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Conserved domains on  [gi|568914609|ref|XP_006498536|]
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protein O-mannosyl-transferase 1 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PMT1 super family cl34376
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
2-515 1.07e-89

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


The actual alignment was detected with superfamily member COG1928:

Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 289.39  E-value: 1.07e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609   2 GIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLYRSGPHDQIMSSAFQASLEG 81
Cdd:COG1928  212 GLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKG 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609  82 glARITQGQPLEVAFGSQVTLKSVsgKPLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFKDINNWWIVKdpgrHQLVV 161
Cdd:COG1928  292 --NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP-------EGSEQQQVTGYGHKDANNEWLIE----LSDEN 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 162 NNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYiDYNISMPAQNLWKLDIVNRESNRD--TWKTILSEVR 239
Cdd:COG1928  357 ATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GDSFEGDEKDDWIIEIVKDEANEDqeRIHPLETKFR 435
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 240 FVHVNTSAILKLSGAHLPDWGFRQLEVVGEKLSpgyHESMVWNVEEHrygksheqkerELELHSPTQLDISRNLSFMARF 319
Cdd:COG1928  436 LYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEEN-----------VNDRLPNPEKKVYKKLSFWKKF 501
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 320 SELQWKMLTLKNE-DLEHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRRRSI 398
Cdd:COG1928  502 IELNKAMFSSNNAlVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKVYLMGNPALWWFSVPALAFFTGIVIWRLIRWRRGY 581
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 399 CDLPEDAWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCRSQLQRNVfsaLVVAW 478
Cdd:COG1928  582 RTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDFILRRPSRERRTLGL---IVVAI 658
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 568914609 479 YSSAC-HVSNMLRPLTYGdTSLSPGELRALRWKDSWDI 515
Cdd:COG1928  659 FVALViYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
2-515 1.07e-89

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 289.39  E-value: 1.07e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609   2 GIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLYRSGPHDQIMSSAFQASLEG 81
Cdd:COG1928  212 GLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKG 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609  82 glARITQGQPLEVAFGSQVTLKSVsgKPLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFKDINNWWIVKdpgrHQLVV 161
Cdd:COG1928  292 --NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP-------EGSEQQQVTGYGHKDANNEWLIE----LSDEN 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 162 NNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYiDYNISMPAQNLWKLDIVNRESNRD--TWKTILSEVR 239
Cdd:COG1928  357 ATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GDSFEGDEKDDWIIEIVKDEANEDqeRIHPLETKFR 435
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 240 FVHVNTSAILKLSGAHLPDWGFRQLEVVGEKLSpgyHESMVWNVEEHrygksheqkerELELHSPTQLDISRNLSFMARF 319
Cdd:COG1928  436 LYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEEN-----------VNDRLPNPEKKVYKKLSFWKKF 501
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 320 SELQWKMLTLKNE-DLEHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRRRSI 398
Cdd:COG1928  502 IELNKAMFSSNNAlVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKVYLMGNPALWWFSVPALAFFTGIVIWRLIRWRRGY 581
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 399 CDLPEDAWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCRSQLQRNVfsaLVVAW 478
Cdd:COG1928  582 RTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDFILRRPSRERRTLGL---IVVAI 658
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 568914609 479 YSSAC-HVSNMLRPLTYGdTSLSPGELRALRWKDSWDI 515
Cdd:COG1928  659 FVALViYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
317-511 6.78e-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: 406576  Cd Length: 198  Bit Score: 198.54  E-value: 6.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609  317 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 395
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609  396 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 472
Cdd:pfam16192  81 RGYYDLSDDdTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFKRlpRSLRKRVGY 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 568914609  473 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 511
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
94-151 1.05e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.49  E-value: 1.05e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609    94 VAFGSQVTLKSVSGkplPCWLHSHKNTYPMIyengrgSSHQQQVTCYPFKDI--NNWWIV 151
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPAIdaNTLWLI 54
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
2-515 1.07e-89

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 289.39  E-value: 1.07e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609   2 GIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLYRSGPHDQIMSSAFQASLEG 81
Cdd:COG1928  212 GLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKG 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609  82 glARITQGQPLEVAFGSQVTLKSVsgKPLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFKDINNWWIVKdpgrHQLVV 161
Cdd:COG1928  292 --NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP-------EGSEQQQVTGYGHKDANNEWLIE----LSDEN 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 162 NNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYiDYNISMPAQNLWKLDIVNRESNRD--TWKTILSEVR 239
Cdd:COG1928  357 ATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GDSFEGDEKDDWIIEIVKDEANEDqeRIHPLETKFR 435
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 240 FVHVNTSAILKLSGAHLPDWGFRQLEVVGEKLSpgyHESMVWNVEEHrygksheqkerELELHSPTQLDISRNLSFMARF 319
Cdd:COG1928  436 LYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEEN-----------VNDRLPNPEKKVYKKLSFWKKF 501
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 320 SELQWKMLTLKNE-DLEHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRRRSI 398
Cdd:COG1928  502 IELNKAMFSSNNAlVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKVYLMGNPALWWFSVPALAFFTGIVIWRLIRWRRGY 581
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609 399 CDLPEDAWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCRSQLQRNVfsaLVVAW 478
Cdd:COG1928  582 RTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDFILRRPSRERRTLGL---IVVAI 658
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 568914609 479 YSSAC-HVSNMLRPLTYGdTSLSPGELRALRWKDSWDI 515
Cdd:COG1928  659 FVALViYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
317-511 6.78e-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: 406576  Cd Length: 198  Bit Score: 198.54  E-value: 6.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609  317 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 395
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609  396 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 472
Cdd:pfam16192  81 RGYYDLSDDdTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFKRlpRSLRKRVGY 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 568914609  473 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 511
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
115-267 3.54e-13

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: 67.77  E-value: 3.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609  115 HSHKNTYPMIYENGRGsSHQQQVTCYPFKDINN----WWIVkdpgrhqLVVNNPP---RPVRHGDIVQLVHGMTTRLLNT 187
Cdd:pfam02815  13 HSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLRHLTTGRYLHS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609  188 HDV-AAPLSPHS---QEVSCYiDYNISmpAQNLWKLDIVNRESN----RDTWKTILSEVRFVHVNTSAILKLSGAHLPDW 259
Cdd:pfam02815  85 HEEqKPPLVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKKSTtgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW 161
                         170
                  ....*....|
gi 568914609  260 GFR--QLEVV 267
Cdd:pfam02815 162 GFGpeQQKVT 171
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
1-62 3.19e-12

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: 66.57  E-value: 3.19e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568914609    1 MGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLY 62
Cdd:pfam02366 184 VGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
94-151 1.05e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 48.49  E-value: 1.05e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914609    94 VAFGSQVTLKSVSGkplPCWLHSHKNTYPMIyengrgSSHQQQVTCYPFKDI--NNWWIV 151
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPAIdaNTLWLI 54
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
236-286 3.45e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.56  E-value: 3.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568914609   236 SEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKlSPGYHESMVWNVEEH 286
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
165-222 2.47e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 38.86  E-value: 2.47e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568914609   165 PRPVRHGDIVQLVHGMTTRLLNTHDVA-APLSPHSQEVSCYIDYNISmpAQNLWKLDIV 222
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
 
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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