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Conserved domains on  [gi|16130192|ref|NP_416760|]
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lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

4-amino-4-deoxy-L-arabinose lipid A transferase( domain architecture ID 10014174)

4-amino-4-deoxy-L-arabinose lipid A transferase catalyzes the addition of 4-amino-4-deoxy-L-arabinose to lipid A

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
arnT PRK13279
lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
1-549 0e+00

lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;


:

Pssm-ID: 237330 [Multi-domain]  Cd Length: 552  Bit Score: 933.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192    1 MKSVRYLIGLFAFIACYYLLPISTRLLWQPDETRYAEISREMLASGDWIVPHLLGLRYFEKPIAGYWINSIGQWLFGANN 80
Cdd:PRK13279   2 MKSIRYLILLALFFALYYLLPLNTRLLWQPDETRYAEISREMLASGDWIVPHFLGLRYFEKPIAGYWINSIGQWLFGDNN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192   81 FGVRAGVIFATLLTAALVTWFTLRLWRDKRLALLATVIYLSLFIVYAIGTYAVLDPFIAFWLVAGMCSFWLAMQAQTWKG 160
Cdd:PRK13279  82 FGVRFGSVFSTLLSALLVYWLALRLWRDRRTALLAALIYLSLFLVYGIGTYAVLDPMITLWLTAAMCSFWLALQAQTRRG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  161 KSAGFLLLGITCGMGVMTKGFLALAVPVLSVLPWVATQKRWKDLFIYGWLAVISCVLTVLPWGLAIAQREPNFWHYFFWV 240
Cdd:PRK13279 162 KIGGYLLLGLACGMGFMTKGFLALAVPVISVLPWVIWQKRWKELLIYGPLAVLSAVLVSLPWALAIAQREPDFWHYFFWV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  241 EHIQRFALDDAQHRAPFWYYVPVIIAGSLPWLGLLPGALYTGWKNRK-HSATVYLLSWTIMPLLFFSVAKGKLPTYILSC 319
Cdd:PRK13279 242 EHIQRFAEDDAQHKAPFWYYLPVLIAGSLPWLGLLPGALKQGWRERKkHPGTFYLLLWVVMPLLFFSIAKGKLPTYILPC 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  320 FASLAMLMAHYAL-LAAKNNPLALRINGWINIAFGVTGIIATFVVSPWGPMNTPVWQTFESYKVFCAWSIFSLWAFFGWY 398
Cdd:PRK13279 322 FAPLAILMAHYAVdCAKNGNPRALRINGWINLAFGLLGLIALLVVSPWGPLKHPVYQPNETYKVFLAWIAFLGWAFFGWL 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  399 TLTNVEKTWPFAALCPLGLALLVGFSIPDRVMEGKHPQFFVEMTQESLQPSRYILTDSVGVAAGLAWSLQRDDIIMYRQT 478
Cdd:PRK13279 402 SLRNPLKRWALAALCPLGLALLVGAAIPDRVIDSKQPQFFIEMHQEELQSSRYILSDSVGVAAGLAWELKRSDIILYDQK 481
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130192  479 GELKYGLNYPDAKGRFVSGDEFANWLNQHRQEGIITLVLSVDRDEDINSLAIPPADAIDRQERLVLIQYRP 549
Cdd:PRK13279 482 GELKYGLSYPDAKGRFVSLDDFPAWLAQHRQEGIVSLVLRLDRDEDLPELALPPADKVYRQGRLVLLQYRQ 552
 
Name Accession Description Interval E-value
arnT PRK13279
lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
1-549 0e+00

lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;


Pssm-ID: 237330 [Multi-domain]  Cd Length: 552  Bit Score: 933.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192    1 MKSVRYLIGLFAFIACYYLLPISTRLLWQPDETRYAEISREMLASGDWIVPHLLGLRYFEKPIAGYWINSIGQWLFGANN 80
Cdd:PRK13279   2 MKSIRYLILLALFFALYYLLPLNTRLLWQPDETRYAEISREMLASGDWIVPHFLGLRYFEKPIAGYWINSIGQWLFGDNN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192   81 FGVRAGVIFATLLTAALVTWFTLRLWRDKRLALLATVIYLSLFIVYAIGTYAVLDPFIAFWLVAGMCSFWLAMQAQTWKG 160
Cdd:PRK13279  82 FGVRFGSVFSTLLSALLVYWLALRLWRDRRTALLAALIYLSLFLVYGIGTYAVLDPMITLWLTAAMCSFWLALQAQTRRG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  161 KSAGFLLLGITCGMGVMTKGFLALAVPVLSVLPWVATQKRWKDLFIYGWLAVISCVLTVLPWGLAIAQREPNFWHYFFWV 240
Cdd:PRK13279 162 KIGGYLLLGLACGMGFMTKGFLALAVPVISVLPWVIWQKRWKELLIYGPLAVLSAVLVSLPWALAIAQREPDFWHYFFWV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  241 EHIQRFALDDAQHRAPFWYYVPVIIAGSLPWLGLLPGALYTGWKNRK-HSATVYLLSWTIMPLLFFSVAKGKLPTYILSC 319
Cdd:PRK13279 242 EHIQRFAEDDAQHKAPFWYYLPVLIAGSLPWLGLLPGALKQGWRERKkHPGTFYLLLWVVMPLLFFSIAKGKLPTYILPC 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  320 FASLAMLMAHYAL-LAAKNNPLALRINGWINIAFGVTGIIATFVVSPWGPMNTPVWQTFESYKVFCAWSIFSLWAFFGWY 398
Cdd:PRK13279 322 FAPLAILMAHYAVdCAKNGNPRALRINGWINLAFGLLGLIALLVVSPWGPLKHPVYQPNETYKVFLAWIAFLGWAFFGWL 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  399 TLTNVEKTWPFAALCPLGLALLVGFSIPDRVMEGKHPQFFVEMTQESLQPSRYILTDSVGVAAGLAWSLQRDDIIMYRQT 478
Cdd:PRK13279 402 SLRNPLKRWALAALCPLGLALLVGAAIPDRVIDSKQPQFFIEMHQEELQSSRYILSDSVGVAAGLAWELKRSDIILYDQK 481
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130192  479 GELKYGLNYPDAKGRFVSGDEFANWLNQHRQEGIITLVLSVDRDEDINSLAIPPADAIDRQERLVLIQYRP 549
Cdd:PRK13279 482 GELKYGLSYPDAKGRFVSLDDFPAWLAQHRQEGIVSLVLRLDRDEDLPELALPPADKVYRQGRLVLLQYRQ 552
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
3-237 6.39e-53

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 180.20  E-value: 6.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192     3 SVRYLIGLFAFIACYYLLPISTRLLWQPDET--RYAEISREMLASGdWIVPHLLGL--RYFEKPIAGYWINSIGQWLFG- 77
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFasYYAEISFFMDVHP-PLGKMLIALggRLAGYDGNFTFISIGGQYYPGn 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192    78 ANNFGVRAGVIFATLLTAALVTWFTLRLWRDKRLALLATVIYLSLFIVYAIGTYAVLDPFIAFWLVAGMCSFWLAM-QAQ 156
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFErKAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192   157 TWKGKSAGFLLLGITCGMGVMTKGFLALAV-PVLSVLPWVATQKRWKDLFIYG----WLAVISCVLTVLPWGLAIAQREP 231
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVlPVGLLTIWHLWQLLGDLSLLLKsiwkHLFARLFCLIVIPWALYLAQFYV 239

                  ....*.
gi 16130192   232 NFWHYF 237
Cdd:pfam02366 240 HFWLLF 245
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
1-363 2.71e-51

PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 177.89  E-value: 2.71e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192   1 MKSVRYLIGLFAFIACYYLLPISTRLLWQPDETRYAEISREMLASGDWIVPHLLGLRYFEKPIAGYWINSIGQWLFGANN 80
Cdd:COG1807   4 TLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREMLESGDWLTPTLAGEPYFDKPPLIYWLIALSYKLFGVSE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  81 FGVRAGVIFATLLTAALVTWFTLRLWrDKRLALLATVIYLSLFIVYAIGTYAVLDPFIAFWLVAGMCSFWLAMQAQTWKg 160
Cdd:COG1807  84 FAARLPSALLGLLTVLLVYLLARRLF-GRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALYALLRALERRRLR- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192 161 ksaGFLLLGITCGMGVMTKGFLALAVPVLSVLPWVATQKRWKDLFIYG-WLAVISCVLTVLPWGLAIAQRE-PNFWHYFF 238
Cdd:COG1807 162 ---WLLLAGLALGLGFLTKGPVALLLPGLALLLYLLLTRRWRRLRRLRlLLGLLLALLLALPWYIANDWATgPAFLEYFF 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192 239 WVEHiqrfalddaqhrapfwyyvpviiagslpwlgllpgalytgwknrkhsatvyllswtIMPLLFFSVAKGKLPTYILS 318
Cdd:COG1807 239 GYEN--------------------------------------------------------LVPLLFFSLSATKLPRYLLP 262
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 16130192 319 CFASLAMLMAHYALLAAKNNPLALRINGWINIAFGVTGIIATFVV 363
Cdd:COG1807 263 LLPALALLAAAGLARLRRRRRALLLLALVLLLALLIALLLALAAL 307
 
Name Accession Description Interval E-value
arnT PRK13279
lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
1-549 0e+00

lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;


Pssm-ID: 237330 [Multi-domain]  Cd Length: 552  Bit Score: 933.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192    1 MKSVRYLIGLFAFIACYYLLPISTRLLWQPDETRYAEISREMLASGDWIVPHLLGLRYFEKPIAGYWINSIGQWLFGANN 80
Cdd:PRK13279   2 MKSIRYLILLALFFALYYLLPLNTRLLWQPDETRYAEISREMLASGDWIVPHFLGLRYFEKPIAGYWINSIGQWLFGDNN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192   81 FGVRAGVIFATLLTAALVTWFTLRLWRDKRLALLATVIYLSLFIVYAIGTYAVLDPFIAFWLVAGMCSFWLAMQAQTWKG 160
Cdd:PRK13279  82 FGVRFGSVFSTLLSALLVYWLALRLWRDRRTALLAALIYLSLFLVYGIGTYAVLDPMITLWLTAAMCSFWLALQAQTRRG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  161 KSAGFLLLGITCGMGVMTKGFLALAVPVLSVLPWVATQKRWKDLFIYGWLAVISCVLTVLPWGLAIAQREPNFWHYFFWV 240
Cdd:PRK13279 162 KIGGYLLLGLACGMGFMTKGFLALAVPVISVLPWVIWQKRWKELLIYGPLAVLSAVLVSLPWALAIAQREPDFWHYFFWV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  241 EHIQRFALDDAQHRAPFWYYVPVIIAGSLPWLGLLPGALYTGWKNRK-HSATVYLLSWTIMPLLFFSVAKGKLPTYILSC 319
Cdd:PRK13279 242 EHIQRFAEDDAQHKAPFWYYLPVLIAGSLPWLGLLPGALKQGWRERKkHPGTFYLLLWVVMPLLFFSIAKGKLPTYILPC 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  320 FASLAMLMAHYAL-LAAKNNPLALRINGWINIAFGVTGIIATFVVSPWGPMNTPVWQTFESYKVFCAWSIFSLWAFFGWY 398
Cdd:PRK13279 322 FAPLAILMAHYAVdCAKNGNPRALRINGWINLAFGLLGLIALLVVSPWGPLKHPVYQPNETYKVFLAWIAFLGWAFFGWL 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  399 TLTNVEKTWPFAALCPLGLALLVGFSIPDRVMEGKHPQFFVEMTQESLQPSRYILTDSVGVAAGLAWSLQRDDIIMYRQT 478
Cdd:PRK13279 402 SLRNPLKRWALAALCPLGLALLVGAAIPDRVIDSKQPQFFIEMHQEELQSSRYILSDSVGVAAGLAWELKRSDIILYDQK 481
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130192  479 GELKYGLNYPDAKGRFVSGDEFANWLNQHRQEGIITLVLSVDRDEDINSLAIPPADAIDRQERLVLIQYRP 549
Cdd:PRK13279 482 GELKYGLSYPDAKGRFVSLDDFPAWLAQHRQEGIVSLVLRLDRDEDLPELALPPADKVYRQGRLVLLQYRQ 552
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
3-237 6.39e-53

Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is the Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as Swiss:O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.


Pssm-ID: 396786 [Multi-domain]  Cd Length: 245  Bit Score: 180.20  E-value: 6.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192     3 SVRYLIGLFAFIACYYLLPISTRLLWQPDET--RYAEISREMLASGdWIVPHLLGL--RYFEKPIAGYWINSIGQWLFG- 77
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFasYYAEISFFMDVHP-PLGKMLIALggRLAGYDGNFTFISIGGQYYPGn 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192    78 ANNFGVRAGVIFATLLTAALVTWFTLRLWRDKRLALLATVIYLSLFIVYAIGTYAVLDPFIAFWLVAGMCSFWLAM-QAQ 156
Cdd:pfam02366  80 VPYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFErKAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192   157 TWKGKSAGFLLLGITCGMGVMTKGFLALAV-PVLSVLPWVATQKRWKDLFIYG----WLAVISCVLTVLPWGLAIAQREP 231
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVlPVGLLTIWHLWQLLGDLSLLLKsiwkHLFARLFCLIVIPWALYLAQFYV 239

                  ....*.
gi 16130192   232 NFWHYF 237
Cdd:pfam02366 240 HFWLLF 245
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
1-363 2.71e-51

PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 177.89  E-value: 2.71e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192   1 MKSVRYLIGLFAFIACYYLLPISTRLLWQPDETRYAEISREMLASGDWIVPHLLGLRYFEKPIAGYWINSIGQWLFGANN 80
Cdd:COG1807   4 TLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREMLESGDWLTPTLAGEPYFDKPPLIYWLIALSYKLFGVSE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  81 FGVRAGVIFATLLTAALVTWFTLRLWrDKRLALLATVIYLSLFIVYAIGTYAVLDPFIAFWLVAGMCSFWLAMQAQTWKg 160
Cdd:COG1807  84 FAARLPSALLGLLTVLLVYLLARRLF-GRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALYALLRALERRRLR- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192 161 ksaGFLLLGITCGMGVMTKGFLALAVPVLSVLPWVATQKRWKDLFIYG-WLAVISCVLTVLPWGLAIAQRE-PNFWHYFF 238
Cdd:COG1807 162 ---WLLLAGLALGLGFLTKGPVALLLPGLALLLYLLLTRRWRRLRRLRlLLGLLLALLLALPWYIANDWATgPAFLEYFF 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192 239 WVEHiqrfalddaqhrapfwyyvpviiagslpwlgllpgalytgwknrkhsatvyllswtIMPLLFFSVAKGKLPTYILS 318
Cdd:COG1807 239 GYEN--------------------------------------------------------LVPLLFFSLSATKLPRYLLP 262
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 16130192 319 CFASLAMLMAHYALLAAKNNPLALRINGWINIAFGVTGIIATFVV 363
Cdd:COG1807 263 LLPALALLAAAGLARLRRRRRALLLLALVLLLALLIALLLALAAL 307
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
61-222 4.83e-10

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: 58.43  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192    61 KPIAGYWINSIGQWLFGANNFGVRAGVIFATLLTAALVtWFTLRLWRDKRLALLATVIYLSLFIVYAIGTYAVLD-PFIA 139
Cdd:pfam13231   2 HPPLAAWLIALFTALFGDSEWAVRLPSALAGVLTILLL-YLLARRLFGKRAALLAALLLAVVPLFVALSRLFTPDaPLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192   140 FWLVAGMCsFWLAMQAQTWKgksaGFLLLGITCGMGVMTKGFLA-LAVPVLSVLPWVATQKRWKDLFIY-GWLAVISCVL 217
Cdd:pfam13231  81 FWALALYF-LLRALEKGRLK----WWLLAGAAAGLGFLSKYTAAlLVLAALLYLLISPGRRRLKSPKPYlGLLLALLLFS 155

                  ....*
gi 16130192   218 TVLPW 222
Cdd:pfam13231 156 PVLIW 160
COG5305 COG5305
Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT ...
66-348 5.85e-09

Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT family [General function prediction only];


Pssm-ID: 444104 [Multi-domain]  Cd Length: 402  Bit Score: 58.11  E-value: 5.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  66 YWINSIGQWLFGANNFGVRAGVIFATLLTAALVTWFTLRLWRDKRLALLATVIY--LSLFIVYAIGT--YAVLdpfiAFW 141
Cdd:COG5305  93 YLLLHLWMQLFGNSEWALRSLSALFGLLAIPLIYWLGRELFRSRRVALLAAALMavSPFHIYYAQEArmYSLL----TLL 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192 142 LVAGMCSFWLAMQAQTWKGksagFLLLGITCGMGVMTKGFLALAVPVLSV-LPWVATQKRWKDLFIYGWLAVISCVLTVL 220
Cdd:COG5305 169 VLLSLLALLRALRRPTRRL----WLLYALANALGLYTHYFFALVLIAHGLyLLLLAWFRRDRKTWLRYLLAAAAAVLLFL 244
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192 221 PWGLAIAQREPNFWHYFFWVEHI----QRFALDDAQHRAPFWYYVPVIIAGSLPWLGLLPGALYTGWKNR-KHSATVYLL 295
Cdd:COG5305 245 PWLLVLLTQLSRGNSQTGWISPPlpllQLLAAWLLMFSLLFVDLNPLTGLLALIFLILLILGLYFLLRRTpRRLSTWLFL 324
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192 296 SWTIMPLLFF---SVAKGKL----PTYILSCFASLAMLMAhyALLAAKNNPLALRINGWI 348
Cdd:COG5305 325 LLILVPLLLLlllSLLLGPDfslvPRYLIPYFPAVLLLVA--YLLATLWRKPWKIALALL 382
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
31-145 4.53e-04

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 42.96  E-value: 4.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130192  31 DETRYAEISREMLASGDWIVPHLLGLRYFEKPIAGYWINSIGQWLFGANN-FGVRAGVIFATLLTAALVTWFTLRLWRDK 109
Cdd:COG1928  49 DETYYVKDAWSLLTNGYERNWPDPGPFFVVHPPLGKWLIALGEWLFGYVNpFGWRFAAALAGTLSVLLVARIARRLTRST 128
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 16130192 110 RLALLATVIYL--SLFIVYAigTYAVLDPFIAFWLVAG 145
Cdd:COG1928 129 LLGAIAGLLLAldGLHLVLS--RTALLDIFLMFFVLAA 164
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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