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Conserved domains on  [gi|2730805882|ref|WP_344923582|]
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phospholipid carrier-dependent glycosyltransferase, partial [Streptosporangium oxazolinicum]

Protein Classification

dolichyl-phosphate-mannose--protein mannosyltransferase( domain architecture ID 1001097)

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 super family cl34376
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
1-167 1.59e-70

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


The actual alignment was detected with superfamily member COG1928:

Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 220.53  E-value: 1.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882   1 HPPLGKWMIGLGEQIFGM-NPYGWRFAGAVVGVLSILILARLARRMTRSTMLGCLAGLLLALDGLHLVLSRTALLDIFLM 79
Cdd:COG1928    79 HPPLGKWLIALGEWLFGYvNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLM 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882  80 FWVLAAFACLVADRDQARGRLVSWYETSPL-SDHGPGLGLRPWRIAAGVCLGAACAVKWSGVFFLVAFAVMSLVWDAGAR 158
Cdd:COG1928   159 FFVLAAFGCLLLDRDQVRRRLAAAVAAGRApSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLYFLAAFGLLTVAWDAGAR 238

                  ....*....
gi 2730805882 159 RAIGLRRPY 167
Cdd:COG1928   239 RAAGVRRPW 247
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
1-167 1.59e-70

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 220.53  E-value: 1.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882   1 HPPLGKWMIGLGEQIFGM-NPYGWRFAGAVVGVLSILILARLARRMTRSTMLGCLAGLLLALDGLHLVLSRTALLDIFLM 79
Cdd:COG1928    79 HPPLGKWLIALGEWLFGYvNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLM 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882  80 FWVLAAFACLVADRDQARGRLVSWYETSPL-SDHGPGLGLRPWRIAAGVCLGAACAVKWSGVFFLVAFAVMSLVWDAGAR 158
Cdd:COG1928   159 FFVLAAFGCLLLDRDQVRRRLAAAVAAGRApSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLYFLAAFGLLTVAWDAGAR 238

                  ....*....
gi 2730805882 159 RAIGLRRPY 167
Cdd:COG1928   239 RAAGVRRPW 247
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
1-155 7.43e-10

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: 55.78  E-value: 7.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882   1 HPPLGKWMIGLGEQIFGMNPYGW------------------RFAGAVVGVLSILILARLARRMTRSTMLGCLAGLLLALD 62
Cdd:pfam02366  45 HPPLGKMLIALGGRLAGYDGNFTfisiggqyypgnvpyfgmRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882  63 GLHLVLSRTALLDIFLMFWVLAAFACLVADRDQARGRLVSWYetsplsdhgpglglrpWRIAAGVCLGAACAVKWSGvFF 142
Cdd:pfam02366 125 NSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPFSRKWWL----------------WLLLTGIALGLALSTKGVG-LF 187
                         170
                  ....*....|...
gi 2730805882 143 LVAFAVMSLVWDA 155
Cdd:pfam02366 188 TVLPVGLLTIWHL 200
arnT PRK13279
lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
2-103 2.42e-05

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


Pssm-ID: 237330 [Multi-domain]  Cd Length: 552  Bit Score: 43.36  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882   2 PPLGKWMIGLGEQIFGMNPYGWRFAGAVVGVLSILILARLARRMTRSTMLGCLAGLLLALDGLHLVLSRTALLDIFLMFW 81
Cdd:PRK13279   63 PIAGYWINSIGQWLFGDNNFGVRFGSVFSTLLSALLVYWLALRLWRDRRTALLAALIYLSLFLVYGIGTYAVLDPMITLW 142
                          90       100
                  ....*....|....*....|....
gi 2730805882  82 VLAAFAC--LVADRDQARGRLVSW 103
Cdd:PRK13279  143 LTAAMCSfwLALQAQTRRGKIGGY 166
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
1-167 1.59e-70

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 220.53  E-value: 1.59e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882   1 HPPLGKWMIGLGEQIFGM-NPYGWRFAGAVVGVLSILILARLARRMTRSTMLGCLAGLLLALDGLHLVLSRTALLDIFLM 79
Cdd:COG1928    79 HPPLGKWLIALGEWLFGYvNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLM 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882  80 FWVLAAFACLVADRDQARGRLVSWYETSPL-SDHGPGLGLRPWRIAAGVCLGAACAVKWSGVFFLVAFAVMSLVWDAGAR 158
Cdd:COG1928   159 FFVLAAFGCLLLDRDQVRRRLAAAVAAGRApSRWGPRLGFRWWRLAAGVLLGLACGVKWSGLYFLAAFGLLTVAWDAGAR 238

                  ....*....
gi 2730805882 159 RAIGLRRPY 167
Cdd:COG1928   239 RAAGVRRPW 247
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
1-148 2.32e-11

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


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 60.78  E-value: 2.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882   1 HPPLGKWMIGLGEQIFGMNPYGWRFAGAVVGVLSILILARLARRMTRSTMLGCLAGLLLALDGLHLVLSRTALLDIFLMF 80
Cdd:COG4346    79 HPPLGKYIIALSMLLLGDKPLYWRLPSIILGALIVILVFLTARRLSGNIVAGLIASLLLALDPLLRVMSSIAMLDIYVAF 158
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2730805882  81 WVLAAFACLVADRdqargrlvswyetsplsdhgpglglrpwRIAAGVCLGAACAVKWSGVFFLVAFAV 148
Cdd:COG4346   159 FTALALYFAVSGR----------------------------LLLSSIALGLAAASKYSGLFLLIPLLL 198
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
1-155 7.43e-10

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: 55.78  E-value: 7.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882   1 HPPLGKWMIGLGEQIFGMNPYGW------------------RFAGAVVGVLSILILARLARRMTRSTMLGCLAGLLLALD 62
Cdd:pfam02366  45 HPPLGKMLIALGGRLAGYDGNFTfisiggqyypgnvpyfgmRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882  63 GLHLVLSRTALLDIFLMFWVLAAFACLVADRDQARGRLVSWYetsplsdhgpglglrpWRIAAGVCLGAACAVKWSGvFF 142
Cdd:pfam02366 125 NSFITLSRYILLDSPLLFFTTLSMYCFWKFERKAPFSRKWWL----------------WLLLTGIALGLALSTKGVG-LF 187
                         170
                  ....*....|...
gi 2730805882 143 LVAFAVMSLVWDA 155
Cdd:pfam02366 188 TVLPVGLLTIWHL 200
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
1-167 7.54e-09

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: 53.47  E-value: 7.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882   1 HPPLGKWMIGLGEQIFGMNPYGWRFAGAVVGVLSILILARLARRMTrSTMLGCLAGLLLALDGLHLVLSRTALLDIFLMF 80
Cdd:COG1807    64 KPPLIYWLIALSYKLFGVSEFAARLPSALLGLLTVLLVYLLARRLF-GRRAALLAALLLLTSPLLLLFGRLATPDALLLL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882  81 WVLAAFACLVADRDQARGRlvswyetsplsdhgpglglrpWRIAAGVCLGAACAVKWSGVFFLVAFAVMSLVWDAGARRA 160
Cdd:COG1807   143 FWTLALYALLRALERRRLR---------------------WLLLAGLALGLGFLTKGPVALLLPGLALLLYLLLTRRWRR 201

                  ....*..
gi 2730805882 161 IGLRRPY 167
Cdd:COG1807   202 LRRLRLL 208
arnT PRK13279
lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
2-103 2.42e-05

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


Pssm-ID: 237330 [Multi-domain]  Cd Length: 552  Bit Score: 43.36  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882   2 PPLGKWMIGLGEQIFGMNPYGWRFAGAVVGVLSILILARLARRMTRSTMLGCLAGLLLALDGLHLVLSRTALLDIFLMFW 81
Cdd:PRK13279   63 PIAGYWINSIGQWLFGDNNFGVRFGSVFSTLLSALLVYWLALRLWRDRRTALLAALIYLSLFLVYGIGTYAVLDPMITLW 142
                          90       100
                  ....*....|....*....|....
gi 2730805882  82 VLAAFAC--LVADRDQARGRLVSW 103
Cdd:PRK13279  143 LTAAMCSfwLALQAQTRRGKIGGY 166
PMT_2 pfam13231
Dolichyl-phosphate-mannose-protein mannosyltransferase; This family contains members that are ...
1-167 1.24e-04

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: 40.32  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882   1 HPPLGKWMIGLGEQIFGMNPYGWRFAGAVVGVLSILILARLARRMTrSTMLGCLAGLLLALDGLHLVLSRTALLDI-FLM 79
Cdd:pfam13231   2 HPPLAAWLIALFTALFGDSEWAVRLPSALAGVLTILLLYLLARRLF-GKRAALLAALLLAVVPLFVALSRLFTPDApLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730805882  80 FWVLAAFACL-VADRDQARgrlvswyetsplsdhgpglglrpWRIAAGVCLGAACAVKWSGVFFLVAFAVMsLVWDaGAR 158
Cdd:pfam13231  81 FWALALYFLLrALEKGRLK-----------------------WWLLAGAAAGLGFLSKYTAALLVLAALLY-LLIS-PGR 135

                  ....*....
gi 2730805882 159 RAIGLRRPY 167
Cdd:pfam13231 136 RRLKSPKPY 144
 
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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