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Conserved domains on  [gi|15600011|ref|NP_253505|]
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hypothetical protein PA4818 [Pseudomonas aeruginosa PAO1]

Protein Classification

ArnT family glycosyltransferase( domain architecture ID 11448528)

ArnT family glycosyltransferase catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds; ArnT is an integral membrane lipid-to-lipid glycosyltransferase and the last enzyme in the aminoarabinose biosynthetic pathway of Gram-negative bacteria

CAZY:  GT83
EC:  2.4.-.-
Gene Ontology:  GO:0016757

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
1-246 1.60e-25

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: 106.25  E-value: 1.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011   1 MRALRGWPLAWFLLALAFAIRLLSLGSYPLMDTTEARYGEVARKMAELGDWITPWYDvGVPFWGKPPLAFWLSAGGQLLL 80
Cdd:COG1807   1 MSKTLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREMLESGDWLTPTLA-GEPYFDKPPLIYWLIALSYKLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011  81 GANEFASRLPHWLLGVLVLWLVWDWQAR-EDRRQARIACVLLGSSALFFVASGAVMTDMALALALVLAMRGFWLGLHGAe 159
Cdd:COG1807  80 GVSEFAARLPSALLGLLTVLLVYLLARRlFGRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALYALLRALERR- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011 160 giRRREGWLMFLGLGLGLLAKGPLTLILAGLPIGLWALLEWRWRALWRGLPWIrGSLLMLLVAAPWYLLAELKT-PGFLE 238
Cdd:COG1807 159 --RLRWLLLAGLALGLGFLTKGPVALLLPGLALLLYLLLTRRWRRLRRLRLLL-GLLLALLLALPWYIANDWATgPAFLE 235

                ....*...
gi 15600011 239 YFLLGEHW 246
Cdd:COG1807 236 YFFGYENL 243
 
Name Accession Description Interval E-value
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
1-246 1.60e-25

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: 106.25  E-value: 1.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011   1 MRALRGWPLAWFLLALAFAIRLLSLGSYPLMDTTEARYGEVARKMAELGDWITPWYDvGVPFWGKPPLAFWLSAGGQLLL 80
Cdd:COG1807   1 MSKTLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREMLESGDWLTPTLA-GEPYFDKPPLIYWLIALSYKLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011  81 GANEFASRLPHWLLGVLVLWLVWDWQAR-EDRRQARIACVLLGSSALFFVASGAVMTDMALALALVLAMRGFWLGLHGAe 159
Cdd:COG1807  80 GVSEFAARLPSALLGLLTVLLVYLLARRlFGRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALYALLRALERR- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011 160 giRRREGWLMFLGLGLGLLAKGPLTLILAGLPIGLWALLEWRWRALWRGLPWIrGSLLMLLVAAPWYLLAELKT-PGFLE 238
Cdd:COG1807 159 --RLRWLLLAGLALGLGFLTKGPVALLLPGLALLLYLLLTRRWRRLRRLRLLL-GLLLALLLALPWYIANDWATgPAFLE 235

                ....*...
gi 15600011 239 YFLLGEHW 246
Cdd:COG1807 236 YFFGYENL 243
arnT PRK13279
lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
10-332 7.03e-10

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


Pssm-ID: 237330 [Multi-domain]  Cd Length: 552  Bit Score: 61.08  E-value: 7.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011   10 AWFLLALAFAI-RLLSLGSYPLMDTTEARYGEVARKMAELGDWITPwYDVGVPFWGKPPLAFWLSAGGQLLLGANEFASR 88
Cdd:PRK13279   7 YLILLALFFALyYLLPLNTRLLWQPDETRYAEISREMLASGDWIVP-HFLGLRYFEKPIAGYWINSIGQWLFGDNNFGVR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011   89 LPHWLLGVLVLWLVWdWQAR---EDRRQARIACVLLGSSALFF-VASGAVMTDMaLALALVLAMRGFWLGLHgAEGIRRR 164
Cdd:PRK13279  86 FGSVFSTLLSALLVY-WLALrlwRDRRTALLAALIYLSLFLVYgIGTYAVLDPM-ITLWLTAAMCSFWLALQ-AQTRRGK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011  165 egwlmflglglgllakgPLTLILAGLPIGL-------------------WALLEWRWRALWRGLPWirGSLLMLLVAAPW 225
Cdd:PRK13279 163 -----------------IGGYLLLGLACGMgfmtkgflalavpvisvlpWVIWQKRWKELLIYGPL--AVLSAVLVSLPW 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011  226 YLLAELKTPGFLEYFLLGEHWQRFvtAGWDGdrygnAHAYPY---------GSV-WLFLLAAAFpwslwlplllWLGWRQ 295
Cdd:PRK13279 224 ALAIAQREPDFWHYFFWVEHIQRF--AEDDA-----QHKAPFwyylpvliaGSLpWLGLLPGAL----------KQGWRE 286
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 15600011  296 RGEvvdgvASRRRYWLFWGLAPCLFFTFAGNVLWTYV 332
Cdd:PRK13279 287 RKK-----HPGTFYLLLWVVMPLLFFSIAKGKLPTYI 318
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
11-240 1.71e-05

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: 46.15  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011    11 WFLLALAFAIRLLSLGSYPLM-------DTTEARYGEVARKMAELGDWITPWYDVGVPFWGKPPLAFWLSAGGQLLLG-A 82
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVvfdevhfGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGnV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011    83 NEFASRLPHWLLGVLVLWLVWdWQARE---DRRQARIACVLLGSSALFFVASGAVMTDMALALALVLAMRGFWLGLHGAE 159
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVY-LTAKRlgfSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011   160 GIRRREGWLMFLGLGLGLLAKGPLTLILAGLPIGLWALLEWrWRALWR------GLPWIRGSLLMLLVAAPWYLLAELKT 233
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHL-WQLLGDlslllkSIWKHLFARLFCLIVIPWALYLAQFY 238

                  ....*..
gi 15600011   234 PGFLEYF 240
Cdd:pfam02366 239 VHFWLLF 245
 
Name Accession Description Interval E-value
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
1-246 1.60e-25

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: 106.25  E-value: 1.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011   1 MRALRGWPLAWFLLALAFAIRLLSLGSYPLMDTTEARYGEVARKMAELGDWITPWYDvGVPFWGKPPLAFWLSAGGQLLL 80
Cdd:COG1807   1 MSKTLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREMLESGDWLTPTLA-GEPYFDKPPLIYWLIALSYKLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011  81 GANEFASRLPHWLLGVLVLWLVWDWQAR-EDRRQARIACVLLGSSALFFVASGAVMTDMALALALVLAMRGFWLGLHGAe 159
Cdd:COG1807  80 GVSEFAARLPSALLGLLTVLLVYLLARRlFGRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALYALLRALERR- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011 160 giRRREGWLMFLGLGLGLLAKGPLTLILAGLPIGLWALLEWRWRALWRGLPWIrGSLLMLLVAAPWYLLAELKT-PGFLE 238
Cdd:COG1807 159 --RLRWLLLAGLALGLGFLTKGPVALLLPGLALLLYLLLTRRWRRLRRLRLLL-GLLLALLLALPWYIANDWATgPAFLE 235

                ....*...
gi 15600011 239 YFLLGEHW 246
Cdd:COG1807 236 YFFGYENL 243
arnT PRK13279
lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
10-332 7.03e-10

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


Pssm-ID: 237330 [Multi-domain]  Cd Length: 552  Bit Score: 61.08  E-value: 7.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011   10 AWFLLALAFAI-RLLSLGSYPLMDTTEARYGEVARKMAELGDWITPwYDVGVPFWGKPPLAFWLSAGGQLLLGANEFASR 88
Cdd:PRK13279   7 YLILLALFFALyYLLPLNTRLLWQPDETRYAEISREMLASGDWIVP-HFLGLRYFEKPIAGYWINSIGQWLFGDNNFGVR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011   89 LPHWLLGVLVLWLVWdWQAR---EDRRQARIACVLLGSSALFF-VASGAVMTDMaLALALVLAMRGFWLGLHgAEGIRRR 164
Cdd:PRK13279  86 FGSVFSTLLSALLVY-WLALrlwRDRRTALLAALIYLSLFLVYgIGTYAVLDPM-ITLWLTAAMCSFWLALQ-AQTRRGK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011  165 egwlmflglglgllakgPLTLILAGLPIGL-------------------WALLEWRWRALWRGLPWirGSLLMLLVAAPW 225
Cdd:PRK13279 163 -----------------IGGYLLLGLACGMgfmtkgflalavpvisvlpWVIWQKRWKELLIYGPL--AVLSAVLVSLPW 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011  226 YLLAELKTPGFLEYFLLGEHWQRFvtAGWDGdrygnAHAYPY---------GSV-WLFLLAAAFpwslwlplllWLGWRQ 295
Cdd:PRK13279 224 ALAIAQREPDFWHYFFWVEHIQRF--AEDDA-----QHKAPFwyylpvliaGSLpWLGLLPGAL----------KQGWRE 286
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 15600011  296 RGEvvdgvASRRRYWLFWGLAPCLFFTFAGNVLWTYV 332
Cdd:PRK13279 287 RKK-----HPGTFYLLLWVVMPLLFFSIAKGKLPTYI 318
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
11-240 1.71e-05

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: 46.15  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011    11 WFLLALAFAIRLLSLGSYPLM-------DTTEARYGEVARKMAELGDWITPWYDVGVPFWGKPPLAFWLSAGGQLLLG-A 82
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVvfdevhfGKFASYYAEISFFMDVHPPLGKMLIALGGRLAGYDGNFTFISIGGQYYPGnV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011    83 NEFASRLPHWLLGVLVLWLVWdWQARE---DRRQARIACVLLGSSALFFVASGAVMTDMALALALVLAMRGFWLGLHGAE 159
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVY-LTAKRlgfSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600011   160 GIRRREGWLMFLGLGLGLLAKGPLTLILAGLPIGLWALLEWrWRALWR------GLPWIRGSLLMLLVAAPWYLLAELKT 233
Cdd:pfam02366 160 FSRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLTIWHL-WQLLGDlslllkSIWKHLFARLFCLIVIPWALYLAQFY 238

                  ....*..
gi 15600011   234 PGFLEYF 240
Cdd:pfam02366 239 VHFWLLF 245
 
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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