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Conserved domains on  [gi|1309054202|gb|PKP42196|]
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hypothetical protein CVT93_05900 [Bacteroidetes bacterium HGW-Bacteroidetes-10]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
55-225 9.31e-19

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: 83.47  E-value: 9.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202  55 DHPPMIGWFIQLFTvNLSFGGELFLRLASIVTGTVNTWIIFVLGRRIKNDLTGIYAALLYTASAYAsIFIGTFINPDTPQ 134
Cdd:pfam13231   1 DHPPLAAWLIALFT-ALFGDSEWAVRLPSALAGVLTILLLYLLARRLFGKRAALLAALLLAVVPLF-VALSRLFTPDAPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 135 SLFYLLSlyflhegLITKYETCEETRTLcrlALVIAGIFIGLAMLSKYSSVFLWFGVAVYAL-SYDRSLLKKPFIYISVI 213
Cdd:pfam13231  79 LLFWALA-------LYFLLRALEKGRLK---WWLLAGAAAGLGFLSKYTAALLVLAALLYLLiSPGRRRLKSPKPYLGLL 148
                         170
                  ....*....|..
gi 1309054202 214 ISGLFMIPVLMW 225
Cdd:pfam13231 149 LALLLFSPVLIW 160
Stt3 super family cl39129
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
94-363 3.76e-03

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


The actual alignment was detected with superfamily member COG1287:

Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 40.16  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202  94 IFVLGRRIKNDLTGIYAALLYtASAYASIFIGTFINPD--TPQSLFYLLSLYFLHEGLITKYETCEETRTLCRLAL--VI 169
Cdd:COG1287   130 VYLLGRRLGGRKAGLLAALLL-ALSPGQLSRSLLGFADhhVAELFFSTLAVLFLVLALKRAKREKRDLEALKRPLLyaVL 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 170 AGIFIGLAMLSKYSSVFLWFGVAVYAL---SYDRSLLKKP--FIYISVIISGLFMIPVLMWnLENNFISF----AFQGSR 240
Cdd:COG1287   209 AGVALGLYLLTWGGYVLFVGILALFALlqlLLDLLRGRSPeyLAIVGAVSFAVAALLVLPF-IPRLGFSGtglsLLQPLL 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 241 LLSFENGLDIELFI-RAIAGTLI--FNNPVTIILIIASVIAFrkrKYISVPQ-YRLMISLSLPMIIFFLMVSLFTEARP- 315
Cdd:COG1287   288 ALALAAGTVFLAWLaRELERRDLprLYYPAALVGLVAAGLAL---LAVLLPRvLAALIPGLRRFFGASALAATIAEAQPl 364
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1309054202 316 ------HWTAPGFFpLILVAAAYLASKYEqRNIRKMIMPAPVVNAFSFLFLLTA 363
Cdd:COG1287   365 tlsdlfSSFGIAFF-LALIGLLLLLYRPL-RERRPELLFLLVWALFSIYAAFTQ 416
 
Name Accession Description Interval E-value
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
55-225 9.31e-19

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: 83.47  E-value: 9.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202  55 DHPPMIGWFIQLFTvNLSFGGELFLRLASIVTGTVNTWIIFVLGRRIKNDLTGIYAALLYTASAYAsIFIGTFINPDTPQ 134
Cdd:pfam13231   1 DHPPLAAWLIALFT-ALFGDSEWAVRLPSALAGVLTILLLYLLARRLFGKRAALLAALLLAVVPLF-VALSRLFTPDAPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 135 SLFYLLSlyflhegLITKYETCEETRTLcrlALVIAGIFIGLAMLSKYSSVFLWFGVAVYAL-SYDRSLLKKPFIYISVI 213
Cdd:pfam13231  79 LLFWALA-------LYFLLRALEKGRLK---WWLLAGAAAGLGFLSKYTAALLVLAALLYLLiSPGRRRLKSPKPYLGLL 148
                         170
                  ....*....|..
gi 1309054202 214 ISGLFMIPVLMW 225
Cdd:pfam13231 149 LALLLFSPVLIW 160
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
8-367 3.08e-16

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: 79.67  E-value: 3.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202   8 DSTFKKYLFALMAVSALIRAALAWSLDL-GANEAYYWTYGAN------------PDISHIDHPPMIGWFIQLFTvNLSFG 74
Cdd:COG1807     3 KTLSARPLLLLLLLALLLRLLGLGSLPLwDPDEARYAEIAREmlesgdwltptlAGEPYFDKPPLIYWLIALSY-KLFGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202  75 GELFLRLASIVTGTVNTWIIFVLGRRIKNDLTGIYAALLYTASAYAsIFIGTFINPDTPQSLFYLLSLYFLHEGLITKYe 154
Cdd:COG1807    82 SEFAARLPSALLGLLTVLLVYLLARRLFGRRAALLAALLLLTSPLL-LLFGRLATPDALLLLFWTLALYALLRALERRR- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 155 tceetrtlcRLALVIAGIFIGLAMLSKYSSVFLWFGVAV---YALSYDRSLLKKPFIYISVIISGLFMIPvlmWNLENNF 231
Cdd:COG1807   160 ---------LRWLLLAGLALGLGFLTKGPVALLLPGLALllyLLLTRRWRRLRRLRLLLGLLLALLLALP---WYIANDW 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 232 ISFAfqgsrllsfengldielfiRAIAGTLIFNNpvtiiliiasviafrkrkyisvpqyrlmislslpmIIFFLMVSLFT 311
Cdd:COG1807   228 ATGP-------------------AFLEYFFGYEN-----------------------------------LVPLLFFSLSA 253
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054202 312 EARPHWTAPGFFPLILVAAAYLASKYEQRNIRKMIMPAPVVNAFSFLFLLTALGIM 367
Cdd:COG1807   254 TKLPRYLLPLLPALALLAAAGLARLRRRRRALLLLALVLLLALLIALLLALAALAL 309
Stt3 COG1287
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
94-363 3.76e-03

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


Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 40.16  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202  94 IFVLGRRIKNDLTGIYAALLYtASAYASIFIGTFINPD--TPQSLFYLLSLYFLHEGLITKYETCEETRTLCRLAL--VI 169
Cdd:COG1287   130 VYLLGRRLGGRKAGLLAALLL-ALSPGQLSRSLLGFADhhVAELFFSTLAVLFLVLALKRAKREKRDLEALKRPLLyaVL 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 170 AGIFIGLAMLSKYSSVFLWFGVAVYAL---SYDRSLLKKP--FIYISVIISGLFMIPVLMWnLENNFISF----AFQGSR 240
Cdd:COG1287   209 AGVALGLYLLTWGGYVLFVGILALFALlqlLLDLLRGRSPeyLAIVGAVSFAVAALLVLPF-IPRLGFSGtglsLLQPLL 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 241 LLSFENGLDIELFI-RAIAGTLI--FNNPVTIILIIASVIAFrkrKYISVPQ-YRLMISLSLPMIIFFLMVSLFTEARP- 315
Cdd:COG1287   288 ALALAAGTVFLAWLaRELERRDLprLYYPAALVGLVAAGLAL---LAVLLPRvLAALIPGLRRFFGASALAATIAEAQPl 364
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1309054202 316 ------HWTAPGFFpLILVAAAYLASKYEqRNIRKMIMPAPVVNAFSFLFLLTA 363
Cdd:COG1287   365 tlsdlfSSFGIAFF-LALIGLLLLLYRPL-RERRPELLFLLVWALFSIYAAFTQ 416
 
Name Accession Description Interval E-value
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
55-225 9.31e-19

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: 83.47  E-value: 9.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202  55 DHPPMIGWFIQLFTvNLSFGGELFLRLASIVTGTVNTWIIFVLGRRIKNDLTGIYAALLYTASAYAsIFIGTFINPDTPQ 134
Cdd:pfam13231   1 DHPPLAAWLIALFT-ALFGDSEWAVRLPSALAGVLTILLLYLLARRLFGKRAALLAALLLAVVPLF-VALSRLFTPDAPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 135 SLFYLLSlyflhegLITKYETCEETRTLcrlALVIAGIFIGLAMLSKYSSVFLWFGVAVYAL-SYDRSLLKKPFIYISVI 213
Cdd:pfam13231  79 LLFWALA-------LYFLLRALEKGRLK---WWLLAGAAAGLGFLSKYTAALLVLAALLYLLiSPGRRRLKSPKPYLGLL 148
                         170
                  ....*....|..
gi 1309054202 214 ISGLFMIPVLMW 225
Cdd:pfam13231 149 LALLLFSPVLIW 160
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
8-367 3.08e-16

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: 79.67  E-value: 3.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202   8 DSTFKKYLFALMAVSALIRAALAWSLDL-GANEAYYWTYGAN------------PDISHIDHPPMIGWFIQLFTvNLSFG 74
Cdd:COG1807     3 KTLSARPLLLLLLLALLLRLLGLGSLPLwDPDEARYAEIAREmlesgdwltptlAGEPYFDKPPLIYWLIALSY-KLFGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202  75 GELFLRLASIVTGTVNTWIIFVLGRRIKNDLTGIYAALLYTASAYAsIFIGTFINPDTPQSLFYLLSLYFLHEGLITKYe 154
Cdd:COG1807    82 SEFAARLPSALLGLLTVLLVYLLARRLFGRRAALLAALLLLTSPLL-LLFGRLATPDALLLLFWTLALYALLRALERRR- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 155 tceetrtlcRLALVIAGIFIGLAMLSKYSSVFLWFGVAV---YALSYDRSLLKKPFIYISVIISGLFMIPvlmWNLENNF 231
Cdd:COG1807   160 ---------LRWLLLAGLALGLGFLTKGPVALLLPGLALllyLLLTRRWRRLRRLRLLLGLLLALLLALP---WYIANDW 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 232 ISFAfqgsrllsfengldielfiRAIAGTLIFNNpvtiiliiasviafrkrkyisvpqyrlmislslpmIIFFLMVSLFT 311
Cdd:COG1807   228 ATGP-------------------AFLEYFFGYEN-----------------------------------LVPLLFFSLSA 253
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054202 312 EARPHWTAPGFFPLILVAAAYLASKYEQRNIRKMIMPAPVVNAFSFLFLLTALGIM 367
Cdd:COG1807   254 TKLPRYLLPLLPALALLAAAGLARLRRRRRALLLLALVLLLALLIALLLALAALAL 309
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
170-221 2.84e-03

Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 39.98  E-value: 2.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1309054202 170 AGIFIGLAMLSKYSSVFLWFGVAVYALSYDRSLLKKpFIYISVIISGLFMIP 221
Cdd:COG4346   175 SSIALGLAAASKYSGLFLLIPLLLYLREIEKSPIKR-FLYGILIPLAVFLIV 225
Stt3 COG1287
Asparagine N-glycosylation enzyme, membrane subunit Stt3 [Posttranslational modification, ...
94-363 3.76e-03

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


Pssm-ID: 440898 [Multi-domain]  Cd Length: 774  Bit Score: 40.16  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202  94 IFVLGRRIKNDLTGIYAALLYtASAYASIFIGTFINPD--TPQSLFYLLSLYFLHEGLITKYETCEETRTLCRLAL--VI 169
Cdd:COG1287   130 VYLLGRRLGGRKAGLLAALLL-ALSPGQLSRSLLGFADhhVAELFFSTLAVLFLVLALKRAKREKRDLEALKRPLLyaVL 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 170 AGIFIGLAMLSKYSSVFLWFGVAVYAL---SYDRSLLKKP--FIYISVIISGLFMIPVLMWnLENNFISF----AFQGSR 240
Cdd:COG1287   209 AGVALGLYLLTWGGYVLFVGILALFALlqlLLDLLRGRSPeyLAIVGAVSFAVAALLVLPF-IPRLGFSGtglsLLQPLL 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054202 241 LLSFENGLDIELFI-RAIAGTLI--FNNPVTIILIIASVIAFrkrKYISVPQ-YRLMISLSLPMIIFFLMVSLFTEARP- 315
Cdd:COG1287   288 ALALAAGTVFLAWLaRELERRDLprLYYPAALVGLVAAGLAL---LAVLLPRvLAALIPGLRRFFGASALAATIAEAQPl 364
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1309054202 316 ------HWTAPGFFpLILVAAAYLASKYEqRNIRKMIMPAPVVNAFSFLFLLTA 363
Cdd:COG1287   365 tlsdlfSSFGIAFF-LALIGLLLLLYRPL-RERRPELLFLLVWALFSIYAAFTQ 416
 
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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