGKYLHVND 406
Cdd:pfam02815  13 HSHQDEYLTGSEQQQkqpflrITLYP-HGDANNSarslWRIEVVRHDAW-----RGGLIKWGSPFRLRHLTTGRYLHSHE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  407 I-RPPISE-HDYSNEVSCSGSRELLGDINyefKVRIMNKKPhsQNNLPMIKLRATESIFQLVHHGTKCVMMSHSDKLPNW 484
Cdd:pfam02815  87 EqKPPLVEkEDWQKEVSAYGFRGFPGDND---IVEIFEKKS--TTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW 161

                         170       180
                  ....*....|....*....|..
gi 149386124  485 GFE--QNEVLCVDEPTIPNTLW 504
Cdd:pfam02815 162 GFGpeQQKVTCAKEGHMDDALT 183
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 534-730 6.34e-15

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 78.01  E-value: 6.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 534 LWEYSKAMVRINSTFKSEHVYSSRPESWPFVMRGISFYSNENENKL----TDEQGSHVYLLGNMAIYWIGffiiTLGMAK 609
Cdd:COG1928  307 LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQTGTlgcgAGKCVRAVLAIGNPALWWLG----LPALLW 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 610 LFFYYLKHLNP---FVITGetlsssvfyqfcfeFILGWLlhyfPAF-YMKRQLFMHHYLPALYFSILLIAQFIE-----Y 680
Cdd:COG1928  383 LLWRWIARRDWragAVLVG--------------YAAGWL----PWFlYLDRTMFFFYAIPFVPFLVLALALVLGlilgpA 444

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 149386124 681 QISKRRLTGYLLMVATAAMAGYCFWAFVPIIYGTDWTRAQCNHAKWFSSW 730
Cdd:COG1928  445 RASERRRLGRLVVGLYVGLVVANFAFFYPILTGLPIPYDEWQARMWFPSW 494
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
321-369 6.91e-12

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 60.82  E-value: 6.91e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 149386124   321 YGSTVTIKHNNLEEYLHSHDHNYPG-GSQEQQVSLYGFS-PDENNEWIIET 369
Cdd:smart00472   6 WGDVVRLRHVTTGRYLHSHDEKLPPwGDGQQEVTGYGNPaIDANTLWLIEP 56
TIGR03663 TIGR03663
TIGR03663 family protein; Members of this protein family, uncommon and rather sporadically ...
 47-245 3.77e-03

TIGR03663 family protein; Members of this protein family, uncommon and rather sporadically distributed, are found almost always in the same genomes as members of family TIGR03662, and frequently as a nearby gene. Members show some N-terminal sequence similarity with pfam02366, dolichyl-phosphate-mannose-protein mannosyltransferase. The few invariant residues in this family, found toward the N-terminus, include a dipeptide DE, a tripeptide HGP, and two different Arg residues. Up to three members may be found in a genome. The function is unknown.


Pssm-ID: 274709  Cd Length: 439  Bit Score: 40.50  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124   47 VLLSASVLVRLYKLPFPTrVVFDEVHFGGFAKDY-FAGEFFLD--VHPPLvklIYYWIAVLFGWNGQFTFeeignlydkd 123
Cdd:TIGR03663   6 LIVLFALLLRLFELGLRV-FHHDEAIHASFILKLlETGVYSYDpaYHGPF---LYHITAAVFHLFGISDA---------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  124 vpyvIMRLFPALCGiftvVLTFLTLRL--TNCRSFVALFGAFLVLIENSLVTQSRFILLDSPLLFFMSISIYGLMKQRVc 201
Cdd:TIGR03663  72 ----TARLLPAVFG----VLLPLTAWLyrKRLGDNEVLWAAVLLAFSPVMVYYSRFMRNDIFVAFFTLLAVGAAFRYLD- 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 149386124  202 qpfTKQWFkSLLLAGMGLGMTVSTKLTG-LYTIAWVGLLTIVELW 245
Cdd:TIGR03663 143 ---TGKRR-YLFLAASALALAFTSKENAyLIILIFGGLLAIYLDW 183
 
Name Accession Description Interval E-value
beta-trefoil_MIR_PMT7-like cd23286
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 319-509 1.47e-91

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: 283.94  E-value: 1.47e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHN-NLEEYLHSHDHNYPGGSQEQQVSLYGFSPDENNEWIIETKNKAREGQLQKNFKAVLDGDTIRLFHKQ 397
Cdd:cd23286    1 LLYGSTVTIRHLeSLGGYLHSHDLTYPSGSNEQQVTLYDFEDDANNEWIIETKTKEQMDKFPGQFREVRDGDVIRLRHVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 398 TGKYLHVNDIRPPISEHDYSNEVSCSGSRELLGDINYEFKVRIMNKKPHSQNNLPMIKLRATESIFQLVHHGTKCVMMSH 477
Cdd:cd23286   81 TGKLLRASNARPPVSEQEYNNEVSCTGNANYSGDMDENWRIDVKGDESHAELKLPNIKIKSTESVFQLYNRGTGCTLLSH 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 149386124 478 SDKLPNWGFEQNEVLCVDEPTIPNTLWYIEEN 509
Cdd:cd23286  161 DTRLPDWAFHQQEVLCVNSPTIPNTLFYVESN 192
beta-trefoil_MIR_PMT1-like cd23283
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 319-511 3.89e-68

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: 222.17  E-value: 3.89e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHNNLEE-YLHSHDHNYPGGSQEQQVSLYGFsPDENNEWIIETKNkAREGQLQKNFKAVLDGDTIRLFHKQ 397
Cdd:cd23283    1 VAYGSTIRIRHLNTRGgYLHSHPHNYPAGSKQQQITLYPH-RDENNDWLVELAN-APEEWSPTTFENLKDGDVVRLEHVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 398 TGKYLHVNDIRPPISEHDYSNEVSCSGSRELLGDINYEFKVRIMNKK---PHSQNNlpmikLRATESIFQLVHHGTKCVM 474
Cdd:cd23283   79 TGRRLHSHDHRPPVSDNDWQNEVSAYGYEGFEGDANDDWRVEILKDDsrpGESKER-----VRAIDTKFRLVHVMTGCYL 153

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 149386124 475 MSHSDKLPNWGFEQNEVLCVDEPTIPNTLWYIEENSH 511
Cdd:cd23283  154 FSHGVKLPEWGFEQQEVTCAKSGLLELSLWYIETNEH 190
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
 52-288 6.68e-67

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: 221.03  E-value: 6.68e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124   52 SVLVRLYKLPFPTRVVFDEVHFGGFAKDYFAGEFFLDVHPPLVKLIYYWIAVLFGWNGQFTFEEIG-NLYDKDVPYVIMR 130
Cdd:pfam02366   7 AFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGgQYYPGNVPYFGMR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  131 LFPALCGIFTVVLTFLTLRLTNCRSFVALFGAFLVLIENSLVTQSRFILLDSPLLFFMSISIYGLMKQRVCQPFTKQWFK 210
Cdd:pfam02366  87 LFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPFSRKWWL 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149386124  211 SLLLAGMGLGMTVSTKLTGLYTIAWVGLLTIVELWDYLGDLNVTMRQWYTHFAARFVALVCVPVTIYLSVFYLHFLSL 288
Cdd:pfam02366 167 WLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLL 244
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
 532-728 1.70e-61

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: 204.70  E-value: 1.70e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  532 SKLWEYSKAMVRINSTFKSEHVYSSRPESWPFVMRGISFYSNenenkltDEQGSHVYLLGNMAIYWIGFFIITLGMAKLF 611
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGW-------DDRNAQIYLLGNPVIWWSSTAAILVFVLLLL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  612 FYYLKHLNPFVITGETLSSSVFYQFCFEFILGWLLHYFPAFYMKRQLFMHHYLPALYFSILLIAQFIEYQIS-------- 683
Cdd:pfam16192  74 AYLLRWQRGYYDLSDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSlfrrlprs 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 149386124  684 KRRLTGYLLMVATAAMAGYCFWAFVPIIYGTDWTRAQCNHAKWFS 728
Cdd:pfam16192 154 LRKRVGYAIVVVLLALVIYVFIYFSPLTYGMPGTSEECKKLKWLS 198
beta-trefoil_MIR_PMT cd23276
MIR domain, beta-trefoil fold, found in the family of dolichyl-phosphate-mannose-protein ...
 319-509 1.42e-51

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: 177.52  E-value: 1.42e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHNNLE-EYLHSHDHNYPGGSQEQQVSLYGFsPDENNEWIIEtKNKAREGQLQKNFKAVLDGDTIRLFHKQ 397
Cdd:cd23276    1 VAYGSQITLRNANSGgGYLHSHNHTYPDGSKQQQVTGYGH-KDENNWWQIL-KPRGDPSSNPPDPEYVRDGDEVRLLHKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 398 TGKYLHVNDIRPPISEHDYsnEVSCSGSRELLGDINYEFKVRIMNKKphsqNNLPMIKLRATESIFQLVHHGTKCVMMSH 477
Cdd:cd23276   79 TNRYLRTHDAAAPVTSKHK--EVSAYPDENEDGDDNDLWVVEIVKDE----GKLEDKRIKPLTTRFRLRNKKTGCYLTSS 152

                        170       180       190
                 ....*....|....*....|....*....|...
gi 149386124 478 SDKLPNWGFEQNEVLCVDEPT-IPNTLWYIEEN 509
Cdd:cd23276  153 GVKLPEWGFRQGEVVCSKNKEsDPSTLWNVEEN 185
beta-trefoil_MIR_PMT2-like cd23284
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 316-511 5.34e-50

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: 173.27  E-value: 5.34e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 316 PVEVSYGSTVTIK-HNNLEEYLHSHDHNYPGGSQEQQVSLYGFSpDENNEWIIEtknKAREGQLQKN----FKAVLDGDT 390
Cdd:cd23284    1 PLDVAYGSKVTIKnQGLGGGLLHSHVQTYPEGSNQQQVTCYGHK-DSNNEWIFE---RPRGLPSWDEndtdIEFIKDGDI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 391 IRLFHKQTGKYLHVNDIRPPISEHDYsnEVSCSGSRElLGDINYEFKVRIMNKKPHSQNNlpmiKLRATESIFQLVHHGT 470
Cdd:cd23284   77 VRLVHKQTGRNLHSHPVPAPISKSDY--EVSGYGDLT-VGDEKDNWVIEIVKQVGSEDPK----KLHTLTTSFRLRHEVL 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 149386124 471 KCVMMSHSDKLPNWGFEQNEVLCVDEPTI--PNTLWYIEENSH 511
Cdd:cd23284  150 GCYLAQTGVSLPEWGFKQGEVVCDKSNFKrdKRTWWNIETHTN 192
beta-trefoil_MIR_POMT2 cd23282
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 2 (POMT2) and similar ...
 319-511 1.63e-39

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: 143.98  E-value: 1.63e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHNNLE-EYLHSHDHNYPGG--SQEQQVSLYgFSPDENNEWIIETKNkaREGQLQKNFKAVLDGDTIRLFH 395
Cdd:cd23282    1 VAYGSVITLKNHRTGgGYLHSHWHLYPEGvgARQQQVTTY-SHKDDNNLWLIKKHN--QSSDLSDPVEYVRHGDLIRLEH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 396 KQTGKYLHVNDIRPPISEHDYsnEVSCSGSRELlGDINYEFKVRIMNKKPHSqnnlpmiKLRATESIFQLVHHGTKCVMM 475
Cdd:cd23282   78 VNTKRNLHSHKEKAPLTKKHY--QVTGYGENGT-GDANDVWRVEVVGGREGD-------PVKTVRSKFRLVHYNTGCALH 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 149386124 476 SHSDKLPNWGFEQNEVLCvdEPTI--PNTLWYIEENSH 511
Cdd:cd23282  148 SHGKQLPKWGWEQLEVTC--NPNVrdKNSLWNVEDNRN 183
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 322-509 6.69e-32

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: 122.11  E-value: 6.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 322 GSTVTIKHNNLEEYLHSHDHNYPGGSQEQQVSLYGFSP--DENNEWIIETKNkaregqlQKNFKAVLDGDTIRLFHKQTG 399
Cdd:cd23263    1 GDVIWLKHSETGKYLHSHRKNYPTGSGQQEVTFESSSRkgDTNGLWIIESEN-------GKQGGPVKWGDKIRLRHLSTG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 400 KYLHV-NDIRPPISEHdysNEVSCSGSRellGDINYEFKVRIMNKKPHSQNNLPmiklraTESIFQLVHHGTKCVMMSHS 478
Cdd:cd23263   74 KYLSSeEGKKSPKSNH---QEVLCLTDN---PDKSSLFKFEPIGSTKYKQKYVK------KDSYFRLKHVNTNFWLHSHE 141

                        170       180       190
                 ....*....|....*....|....*....|.
gi 149386124 479 DKLPNWGFEQNEVLCVDEPTIPNTLWYIEEN 509
Cdd:cd23263  142 KKFNINNKTQQEVICHGEREEVFKLWKAELI 172
beta-trefoil_MIR_PMT4-like cd23285
MIR domain, beta-trefoil fold, found in Saccharomyces cerevisiae ...
 319-508 1.99e-31

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: 121.25  E-value: 1.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHNNLEEYLHSHDHNYP-----G--GSQEQQVSLYGFsPDENNEWIIE-TKNKAregQLQKNFKAVLDGDT 390
Cdd:cd23285    1 VHYGDVITIKHRDTNAFLHSHPERYPlryedGriSSQGQQVTGYPH-KDANNQWQILpTDPID---EHEGTGRPVRNGDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 391 IRLFHKQTGKYLHVNDIRPPIseHDYSNEVSCSGSRELLGDINY-EFKVRIMNKKPHSqnnlpmiKLRATESIFQLVHHG 469
Cdd:cd23285   77 IRLRHVSTDTYLLTHDVASPL--TPTNMEFTTVSDDDTDERYNEtLFRVEIEDTDEGD-------VLKTKSSHFRLIHVD 147

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 149386124 470 TKCVMMSHSDKLPNWGFEQNEVLCVDEPTIPNTLWYIEE 508
Cdd:cd23285  148 TNVALWTHKKPLPDWGFGQQEVNGNKNIKDKSNIWVVDD 186
beta-trefoil_MIR_POMT1 cd23281
MIR domain, beta-trefoil fold, found in protein O-mannosyl-transferase 1 (POMT1) and similar ...
 319-511 7.74e-29

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: 113.94  E-value: 7.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHNNLEE-YLHSHDHNYP-------GGSQEQQVSLYGFSpDENNEWIIetKNKAREGQLQKN-FKAVLDGD 389
Cdd:cd23281    1 VAYGSQVTLRNTHGSPcWLHSHKHRYPikypdgrGSSHQQQVTCYPFK-DVNNWWII--KDPGRQDLAVDDpPRPVRHGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 390 TIRLFHKQTGKYLHVNDIRPPISEHdySNEVSCSgsrellgdINYE--------FKVRIMNKkphsqnNLPMIKLRATES 461
Cdd:cd23281   78 IIQLVHGKTGRFLNSHDVAAPLSPT--HQEVSCY--------IDYNismpaqnlWRIEIVNR------DSEGDTWKAIKS 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 149386124 462 IFQLVHHGTKCVMMSHSDKLPNWGFEQNEVLCVDEPTIPNTLWYIEENSH 511
Cdd:cd23281  142 QFRLIHVNTSAALKLSGKQLPDWGFGQLEVATDRAGNQSSTVWNVEEHRY 191
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 45-287 1.60e-21

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 98.81  E-value: 1.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  45 IAVLLSASVLvRLYKLPFPTRVVFDEVHF---------GGFAKDYFAGEFFLDVHPPLVKliyYWIAV---LFGWNGQFT 112
Cdd:COG1928   26 LLVTLLAGVL-RFWGLGRPNTLVFDETYYvkdawslltNGYERNWPDPGPFFVVHPPLGK---WLIALgewLFGYVNPFG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 113 FeeignlydkdvpyvimRLFPALCGIFTVVLTF-LTLRLTNcRSFVALFGAFLVLIENSLVTQSRFILLDSPLLFFMSIS 191
Cdd:COG1928  102 W----------------RFAAALAGTLSVLLVArIARRLTR-STLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 192 IYGL------MKQRVCQPFTKQWFKS-----------LLLAGMGLGMTVSTKLTGLYTIAWVGLLTIveLWDYLGDLNVT 254
Cdd:COG1928  165 FGCLlldrdqVRRRLAAAVAAGRAPSrwgprlgfrwwRLAAGVLLGLACGVKWSGLYFLAAFGLLTV--AWDAGARRAAG 242

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 149386124 255 MRQWYTHFAAR-----FVALVCVPVTIYLSVFYLHFLS 287
Cdd:COG1928  243 VRRPWLGALLRdgipaFFALVIVPLLTYLASWTGWFAS 280
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 337-504 9.00e-21

MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.


Pssm-ID: 397103 [Multi-domain]  Cd Length: 185  Bit Score: 90.50  E-value: 9.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  337 HSHDHNYPGGSQEQQ------VSLYGfSPDENNE----WIIETKNKAREgqlqkNFKAVLDGDTIRLFHKQTGKYLHVND 406
Cdd:pfam02815  13 HSHQDEYLTGSEQQQkqpflrITLYP-HGDANNSarslWRIEVVRHDAW-----RGGLIKWGSPFRLRHLTTGRYLHSHE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  407 I-RPPISE-HDYSNEVSCSGSRELLGDINyefKVRIMNKKPhsQNNLPMIKLRATESIFQLVHHGTKCVMMSHSDKLPNW 484
Cdd:pfam02815  87 EqKPPLVEkEDWQKEVSAYGFRGFPGDND---IVEIFEKKS--TTGMGSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW 161

                         170       180
                  ....*....|....*....|..
gi 149386124  485 GFE--QNEVLCVDEPTIPNTLW 504
Cdd:pfam02815 162 GFGpeQQKVTCAKEGHMDDALT 183
beta-trefoil_MIR_SDF2-like cd23279
MIR domain, beta-trefoil fold, found in family of stromal cell-derived factor 2 (SDF-2); The ...
 321-508 1.13e-19

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: 86.97  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 321 YGSTVTIKHNNLEEYLHSHDHNYPGGSQEQQVSLYGFSPDENNEWIIETKNKAREgqlQKNFKAVLDGDTIRLFHKQTGK 400
Cdd:cd23279    1 YGSAIKLKHVNSGYRLHSHEVSYGSGSGQQSVTAVPSADDANSLWTVLPGLGEPC---QEQGKPVKCGDIIRLQHVNTRK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 401 YLHVNDIRPPISehdySN-EVSCSGSREllGDINYEFKVRIMNKKphsqnnlpmIKLRATESIFQLVHHGTK---CVMMS 476
Cdd:cd23279   78 NLHSHNHSSPLS----GNqEVSAFGGGD--EDSGDNWIVECEGKK---------AKFWKRGEPVRLKHVDTGkylSASKT 142

                        170       180       190
                 ....*....|....*....|....*....|...
gi 149386124 477 HS-DKLPNWGfeQNEVLCVDEPTiPNTLWYIEE 508
Cdd:cd23279  143 HKfTQQPIAG--QLEVSAASSKD-SDSQWKAVE 172
beta-trefoil_MIR_AtSDF2-like cd23294
MIR domain, beta-trefoil fold, found in Arabidopsis thaliana stromal cell-derived factor ...
 319-508 1.05e-18

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: 84.35  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHNNLEEYLHSHDHNYPGGSQEQQVSLYGFSPDENNEWIIETKNKAREGQlqknFKAVLDGDTIRLFHKQT 398
Cdd:cd23294    1 VTCGSVIKLQHERTKFRLHSHEVPYGSGSGQQSVTGFPGVDDSNSYWIVKPANGERCKQ----GDVIKNGDVIRLQHVST 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 399 GKYLHVNDIRPPISEhdySNEVSCSGSrELLGDINYEFKVRIMNKKPHSQNNLPmIKLRatesifqlvHHGTKCVMMSHS 478
Cdd:cd23294   77 RKWLHSHLHASPLSG---NQEVSCFGG-DGNSDTGDNWIVEIEGGGKVWERDQK-VRLK---------HVDTGGYLHSHD 142

                        170       180       190
                 ....*....|....*....|....*....|..
gi 149386124 479 DKL--PNWGfeQNEVLCVDEPTiPNTLWYIEE 508
Cdd:cd23294  143 KKYgrPIPG--QQEVCAVASKN-SNTLWLAAE 171
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
 534-730 6.34e-15

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 78.01  E-value: 6.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 534 LWEYSKAMVRINSTFKSEHVYSSRPESWPFVMRGISFYSNENENKL----TDEQGSHVYLLGNMAIYWIGffiiTLGMAK 609
Cdd:COG1928  307 LWHYHQQILSFHTGLSSPHPYESKPWSWPLMLRPVSYYYETGQTGTlgcgAGKCVRAVLAIGNPALWWLG----LPALLW 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 610 LFFYYLKHLNP---FVITGetlsssvfyqfcfeFILGWLlhyfPAF-YMKRQLFMHHYLPALYFSILLIAQFIE-----Y 680
Cdd:COG1928  383 LLWRWIARRDWragAVLVG--------------YAAGWL----PWFlYLDRTMFFFYAIPFVPFLVLALALVLGlilgpA 444

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 149386124 681 QISKRRLTGYLLMVATAAMAGYCFWAFVPIIYGTDWTRAQCNHAKWFSSW 730
Cdd:COG1928  445 RASERRRLGRLVVGLYVGLVVANFAFFYPILTGLPIPYDEWQARMWFPSW 494
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
321-369 6.91e-12

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 60.82  E-value: 6.91e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 149386124   321 YGSTVTIKHNNLEEYLHSHDHNYPG-GSQEQQVSLYGFS-PDENNEWIIET 369
Cdd:smart00472   6 WGDVVRLRHVTTGRYLHSHDEKLPPwGDGQQEVTGYGNPaIDANTLWLIEP 56
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 319-424 1.04e-11

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: 63.83  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHNNLEEYLHSHDHNYPGGSQEQQVSLYGFSPDENNEWIIetknKAREGQLQKNFKAVLDGDTIRLFHKQT 398
Cdd:cd23293    1 VTCGSVVKLLNTRHNVRLHSHDVKYGSGSGQQSVTGVESSDDSNSYWQI----RGPTGADCERGTPIKCGQTIRLTHLNT 76

                         90       100
                 ....*....|....*....|....*.
gi 149386124 399 GKYLHVNDIRPPISEHdysNEVSCSG 424
Cdd:cd23293   77 GKNLHSHHFQSPLSGN---QEVSAFG 99
beta-trefoil_MIR cd23263
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ...
 319-438 1.44e-11

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


Pssm-ID: 467746 [Multi-domain]  Cd Length: 172  Bit Score: 63.56  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 319 VSYGSTVTIKHNNLEEYLHSHDHNYPGGSQEQQVSLYGFSPDENNEWIIE--TKNKAREGQLQKNfkavldgDTIRLFHK 396
Cdd:cd23263   59 VKWGDKIRLRHLSTGKYLSSEEGKKSPKSNHQEVLCLTDNPDKSSLFKFEpiGSTKYKQKYVKKD-------SYFRLKHV 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 149386124 397 QTGKYLHVNDIrPPISEHDYSNEVSCSGSREllgDINYEFKV 438
Cdd:cd23263  132 NTNFWLHSHEK-KFNINNKTQQEVICHGERE---EVFKLWKA 169
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
 38-239 1.70e-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: 62.72  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  38 TKFDHFLIAVLLSASVLVRLYKLPFPTRVVFDEVHFGGFAKD----------YFAGEFFLDvHPPLvkliYYWIAVLFGW 107
Cdd:COG1807    3 KTLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREmlesgdwltpTLAGEPYFD-KPPL----IYWLIALSYK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 108 NgqFTFEEIGnlydkdvpyviMRLFPALCGIFTVVLTFLTLR-LTNCRsfVALFGAFLVLIENSLVTQSRFILLDSPLLF 186
Cdd:COG1807   78 L--FGVSEFA-----------ARLPSALLGLLTVLLVYLLARrLFGRR--AALLAALLLLTSPLLLLFGRLATPDALLLL 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 149386124 187 FMSISIYGLMKQrvcqpFTKQWFKSLLLAGMGLGMTVSTKLTGLYTIAWVGLL 239
Cdd:COG1807  143 FWTLALYALLRA-----LERRRLRWLLLAGLALGLGFLTKGPVALLLPGLALL 190
beta-trefoil_MIR_SDF2_meta cd23293
MIR domain, beta-trefoil fold, found in family of metazoan stromal cell-derived factor 2 ...
 292-404 8.69e-07

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: 49.58  E-value: 8.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 292 GSGSGAMSpifkSTLLDSDFLTN----------------EPVEVsyGSTVTIKHNNLEEYLHSHDHNYPGgSQEQQVSLY 355
Cdd:cd23293   26 GSGSGQQS----VTGVESSDDSNsywqirgptgadcergTPIKC--GQTIRLTHLNTGKNLHSHHFQSPL-SGNQEVSAF 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149386124 356 GfspdENNEwiietknkareGQLQKNFKAVLDG------DTIRLFHKQTGKYLHV 404
Cdd:cd23293   99 G----EDGE-----------GDTGDNWTVVCSGtywerdEAVRLKHVDTEVYLHV 138
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
461-509 2.44e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 45.02  E-value: 2.44e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 149386124   461 SIFQLVHHGTKCVMMSHSDKLPNWGFEQNEVLCVDEPTI-PNTLWYIEEN 509
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
384-425 5.15e-06

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 44.25  E-value: 5.15e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 149386124   384 AVLDGDTIRLFHKQTGKYLHVNDIRPPISEhDYSNEVSCSGS 425
Cdd:smart00472   3 FVRWGDVVRLRHVTTGRYLHSHDEKLPPWG-DGQQEVTGYGN 43
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
 89-277 3.10e-05

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: 44.95  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124   89 VHPPLVKLIYYWIAVLFGWNGqftfeeignlydkdvpyVIMRLFPALCGIFTVVLTFLTLRltncRSF---VALFGAFLV 165
Cdd:pfam13231   1 DHPPLAAWLIALFTALFGDSE-----------------WAVRLPSALAGVLTILLLYLLAR----RLFgkrAALLAALLL 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  166 LIENSLVTQSRFILLDSPLLFFMSISIYGLMkqRVCQpftKQWFKSLLLAGMGLGMTVSTKltglYTIAWVGL-LTIVEL 244
Cdd:pfam13231  60 AVVPLFVALSRLFTPDAPLLLFWALALYFLL--RALE---KGRLKWWLLAGAAAGLGFLSK----YTAALLVLaALLYLL 130

                         170       180       190
                  ....*....|....*....|....*....|...
gi 149386124  245 WDYLGDLNVTMRQWYthfAARFVALVCVPVTIY 277
Cdd:pfam13231 131 ISPGRRRLKSPKPYL---GLLLALLLFSPVLIW 160
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
 44-242 2.69e-04

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


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 44.27  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  44 LIAVLLSASVLVRLYKLPFptRVV-FDEVHFGGFAKDYFA-GEFFLD--VHPPLvklIYYWIAVLFGWNGQ--FTfeeig 117
Cdd:COG4745   18 AVLAITALALLLRLVGLGA--RPFhWDEARVAYWSLRLLEtGAYEYRpiYHGPF---LYHVTAALFGLFGAsdFT----- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 118 nlydkdvpyviMRLFPALCGIFTVVLTFLtLRlTNCRSFVALFGAFLVLIENSLVTQSRFILLDSPLLFFMSISIYGLMK 197
Cdd:COG4745   88 -----------ARLPVALVGGLLPLLALL-LR-ERLGDAEVLALALLLAFSPVLVYYSRFMRNDVLLAAFTLLALGAAVR 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 149386124 198 QRVcqpfTKQWfKSLLLAGMGLGMTVSTKLTG-LYTIAWVGLLTIV 242
Cdd:COG4745  155 AID----TRRR-RYLYLAAVALALAFATKENAvLYLLCWLGALLLL 195
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
 319-403 1.60e-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: 40.04  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  319 VSYGSTVTIKHNNLEEYLHSHDHN----YPGGSQEQQVSLYGF-SPDENNEWIIETKNKAREGQLQKNFKAvldGDTI-R 392
Cdd:pfam02815  65 IKWGSPFRLRHLTTGRYLHSHEEQkpplVEKEDWQKEVSAYGFrGFPGDNDIVEIFEKKSTTGMGSDRIKP---GDSYfR 141

                          90
                  ....*....|.
gi 149386124  393 LFHKQTGKYLH 403
Cdd:pfam02815 142 LQHVCTGCWLF 152
TIGR03663 TIGR03663
TIGR03663 family protein; Members of this protein family, uncommon and rather sporadically ...
 47-245 3.77e-03

TIGR03663 family protein; Members of this protein family, uncommon and rather sporadically distributed, are found almost always in the same genomes as members of family TIGR03662, and frequently as a nearby gene. Members show some N-terminal sequence similarity with pfam02366, dolichyl-phosphate-mannose-protein mannosyltransferase. The few invariant residues in this family, found toward the N-terminus, include a dipeptide DE, a tripeptide HGP, and two different Arg residues. Up to three members may be found in a genome. The function is unknown.


Pssm-ID: 274709  Cd Length: 439  Bit Score: 40.50  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124   47 VLLSASVLVRLYKLPFPTrVVFDEVHFGGFAKDY-FAGEFFLD--VHPPLvklIYYWIAVLFGWNGQFTFeeignlydkd 123
Cdd:TIGR03663   6 LIVLFALLLRLFELGLRV-FHHDEAIHASFILKLlETGVYSYDpaYHGPF---LYHITAAVFHLFGISDA---------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  124 vpyvIMRLFPALCGiftvVLTFLTLRL--TNCRSFVALFGAFLVLIENSLVTQSRFILLDSPLLFFMSISIYGLMKQRVc 201
Cdd:TIGR03663  72 ----TARLLPAVFG----VLLPLTAWLyrKRLGDNEVLWAAVLLAFSPVMVYYSRFMRNDIFVAFFTLLAVGAAFRYLD- 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 149386124  202 qpfTKQWFkSLLLAGMGLGMTVSTKLTG-LYTIAWVGLLTIVELW 245
Cdd:TIGR03663 143 ---TGKRR-YLFLAASALALAFTSKENAyLIILIFGGLLAIYLDW 183
Stt3 COG1287
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
 31-242 5.05e-03

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


Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 40.16  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  31 RISGTVLTKFDHFLIAVLLSA----SVLVRLYklPFPTRVVFDEVHFGGF-----------AKDYFAGEFFLDVH----- 90
Cdd:COG1287    2 SEKTSVLDKLKRLLHLPALLLilalALWIRLL--PYDNVFRDGGVYLGGNdpwyhlrqieyILANGPSTLPFDPLtwypw 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124  91 -------PPLVKLIYYWIAVLFGWnGQFTFEEIgnlydkdvpYVIMRLFPALCGIFTVVLTFLTLR-LTNcrSFVALFGA 162
Cdd:COG1287   80 grdigqfGPLFDQLIALLALILGL-GSPSQSSV---------YTVAAWFPPIFGALTVIPVYLLGRrLGG--RKAGLLAA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149386124 163 FLVLIENSLVTQSRFILLD--SPLLFFMSISIYGLMK--------QRVCQPFTKQWFKSlLLAGMGLgmtvstkltGLYT 232
Cdd:COG1287  148 LLLALSPGQLSRSLLGFADhhVAELFFSTLAVLFLVLalkrakreKRDLEALKRPLLYA-VLAGVAL---------GLYL 217

                        250
                 ....*....|
gi 149386124 233 IAWVGLLTIV 242
Cdd:COG1287  218 LTWGGYVLFV 227
 
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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