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Conserved domains on  [gi|344303540|gb|EGW33789|]
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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
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
3-689 1.33e-172

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


:

Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 510.11  E-value: 1.33e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540   3 LITLAIVIRLYKIYLPPRVVFDEVHFGTFARDYYRGEFFMDVHPPLGKLTYYWVSVLFGWNGEFTFEEIGKQ-FDDNVPY 81
Cdd:COG1928   30 LTVLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFDVHPPLGKMLIALVGGLEGYDPPFDFQLIGLTeYPFGYNY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  82 VAMRMVSGVAGVLTVLFTYLTVR-LNCRSSVAWFTAVLLMIENSQVTQSRLILLDTPLICAQSLAIYQFKKFSQTPvAFS 160
Cdd:COG1928  110 VGMRFFNALLGSLTVPLVYLIARrIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLRFHRQQ-PFS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 161 GTWFRSLLITGISLGIAMSIKLTGLYTMGWVGILTIFQLWTILGDLNVSTRQWIMHFFSRVVCLIIVPTTIYLAAFYIHF 240
Cdd:COG1928  189 RRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHF 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 241 VALPFNGSGSGSVSSHFRSTLNDTDFTDMPVEVHYG-STVTIKHLNVER-YLHSHDHNYPTGSNEQQVTLYGYDyDDNND 318
Cdd:COG1928  269 NILTDSGPGDSFMPSLFQATLKGNPVYLNSRDPAYGsSTITIRHAGTGGgYLHSHNQLYPEGSEQQQVTGYGHK-DANNE 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 319 WMIESQnkfNERLFQKGPVKDGDTIRLYHRSTGKYLHVNDVRPPLSEHEYanEVSCDGDrNLLGDINYEFTVRIVSKKPH 398
Cdd:COG1928  348 WLIELS---DENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQY--EVSGYGD-SFEGDEKDDWIIEIVKDEAN 421
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 399 SKNDlpliKLRATESIFQLIHRGTKCVVMSHEAKLPKWGMGYNEVLCVDQpTIPNTLWYIESNSNPKFNETEndfaKIEF 478
Cdd:COG1928  422 EDQE----RIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKD-RDPSTTWNIEENVNDRLPNPE----KKVY 492
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 479 TPFTFWNKVWEYHKIMFKLNKSMTDDHVYASEPSTWPFVLRGVAYYGNeslehltDENGSVIYMLGNVAIYYAGSIFILI 558
Cdd:COG1928  493 KKLSFWKKFIELNKAMFSSNNALVPDHDYSSEPYQWPTLLRGLRFWGW-------GECIKKVYLMGNPALWWFSVPALAF 565
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 559 SIIRYVFYLF-WYLNPFIIPKESKEH---SIFYtnirdSILGWILNYFPAFAMSRKLFLHHYFPALYFAILIIGQYVD-- 632
Cdd:COG1928  566 FTGIVIWRLIrWRRGYRTLSDPAIRNfhwGYFY-----FLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDfi 640
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 344303540 633 --YQITRRKYFGFALLLAVLAGGLYCYVHFVPIIYGLEWTLQECNHSKWLPTWDINCMT 689
Cdd:COG1928  641 lrRPSRERRTLGLIVVAIFVALVIYFFFWFSPVTYGLPLSPQEFRRLMWLPSWDFHCNK 699
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
3-689 1.33e-172

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 510.11  E-value: 1.33e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540   3 LITLAIVIRLYKIYLPPRVVFDEVHFGTFARDYYRGEFFMDVHPPLGKLTYYWVSVLFGWNGEFTFEEIGKQ-FDDNVPY 81
Cdd:COG1928   30 LTVLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFDVHPPLGKMLIALVGGLEGYDPPFDFQLIGLTeYPFGYNY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  82 VAMRMVSGVAGVLTVLFTYLTVR-LNCRSSVAWFTAVLLMIENSQVTQSRLILLDTPLICAQSLAIYQFKKFSQTPvAFS 160
Cdd:COG1928  110 VGMRFFNALLGSLTVPLVYLIARrIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLRFHRQQ-PFS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 161 GTWFRSLLITGISLGIAMSIKLTGLYTMGWVGILTIFQLWTILGDLNVSTRQWIMHFFSRVVCLIIVPTTIYLAAFYIHF 240
Cdd:COG1928  189 RRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHF 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 241 VALPFNGSGSGSVSSHFRSTLNDTDFTDMPVEVHYG-STVTIKHLNVER-YLHSHDHNYPTGSNEQQVTLYGYDyDDNND 318
Cdd:COG1928  269 NILTDSGPGDSFMPSLFQATLKGNPVYLNSRDPAYGsSTITIRHAGTGGgYLHSHNQLYPEGSEQQQVTGYGHK-DANNE 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 319 WMIESQnkfNERLFQKGPVKDGDTIRLYHRSTGKYLHVNDVRPPLSEHEYanEVSCDGDrNLLGDINYEFTVRIVSKKPH 398
Cdd:COG1928  348 WLIELS---DENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQY--EVSGYGD-SFEGDEKDDWIIEIVKDEAN 421
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 399 SKNDlpliKLRATESIFQLIHRGTKCVVMSHEAKLPKWGMGYNEVLCVDQpTIPNTLWYIESNSNPKFNETEndfaKIEF 478
Cdd:COG1928  422 EDQE----RIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKD-RDPSTTWNIEENVNDRLPNPE----KKVY 492
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 479 TPFTFWNKVWEYHKIMFKLNKSMTDDHVYASEPSTWPFVLRGVAYYGNeslehltDENGSVIYMLGNVAIYYAGSIFILI 558
Cdd:COG1928  493 KKLSFWKKFIELNKAMFSSNNALVPDHDYSSEPYQWPTLLRGLRFWGW-------GECIKKVYLMGNPALWWFSVPALAF 565
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 559 SIIRYVFYLF-WYLNPFIIPKESKEH---SIFYtnirdSILGWILNYFPAFAMSRKLFLHHYFPALYFAILIIGQYVD-- 632
Cdd:COG1928  566 FTGIVIWRLIrWRRGYRTLSDPAIRNfhwGYFY-----FLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDfi 640
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 344303540 633 --YQITRRKYFGFALLLAVLAGGLYCYVHFVPIIYGLEWTLQECNHSKWLPTWDINCMT 689
Cdd:COG1928  641 lrRPSRERRTLGLIVVAIFVALVIYFFFWFSPVTYGLPLSPQEFRRLMWLPSWDFHCNK 699
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
1-243 2.87e-64

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 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 undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 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: 212.94  E-value: 2.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540    1 MSLITLAIVIRLYKIYLPPRVVFDEVHFGTFARDYYRGEFFMDVHPPLGKLTYYWVSVLFGWNGEFTFEEIGKQ-FDDNV 79
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQyYPGNV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540   80 PYVAMRMVSGVAGVLTVLFTYLTVR-LNCRSSVAWFTAVLLMIENSQVTQSRLILLDTPLICAQSLAIYQFKKFsQTPVA 158
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKrLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKF-ERKAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  159 FSGTWFRSLLITGISLGIAMSIKLTGLYTMGWVGILTIFQLWTILGDLNVSTRQWIMHFFSRVVCLIIVPTTIYLAAFYI 238
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYV 239

                  ....*
gi 344303540  239 HFVAL 243
Cdd:pfam02366 240 HFWLL 244
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
273-322 7.63e-13

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 63.51  E-value: 7.63e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 344303540   273 VHYGSTVTIKHLNVERYLHSHDHNYP-TGSNEQQVTLYGY-DYDDNNDWMIE 322
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLPpWGDGQQEVTGYGNpAIDANTLWLIE 55
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
3-689 1.33e-172

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 510.11  E-value: 1.33e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540   3 LITLAIVIRLYKIYLPPRVVFDEVHFGTFARDYYRGEFFMDVHPPLGKLTYYWVSVLFGWNGEFTFEEIGKQ-FDDNVPY 81
Cdd:COG1928   30 LTVLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFDVHPPLGKMLIALVGGLEGYDPPFDFQLIGLTeYPFGYNY 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  82 VAMRMVSGVAGVLTVLFTYLTVR-LNCRSSVAWFTAVLLMIENSQVTQSRLILLDTPLICAQSLAIYQFKKFSQTPvAFS 160
Cdd:COG1928  110 VGMRFFNALLGSLTVPLVYLIARrIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLRFHRQQ-PFS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 161 GTWFRSLLITGISLGIAMSIKLTGLYTMGWVGILTIFQLWTILGDLNVSTRQWIMHFFSRVVCLIIVPTTIYLAAFYIHF 240
Cdd:COG1928  189 RRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHF 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 241 VALPFNGSGSGSVSSHFRSTLNDTDFTDMPVEVHYG-STVTIKHLNVER-YLHSHDHNYPTGSNEQQVTLYGYDyDDNND 318
Cdd:COG1928  269 NILTDSGPGDSFMPSLFQATLKGNPVYLNSRDPAYGsSTITIRHAGTGGgYLHSHNQLYPEGSEQQQVTGYGHK-DANNE 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 319 WMIESQnkfNERLFQKGPVKDGDTIRLYHRSTGKYLHVNDVRPPLSEHEYanEVSCDGDrNLLGDINYEFTVRIVSKKPH 398
Cdd:COG1928  348 WLIELS---DENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQY--EVSGYGD-SFEGDEKDDWIIEIVKDEAN 421
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 399 SKNDlpliKLRATESIFQLIHRGTKCVVMSHEAKLPKWGMGYNEVLCVDQpTIPNTLWYIESNSNPKFNETEndfaKIEF 478
Cdd:COG1928  422 EDQE----RIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKD-RDPSTTWNIEENVNDRLPNPE----KKVY 492
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 479 TPFTFWNKVWEYHKIMFKLNKSMTDDHVYASEPSTWPFVLRGVAYYGNeslehltDENGSVIYMLGNVAIYYAGSIFILI 558
Cdd:COG1928  493 KKLSFWKKFIELNKAMFSSNNALVPDHDYSSEPYQWPTLLRGLRFWGW-------GECIKKVYLMGNPALWWFSVPALAF 565
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540 559 SIIRYVFYLF-WYLNPFIIPKESKEH---SIFYtnirdSILGWILNYFPAFAMSRKLFLHHYFPALYFAILIIGQYVD-- 632
Cdd:COG1928  566 FTGIVIWRLIrWRRGYRTLSDPAIRNfhwGYFY-----FLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDfi 640
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 344303540 633 --YQITRRKYFGFALLLAVLAGGLYCYVHFVPIIYGLEWTLQECNHSKWLPTWDINCMT 689
Cdd:COG1928  641 lrRPSRERRTLGLIVVAIFVALVIYFFFWFSPVTYGLPLSPQEFRRLMWLPSWDFHCNK 699
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
1-243 2.87e-64

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 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 undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 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: 212.94  E-value: 2.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540    1 MSLITLAIVIRLYKIYLPPRVVFDEVHFGTFARDYYRGEFFMDVHPPLGKLTYYWVSVLFGWNGEFTFEEIGKQ-FDDNV 79
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQyYPGNV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540   80 PYVAMRMVSGVAGVLTVLFTYLTVR-LNCRSSVAWFTAVLLMIENSQVTQSRLILLDTPLICAQSLAIYQFKKFsQTPVA 158
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKrLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKF-ERKAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  159 FSGTWFRSLLITGISLGIAMSIKLTGLYTMGWVGILTIFQLWTILGDLNVSTRQWIMHFFSRVVCLIIVPTTIYLAAFYI 238
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYV 239

                  ....*
gi 344303540  239 HFVAL 243
Cdd:pfam02366 240 HFWLL 244
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
486-681 3.26e-57

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: 406576  Cd Length: 198  Bit Score: 192.37  E-value: 3.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  486 KVWEYHKIMFKLNKSMTDDHVYASEPSTWPFVLRGVAYYGNeslehltDENGSVIYMLGNVAIYYAGSIFILISIIRYVF 565
Cdd:pfam16192   2 KFIELQKAMLTSNNGLTPSHPYASRPWEWPLLLRGIRFWGW-------DDRNAQIYLLGNPVIWWSSTAAILVFVLLLLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  566 YLFWYLNPFIIPKESKEHSIFYTNIRDSILGWILNYFPAFAMSRKLFLHHYFPALYFAILIIGQYVDYQITRRKYFGFAL 645
Cdd:pfam16192  75 YLLRWQRGYYDLSDDDTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFKRLPRSL 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 344303540  646 LLAVLAGGL--------YCYVHFVPIIYGLEWTLQECNHSKWLP 681
Cdd:pfam16192 155 RKRVGYAIVvvllalviYVFIYFSPLTYGMPGTSEECKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
282-456 7.55e-25

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: 102.06  E-value: 7.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  282 KHLNVERYLHSHDHNYPTGSNEQQ------VTLYGYDyDDNND----WMIESQNKfneRLFQKGPVKDGDTIRLYHRSTG 351
Cdd:pfam02815   4 KGGDVVRLFHSHQDEYLTGSEQQQkqpflrITLYPHG-DANNSarslWRIEVVRH---DAWRGGLIKWGSPFRLRHLTTG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  352 KYLHVNDV-RPPLSEHE-YANEVSCDGDRNLLGDiNYEftVRIVSKKPHSKNDLPliKLRATESIFQLIHRGTKCVVMSH 429
Cdd:pfam02815  80 RYLHSHEEqKPPLVEKEdWQKEVSAYGFRGFPGD-NDI--VEIFEKKSTTGMGSD--RIKPGDSYFRLQHVCTGCWLFSH 154
                         170       180
                  ....*....|....*....|....*....
gi 344303540  430 EAKLPKWGMGYN--EVLCVDQPTIPNTLW 456
Cdd:pfam02815 155 SVKLPKWGFGPEqqKVTCAKEGHMDDALT 183
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
273-322 7.63e-13

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 63.51  E-value: 7.63e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 344303540   273 VHYGSTVTIKHLNVERYLHSHDHNYP-TGSNEQQVTLYGY-DYDDNNDWMIE 322
Cdd:smart00472   4 VRWGDVVRLRHVTTGRYLHSHDEKLPpWGDGQQEVTGYGNpAIDANTLWLIE 55
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
82-232 3.34e-08

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


Pssm-ID: 404170 [Multi-domain]  Cd Length: 160  Bit Score: 53.42  E-value: 3.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540   82 VAMRMVSGVAGVLTVLFTYLTVRLNCRSSVAWFTAVLLMIENSQVTQSRLILLDTPLICAQSLAIYQFKKFSQtpvafSG 161
Cdd:pfam13231  22 WAVRLPSALAGVLTILLLYKLARRLFGKRAALLAALLLAVVPLFVALSRLFTPDAPLLLFWALALYFLLRALE-----KG 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 344303540  162 TWfRSLLITGISLGIAMSIKltglYTMGWVGI-LTIFQLWTILGDLNVSTRQWIMhffsRVVCLIIVPTTIY 232
Cdd:pfam13231  97 RL-RWWLLAGAAAGLGFLSK----YTAALLVPaALLYLLISPGRRRLKSPKPYLA----LLIALLVFSPVLI 159
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
335-377 1.69e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.11  E-value: 1.69e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 344303540   335 GPVKDGDTIRLYHRSTGKYLHVNDVRPPLSEHEyANEVSCDGD 377
Cdd:smart00472   2 GFVRWGDVVRLRHVTTGRYLHSHDEKLPPWGDG-QQEVTGYGN 43
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
273-355 3.44e-07

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: 50.83  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  273 VHYGSTVTIKHLNVERYLHSHDHN----YPTGSNEQQVTLYGYD-YDDNNDW--MIESQNKFNERlfqKGPVKDGDTI-R 344
Cdd:pfam02815  65 IKWGSPFRLRHLTTGRYLHSHEEQkpplVEKEDWQKEVSAYGFRgFPGDNDIveIFEKKSTTGMG---SDRIKPGDSYfR 141
                          90
                  ....*....|.
gi 344303540  345 LYHRSTGKYLH 355
Cdd:pfam02815 142 LQHVCTGCWLF 152
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
413-461 1.70e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.71  E-value: 1.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 344303540   413 SIFQLIHRGTKCVVMSHEAKLPKWGMGYNEVLCVDQPTI-PNTLWYIESN 461
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAIdANTLWLIEPV 57
ArnT COG1807
4-amino-4-deoxy-L-arabinose transferase or related glycosyltransferase of PMT family [Cell ...
35-186 1.41e-04

4-amino-4-deoxy-L-arabinose transferase or related glycosyltransferase of PMT family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224720 [Multi-domain]  Cd Length: 535  Bit Score: 44.77  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344303540  35 YYRGEFFMDvHPPLgkltYYWVSV----LFGWNGeftfeeigkqfddnvpyVAMRMVSGVAGVLTVLFTYLTVRLNCRSS 110
Cdd:COG1807   55 QLLGLPYFE-KPPL----VYWLQAlsylLFGVNE-----------------WSARLPSALAGALTALLVYWLAKRLFGRL 112
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 344303540 111 VAWFTAVLLMIENSQVTQSRLILLDTPLICAQSLAIYQF---KKFSQTPVAfsgtwfrsLLITGISLGIAMSIKLTGLY 186
Cdd:COG1807  113 AALLAALILLLTPLFFLIGRLALLDAALAFFLTLALALLylaLRARGKLKW--------LLLLGLALGLGFLTKGPGAL 183
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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