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Conserved domains on  [gi|544824155|ref|WP_021240158|]
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MULTISPECIES: glycosyltransferase [Enterobacter]

Protein Classification

CESA_CelA_like domain-containing protein; cellulose synthase catalytic subunit; cellulose synthase catalytic subunit( domain architecture ID 10157530)

CESA_CelA_like domain-containing protein; cellulose synthase catalytic subunit is a glycosyltransferase family protein that is part of the cellulose synthase complex in the bacterial membrane, which polymerizes UDP-glucose to cellulose; cellulose synthase catalytic subunit is part of the cellulose synthase complex in the bacterial membrane, which polymerizes UDP-glucose to cellulose; cellulose synthase catalytic subunit is part of the cellulose synthase complex in the bacterial membrane, which polymerizes UDP-glucose to cellulose

Gene Ontology:  GO:0016759|GO:0030244|GO:0016757
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
110-412 1.42e-75

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


:

Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 240.55  E-value: 1.42e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 110 KVDLFIATYSEDTELVRLSIRDALKMAYPfPIDYRIHVLDDGRRPEMKAVCEEEGV----NYITRQTNIGFKAGNLRNGL 185
Cdd:cd06421    2 TVDVFIPTYNEPLEIVRKTLRAALAIDYP-HDKLRVYVLDDGRRPELRALAAELGVeygyRYLTRPDNRHAKAGNLNNAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 186 EQTDGDFIVICDADTRVFPTLLSHTLGYFRD-PDVAWVQTPQWFFDLPEGENLSRwgqrkagkvgyglgwliqkcvgpit 264
Cdd:cd06421   81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDdPKVALVQTPQFFYNPDPFDWLAD------------------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 265 igrdPFFNDPRMFYDVILRRRNWANAAFCCGAASIHRREAVMQAALrsyvwsveeeihrhtrdirdeetrdalqnamrph 344
Cdd:cd06421  136 ----GAPNEQELFYGVIQPGRDRWGAAFCCGSGAVVRREALDEIGG---------------------------------- 177
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544824155 345 vaFDTEltpykfHVSEDIYTSVLLHgdaARRWRSVMHPRVESKMLSPQDMLTWMIQRFKYAAGSLDIL 412
Cdd:cd06421  178 --FPTD------SVTEDLATSLRLH---AKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
PLN02638 super family cl33534
cellulose synthase A (UDP-forming), catalytic subunit
358-557 9.32e-07

cellulose synthase A (UDP-forming), catalytic subunit


The actual alignment was detected with superfamily member PLN02638:

Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 52.23  E-value: 9.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  358 VSEDIYTSVLLHgdaARRWRSV--MHPRVESKMLSPQDMLTWMIQRFKYAAGSLDILF--HDNIFSRRRFRLSLPQTLMY 433
Cdd:PLN02638  776 VTEDILTGFKMH---ARGWRSIycMPKRPAFKGSAPINLSDRLNQVLRWALGSVEILFsrHCPIWYGYGGRLKWLERFAY 852
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  434 ATTFWSYMACVWNTVFLISPIIYLFTG---IPPVSAWSTPFYLH-FLPFFIFSELAFMFGTWGISAW---------DGRA 500
Cdd:PLN02638  853 VNTTIYPITSIPLLLYCTLPAVCLLTGkfiIPQISNIASIWFISlFLSIFATGILEMRWSGVGIDEWwrneqfwviGGVS 932
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544824155  501 SYLsfFSMnLRALNTVLRGEQIKFHVTPKER-QTGRF--LYLVK------PQIAIVVLTLAGLIWG 557
Cdd:PLN02638  933 AHL--FAV-FQGLLKVLAGIDTNFTVTSKASdEDGDFaeLYMFKwttlliPPTTLLIINLVGVVAG 995
 
Name Accession Description Interval E-value
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
110-412 1.42e-75

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 240.55  E-value: 1.42e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 110 KVDLFIATYSEDTELVRLSIRDALKMAYPfPIDYRIHVLDDGRRPEMKAVCEEEGV----NYITRQTNIGFKAGNLRNGL 185
Cdd:cd06421    2 TVDVFIPTYNEPLEIVRKTLRAALAIDYP-HDKLRVYVLDDGRRPELRALAAELGVeygyRYLTRPDNRHAKAGNLNNAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 186 EQTDGDFIVICDADTRVFPTLLSHTLGYFRD-PDVAWVQTPQWFFDLPEGENLSRwgqrkagkvgyglgwliqkcvgpit 264
Cdd:cd06421   81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDdPKVALVQTPQFFYNPDPFDWLAD------------------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 265 igrdPFFNDPRMFYDVILRRRNWANAAFCCGAASIHRREAVMQAALrsyvwsveeeihrhtrdirdeetrdalqnamrph 344
Cdd:cd06421  136 ----GAPNEQELFYGVIQPGRDRWGAAFCCGSGAVVRREALDEIGG---------------------------------- 177
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544824155 345 vaFDTEltpykfHVSEDIYTSVLLHgdaARRWRSVMHPRVESKMLSPQDMLTWMIQRFKYAAGSLDIL 412
Cdd:cd06421  178 --FPTD------SVTEDLATSLRLH---AKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
30-457 1.41e-38

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 152.10  E-value: 1.41e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  30 LAVAALILGANYIYWRWTASLNTD---ALWYAIPLVLAETLAWIGTVL-FTINLWKEQDPPQSPPpgeINECLSPEeave 105
Cdd:PRK11498 189 LIVLSLTVSCRYIWWRYTSTLNWDdpvSLVCGLILLFAETYAWIVLVLgYFQVVWPLNRQPVPLP---KDMSLWPT---- 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 106 prpvkVDLFIATYSEDTELVRLSIRDALKMAYPfPIDYRIHVLDDGRRPEMKAVCEEEGVNYITRQTNIGFKAGNLRNGL 185
Cdd:PRK11498 262 -----VDIFVPTYNEDLNVVKNTIYASLGIDWP-KDKLNIWILDDGGREEFRQFAQEVGVKYIARPTHEHAKAGNINNAL 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 186 EQTDGDFIVICDAD---TRVFptlLSHTLGYF-RDPDVAWVQTPQWFF--DlPEGENLSRWGQR-KAGKVGYGLgwlIQK 258
Cdd:PRK11498 336 KYAKGEFVAIFDCDhvpTRSF---LQMTMGWFlKDKKLAMMQTPHHFFspD-PFERNLGRFRKTpNEGTLFYGL---VQD 408
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 259 cvgpitiGRDpffndprMfydvilrrrnWaNAAFCCGAASIHRREAVmqaalrsyvwsveEEIHrhtrdirdeetrdalq 338
Cdd:PRK11498 409 -------GND-------M----------W-DATFFCGSCAVIRRKPL-------------DEIG---------------- 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 339 namrpHVAFDTeltpykfhVSEDIYTSVLLHgdaaRR-WRSVMHPRVESKMLSPQDMLTWMIQRFKYAAGSLDILFHDN- 416
Cdd:PRK11498 435 -----GIAVET--------VTEDAHTSLRLH----RRgYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNp 497
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 544824155 417 IFSRrrfRLSLPQTLMYATTFWSYMACVWNTVFLISPIIYL 457
Cdd:PRK11498 498 LTGK---GLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFL 535
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
110-492 3.23e-20

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 91.73  E-value: 3.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 110 KVDLFIATYSEDTELVRLsIRDALKMAYPfPIDYRIHVLDDGRRPEMKAVCEEEG-----VNYITRQTNIGfKAGNLRNG 184
Cdd:COG1215   30 RVSVIIPAYNEEAVIEET-LRSLLAQDYP-KEKLEVIVVDDGSTDETAEIARELAaeyprVRVIERPENGG-KAAALNAG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 185 LEQTDGDFIVICDADTRVFPTLLSHTLGYFRDPDVAwvqtpqwffdlpegenlsrwgqrkagkvgyglgwliqkcvgpit 264
Cdd:COG1215  107 LKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVG-------------------------------------------- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 265 igrdpffndprmfydvilrrrnwanaafCCGAASIHRREAVMQAALrsyvwsveeeihrhtrdirdeetrdalqnamrph 344
Cdd:COG1215  143 ----------------------------ASGANLAFRREALEEVGG---------------------------------- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 345 vaFDTEltpykfHVSEDIYTSVLLHgdaARRWRSVMHPRVESKMLSPQDMLTWMIQRFKYAAGSLDILFHDNIFSRRRFR 424
Cdd:COG1215  161 --FDED------TLGEDLDLSLRLL---RAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRL 229
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 425 LSLPQTLMYATTFWSYMACVWNTVFLISP--IIYLFTGIPPVSAWSTPFYLHFLPFFIFSELAFMFGTWG 492
Cdd:COG1215  230 LLFLLLLLLPLLLLLLLLALLALLLLLLPalLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWK 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
112-307 8.15e-12

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 63.95  E-value: 8.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  112 DLFIATYSEDTELVRlSIRDALKMAYPfpiDYRIHVLDDGRRPEMKAVCEE-----EGVNYITRQTNIGfKAGNLRNGLE 186
Cdd:pfam00535   1 SVIIPTYNEEKYLLE-TLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEyakkdPRVRVIRLPENRG-KAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  187 QTDGDFIVICDADTRVFPTLLSHTLGYFRDPDVAWVqtpqwffdlpegenlsrWGQRKAGKVGYGLGWliqkcvgpitig 266
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVV-----------------VGSRYVIFGETGEYR------------ 126
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 544824155  267 RDPFFNDPRMFYDVILRRRNWaNAAFCCGAASIHRREAVMQ 307
Cdd:pfam00535 127 RASRITLSRLPFFLGLRLLGL-NLPFLIGGFALYRREALEE 166
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
358-557 9.32e-07

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 52.23  E-value: 9.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  358 VSEDIYTSVLLHgdaARRWRSV--MHPRVESKMLSPQDMLTWMIQRFKYAAGSLDILF--HDNIFSRRRFRLSLPQTLMY 433
Cdd:PLN02638  776 VTEDILTGFKMH---ARGWRSIycMPKRPAFKGSAPINLSDRLNQVLRWALGSVEILFsrHCPIWYGYGGRLKWLERFAY 852
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  434 ATTFWSYMACVWNTVFLISPIIYLFTG---IPPVSAWSTPFYLH-FLPFFIFSELAFMFGTWGISAW---------DGRA 500
Cdd:PLN02638  853 VNTTIYPITSIPLLLYCTLPAVCLLTGkfiIPQISNIASIWFISlFLSIFATGILEMRWSGVGIDEWwrneqfwviGGVS 932
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544824155  501 SYLsfFSMnLRALNTVLRGEQIKFHVTPKER-QTGRF--LYLVK------PQIAIVVLTLAGLIWG 557
Cdd:PLN02638  933 AHL--FAV-FQGLLKVLAGIDTNFTVTSKASdEDGDFaeLYMFKwttlliPPTTLLIINLVGVVAG 995
 
Name Accession Description Interval E-value
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
110-412 1.42e-75

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 240.55  E-value: 1.42e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 110 KVDLFIATYSEDTELVRLSIRDALKMAYPfPIDYRIHVLDDGRRPEMKAVCEEEGV----NYITRQTNIGFKAGNLRNGL 185
Cdd:cd06421    2 TVDVFIPTYNEPLEIVRKTLRAALAIDYP-HDKLRVYVLDDGRRPELRALAAELGVeygyRYLTRPDNRHAKAGNLNNAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 186 EQTDGDFIVICDADTRVFPTLLSHTLGYFRD-PDVAWVQTPQWFFDLPEGENLSRwgqrkagkvgyglgwliqkcvgpit 264
Cdd:cd06421   81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDdPKVALVQTPQFFYNPDPFDWLAD------------------------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 265 igrdPFFNDPRMFYDVILRRRNWANAAFCCGAASIHRREAVMQAALrsyvwsveeeihrhtrdirdeetrdalqnamrph 344
Cdd:cd06421  136 ----GAPNEQELFYGVIQPGRDRWGAAFCCGSGAVVRREALDEIGG---------------------------------- 177
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544824155 345 vaFDTEltpykfHVSEDIYTSVLLHgdaARRWRSVMHPRVESKMLSPQDMLTWMIQRFKYAAGSLDIL 412
Cdd:cd06421  178 --FPTD------SVTEDLATSLRLH---AKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
30-457 1.41e-38

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 152.10  E-value: 1.41e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  30 LAVAALILGANYIYWRWTASLNTD---ALWYAIPLVLAETLAWIGTVL-FTINLWKEQDPPQSPPpgeINECLSPEeave 105
Cdd:PRK11498 189 LIVLSLTVSCRYIWWRYTSTLNWDdpvSLVCGLILLFAETYAWIVLVLgYFQVVWPLNRQPVPLP---KDMSLWPT---- 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 106 prpvkVDLFIATYSEDTELVRLSIRDALKMAYPfPIDYRIHVLDDGRRPEMKAVCEEEGVNYITRQTNIGFKAGNLRNGL 185
Cdd:PRK11498 262 -----VDIFVPTYNEDLNVVKNTIYASLGIDWP-KDKLNIWILDDGGREEFRQFAQEVGVKYIARPTHEHAKAGNINNAL 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 186 EQTDGDFIVICDAD---TRVFptlLSHTLGYF-RDPDVAWVQTPQWFF--DlPEGENLSRWGQR-KAGKVGYGLgwlIQK 258
Cdd:PRK11498 336 KYAKGEFVAIFDCDhvpTRSF---LQMTMGWFlKDKKLAMMQTPHHFFspD-PFERNLGRFRKTpNEGTLFYGL---VQD 408
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 259 cvgpitiGRDpffndprMfydvilrrrnWaNAAFCCGAASIHRREAVmqaalrsyvwsveEEIHrhtrdirdeetrdalq 338
Cdd:PRK11498 409 -------GND-------M----------W-DATFFCGSCAVIRRKPL-------------DEIG---------------- 434
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 339 namrpHVAFDTeltpykfhVSEDIYTSVLLHgdaaRR-WRSVMHPRVESKMLSPQDMLTWMIQRFKYAAGSLDILFHDN- 416
Cdd:PRK11498 435 -----GIAVET--------VTEDAHTSLRLH----RRgYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRLDNp 497
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 544824155 417 IFSRrrfRLSLPQTLMYATTFWSYMACVWNTVFLISPIIYL 457
Cdd:PRK11498 498 LTGK---GLKLAQRLCYANAMLHFLSGIPRLIFLTAPLAFL 535
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
110-492 3.23e-20

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 91.73  E-value: 3.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 110 KVDLFIATYSEDTELVRLsIRDALKMAYPfPIDYRIHVLDDGRRPEMKAVCEEEG-----VNYITRQTNIGfKAGNLRNG 184
Cdd:COG1215   30 RVSVIIPAYNEEAVIEET-LRSLLAQDYP-KEKLEVIVVDDGSTDETAEIARELAaeyprVRVIERPENGG-KAAALNAG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 185 LEQTDGDFIVICDADTRVFPTLLSHTLGYFRDPDVAwvqtpqwffdlpegenlsrwgqrkagkvgyglgwliqkcvgpit 264
Cdd:COG1215  107 LKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVG-------------------------------------------- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 265 igrdpffndprmfydvilrrrnwanaafCCGAASIHRREAVMQAALrsyvwsveeeihrhtrdirdeetrdalqnamrph 344
Cdd:COG1215  143 ----------------------------ASGANLAFRREALEEVGG---------------------------------- 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 345 vaFDTEltpykfHVSEDIYTSVLLHgdaARRWRSVMHPRVESKMLSPQDMLTWMIQRFKYAAGSLDILFHDNIFSRRRFR 424
Cdd:COG1215  161 --FDED------TLGEDLDLSLRLL---RAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRL 229
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 425 LSLPQTLMYATTFWSYMACVWNTVFLISP--IIYLFTGIPPVSAWSTPFYLHFLPFFIFSELAFMFGTWG 492
Cdd:COG1215  230 LLFLLLLLLPLLLLLLLLALLALLLLLLPalLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWK 299
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
113-308 1.39e-18

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 83.82  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 113 LFIATYSEDTELVRlSIRDALKMAYPfpiDYRIHVLDDGRRPEMKAVCEEEGVNYIT-----RQTNIGFKAGNLRNGLEQ 187
Cdd:cd06423    1 IIVPAYNEEAVIER-TIESLLALDYP---KLEVIVVDDGSTDDTLEILEELAALYIRrvlvvRDKENGGKAGALNAGLRH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 188 TDGDFIVICDADTRVFPTLLSH-TLGYFRDPDVAWVQtpqwffdlpegenlsrwgqrkaGKVGYglgwlIQKCVGPITIG 266
Cdd:cd06423   77 AKGDIVVVLDADTILEPDALKRlVVPFFADPKVGAVQ----------------------GRVRV-----RNGSENLLTRL 129
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 544824155 267 RDPFFNdprMFYDVILRRRNWANAAFCC-GAASIHRREAVMQA 308
Cdd:cd06423  130 QAIEYL---SIFRLGRRAQSALGGVLVLsGAFGAFRREALREV 169
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
121-224 1.73e-15

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 76.19  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 121 DTELVRLSIRDALKMAYPFPiDYRIHVLDDGRRPEMKA----VCE--EEGVN--YITRQTNIGFKAGNLRNGLEQTDGDF 192
Cdd:cd06437   12 EKYVVERLIEAACALDYPKD-RLEIQVLDDSTDETVRLareiVEEyaAQGVNikHVRRADRTGYKAGALAEGMKVAKGEY 90
                         90       100       110
                 ....*....|....*....|....*....|..
gi 544824155 193 IVICDADTRVFPTLLSHTLGYFRDPDVAWVQT 224
Cdd:cd06437   91 VAIFDADFVPPPDFLQKTPPYFADPKLGFVQT 122
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
112-307 8.15e-12

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 63.95  E-value: 8.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  112 DLFIATYSEDTELVRlSIRDALKMAYPfpiDYRIHVLDDGRRPEMKAVCEE-----EGVNYITRQTNIGfKAGNLRNGLE 186
Cdd:pfam00535   1 SVIIPTYNEEKYLLE-TLESLLNQTYP---NFEIIVVDDGSTDGTVEIAEEyakkdPRVRVIRLPENRG-KAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  187 QTDGDFIVICDADTRVFPTLLSHTLGYFRDPDVAWVqtpqwffdlpegenlsrWGQRKAGKVGYGLGWliqkcvgpitig 266
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVV-----------------VGSRYVIFGETGEYR------------ 126
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 544824155  267 RDPFFNDPRMFYDVILRRRNWaNAAFCCGAASIHRREAVMQ 307
Cdd:pfam00535 127 RASRITLSRLPFFLGLRLLGL-NLPFLIGGFALYRREALEE 166
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
118-308 1.82e-11

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 64.34  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 118 YSEDTELVRLSIRDALKMAYPfpiDYRIHVLDDGRRPE-----MKAVCEEEGVN--YITRQTNIGFKAGNLRNGLEQTDG 190
Cdd:cd06435    7 YEEPPEMVKETLDSLAALDYP---NFEVIVIDNNTKDEalwkpVEAHCAQLGERfrFFHVEPLPGAKAGALNYALERTAP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 191 D--FIVICDADTRVFPTLLSHTLGYFRDPDVAWVQTPQWFFDlpegenlsrwGQRKAGKvgYGLGWliqkcvgpitigrd 268
Cdd:cd06435   84 DaeIIAVIDADYQVEPDWLKRLVPIFDDPRVGFVQAPQDYRD----------GEESLFK--RMCYA-------------- 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 544824155 269 pffnDPRMFYDVILRRRNWANAAFCCGAASIHRREAVMQA 308
Cdd:cd06435  138 ----EYKGFFDIGMVSRNERNAIIQHGTMCLIRRSALDDV 173
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
115-229 1.39e-09

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 57.13  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 115 IATYSEDTELVRlSIRDALKMAYPfpiDYRIHVLDDGRRPEMKAVCEEEG-----VNYITRQTNIGfKAGNLRNGLEQTD 189
Cdd:cd00761    3 IPAYNEEPYLER-CLESLLAQTYP---NFEVIVVDDGSTDGTLEILEEYAkkdprVIRVINEENQG-LAAARNAGLKAAR 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 544824155 190 GDFIVICDADTRVFPTLLSHTLGYFRDPDVAWVQTPQWFF 229
Cdd:cd00761   78 GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNL 117
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
110-284 5.41e-09

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 56.63  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 110 KVDLFIATYSEDTELVRLsIRDALKMAYPfpiDYRIHVLDDGRRPEMKAVCEE-----EGVNYITRQTNIGfKAGNLRNG 184
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEA-LESLLAQTYP---DFEIIVVDDGSTDGTAEILRElaakdPRIRVIRLERNRG-KGAARNAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 185 LEQTDGDFIVICDADTRVFPTLLSHTLGYFRDPDVAWVQTPQWFfdlPEGENLSRWGQRKAGKVGYGLGWLIQKCVGPIT 264
Cdd:COG0463   78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI---REGESDLRRLGSRLFNLVRLLTNLPDSTSGFRL 154
                        170       180
                 ....*....|....*....|...
gi 544824155 265 IGRDPFFN---DPRMFYDVILRR 284
Cdd:COG0463  155 FRREVLEElgfDEGFLEDTELLR 177
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
108-243 1.23e-08

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 55.84  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  108 PVKVDLFIATYSEDTELVRLsIRDALKMAYPfpiDYRIHVLDDGRRPEMKAVCEE-------EGVNYITRQTNIGF--KA 178
Cdd:pfam13641   1 PPDVSVVVPAFNEDSVLGRV-LEAILAQPYP---PVEVVVVVNPSDAETLDVAEEiaarfpdVRLRVIRNARLLGPtgKS 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544824155  179 GNLRNGLEQTDGDFIVICDADTRVFPTLLSHTLGYFRDPDVAWVQTPQWFfdlpegENLSRWGQR 243
Cdd:pfam13641  77 RGLNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFS------LNRSTMLSA 135
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
154-225 1.75e-07

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 51.51  E-value: 1.75e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544824155  154 PEMKAVC---EEEGVNYitrqtnigfKAGNLRNGLEQTDGDFIVICDADTRVFPTLLSHTLGYFRDPDVAWVQTP 225
Cdd:pfam13506   1 PSVRALVvggPPVGVNP---------KVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADPKVGLVTSP 66
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
358-557 9.32e-07

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 52.23  E-value: 9.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  358 VSEDIYTSVLLHgdaARRWRSV--MHPRVESKMLSPQDMLTWMIQRFKYAAGSLDILF--HDNIFSRRRFRLSLPQTLMY 433
Cdd:PLN02638  776 VTEDILTGFKMH---ARGWRSIycMPKRPAFKGSAPINLSDRLNQVLRWALGSVEILFsrHCPIWYGYGGRLKWLERFAY 852
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  434 ATTFWSYMACVWNTVFLISPIIYLFTG---IPPVSAWSTPFYLH-FLPFFIFSELAFMFGTWGISAW---------DGRA 500
Cdd:PLN02638  853 VNTTIYPITSIPLLLYCTLPAVCLLTGkfiIPQISNIASIWFISlFLSIFATGILEMRWSGVGIDEWwrneqfwviGGVS 932
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544824155  501 SYLsfFSMnLRALNTVLRGEQIKFHVTPKER-QTGRF--LYLVK------PQIAIVVLTLAGLIWG 557
Cdd:PLN02638  933 AHL--FAV-FQGLLKVLAGIDTNFTVTSKASdEDGDFaeLYMFKwttlliPPTTLLIINLVGVVAG 995
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
110-214 4.04e-06

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 48.07  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 110 KVDLFIATYSEDTELVRLsIRDALKMAYPfpiDYRIHVLDDGRRPEMKAVCEE---EGVNYITRQTNIGFkAGNLRNGLE 186
Cdd:COG1216    4 KVSVVIPTYNRPELLRRC-LESLLAQTYP---PFEVIVVDNGSTDGTAELLAAlafPRVRVIRNPENLGF-AAARNLGLR 78
                         90       100
                 ....*....|....*....|....*...
gi 544824155 187 QTDGDFIVICDADTRVFPTLLSHTLGYF 214
Cdd:COG1216   79 AAGGDYLLFLDDDTVVEPDWLERLLAAA 106
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
140-220 4.32e-05

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 44.09  E-value: 4.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 140 PIDYRIHVLD----DGRRPEMKAvcEEEGVNYITRQTNIGFKAGNlrN-GLEQTDGDFIVICDADTRVFPTLLSHTLGYF 214
Cdd:cd04186   24 YPDFEVIVVDnastDGSVELLRE--LFPEVRLIRNGENLGFGAGN--NqGIREAKGDYVLLLNPDTVVEPGALLELLDAA 99

                 ....*..
gi 544824155 215 R-DPDVA 220
Cdd:cd04186  100 EqDPDVG 106
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
111-226 1.23e-04

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 43.78  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155 111 VDLFIATYSEDTELVRLSIRDALKMAypfpiDYRIHVLDDGRRPEMKAVCEEEgVNYITRQ---TNIGFKAGNLRNGLEQ 187
Cdd:cd06434    2 VTVIIPVYDEDPDVFRECLRSILRQK-----PLEIIVVTDGDDEPYLSILSQT-VKYGGIFvitVPHPGKRRALAEGIRH 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 544824155 188 TDGDFIVICDADTRVFPTLLSHTLGYFRDPDVAWVQTPQ 226
Cdd:cd06434   76 VTTDIVVLLDSDTVWPPNALPEMLKPFEDPKVGGVGTNQ 114
PLN02400 PLN02400
cellulose synthase
358-557 1.57e-04

cellulose synthase


Pssm-ID: 215224 [Multi-domain]  Cd Length: 1085  Bit Score: 44.97  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  358 VSEDIYTSVLLHgdaARRWRSV--MHPRVESKMLSPQDMLTWMIQRFKYAAGSLDILF--HDNIFSRRRFRLSLPQTLMY 433
Cdd:PLN02400  781 VTEDILTGFKMH---ARGWISIycMPPRPAFKGSAPINLSDRLNQVLRWALGSIEILLsrHCPIWYGYNGRLKLLERLAY 857
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  434 attfwsymacvwntvflISPIIYLFTGIPPVSAWSTPFYLHFLPFFIFSELAFMFGTW---------------------G 492
Cdd:PLN02400  858 -----------------INTIVYPITSIPLLAYCVLPAFCLITNKFIIPEISNYASMWfillfisifatgilelrwsgvG 920
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  493 ISAW---------DGRASYLsfFSMnLRALNTVLRGEQIKFHVTPKER-QTGRF--LYLVK------PQIAIVVLTLAGL 554
Cdd:PLN02400  921 IEDWwrneqfwviGGTSAHL--FAV-FQGLLKVLAGIDTNFTVTSKASdEDGDFaeLYVFKwtslliPPTTVLLVNLVGI 997

                  ...
gi 544824155  555 IWG 557
Cdd:PLN02400  998 VAG 1000
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
356-467 2.81e-04

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 42.32  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824155  356 FHVSEDIYTSVLLhgdAARRWRSVMHPRVESKMLSPQDMLTWMIQRFKYAAGSLDILFHDNIFSRRRFrlslpqtlmyat 435
Cdd:pfam13632  93 GSVSEDFDFGLRL---QRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRLLGYLGTL------------ 157
                          90       100       110
                  ....*....|....*....|....*....|..
gi 544824155  436 tFWSYMACVWNTVFLISPIIYLFTGIPPVSAW 467
Cdd:pfam13632 158 -LWSGLPLALLLLLLFSISSLALVLLLLALLA 188
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
131-199 3.09e-03

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 39.09  E-value: 3.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544824155 131 DALKMAYPFPIDYRIHVLDDGRRPEMKAVCEEEGVNY-----ITRQTNIGfKAGNLRNGLEQTDGDFIVICDAD 199
Cdd:cd04179   17 ERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVprvrvIRLSRNFG-KGAAVRAGFKAARGDIVVTMDAD 89
 
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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