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Conserved domains on  [gi|752744720|ref|WP_041391842|]
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dolichyl-phosphate-mannose--protein mannosyltransferase [Pleurocapsa sp. PCC 7327]

Protein Classification

dolichyl-phosphate-mannose--protein mannosyltransferase( domain architecture ID 11449133)

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 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
17-460 9.09e-136

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


:

Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 400.04  E-value: 9.09e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  17 SWFWMAIAILLATSLALRFWELGRFNQLVFDEVYYVKYAQNYLSR---------TPFFDVHPPLGKYLIAFGIWVsklhf 87
Cdd:COG1928   19 LRGWLGTLLVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPLGKWLIALGEWL----- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  88 wnpTGQTTAFGYRWLNALTGSLILLIVAGIAYQLSYRRSYAFIAAWFACADGLLLVESRYAFLNIYLVFFGLLAQWCFLI 167
Cdd:COG1928   94 ---FGYVNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGCLLL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 168 ALAQK-------------------SLLRWLYLVLAGIFFGCSAAVKWYGLGFWLGIGAVWasariVSWWQRDRKLSFNQP 228
Cdd:COG1928  171 DRDQVrrrlaaavaagrapsrwgpRLGFRWWRLAAGVLLGLACGVKWSGLYFLAAFGLLT-----VAWDAGARRAAGVRR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 229 FWQNLSKFKLWPLLVFLGVIPVVVYCLLWIPHWQLDRD---------------------RGFWELHQKSWTFHQQLgssS 287
Cdd:COG1928  246 PWLGALLRDGIPAFFALVIVPLLTYLASWTGWFASDTGydrhwaaqnpgsglgwvpdalRSLWHYHQQILSFHTGL---S 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 288 QIHPYCSPWYSWVLMVRPVAYFFEKSGN-----SAQSTVYDVHGMGNPILWWLGTIAMLILVGKIAQQvypiqkkrqref 362
Cdd:COG1928  323 SPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcGAGKCVRAVLAIGNPALWWLGLPALLWLLWRWIAR------------ 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 363 DFSIPLYLLLNYGANWLPWMLV-HRCAFLYYYMPASIFGFLAIAYLVDRWLYSDNLWWRAIAINIIFFILMGL-----AY 436
Cdd:COG1928  391 RDWRAGAVLVGYAAGWLPWFLYlDRTMFFFYAIPFVPFLVLALALVLGLILGPARASERRRLGRLVVGLYVGLvvanfAF 470
                        490       500
                 ....*....|....*....|....
gi 752744720 437 WLPIYLGLPLSREAFDHRMWFRSW 460
Cdd:COG1928  471 FYPILTGLPIPYDEWQARMWFPSW 494
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
17-460 9.09e-136

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 400.04  E-value: 9.09e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  17 SWFWMAIAILLATSLALRFWELGRFNQLVFDEVYYVKYAQNYLSR---------TPFFDVHPPLGKYLIAFGIWVsklhf 87
Cdd:COG1928   19 LRGWLGTLLVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPLGKWLIALGEWL----- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  88 wnpTGQTTAFGYRWLNALTGSLILLIVAGIAYQLSYRRSYAFIAAWFACADGLLLVESRYAFLNIYLVFFGLLAQWCFLI 167
Cdd:COG1928   94 ---FGYVNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGCLLL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 168 ALAQK-------------------SLLRWLYLVLAGIFFGCSAAVKWYGLGFWLGIGAVWasariVSWWQRDRKLSFNQP 228
Cdd:COG1928  171 DRDQVrrrlaaavaagrapsrwgpRLGFRWWRLAAGVLLGLACGVKWSGLYFLAAFGLLT-----VAWDAGARRAAGVRR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 229 FWQNLSKFKLWPLLVFLGVIPVVVYCLLWIPHWQLDRD---------------------RGFWELHQKSWTFHQQLgssS 287
Cdd:COG1928  246 PWLGALLRDGIPAFFALVIVPLLTYLASWTGWFASDTGydrhwaaqnpgsglgwvpdalRSLWHYHQQILSFHTGL---S 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 288 QIHPYCSPWYSWVLMVRPVAYFFEKSGN-----SAQSTVYDVHGMGNPILWWLGTIAMLILVGKIAQQvypiqkkrqref 362
Cdd:COG1928  323 SPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcGAGKCVRAVLAIGNPALWWLGLPALLWLLWRWIAR------------ 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 363 DFSIPLYLLLNYGANWLPWMLV-HRCAFLYYYMPASIFGFLAIAYLVDRWLYSDNLWWRAIAINIIFFILMGL-----AY 436
Cdd:COG1928  391 RDWRAGAVLVGYAAGWLPWFLYlDRTMFFFYAIPFVPFLVLALALVLGLILGPARASERRRLGRLVVGLYVGLvvanfAF 470
                        490       500
                 ....*....|....*....|....
gi 752744720 437 WLPIYLGLPLSREAFDHRMWFRSW 460
Cdd:COG1928  471 FYPILTGLPIPYDEWQARMWFPSW 494
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
269-458 8.72e-37

C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes.


Pssm-ID: 465056  Cd Length: 198  Bit Score: 133.82  E-value: 8.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  269 FWELHQKSWTFHQQLGSSsqiHPYCSPWYSWVLMVRPVAYFFEKSGNsaqstvYDVHGMGNPILWWLGTIAMLILVGKIA 348
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPS---HPYASRPWEWPLLLRGIRFWGWDDRN------AQIYLLGNPVIWWSSTAAILVFVLLLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  349 -------QQVYPIQKKRQREFDFSIPLYLLLNYGANWLPWMLVHRCAFLYYYMPASIFGFLAIAYLVDRWLYSDNLWWRA 421
Cdd:pfam16192  74 ayllrwqRGYYDLSDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRS 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 752744720  422 IAINIIFFILMGLA--------YWLPIYLGLPLSREAFDHRMWFR 458
Cdd:pfam16192 154 LRKRVGYAIVVVLLalviyvfiYFSPLTYGMPGTSEECKKLKWLS 198
 
Name Accession Description Interval E-value
PMT1 COG1928
Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, ...
17-460 9.09e-136

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


Pssm-ID: 441531 [Multi-domain]  Cd Length: 495  Bit Score: 400.04  E-value: 9.09e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  17 SWFWMAIAILLATSLALRFWELGRFNQLVFDEVYYVKYAQNYLSR---------TPFFDVHPPLGKYLIAFGIWVsklhf 87
Cdd:COG1928   19 LRGWLGTLLVTLLAGVLRFWGLGRPNTLVFDETYYVKDAWSLLTNgyernwpdpGPFFVVHPPLGKWLIALGEWL----- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  88 wnpTGQTTAFGYRWLNALTGSLILLIVAGIAYQLSYRRSYAFIAAWFACADGLLLVESRYAFLNIYLVFFGLLAQWCFLI 167
Cdd:COG1928   94 ---FGYVNPFGWRFAAALAGTLSVLLVARIARRLTRSTLLGAIAGLLLALDGLHLVLSRTALLDIFLMFFVLAAFGCLLL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 168 ALAQK-------------------SLLRWLYLVLAGIFFGCSAAVKWYGLGFWLGIGAVWasariVSWWQRDRKLSFNQP 228
Cdd:COG1928  171 DRDQVrrrlaaavaagrapsrwgpRLGFRWWRLAAGVLLGLACGVKWSGLYFLAAFGLLT-----VAWDAGARRAAGVRR 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 229 FWQNLSKFKLWPLLVFLGVIPVVVYCLLWIPHWQLDRD---------------------RGFWELHQKSWTFHQQLgssS 287
Cdd:COG1928  246 PWLGALLRDGIPAFFALVIVPLLTYLASWTGWFASDTGydrhwaaqnpgsglgwvpdalRSLWHYHQQILSFHTGL---S 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 288 QIHPYCSPWYSWVLMVRPVAYFFEKSGN-----SAQSTVYDVHGMGNPILWWLGTIAMLILVGKIAQQvypiqkkrqref 362
Cdd:COG1928  323 SPHPYESKPWSWPLMLRPVSYYYETGQTgtlgcGAGKCVRAVLAIGNPALWWLGLPALLWLLWRWIAR------------ 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 363 DFSIPLYLLLNYGANWLPWMLV-HRCAFLYYYMPASIFGFLAIAYLVDRWLYSDNLWWRAIAINIIFFILMGL-----AY 436
Cdd:COG1928  391 RDWRAGAVLVGYAAGWLPWFLYlDRTMFFFYAIPFVPFLVLALALVLGLILGPARASERRRLGRLVVGLYVGLvvanfAF 470
                        490       500
                 ....*....|....*....|....
gi 752744720 437 WLPIYLGLPLSREAFDHRMWFRSW 460
Cdd:COG1928  471 FYPILTGLPIPYDEWQARMWFPSW 494
PMT_4TMC pfam16192
C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four ...
269-458 8.72e-37

C-terminal four TMM region of protein-O-mannosyltransferase; PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes.


Pssm-ID: 465056  Cd Length: 198  Bit Score: 133.82  E-value: 8.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  269 FWELHQKSWTFHQQLGSSsqiHPYCSPWYSWVLMVRPVAYFFEKSGNsaqstvYDVHGMGNPILWWLGTIAMLILVGKIA 348
Cdd:pfam16192   3 FIELQKAMLTSNNGLTPS---HPYASRPWEWPLLLRGIRFWGWDDRN------AQIYLLGNPVIWWSSTAAILVFVLLLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  349 -------QQVYPIQKKRQREFDFSIPLYLLLNYGANWLPWMLVHRCAFLYYYMPASIFGFLAIAYLVDRWLYSDNLWWRA 421
Cdd:pfam16192  74 ayllrwqRGYYDLSDDWTRSRFYYSGGFLLLGWALHYLPFFLMGRQLFLHHYLPALYFAILALGALLDFLLSLFRRLPRS 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 752744720  422 IAINIIFFILMGLA--------YWLPIYLGLPLSREAFDHRMWFR 458
Cdd:pfam16192 154 LRKRVGYAIVVVLLalviyvfiYFSPLTYGMPGTSEECKKLKWLS 198
PMT pfam02366
Dolichyl-phosphate-mannose-protein mannosyltransferase; This is a family of ...
24-263 7.72e-28

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: 110.86  E-value: 7.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720   24 AILLATSLALRFWELGRFNQLVFDEVYYVKYAQNYLSRTPFFDVHPPLGKYLIAFGIWVS--KLHFWNPT-------GQT 94
Cdd:pfam02366   1 VILTLLAFLIRFWNLYNPNLVVFDEVHFGKFASYYAEISFFMDVHPPLGKMLIALGGRLAgyDGNFTFISiggqyypGNV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720   95 TAFGYRWLNALTGSLILLIVAGIAYQLSYRRSYAFIAAWFACADGLLLVESRYAFLNIYLVFFGLLAQWCFLIALAQK-- 172
Cdd:pfam02366  81 PYFGMRLFSALLGSLTVPLVYLTAKRLGFSKNTALLAALLVILENSFITLSRYILLDSPLLFFTTLSMYCFWKFERKApf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  173 SLLRWLYLVLAGIFFGCSAAVKWYGLGFWLGIGAVWasarIVSWWQRDRKLSfnqpfWQNLSKFKLW-PLLVFLGVIPVV 251
Cdd:pfam02366 161 SRKWWLWLLLTGIALGLALSTKGVGLFTVLPVGLLT----IWHLWQLLGDLS-----LLLKSIWKHLfARLFCLIVIPWA 231
                         250
                  ....*....|..
gi 752744720  252 VYCLLWIPHWQL 263
Cdd:pfam02366 232 LYLAQFYVHFWL 243
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
19-420 7.52e-11

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


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 63.47  E-value: 7.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  19 FWMAIAILLATSLALRFWELGR--FNQLVFDEVYYVKYAQNYLS-------RTPFFDV----------HPPLGKYLIAFG 79
Cdd:COG4346   11 ILIALAVLISLYTYYTASTFKApgGNGYVSDEVWYVSAARNILRkvfgltpRYPYPDKenintylnleHPPLGKYIIALS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  80 IWvsklhfwnptgqttAFGYRWLN-----ALTGSLILLIVAGIAYQLSYRRSYAFIAAWFACADGLLLVESRYAFLNIYL 154
Cdd:COG4346   91 ML--------------LLGDKPLYwrlpsIILGALIVILVFLTARRLSGNIVAGLIASLLLALDPLLRVMSSIAMLDIYV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 155 VFFGLLAqwcFLIALAQKsllrwlyLVLAGIFFGCSAAVKWYGLGFWLgigAVWASARIvswWQRDRKLSFnqpfwqnls 234
Cdd:COG4346  157 AFFTALA---LYFAVSGR-------LLLSSIALGLAAASKYSGLFLLI---PLLLYLRE---IEKSPIKRF--------- 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 235 kfklwpllVFLGVIPVVVYCLLWIPhwqLDRDRGFwelhqkSWTFHQQLG------SSSQIHPYCSPWYSWVLMVRPVAY 308
Cdd:COG4346  212 --------LYGILIPLAVFLIVSIP---LIIYFGF------GRWLQEFLGalkwhtTSRPPGPPASTPWDWFLGVNPFPL 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 309 FFEKsgnsaqstvyDVHGMGNPILWWLGTIAMLILvgkiaqqvYPIQKKRQREfdFSIPLYLLLNYGANWLPWMLVHRCA 388
Cdd:COG4346  275 YYNP----------DLYASTNPVIMILALVSTLLL--------FPAYLKDKKL--AIASVFLWSIFLGYALVYLLGNHTL 334
                        410       420       430
                 ....*....|....*....|....*....|....
gi 752744720 389 FLYYYMPASIFGFLAIAYLVDRWLYSDNL--WWR 420
Cdd:COG4346  335 YSFYVVQLAPLAAVYLAVSLFLLIKWDYLisWAG 368
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
17-230 7.42e-10

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: 60.02  E-value: 7.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  17 SWFWMAIAILLATSLALRFWELGRFNQLVFDEVYYVKYAQNYLSR----------TPFFDvHPPLGKYLIAFGIWVsklh 86
Cdd:COG1807    4 TLSARPLLLLLLLALLLRLLGLGSLPLWDPDEARYAEIAREMLESgdwltptlagEPYFD-KPPLIYWLIALSYKL---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  87 fwnptGQTTAFGYRWLNALTGSLILLIVAGIAYQLsYRRSYAFIAAWFACADGLLLVESRYAFLNIYLVFFGLLAQWCFL 166
Cdd:COG1807   79 -----FGVSEFAARLPSALLGLLTVLLVYLLARRL-FGRRAALLAALLLLTSPLLLLFGRLATPDALLLLFWTLALYALL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 752744720 167 IALAQKsllRWLYLVLAGIFFGCSAAVKWYGLGFWLGIGAVwasarIVSWWQRDRKLSFNQPFW 230
Cdd:COG1807  153 RALERR---RLRWLLLAGLALGLGFLTKGPVALLLPGLALL-----LYLLLTRRWRRLRRLRLL 208
PMT COG4745
Predicted membrane-bound mannosyltransferase, involved in protein glycosylation [General ...
15-264 3.46e-05

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


Pssm-ID: 443779 [Multi-domain]  Cd Length: 550  Bit Score: 46.20  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  15 APSWFWMAIAILLATSLALRFWELGrFNQLVFDEVYYVKYAQNYLSRTPF-FD--VHPPLGKYL--IAFGIWvsklhfwn 89
Cdd:COG4745   11 RRDRTLLAVLAITALALLLRLVGLG-ARPFHWDEARVAYWSLRLLETGAYeYRpiYHGPFLYHVtaALFGLF-------- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  90 PTGQTTAfgyRWLNALTGSLILLIVAGIAYQLsyRRSYAFIAAWFACADGLLLVESRYAFLNIYLVFFGLLAQWCFLIAL 169
Cdd:COG4745   82 GASDFTA---RLPVALVGGLLPLLALLLRERL--GDAEVLALALLLAFSPVLVYYSRFMRNDVLLAAFTLLALGAAVRAI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720 170 AQKsllRWLYLVLAGIFFGCSAAVKwyglGFWLGIGAVWASARIVSWWQRDRKLSFNQPFWQNLSK------------FK 237
Cdd:COG4745  157 DTR---RRRYLYLAAVALALAFATK----ENAVLYLLCWLGALLLLLDHRLFRARRRGTSVLLVLRrlrrlvrrlrllLR 229
                        250       260
                 ....*....|....*....|....*..
gi 752744720 238 LWPLLVFLGVIPVVVYCLLWIPHWQLD 264
Cdd:COG4745  230 WWRHLVGALAVFLAVAVFFYAPRGGPG 256
COG5305 COG5305
Uncharacterized membrane protein PF0508, contains N-terminal glycosyltransferase domain of PMT ...
7-186 8.17e-04

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: 41.55  E-value: 8.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720   7 TKIRSFFFAPSWFWMAIAILLATSLALRFWELGR------------------FNQLVFDEVYYVKYAQN-------YLSR 61
Cdd:COG5305    2 SFSLLKSRRPRWLRLLLLLILLLGIALRFANLDRkslwydeaatllrslgytFAEVPLDQIISLEELLNaerslgdLIRA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 752744720  62 TPFFDVHPPLgKYLIafgiwvskLHFWNPTGQTTAFGYRWLNALTGSLILLIVAGIAYQLSYRRSYAFIAAWFACADGLL 141
Cdd:COG5305   82 LAEEDAHPPL-YYLL--------LHLWMQLFGNSEWALRSLSALFGLLAIPLIYWLGRELFRSRRVALLAAALMAVSPFH 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 752744720 142 LVESRYAFLNIYLVFFGLLAQWCFLIALAQKSLLRWLYLVLAGIF 186
Cdd:COG5305  153 IYYAQEARMYSLLTLLVLLSLLALLRALRRPTRRLWLLYALANAL 197
 
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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