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Conserved domains on  [gi|2543367230|ref|WP_299255819|]
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glycosyltransferase family 39 protein [uncultured Cytophaga sp.]

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 ...
14-233 9.80e-31

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: 120.88  E-value: 9.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  14 YFLFAILVLYPLLEFLNALPLYLWDESRQAANAIEMFTNHNWLVTYYNGSPdmWNTKPPLLIWLQVLSMHIFGLTTSALR 93
Cdd:COG1807    10 LLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREMLESGDWLTPTLAGEP--YFDKPPLIYWLIALSYKLFGVSEFAAR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  94 APSVIAAFATILSLFFFLKKETNNiWIAFFSGIVLVALPGFNGYhvARTGDYDSLLILFMIQCAIQFYYYIETKNRIHII 173
Cdd:COG1807    88 LPSALLGLLTVLLVYLLARRLFGR-RAALLAALLLLTSPLLLLF--GRLATPDALLLLFWTLALYALLRALERRRLRWLL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543367230 174 LFGLFLTLGSLTKG-IAPLLFLPGFLVYAFFQKKiYAILKDPYFYISCLGYLVIIGSYYIL 233
Cdd:COG1807   165 LAGLALGLGFLTKGpVALLLPGLALLLYLLLTRR-WRRLRRLRLLLGLLLALLLALPWYIA 224
 
Name Accession Description Interval E-value
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
14-233 9.80e-31

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: 120.88  E-value: 9.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  14 YFLFAILVLYPLLEFLNALPLYLWDESRQAANAIEMFTNHNWLVTYYNGSPdmWNTKPPLLIWLQVLSMHIFGLTTSALR 93
Cdd:COG1807    10 LLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREMLESGDWLTPTLAGEP--YFDKPPLIYWLIALSYKLFGVSEFAAR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  94 APSVIAAFATILSLFFFLKKETNNiWIAFFSGIVLVALPGFNGYhvARTGDYDSLLILFMIQCAIQFYYYIETKNRIHII 173
Cdd:COG1807    88 LPSALLGLLTVLLVYLLARRLFGR-RAALLAALLLLTSPLLLLF--GRLATPDALLLLFWTLALYALLRALERRRLRWLL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543367230 174 LFGLFLTLGSLTKG-IAPLLFLPGFLVYAFFQKKiYAILKDPYFYISCLGYLVIIGSYYIL 233
Cdd:COG1807   165 LAGLALGLGFLTKGpVALLLPGLALLLYLLLTRR-WRRLRRLRLLLGLLLALLLALPWYIA 224
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
70-227 1.78e-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: 59.58  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  70 KPPLLIWLQVLSMHIFGLTTSALRAPSVIAAFATILSLFFFLKKETNNiWIAFFSGIVLVALPGFNGYhvARTGDYDSLL 149
Cdd:pfam13231   2 HPPLAAWLIALFTALFGDSEWAVRLPSALAGVLTILLLYLLARRLFGK-RAALLAALLLAVVPLFVAL--SRLFTPDAPL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543367230 150 ILFMIQCAIQFYYYIETKNRIHIILFGLFLTLGSLTKGIAPLLfLPGFLVYAFFQKKiYAILKDPYFYISCLGYLVII 227
Cdd:pfam13231  79 LLFWALALYFLLRALEKGRLKWWLLAGAAAGLGFLSKYTAALL-VLAALLYLLISPG-RRRLKSPKPYLGLLLALLLF 154
arnT PRK13279
lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
16-211 6.98e-08

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


Pssm-ID: 237330 [Multi-domain]  Cd Length: 552  Bit Score: 54.91  E-value: 6.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  16 LFAILVLYPLLEfLNALPLYLWDESRQAANAIEMFTNHNWLVTYYNGSpdMWNTKPPLLIWLQVLSMHIFGLTTSALRAP 95
Cdd:PRK13279   11 LALFFALYYLLP-LNTRLLWQPDETRYAEISREMLASGDWIVPHFLGL--RYFEKPIAGYWINSIGQWLFGDNNFGVRFG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  96 SVIAAFATILSLFFFLKKETNNIWIAFFSGIV-----LVAlpGFNGYHVartgdYDSLLILFMIQCAIQFYYYIETKNR- 169
Cdd:PRK13279   88 SVFSTLLSALLVYWLALRLWRDRRTALLAALIylslfLVY--GIGTYAV-----LDPMITLWLTAAMCSFWLALQAQTRr 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2543367230 170 ---IHIILFGLFLTLGSLTKG-IAPLLFLPGFLVYAFFQKKIYAIL 211
Cdd:PRK13279  161 gkiGGYLLLGLACGMGFMTKGfLALAVPVISVLPWVIWQKRWKELL 206
 
Name Accession Description Interval E-value
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
14-233 9.80e-31

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: 120.88  E-value: 9.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  14 YFLFAILVLYPLLEFLNALPLYLWDESRQAANAIEMFTNHNWLVTYYNGSPdmWNTKPPLLIWLQVLSMHIFGLTTSALR 93
Cdd:COG1807    10 LLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREMLESGDWLTPTLAGEP--YFDKPPLIYWLIALSYKLFGVSEFAAR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  94 APSVIAAFATILSLFFFLKKETNNiWIAFFSGIVLVALPGFNGYhvARTGDYDSLLILFMIQCAIQFYYYIETKNRIHII 173
Cdd:COG1807    88 LPSALLGLLTVLLVYLLARRLFGR-RAALLAALLLLTSPLLLLF--GRLATPDALLLLFWTLALYALLRALERRRLRWLL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2543367230 174 LFGLFLTLGSLTKG-IAPLLFLPGFLVYAFFQKKiYAILKDPYFYISCLGYLVIIGSYYIL 233
Cdd:COG1807   165 LAGLALGLGFLTKGpVALLLPGLALLLYLLLTRR-WRRLRRLRLLLGLLLALLLALPWYIA 224
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
70-227 1.78e-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: 59.58  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  70 KPPLLIWLQVLSMHIFGLTTSALRAPSVIAAFATILSLFFFLKKETNNiWIAFFSGIVLVALPGFNGYhvARTGDYDSLL 149
Cdd:pfam13231   2 HPPLAAWLIALFTALFGDSEWAVRLPSALAGVLTILLLYLLARRLFGK-RAALLAALLLAVVPLFVAL--SRLFTPDAPL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2543367230 150 ILFMIQCAIQFYYYIETKNRIHIILFGLFLTLGSLTKGIAPLLfLPGFLVYAFFQKKiYAILKDPYFYISCLGYLVII 227
Cdd:pfam13231  79 LLFWALALYFLLRALEKGRLKWWLLAGAAAGLGFLSKYTAALL-VLAALLYLLISPG-RRRLKSPKPYLGLLLALLLF 154
arnT PRK13279
lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
16-211 6.98e-08

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


Pssm-ID: 237330 [Multi-domain]  Cd Length: 552  Bit Score: 54.91  E-value: 6.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  16 LFAILVLYPLLEfLNALPLYLWDESRQAANAIEMFTNHNWLVTYYNGSpdMWNTKPPLLIWLQVLSMHIFGLTTSALRAP 95
Cdd:PRK13279   11 LALFFALYYLLP-LNTRLLWQPDETRYAEISREMLASGDWIVPHFLGL--RYFEKPIAGYWINSIGQWLFGDNNFGVRFG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  96 SVIAAFATILSLFFFLKKETNNIWIAFFSGIV-----LVAlpGFNGYHVartgdYDSLLILFMIQCAIQFYYYIETKNR- 169
Cdd:PRK13279   88 SVFSTLLSALLVYWLALRLWRDRRTALLAALIylslfLVY--GIGTYAV-----LDPMITLWLTAAMCSFWLALQAQTRr 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2543367230 170 ---IHIILFGLFLTLGSLTKG-IAPLLFLPGFLVYAFFQKKIYAIL 211
Cdd:PRK13279  161 gkiGGYLLLGLACGMGFMTKGfLALAVPVISVLPWVIWQKRWKELL 206
Stt3 COG1287
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
41-225 1.54e-03

Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 41.32  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  41 RQAANAIEMFTNHNWLVTYYN---GSPdmWNTKPPLLIWLQVLSMHIFGLT--------TSALRAPSVIAAFATIlsLFF 109
Cdd:COG1287    56 RQIEYILANGPSTLPFDPLTWypwGRD--IGQFGPLFDQLIALLALILGLGspsqssvyTVAAWFPPIFGALTVI--PVY 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230 110 FLKKETNNIWIAFFSGIVLVALPGfngyHVART----GDYDSLLILFMIQCAIQFYYYIETKNR------------IHII 173
Cdd:COG1287   132 LLGRRLGGRKAGLLAALLLALSPG----QLSRSllgfADHHVAELFFSTLAVLFLVLALKRAKRekrdlealkrplLYAV 207
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2543367230 174 LFGLFLTLGSLTKGIAPLLFLPgFLVYAFFQKKIYAILKDPYFYISCLGYLV 225
Cdd:COG1287   208 LAGVALGLYLLTWGGYVLFVGI-LALFALLQLLLDLLRGRSPEYLAIVGAVS 258
COG5305 COG5305
Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT ...
71-185 1.82e-03

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: 40.78  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  71 PPLLIWLQVLSMHIFGLTTSALRAPSVIAAFATILSLFFFlkketnnIWIAFFS---GIVLVALPGFNGYHV-----ART 142
Cdd:COG5305    89 PPLYYLLLHLWMQLFGNSEWALRSLSALFGLLAIPLIYWL-------GRELFRSrrvALLAAALMAVSPFHIyyaqeARM 161
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2543367230 143 gdYdSLLILFMIQCAIQFYYYIETKNRIHIILFGLFLTLGSLT 185
Cdd:COG5305   162 --Y-SLLTLLVLLSLLALLRALRRPTRRLWLLYALANALGLYT 201
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
16-202 2.67e-03

Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General function prediction only];


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 40.42  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  16 LFAILVLYPLLEF--LNALPLYlWDESRQAANAIEMFTNHNWlvTY---YNGspdmwntkpPLLIWLQVLSMHIFGLTTS 90
Cdd:COG4745    19 VLAITALALLLRLvgLGARPFH-WDEARVAYWSLRLLETGAY--EYrpiYHG---------PFLYHVTAALFGLFGASDF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2543367230  91 ALRAPSVIAAFATILSLFFFLKKETNN--IWIAFFSGI--VLValpgfngyHVARTGDYDSLLILFMIQCAIQFYYYIET 166
Cdd:COG4745    87 TARLPVALVGGLLPLLALLLRERLGDAevLALALLLAFspVLV--------YYSRFMRNDVLLAAFTLLALGAAVRAIDT 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2543367230 167 KNRIHIILFGLFLTLGSLTKGIAP--LLFLPGFLVYAF 202
Cdd:COG4745   159 RRRRYLYLAAVALALAFATKENAVlyLLCWLGALLLLL 196
 
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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