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Conserved domains on  [gi|1907144095|ref|XP_036018637|]
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protein O-mannosyl-transferase 1 isoform X1 [Mus musculus]

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, ...
56-744 6.42e-133

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


:

Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 409.57  E-value: 6.42e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095  56 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDdSGPPFGHMLLALGGWLGGFDGNFLWNRIG-AEYSSNVPIWSLRLLPAL 134
Cdd:COG1928    40 WKIGNPNTVVFDEAHFGKFASYYLNGTPFFD-VHPPLGKMLIALVGGLEGYDPPFDFQLIGlTEYPFGYNYVGMRFFNAL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 135 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQthsPFSVHWWLWL 214
Cdd:COG1928   119 LGSLTVPLVYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLRFHRQQ---PFSRRWLKWL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 215 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLYRSG 294
Cdd:COG1928   196 LLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHFNILTDSG 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 295 PHDQIMSSAFQASLEGglARITQGQPLEVAFGSQVTLKSVsgKPLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFKDI 374
Cdd:COG1928   276 PGDSFMPSLFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP-------EGSEQQQVTGYGHKDA 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 375 NNWWIVKdpgrHQLVVNNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYiDYNISMPAQNLWKLDIVNRE 454
Cdd:COG1928   345 NNEWLIE----LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GDSFEGDEKDDWIIEIVKDE 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 455 SNRD--TWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKLSpgyHESMVWNVEEHrygksheqkerELELHS 532
Cdd:COG1928   420 ANEDqeRIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEEN-----------VNDRLP 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 533 PTQLDISRNLSFMARFSELQWKMLTLKNE-DLEHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVV 611
Cdd:COG1928   486 NPEKKVYKKLSFWKKFIELNKAMFSSNNAlVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKVYLMGNPALWWFSVPALAF 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 612 YTLLFFWYLLRRRRSICDLPEDAWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLC 691
Cdd:COG1928   566 FTGIVIWRLIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDFILRRPS 645
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907144095 692 RSQLQRNVfsaLVVAWYSSAC-HVSNMLRPLTYGdTSLSPGELRALRWKDSWDI 744
Cdd:COG1928   646 RERRTLGL---IVVAIFVALViYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
56-744 6.42e-133

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 409.57  E-value: 6.42e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095  56 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDdSGPPFGHMLLALGGWLGGFDGNFLWNRIG-AEYSSNVPIWSLRLLPAL 134
Cdd:COG1928    40 WKIGNPNTVVFDEAHFGKFASYYLNGTPFFD-VHPPLGKMLIALVGGLEGYDPPFDFQLIGlTEYPFGYNYVGMRFFNAL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 135 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQthsPFSVHWWLWL 214
Cdd:COG1928   119 LGSLTVPLVYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLRFHRQQ---PFSRRWLKWL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 215 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLYRSG 294
Cdd:COG1928   196 LLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHFNILTDSG 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 295 PHDQIMSSAFQASLEGglARITQGQPLEVAFGSQVTLKSVsgKPLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFKDI 374
Cdd:COG1928   276 PGDSFMPSLFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP-------EGSEQQQVTGYGHKDA 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 375 NNWWIVKdpgrHQLVVNNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYiDYNISMPAQNLWKLDIVNRE 454
Cdd:COG1928   345 NNEWLIE----LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GDSFEGDEKDDWIIEIVKDE 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 455 SNRD--TWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKLSpgyHESMVWNVEEHrygksheqkerELELHS 532
Cdd:COG1928   420 ANEDqeRIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEEN-----------VNDRLP 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 533 PTQLDISRNLSFMARFSELQWKMLTLKNE-DLEHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVV 611
Cdd:COG1928   486 NPEKKVYKKLSFWKKFIELNKAMFSSNNAlVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKVYLMGNPALWWFSVPALAF 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 612 YTLLFFWYLLRRRRSICDLPEDAWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLC 691
Cdd:COG1928   566 FTGIVIWRLIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDFILRRPS 645
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907144095 692 RSQLQRNVfsaLVVAWYSSAC-HVSNMLRPLTYGdTSLSPGELRALRWKDSWDI 744
Cdd:COG1928   646 RERRTLGL---IVVAIFVALViYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
56-291 1.95e-70

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: 230.66  E-value: 1.95e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095  56 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDDSgPPFGHMLLALGGWLGGFDGNFLWNRIGAEYS-SNVPIWSLRLLPAL 134
Cdd:pfam02366  13 WNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 135 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFnsqTHSPFSVHWWLWL 214
Cdd:pfam02366  92 LGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---RKAPFSRKWWLWL 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907144095 215 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLY 291
Cdd:pfam02366 169 LLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
323-380 6.67e-08

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 49.65  E-value: 6.67e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095  323 VAFGSQVTLKSVSGkplPCWLHSHKNTYPMIyengrgSSHQQQVTCYPFKDI--NNWWIV 380
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPAIdaNTLWLI 54
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
56-744 6.42e-133

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


Pssm-ID: 224839 [Multi-domain]  Cd Length: 699  Bit Score: 409.57  E-value: 6.42e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095  56 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDdSGPPFGHMLLALGGWLGGFDGNFLWNRIG-AEYSSNVPIWSLRLLPAL 134
Cdd:COG1928    40 WKIGNPNTVVFDEAHFGKFASYYLNGTPFFD-VHPPLGKMLIALVGGLEGYDPPFDFQLIGlTEYPFGYNYVGMRFFNAL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 135 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQthsPFSVHWWLWL 214
Cdd:COG1928   119 LGSLTVPLVYLIARRIGYSRLVAALAGLLVAFDNSFVTESRFILLDSFLLFFIVAAAYCFLRFHRQQ---PFSRRWLKWL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 215 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLYRSG 294
Cdd:COG1928   196 LLTGISLGCAISVKWVGLFTTGVVGLLAVYELWSLLYDKSVSWKQIIKHWLARFFGLIIIPFDIYLLSFYVHFNILTDSG 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 295 PHDQIMSSAFQASLEGglARITQGQPLEVAFGSQVTLKSVsgKPLPCWLHSHKNTYPmiyengrGSSHQQQVTCYPFKDI 374
Cdd:COG1928   276 PGDSFMPSLFQATLKG--NPVYLNSRDPAYGSSTITIRHA--GTGGGYLHSHNQLYP-------EGSEQQQVTGYGHKDA 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 375 NNWWIVKdpgrHQLVVNNPPRPVRHGDIVQLVHGMTTRLLNTHDVAAPLSPHSQEVSCYiDYNISMPAQNLWKLDIVNRE 454
Cdd:COG1928   345 NNEWLIE----LSDENATQIEPLKDGQSVRLRHKYTGKNLHFHDVKPPVSGNQYEVSGY-GDSFEGDEKDDWIIEIVKDE 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 455 SNRD--TWKTILSEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKLSpgyHESMVWNVEEHrygksheqkerELELHS 532
Cdd:COG1928   420 ANEDqeRIHPLETKFRLYHVLTGCYLASHDLKLPEWGFSQREVLCAKDR---DPSTTWNIEEN-----------VNDRLP 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 533 PTQLDISRNLSFMARFSELQWKMLTLKNE-DLEHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVV 611
Cdd:COG1928   486 NPEKKVYKKLSFWKKFIELNKAMFSSNNAlVPDHDYSSEPYQWPTLLRGLRFWGWGECIKKVYLMGNPALWWFSVPALAF 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 612 YTLLFFWYLLRRRRSICDLPEDAWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLC 691
Cdd:COG1928   566 FTGIVIWRLIRWRRGYRTLSDPAIRNFHWGYFYFLVGWAAHYLPWFIMSRQMYLHHYLPALYFAILALALVLDFILRRPS 645
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907144095 692 RSQLQRNVfsaLVVAWYSSAC-HVSNMLRPLTYGdTSLSPGELRALRWKDSWDI 744
Cdd:COG1928   646 RERRTLGL---IVVAIFVALViYFFFWFSPVTYG-LPLSPQEFRRLMWLPSWDF 695
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
56-291 1.95e-70

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: 230.66  E-value: 1.95e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095  56 WQLSYPRAVVFDEVYYGQYISFYMKRIFFLDDSgPPFGHMLLALGGWLGGFDGNFLWNRIGAEYS-SNVPIWSLRLLPAL 134
Cdd:pfam02366  13 WNLYNPNLVVFDEVHFGKFASYYAEISFFMDVH-PPLGKMLIALGGRLAGYDGNFTFISIGGQYYpGNVPYFGMRLFSAL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 135 AGALSVPMAYQIVLELHFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFnsqTHSPFSVHWWLWL 214
Cdd:pfam02366  92 LGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFE---RKAPFSRKWWLWL 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907144095 215 LLTGVSCSCAVGIKYMGIFTYLLVLGIAAVHAWNLIGDQTLSNMRVLSHLLARIVALLVVPVFLYLLFFYVHLMLLY 291
Cdd:pfam02366 169 LLTGIALGLALSTKGVGLFTVLPVGLLTIWHLWQLLGDLSLLLKSIWKHLFARLFCLIVIPWALYLAQFYVHFWLLF 245
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
546-740 1.73e-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: 193.91  E-value: 1.73e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 546 ARFSELQWKMLTLKNEDL-EHQYSSTPLEWLTLDTNIAYWLHPRTSAQIHLLGNIVIWTSASLATVVYTLLFFWYLLRRR 624
Cdd:pfam16192   1 KKFIELQKAMLTSNNGLTpSHPYASRPWEWPLLLRGIRFWGWDDRNAQIYLLGNPVIWWSSTAAILVFVLLLLAYLLRWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 625 RSICDLPED-AWSRWVLAGALCTGGWALNYLPFFLMERVLFLYHYLPALTFQILLLPIVLQHASDHLCR--SQLQRNVFS 701
Cdd:pfam16192  81 RGYYDLSDDdTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFKRlpRSLRKRVGY 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907144095 702 ALVVAWYSSACHVSNMLRPLTYGDTSLSpGELRALRWKD 740
Cdd:pfam16192 161 AIVVVLLALVIYVFIYFSPLTYGMPGTS-EECKKLKWLS 198
MIR pfam02815
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ...
344-496 1.23e-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: 69.70  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 344 HSHKNTYPMIYENGRGsSHQQQVTCYPFKDINN----WWIVkdpgrhqLVVNNPP---RPVRHGDIVQLVHGMTTRLLNT 416
Cdd:pfam02815  13 HSHQDEYLTGSEQQQK-QPFLRITLYPHGDANNsarsLWRI-------EVVRHDAwrgGLIKWGSPFRLRHLTTGRYLHS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 417 HDV-AAPLSPHS---QEVSCYiDYNISmpAQNLWKLDIVNRESN----RDTWKTILSEVRFVHVNTSAILKLSGAHLPDW 488
Cdd:pfam02815  85 HEEqKPPLVEKEdwqKEVSAY-GFRGF--PGDNDIVEIFEKKSTtgmgSDRIKPGDSYFRLQHVCTGCWLFSHSVKLPKW 161
                         170
                  ....*....|
gi 1907144095 489 GFR--QLEVV 496
Cdd:pfam02815 162 GFGpeQQKVT 171
ArnT COG1807
4-amino-4-deoxy-L-arabinose transferase or related glycosyltransferase of PMT family [Cell ...
123-274 6.62e-09

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: 59.02  E-value: 6.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 123 VPIWSLRLLPALAGALSVPMAYQIVLELhFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQT 202
Cdd:COG1807    81 VNEWSARLPSALAGALTALLVYWLAKRL-FGRLAALLAALILLLTPLFFLIGRLALLDAALAFFLTLALALLYLALRARG 159
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907144095 203 HspfsvhwWLWLLLTGVSCSCAVGIKYMGIFtyLLVLGIAAVhawnLIGDQTLSNMRVLSHLLARIVALLVV 274
Cdd:COG1807   160 K-------LKWLLLLGLALGLGFLTKGPGAL--LLPLILLLL----LLAPRLRRLLRDLRLWLGLLLGLLPV 218
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
323-380 6.67e-08

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 49.65  E-value: 6.67e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095  323 VAFGSQVTLKSVSGkplPCWLHSHKNTYPMIyengrgSSHQQQVTCYPFKDI--NNWWIV 380
Cdd:smart00472   4 VRWGDVVRLRHVTT---GRYLHSHDEKLPPW------GDGQQEVTGYGNPAIdaNTLWLI 54
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
123-276 9.70e-06

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: 46.10  E-value: 9.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907144095 123 VPIWSLRLLPALAGALSVPMAYQIVLELhFSHGAAIGAALLMLIENALITQSRLMLLESILIFFNLLAVLSYLKFFNSQT 202
Cdd:pfam13231  19 DSEWAVRLPSALAGVLTILLLYKLARRL-FGKRAALLAALLLAVVPLFVALSRLFTPDAPLLLFWALALYFLLRALEKGR 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907144095 203 hspfsvhwWLWLLLTGVSCSCAVGIKYMGIFtyllvLGIAAVhAWNLIGDQTLSNMRVLSHLLARIVALLVVPV 276
Cdd:pfam13231  98 --------LRWWLLAGAAAGLGFLSKYTAAL-----LVPAAL-LYLLISPGRRRLKSPKPYLALLIALLVFSPV 157
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
465-515 2.92e-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: 2.92e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907144095  465 SEVRFVHVNTSAILKLSGAHLPDWGFRQLEVVGEKlSPGYHESMVWNVEEH 515
Cdd:smart00472   8 DVVRLRHVTTGRYLHSHDEKLPPWGDGQQEVTGYG-NPAIDANTLWLIEPV 57
MIR smart00472
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases;
394-451 1.99e-04

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


Pssm-ID: 197746 [Multi-domain]  Cd Length: 57  Bit Score: 39.63  E-value: 1.99e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907144095  394 PRPVRHGDIVQLVHGMTTRLLNTHDVA-APLSPHSQEVSCYIDYNISmpAQNLWKLDIV 451
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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