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Conserved domains on  [gi|1953099264|ref|XP_038404906|]
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protein O-mannosyl-transferase 1 isoform X4 [Canis lupus familiaris]

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, ...
14-720 3.04e-130

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


:

Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 401.87  E-value: 3.04e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  14 DINLNVVALTAVGLLSRLWHLAYPRAVVFDEVYYGQYISFYMKRIFFLDgSGPPFGHMLLALGGYLGGFDGNFLWNRIG- 92
Cdd:COG1928    22 PYKLGPVLLTVLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFD-VHPPLGKMLIALVGGLEGYDPPFDFQLIGl 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  93 AEYSSNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLK 172
Cdd:COG1928   101 TEYPFGYNYVGMRFFNALLGSLTVPLVYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLR 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 173 FSNSQkhrPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLARAAALLVIPT 252
Cdd:COG1928   181 FHRQQ---PFSRRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPF 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 253 LMYLLFFYVHLILVYRSGPHDQIMSSAFQASLEGglARITQGQPLEVAYGSQVTLKNVfgKPVPCWLHSHQSTYPmiyen 332
Cdd:COG1928   258 DIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP----- 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 333 grGSSHQQQVTCYPFKDVNNWWIVKdpgrHQLVVNNPPRPVRHGDVVQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYvDY 412
Cdd:COG1928   329 --EGSEQQQVTGYGHKDANNEWLIE----LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GD 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 413 NISMPSQNLWRLDIVNRES--DTEVWKTILSEVRLVHVNTSAVLKLSGAHLPDWGFQQLEVVGEKLSrgyHESMVWNVEE 490
Cdd:COG1928   402 SFEGDEKDDWIIEIVKDEAneDQERIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 491 HrygksqeqkerELELHSPAQMDVSRNLSFMARFLELQWRML-TAKSDDSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQI 569
Cdd:COG1928   479 N-----------VNDRLPNPEKKVYKKLSFWKKFIELNKAMFsSNNALVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKV 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 570 HLLGNIVIWASASLAMVVYVLLFFWYLLRRRRSICDIPEDSWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALT 649
Cdd:COG1928   548 YLMGNPALWWFSVPALAFFTGIVIWRLIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALY 627
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953099264 650 FQILLLPVVLQHVSDHLCRSQllRSLFSALVVAWYSCACHVFNTLRPLTYGdKSLSPSELKALRWKDSWDI 720
Cdd:COG1928   628 FAILALALVLDFILRRPSRER--RTLGLIVVAIFVALVIYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
14-720 3.04e-130

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 401.87  E-value: 3.04e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  14 DINLNVVALTAVGLLSRLWHLAYPRAVVFDEVYYGQYISFYMKRIFFLDgSGPPFGHMLLALGGYLGGFDGNFLWNRIG- 92
Cdd:COG1928    22 PYKLGPVLLTVLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFD-VHPPLGKMLIALVGGLEGYDPPFDFQLIGl 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  93 AEYSSNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLK 172
Cdd:COG1928   101 TEYPFGYNYVGMRFFNALLGSLTVPLVYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLR 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 173 FSNSQkhrPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLARAAALLVIPT 252
Cdd:COG1928   181 FHRQQ---PFSRRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPF 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 253 LMYLLFFYVHLILVYRSGPHDQIMSSAFQASLEGglARITQGQPLEVAYGSQVTLKNVfgKPVPCWLHSHQSTYPmiyen 332
Cdd:COG1928   258 DIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP----- 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 333 grGSSHQQQVTCYPFKDVNNWWIVKdpgrHQLVVNNPPRPVRHGDVVQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYvDY 412
Cdd:COG1928   329 --EGSEQQQVTGYGHKDANNEWLIE----LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GD 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 413 NISMPSQNLWRLDIVNRES--DTEVWKTILSEVRLVHVNTSAVLKLSGAHLPDWGFQQLEVVGEKLSrgyHESMVWNVEE 490
Cdd:COG1928   402 SFEGDEKDDWIIEIVKDEAneDQERIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 491 HrygksqeqkerELELHSPAQMDVSRNLSFMARFLELQWRML-TAKSDDSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQI 569
Cdd:COG1928   479 N-----------VNDRLPNPEKKVYKKLSFWKKFIELNKAMFsSNNALVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKV 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 570 HLLGNIVIWASASLAMVVYVLLFFWYLLRRRRSICDIPEDSWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALT 649
Cdd:COG1928   548 YLMGNPALWWFSVPALAFFTGIVIWRLIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALY 627
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953099264 650 FQILLLPVVLQHVSDHLCRSQllRSLFSALVVAWYSCACHVFNTLRPLTYGdKSLSPSELKALRWKDSWDI 720
Cdd:COG1928   628 FAILALALVLDFILRRPSRER--RTLGLIVVAIFVALVIYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
20-267 1.66e-69

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: 227.58  E-value: 1.66e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  20 VALTAVGLLSRLWHLAYPRAVVFDEVYYGQYISFYMKRIFFLDGSgPPFGHMLLALGGYLGGFDGNFLWNRIGAEYS-SN 98
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  99 VPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFsnsQK 178
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKF---ER 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 179 HRPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLARAAALLVIPTLMYLLF 258
Cdd:pfam02366 157 KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236

                  ....*....
gi 1953099264 259 FYVHLILVY 267
Cdd:pfam02366 237 FYVHFWLLF 245
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
299-356 9.41e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 9.41e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  299 VAYGSQVTLKNVFGkpvPCWLHSHQSTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 356
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPaiDANTLWLI 54
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
14-720 3.04e-130

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 401.87  E-value: 3.04e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  14 DINLNVVALTAVGLLSRLWHLAYPRAVVFDEVYYGQYISFYMKRIFFLDgSGPPFGHMLLALGGYLGGFDGNFLWNRIG- 92
Cdd:COG1928    22 PYKLGPVLLTVLSFIVRFWKIGNPNTVVFDEAHFGKFASYYLNGTPFFD-VHPPLGKMLIALVGGLEGYDPPFDFQLIGl 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  93 AEYSSNVPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLK 172
Cdd:COG1928   101 TEYPFGYNYVGMRFFNALLGSLTVPLVYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLR 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 173 FSNSQkhrPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLARAAALLVIPT 252
Cdd:COG1928   181 FHRQQ---PFSRRWLKWLLLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPF 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 253 LMYLLFFYVHLILVYRSGPHDQIMSSAFQASLEGglARITQGQPLEVAYGSQVTLKNVfgKPVPCWLHSHQSTYPmiyen 332
Cdd:COG1928   258 DIYLLSFYVHFNILTDSGPGDSFMPSLFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP----- 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 333 grGSSHQQQVTCYPFKDVNNWWIVKdpgrHQLVVNNPPRPVRHGDVVQLVHGMTTRFLNTHDVAAPLSPHSQEVSCYvDY 412
Cdd:COG1928   329 --EGSEQQQVTGYGHKDANNEWLIE----LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GD 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 413 NISMPSQNLWRLDIVNRES--DTEVWKTILSEVRLVHVNTSAVLKLSGAHLPDWGFQQLEVVGEKLSrgyHESMVWNVEE 490
Cdd:COG1928   402 SFEGDEKDDWIIEIVKDEAneDQERIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEE 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 491 HrygksqeqkerELELHSPAQMDVSRNLSFMARFLELQWRML-TAKSDDSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQI 569
Cdd:COG1928   479 N-----------VNDRLPNPEKKVYKKLSFWKKFIELNKAMFsSNNALVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKV 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 570 HLLGNIVIWASASLAMVVYVLLFFWYLLRRRRSICDIPEDSWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALT 649
Cdd:COG1928   548 YLMGNPALWWFSVPALAFFTGIVIWRLIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALY 627
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953099264 650 FQILLLPVVLQHVSDHLCRSQllRSLFSALVVAWYSCACHVFNTLRPLTYGdKSLSPSELKALRWKDSWDI 720
Cdd:COG1928   628 FAILALALVLDFILRRPSRER--RTLGLIVVAIFVALVIYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
20-267 1.66e-69

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: 227.58  E-value: 1.66e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  20 VALTAVGLLSRLWHLAYPRAVVFDEVYYGQYISFYMKRIFFLDGSgPPFGHMLLALGGYLGGFDGNFLWNRIGAEYS-SN 98
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  99 VPVWSLRLLPALTGAFSIPMAYQILLELGFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFsnsQK 178
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKF---ER 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 179 HRPFSLSWWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAWHLIGDQTLSNVCVLCHLLARAAALLVIPTLMYLLF 258
Cdd:pfam02366 157 KAPFSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQ 236

                  ....*....
gi 1953099264 259 FYVHLILVY 267
Cdd:pfam02366 237 FYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
522-716 3.60e-59

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: 435204 [Multi-domain]  Cd Length: 198  Bit Score: 198.15  E-value: 3.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 522 ARFLELQWRMLTAKSD-DSEHKYSSSPLDWVTLDTSIAYWLHPRTSAQIHLLGNIVIWASASLAMVVYVLLFFWYLLRRR 600
Cdd:pfam16192   1 KKFIELQKAMLTSNNGlTPSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 601 RSICDIPED-SWLRWVLAGALCAGGWAVNYLPFFMMEKTLFLYHYLPALTFQILLLPVVLQHVSDHLCR--SQLLRSLFS 677
Cdd:pfam16192  81 RGYYDLSDDwTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFKRlpRSLRKRVGY 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1953099264 678 ALVVAWYSCACHVFNTLRPLTYGDKSLSpSELKALRWKD 716
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
310-472 6.17e-17

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: 79.33  E-value: 6.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 310 VFGKPVPCWLHSHQSTYPMIYENGRGSsHQQQVTCYPFKDVNN----WWIVkdpgrhqLVVNNPP---RPVRHGDVVQLV 382
Cdd:pfam02815   3 LKGGDVVRLFHSHQDEYLTGSEQQQKQ-PFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 383 HGMTTRFLNTHDV-AAPLSPHS---QEVSCYvDYNISM----PSQNLWRLDIVNRESDTEvwKTILSEVRLVHVNTSAVL 454
Cdd:pfam02815  75 HLTTGRYLHSHEEqKPPLVEKEdwqKEVSAY-GFRGFPgdndIVEIFEKKSTTGMGSDRI--KPGDSYFRLQHVCTGCWL 151
                         170       180
                  ....*....|....*....|
gi 1953099264 455 KLSGAHLPDWGF--QQLEVV 472
Cdd:pfam02815 152 FSHSVKLPKWGFgpEQQKVT 171
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
299-356 9.41e-07

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 46.18  E-value: 9.41e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  299 VAYGSQVTLKNVFGkpvPCWLHSHQSTYPMIyengrgSSHQQQVTCYPFK--DVNNWWIV 356
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPaiDANTLWLI 54
ArnT COG1807
4-amino-4-deoxy-L-arabinose transferase or related glycosyltransferase of PMT family [Cell ...
102-218 5.43e-06

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: 49.78  E-value: 5.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 102 WSLRLLPALTGAFSIPMAYQILLELgFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKfsnsQKHRP 181
Cdd:COG1807    84 WSARLPSALAGALTALLVYWLAKRL-FGRLAALLAALILLLTPLFFLIGRLALLDAALAFFLTLALALLYL----ALRAR 158
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1953099264 182 FSLSWWFwlmLTGVACSCAVGVKYMGIFtYLLVLAVA 218
Cdd:COG1807   159 GKLKWLL---LLGLALGLGFLTKGPGAL-LLPLILLL 191
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
370-427 2.35e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 42.33  E-value: 2.35e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953099264  370 PRPVRHGDVVQLVHGMTTRFLNTHDVA-APLSPHSQEVSCYVDYNISmpSQNLWRLDIV 427
Cdd:smart00472   1 GGFVRWGDVVRLRHVTTGRYLHSHDEKlPPWGDGQQEVTGYGNPAID--ANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
441-491 2.98e-05

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 41.94  E-value: 2.98e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1953099264  441 SEVRLVHVNTSAVLKLSGAHLPDWGFQQLEVVGEKLSRGyHESMVWNVEEH 491
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYGNPAI-DANTLWLIEPV 57
COG4745 COG4745
Predicted membrane-bound mannosyltransferase [General function prediction only];
17-216 9.09e-03

Predicted membrane-bound mannosyltransferase [General function prediction only];


Pssm-ID: 227088  Cd Length: 556  Bit Score: 39.08  E-value: 9.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  17 LNVVALTAVGLLSRLWHLAYpRAVVFDEVYYGQYISFYMkriFFLDGSGPPFGHmllalggylggfdGNFLWnrigaeYS 96
Cdd:COG4745    16 LAVIAVVAIALLARLYNLGL-RPFHFDESRHATWILKYL---EQGAWSYRPIYH-------------GPFLY------HV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264  97 SNVPV-------WSLRLLPALTGAFSIPMAYQILLELGfsHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVls 169
Cdd:COG4745    73 NYAVFgllgasdATARLVVAVTGVLLPLTAWLYRTRLG--DKEVLALATLLAFSPVLVYYSRFMRNDLLLAAFTLLAV-- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953099264 170 YLKFSNSQKHRPfslswwFWLMLTGVACSCAVGVK-----YMGIFTYLLVLA 216
Cdd:COG4745   149 GFAVRYLDTERF------RYLYASAVSLALAFTAKenallYVAAFLGASALV 194
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
102-223 9.98e-03

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: 37.24  E-value: 9.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953099264 102 WSLRLLPALTGAFSIPMAYQILLELgFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFSNSQKhrp 181
Cdd:pfam13231  22 WAVRLPSALAGVLTILLLYLLARRL-FGKRAALLAALLLAVVPLFVALSRLFTPDAPLLLFWALALYFLLRALEKGR--- 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953099264 182 fslswWFWLMLTGVACSCAVGVKYMGIFTYLLVLAVASVHAW 223
Cdd:pfam13231  98 -----LKWWLLAGAAAGLGFLSKYTAALLVLAALLYLLISPG 134
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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