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Conserved domains on  [gi|489829408|ref|WP_003733162|]
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glycosyltransferase family 2 protein [Listeria monocytogenes]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10118426)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  9445404|12691742|10508766|12200473|10521532
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-209 2.38e-56

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


:

Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 190.58  E-value: 2.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   5 ISICMIVKNEAHILRQSLASFRKFTEEIIIVDTGSTDETKEIAQEFTDFVYDFEWtGNFSDARNFAAKHATGKWILAIDA 84
Cdd:cd02511    2 LSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWW-DGFGAQRNFALELATNDWVLSLDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  85 DECLEEESYRKLEKQLKSPTEP-IQMAQIISFTGEKGRVT--TTNQMARVYKNDGTICFRGVIHEQLEAIDKRPIaagVA 161
Cdd:cd02511   81 DERLTPELADEILALLATDDYDgYYVPRRNFFLGRWIRHGgwYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGI---VL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489829408 162 EVKIYHYGYMSeIVEKQDKSDRNLRLLEK-EVKNNKNSGFVHFNIGQEM 209
Cdd:cd02511  158 KGDILHYGYKS-LEEFLEKHNRYSSLEAKdLAAKGKKRSLLKGLLLGRP 205
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 170-409 3.78e-16

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 79.00  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 170 YMSEIVEKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWAKLsayhiAELLE 249
Cdd:COG2956   47 ALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLL-----AEIYE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 250 QEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQsllenAAIDYQPivlyeaTNFMPHKMLGTIYLE 329
Cdd:COG2956  122 QEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALE-----KALKLDP------DCARALLLLAELYLE 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 330 EKDYTRAMTHFSKAYAENSSDYGVMFQMIMLLSKFHQPKEIFAFMERHHFISSTETGLRLLS--MTTQQGYAELSELIVQ 407
Cdd:COG2956  191 QGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALAdlLERKEGLEAALALLER 270


                 ..
gi 489829408 408 SL 409
Cdd:COG2956  271 QL 272
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-209 2.38e-56

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 190.58  E-value: 2.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   5 ISICMIVKNEAHILRQSLASFRKFTEEIIIVDTGSTDETKEIAQEFTDFVYDFEWtGNFSDARNFAAKHATGKWILAIDA 84
Cdd:cd02511    2 LSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWW-DGFGAQRNFALELATNDWVLSLDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  85 DECLEEESYRKLEKQLKSPTEP-IQMAQIISFTGEKGRVT--TTNQMARVYKNDGTICFRGVIHEQLEAIDKRPIaagVA 161
Cdd:cd02511   81 DERLTPELADEILALLATDDYDgYYVPRRNFFLGRWIRHGgwYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGI---VL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489829408 162 EVKIYHYGYMSeIVEKQDKSDRNLRLLEK-EVKNNKNSGFVHFNIGQEM 209
Cdd:cd02511  158 KGDILHYGYKS-LEEFLEKHNRYSSLEAKdLAAKGKKRSLLKGLLLGRP 205
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-101 3.43e-20

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 89.38  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   2 RPLISICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEIAQEFTD-----FVYDFEWTGNFSDARNFAAKH 73
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYpdfEIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAA 80

                         90       100
                 ....*....|....*....|....*...
gi 489829408  74 ATGKWILAIDADECLEEEsyrKLEKQLK 101
Cdd:COG0463   81 ARGDYIAFLDADDQLDPE---KLEELVA 105
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-101 4.95e-19

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: 84.75  E-value: 4.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408    6 SICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEIAQEFTD-----FVYDFEWTGNFSDARNFAAKHATGK 77
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYpnfEIIVVDDGSTDGTVEIAEEYAKkdprvRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100
                  ....*....|....*....|....
gi 489829408   78 WILAIDADECLEEEsyrKLEKQLK 101
Cdd:pfam00535  81 YIAFLDADDEVPPD---WLEKLVE 101
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 170-409 3.78e-16

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 79.00  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 170 YMSEIVEKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWAKLsayhiAELLE 249
Cdd:COG2956   47 ALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLL-----AEIYE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 250 QEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQsllenAAIDYQPivlyeaTNFMPHKMLGTIYLE 329
Cdd:COG2956  122 QEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALE-----KALKLDP------DCARALLLLAELYLE 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 330 EKDYTRAMTHFSKAYAENSSDYGVMFQMIMLLSKFHQPKEIFAFMERHHFISSTETGLRLLS--MTTQQGYAELSELIVQ 407
Cdd:COG2956  191 QGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALAdlLERKEGLEAALALLER 270


                 ..
gi 489829408 408 SL 409
Cdd:COG2956  271 QL 272
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-96 7.41e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 51.59  E-value: 7.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   3 PLISICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEI----AQEFTDFVYDFEWTGNFSDARNFAAKHAT 75
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWtalEIIIVNDGSTDNSVEIakhyAENYPHVRLLHQANAGVSVARNTGLAVAT 85

                         90       100
                 ....*....|....*....|.
gi 489829408  76 GKWILAIDADECLEEESYRKL 96
Cdd:PRK10073  86 GKYVAFPDADDVVYPTMYETL 106
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 212-393 8.84e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.93  E-value: 8.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  212 LGNKKEALKEFSEAFRLRDHNhyiwaklSAYHIAE--LLEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLE 289
Cdd:TIGR02917 206 LGNIELALAAYRKAIALRPNN-------IAVLLALatILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYE 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  290 DAKEIYQSllenaaidyqpiVLYEATNFMPHKML-GTIYLEEKDYTRAMTHFSK--AYAENSSDYGVMFQMIMLLSKfhQ 366
Cdd:TIGR02917 279 DARETLQD------------ALKSAPEYLPALLLaGASEYQLGNLEQAYQYLNQilKYAPNSHQARRLLASIQLRLG--R 344

                         170       180
                  ....*....|....*....|....*...
gi 489829408  367 PKEIFAFMERHHFISSTETGLR-LLSMT 393
Cdd:TIGR02917 345 VDEAIATLSPALGLDPDDPAALsLLGEA 372
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-209 2.38e-56

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 190.58  E-value: 2.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   5 ISICMIVKNEAHILRQSLASFRKFTEEIIIVDTGSTDETKEIAQEFTDFVYDFEWtGNFSDARNFAAKHATGKWILAIDA 84
Cdd:cd02511    2 LSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRWW-DGFGAQRNFALELATNDWVLSLDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  85 DECLEEESYRKLEKQLKSPTEP-IQMAQIISFTGEKGRVT--TTNQMARVYKNDGTICFRGVIHEQLEAIDKRPIaagVA 161
Cdd:cd02511   81 DERLTPELADEILALLATDDYDgYYVPRRNFFLGRWIRHGgwYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGI---VL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489829408 162 EVKIYHYGYMSeIVEKQDKSDRNLRLLEK-EVKNNKNSGFVHFNIGQEM 209
Cdd:cd02511  158 KGDILHYGYKS-LEEFLEKHNRYSSLEAKdLAAKGKKRSLLKGLLLGRP 205
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-101 3.43e-20

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 89.38  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   2 RPLISICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEIAQEFTD-----FVYDFEWTGNFSDARNFAAKH 73
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYpdfEIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAA 80

                         90       100
                 ....*....|....*....|....*...
gi 489829408  74 ATGKWILAIDADECLEEEsyrKLEKQLK 101
Cdd:COG0463   81 ARGDYIAFLDADDQLDPE---KLEELVA 105
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-101 4.95e-19

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: 84.75  E-value: 4.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408    6 SICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEIAQEFTD-----FVYDFEWTGNFSDARNFAAKHATGK 77
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYpnfEIIVVDDGSTDGTVEIAEEYAKkdprvRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100
                  ....*....|....*....|....
gi 489829408   78 WILAIDADECLEEEsyrKLEKQLK 101
Cdd:pfam00535  81 YIAFLDADDEVPPD---WLEKLVE 101
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 170-409 3.78e-16

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 79.00  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 170 YMSEIVEKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWAKLsayhiAELLE 249
Cdd:COG2956   47 ALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLL-----AEIYE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 250 QEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQsllenAAIDYQPivlyeaTNFMPHKMLGTIYLE 329
Cdd:COG2956  122 QEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALE-----KALKLDP------DCARALLLLAELYLE 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 330 EKDYTRAMTHFSKAYAENSSDYGVMFQMIMLLSKFHQPKEIFAFMERHHFISSTETGLRLLS--MTTQQGYAELSELIVQ 407
Cdd:COG2956  191 QGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALAdlLERKEGLEAALALLER 270


                 ..
gi 489829408 408 SL 409
Cdd:COG2956  271 QL 272
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-96 4.50e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 76.96  E-value: 4.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   1 MRPLISICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEIAQEFTDF---VYDFEWTGNFSDARNFAAKHA 74
Cdd:COG1216    1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYppfEVIVVDNGSTDGTAELLAALAFPrvrVIRNPENLGFAAARNLGLRAA 80

                         90       100
                 ....*....|....*....|..
gi 489829408  75 TGKWILAIDADECLEEESYRKL 96
Cdd:COG1216   81 GGDYLLFLDDDTVVEPDWLERL 102
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 7-105 2.49e-15

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: 73.69  E-value: 2.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   7 ICMIVKNEAHILRQSLASFRKFT---EEIIIVDTGSTDETKEIAQEFTD-----FVYDFEWTGNFSDARNFAAKHATGKW 78
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTypnFEVIVVDDGSTDGTLEILEEYAKkdprvIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100
                 ....*....|....*....|....*..
gi 489829408  79 ILAIDADECLEEESYRKLEKQLKSPTE 105
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADPE 107
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-103 1.44e-14

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: 74.78  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   1 MRPLISICMIVKNEAHILRQSLASFR-----KFTEEIIIVDTGSTDETKEIAQEFTD-----FVYDFEWTGNFSDARNFA 70
Cdd:COG1215   27 DLPRVSVIIPAYNEEAVIEETLRSLLaqdypKEKLEVIVVDDGSTDETAEIARELAAeyprvRVIERPENGGKAAALNAG 106

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489829408  71 AKHATGKWILAIDADECLEEESYRKLEKQLKSP 103
Cdd:COG1215  107 LKAARGDIVVFLDADTVLDPDWLRRLVAAFADP 139
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 206-392 5.29e-11

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 65.78  E-value: 5.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 206 GQEMNRLGNKKEALKEFSEAFRLRDHNHYIWaklsaYHIAELLEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVN 285
Cdd:COG3914   85 ALLLQALGRYEEALALYRRALALNPDNAEAL-----FNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 286 HQLEDAKEIYQsllenAAIDYQPivlyeaTNFMPHKMLGTIYLEEKDYTRAMTHFSKAYAENSSDYGVMFQMIMLLSKFH 365
Cdd:COG3914  160 GRLEEAIAALR-----RALELDP------DNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQAC 228

                        170       180
                 ....*....|....*....|....*..
gi 489829408 366 QPKEIFAFMERHHFISSTETGLRLLSM 392
Cdd:COG3914  229 DWEVYDRFEELLAALARGPSELSPFAL 255
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 201-350 8.35e-11

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 60.21  E-value: 8.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 201 VHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWAKLsayhiAELLEQEKRYDESLAIIEEARVIWPNVPEFPLKKAN 280
Cdd:COG4783    6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALL-----GEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 281 ILYVNHQLEDAKEIYQsllenAAIDYQPivlyeaTNFMPHKMLGTIYLEEKDYTRAMTHFSKAYAENSSD 350
Cdd:COG4783   81 ALLKAGDYDEALALLE-----KALKLDP------EHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
195-376 2.54e-10

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.18  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 195 NKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWaklsaYHIAELLEQEKRYDESLAIIEEARVIWPNVPEF 274
Cdd:COG0457    4 DPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEAL-----YNLGLAYLRLGRYEEALADYEQALELDPDDAEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 275 PLKKANILYVNHQLEDAKEIYQsllenAAIDYQPivlyeaTNFMPHKMLGTIYLEEKDYTRAMTHFSKAYAENSSDYGVM 354
Cdd:COG0457   79 LNNLGLALQALGRYEEALEDYD-----KALELDP------DDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADAL 147

                        170       180
                 ....*....|....*....|..
gi 489829408 355 FQMIMLLSKFHQPKEIFAFMER 376
Cdd:COG0457  148 YNLGIALEKLGRYEEALELLEK 169
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 4-85 5.72e-10

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 60.32  E-value: 5.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   4 LISICMIVKNEAHILRQSLASFR-----KFTEEIIIVDTGSTDETKEIAQEFTDFVYDFEWTGN----FSDARNFAAKHA 74
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLnqsypKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNpkriQSAGLNIGIRNS 80

                         90
                 ....*....|.
gi 489829408  75 TGKWILAIDAD 85
Cdd:cd02525   81 RGDIIIRVDAH 91
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
168-346 2.15e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.48  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 168 YGYMSEIVEKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWaklsaYHIAEL 247
Cdd:COG0457   11 YNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEAL-----NNLGLA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 248 LEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQsllenAAIDYQPivlyeaTNFMPHKMLGTIY 327
Cdd:COG0457   86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYE-----RALELDP------DDADALYNLGIAL 154

                        170
                 ....*....|....*....
gi 489829408 328 LEEKDYTRAMTHFSKAYAE 346
Cdd:COG0457  155 EKLGRYEEALELLEKLEAA 173
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
168-336 3.29e-09

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.09  E-value: 3.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 168 YGYMSEIVEKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWaklsaYHIAEL 247
Cdd:COG0457   45 LYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEAL-----YNLGLA 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 248 LEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQSLLENAAIDYQPIVLYEATNFMPHKMLGTIY 327
Cdd:COG0457  120 LLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLAL 199


                 ....*....
gi 489829408 328 LEEKDYTRA 336
Cdd:COG0457  200 LLALEQALR 208
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 176-303 4.00e-09

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 55.58  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 176 EKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWAKLsayhiAELLEQEKRYD 255
Cdd:COG4783   15 LLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNL-----GLALLKAGDYD 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489829408 256 ESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQSLLENAA 303
Cdd:COG4783   90 EALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDP 137
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 5-103 5.47e-09

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 56.81  E-value: 5.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   5 ISICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEIAQEFTDFVYdfewTGNFSDAR--NFAAKHATGKWI 79
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPlplEIIVVDGGSTDGTVAIARSAGVVVI----SSPKGRARqmNAGAAAARGDWL 76

                         90       100
                 ....*....|....*....|....
gi 489829408  80 LAIDADECLEEESYRKLEKQLKSP 103
Cdd:cd02522   77 LFLHADTRLPPDWDAAIIETLRAD 100
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 12-113 5.78e-09

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: 56.08  E-value: 5.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  12 KNEAHILRQSLASFRKFT---EEIIIVDTGSTDETKEIAQEFTDFVYDFEW------TGNFSDARNFAAKHATGKWILAI 82
Cdd:cd06423    6 YNEEAVIERTIESLLALDypkLEVIVVDDGSTDDTLEILEELAALYIRRVLvvrdkeNGGKAGALNAGLRHAKGDIVVVL 85

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489829408  83 DADECLEEESYRKLEKQLKSPTEPIQMAQII 113
Cdd:cd06423   86 DADTILEPDALKRLVVPFFADPKVGAVQGRV 116
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 185-300 8.84e-09

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 58.47  E-value: 8.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 185 LRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWAKLsayhiAELLEQEKRYDESLAIIEEA 264
Cdd:COG3914   98 LALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNL-----GEALRRLGRLEEAIAALRRA 172

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489829408 265 RVIWPNVPEFPLKKANILYVNHQLEDAKEIYQSLLE 300
Cdd:COG3914  173 LELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALE 208
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 217-350 6.53e-08

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 51.55  E-value: 6.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 217 EALKEFSEAFRLRDHNHYIWAKLsayhiAELLEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQ 296
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLL-----GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLE 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489829408 297 sllenAAIDYQPivlyeaTNFMPHKMLGTIYLEEKDYTRAMTHFSKAYAENSSD 350
Cdd:COG4235   76 -----RALALDP------DNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPAD 118
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 185-302 1.03e-07

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 51.16  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 185 LRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWAKLsayhiAELLEQEKRYDESLAIIEEA 264
Cdd:COG4235    3 IARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDL-----AEALLAAGDTEEAEELLERA 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489829408 265 RVIWPNVPEFPLKKANILYVNHQLEDAKEIYQSLLENA 302
Cdd:COG4235   78 LALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALL 115
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-85 1.91e-07

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: 51.02  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   7 ICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEIAQEFTDFVYDFEWTGN--FSDARNFAAKHATGKWILA 81
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYpdfEVIVVDNASTDGSVELLRELFPEVRLIRNGENlgFGAGNNQGIREAKGDYVLL 80


                 ....
gi 489829408  82 IDAD 85
Cdd:cd04186   81 LNPD 84
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 241-376 2.29e-07

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 53.84  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 241 AYHIAELLEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQsllenAAIDYQPivlyeaTNFMPH 320
Cdd:COG3914   81 LELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALR-----RALALNP------DFAEAY 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489829408 321 KMLGTIYLEEKDYTRAMTHFSKAYAENSSDYGVMFQMIMLLSKFHQPKEIFAFMER 376
Cdd:COG3914  150 LNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRR 205
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-96 7.41e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 51.59  E-value: 7.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   3 PLISICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEI----AQEFTDFVYDFEWTGNFSDARNFAAKHAT 75
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWtalEIIIVNDGSTDNSVEIakhyAENYPHVRLLHQANAGVSVARNTGLAVAT 85

                         90       100
                 ....*....|....*....|.
gi 489829408  76 GKWILAIDADECLEEESYRKL 96
Cdd:PRK10073  86 GKYVAFPDADDVVYPTMYETL 106
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 12-86 1.29e-06

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 46.85  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   12 KNEAHILRQSLASFRKFT-EEIIIVDTGSTDETKEIAQEFTDfVYDFEWTGNFSDAR-------NFAAKHATGKWILAID 83
Cdd:pfam13704   1 RNEADILPQWLAHHLALGfDHIYVYDNGSDDGTAEILARLPD-VSILRSDLSYKDARfqvdwrnALLARYAEADWVLVVD 79


                  ...
gi 489829408   84 ADE 86
Cdd:pfam13704  80 ADE 82
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 242-376 1.71e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 47.88  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 242 YHIAELLEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQsllenAAIDYQPivlyeaTNFMPHK 321
Cdd:COG4783    8 YALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLH-----EALELDP------DEPEARL 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489829408 322 MLGTIYLEEKDYTRAMTHFSKAYAENSSDYGVMFQMIMLLSKFHQPKEIFAFMER 376
Cdd:COG4783   77 NLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEK 131
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 144-269 2.98e-06

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 47.65  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 144 IHEQLEAIDKRPIAAGVAEVKIYHYGYMSEIVEKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFS 223
Cdd:COG5010   33 GANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYE 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489829408 224 EAFRLRDHNHYIWaklsaYHIAELLEQEKRYDESLAIIEEARVIWP 269
Cdd:COG5010  113 KALALSPDNPNAY-----SNLAALLLSLGQDDEAKAALQRALGTSP 153
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 13-85 3.54e-06

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: 47.95  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  13 NEAHILRQSLASFRKFTE-----EIIIVDTGSTDETKEIAQEF-----TDFVYDFEwtgnfsdaRNF---AA-----KHA 74
Cdd:cd04179    7 NEEENIPELVERLLAVLEegydyEIIVVDDGSTDGTAEIARELaarvpRVRVIRLS--------RNFgkgAAvragfKAA 78

                         90
                 ....*....|.
gi 489829408  75 TGKWILAIDAD 85
Cdd:cd04179   79 RGDIVVTMDAD 89
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 6-89 3.93e-06

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 47.93  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   6 SICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEIAQEFTDFVYDFewtgnFS-------DARNFAAKHAT 75
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYpniEYIVIDGGSTDGTVDIIKKYEDKITYW-----ISepdkgiyDAMNKGIALAT 75

                         90
                 ....*....|....
gi 489829408  76 GKWILAIDADECLE 89
Cdd:cd06433   76 GDIIGFLNSDDTLL 89
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 235-376 5.92e-06

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.19  E-value: 5.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 235 IWAKLSAYHIAELLEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQSLLENAaiDYQPIVLYEa 314
Cdd:COG2956    5 VAAALGWYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERD--PDRAEALLE- 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489829408 315 tnfmphkmLGTIYLEEKDYTRAMTHFSKAYAENSSDYGVMFQMIMLLSKFHQPKEIFAFMER 376
Cdd:COG2956   82 --------LAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLER 135
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 168-270 6.19e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 46.34  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 168 YGYMSEIVEKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRLRDHNHYIWaklsaYHIAEL 247
Cdd:COG4783   41 FALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAY-----LRLARA 115

                         90       100
                 ....*....|....*....|...
gi 489829408 248 LEQEKRYDESLAIIEEARVIWPN 270
Cdd:COG4783  116 YRALGRPDEAIAALEKALELDPD 138
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 212-393 8.84e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.93  E-value: 8.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  212 LGNKKEALKEFSEAFRLRDHNhyiwaklSAYHIAE--LLEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLE 289
Cdd:TIGR02917 206 LGNIELALAAYRKAIALRPNN-------IAVLLALatILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYE 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  290 DAKEIYQSllenaaidyqpiVLYEATNFMPHKML-GTIYLEEKDYTRAMTHFSK--AYAENSSDYGVMFQMIMLLSKfhQ 366
Cdd:TIGR02917 279 DARETLQD------------ALKSAPEYLPALLLaGASEYQLGNLEQAYQYLNQilKYAPNSHQARRLLASIQLRLG--R 344

                         170       180
                  ....*....|....*....|....*...
gi 489829408  367 PKEIFAFMERHHFISSTETGLR-LLSMT 393
Cdd:TIGR02917 345 VDEAIATLSPALGLDPDDPAALsLLGEA 372
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 211-304 1.37e-05

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 45.72  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 211 RLGNKKEALKEFSEAFRLRDHNHYIWaklsaYHIAELLEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLED 290
Cdd:COG5010   66 KLGDFEESLALLEQALQLDPNNPELY-----YNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDE 140

                         90
                 ....*....|....
gi 489829408 291 AKEIYQSLLENAAI 304
Cdd:COG5010  141 AKAALQRALGTSPL 154
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-79 4.27e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 44.93  E-value: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   6 SICMIVKNEAHILRQSLASFRKFTE---EIIIVDTGSTDETKEIAQEFTDfVYDFEWT-----GNFSDARNF--AAKHAT 75
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYkndELIISDDGSTDGTVEIIKEYID-KDPFIIIlirngKNLGVARNFesLLQAAD 79


                 ....
gi 489829408  76 GKWI 79
Cdd:cd04196   80 GDYV 83
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 22-101 4.66e-05

DPG_synthase is involved in protein N-linked glycosylation; 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.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 44.87  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  22 LASFRKFTEEIIIVDTGSTDETKEIAQEFtdfvydfeWTGNFSDARNFAAK--------------HATGKWILAIDAD-- 85
Cdd:cd04188   23 LEERPSFSYEIIVVDDGSKDGTAEVARKL--------ARKNPALIRVLTLPknrgkggavragmlAARGDYILFADADla 94

                         90
                 ....*....|....*....
gi 489829408  86 ---ECLEeesyrKLEKQLK 101
Cdd:cd04188   95 tpfEELE-----KLEEALK 108
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 211-301 5.07e-05

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 43.06  E-value: 5.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 211 RLGNKKEALKEFSEAfrLRDHNHYIWAKLSAYHIAELLEQEKRYDESLAIIEEARVIWPN---VPEFPLKKANILYVNHQ 287
Cdd:COG1729    5 KAGDYDEAIAAFKAF--LKRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDspkAPDALLKLGLSYLELGD 82

                         90
                 ....*....|....
gi 489829408 288 LEDAKEIYQSLLEN 301
Cdd:COG1729   83 YDKARATLEELIKK 96
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 171-354 5.80e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 46.23  E-value: 5.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  171 MSEIVEKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAFRL-RDHNHYI-------------- 235
Cdd:TIGR02917 539 LAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKALAILNEAADAaPDSPEAWlmlgraqlaagdln 618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  236 --------WAKLSAYHIAELL------EQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQSLLEN 301
Cdd:TIGR02917 619 kavssfkkLLALQPDSALALLlladayAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQKQ 698

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 489829408  302 AAIDYQPivlyeatnfmpHKMLGTIYLEEKDYTRAMTHFSKAYAENSSDYGVM 354
Cdd:TIGR02917 699 HPKAALG-----------FELEGDLYLRQKDYPAAIQAYRKALKRAPSSQNAI 740
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-112 7.39e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 44.59  E-value: 7.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   5 ISICmiVKNEA-HILR--QSLASF----RKFteEIIIVDTGSTDETKEIAQEFTD---------FVYDFEWTGNfSDARN 68
Cdd:cd04192    1 VVIA--ARNEAeNLPRllQSLSALdypkEKF--EVILVDDHSTDGTVQILEFAAAkpnfqlkilNNSRVSISGK-KNALT 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489829408  69 FAAKHATGKWILAIDADeCleeesyRKLEKQLKSPTEPIQMAQI 112
Cdd:cd04192   76 TAIKAAKGDWIVTTDAD-C------VVPSNWLLTFVAFIQKEQI 112
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 3-103 8.03e-05

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. 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 of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 44.50  E-value: 8.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   3 PLISICMIVKNEAHILRQSLASFR-------KFteEIIIVDTGSTDETKEIAQEFTD---FVYDFEWTGNFSDARNFAAK 72
Cdd:cd06439   29 PTVTIIIPAYNEEAVIEAKLENLLaldyprdRL--EIIVVSDGSTDGTAEIAREYADkgvKLLRFPERRGKAAALNRALA 106

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489829408  73 HATGKWILAIDADECLEEESYRKLEKQLKSP 103
Cdd:cd06439  107 LATGEIVVFTDANALLDPDALRLLVRHFADP 137
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
211-307 8.63e-05

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 41.69  E-value: 8.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 211 RLGNKKEALKEFSEAFRLRDHNHYIWaklsaYHIAELLEQEKRYDESLAIiEEARVIWPNVPEFPLKKANILYVNHQLED 290
Cdd:COG3063    4 KLGDLEEAEEYYEKALELDPDNADAL-----NNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLAELLLELGDYDE 77

                         90
                 ....*....|....*..
gi 489829408 291 AKEIYQSLLENAAIDYQ 307
Cdd:COG3063   78 ALAYLERALELDPSALR 94
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 2-85 1.59e-04

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 43.53  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   2 RPLISICMIVKNE-------AHILRQSLASFRKFteEIIIVDTGSTDETKEIAQEF-----TDFVYDFEWTGNFSDARNF 69
Cdd:PLN02726   8 AMKYSIIVPTYNErlnialiVYLIFKALQDVKDF--EIIVVDDGSPDGTQDVVKQLqkvygEDRILLRPRPGKLGLGTAY 85

                         90
                 ....*....|....*...
gi 489829408  70 AA--KHATGKWILAIDAD 85
Cdd:PLN02726  86 IHglKHASGDFVVIMDAD 103
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 27-105 2.21e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 43.99  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  27 KFTEEIIIVDTGSTDETKEIAQEF-TDFVYDFEWTGNFSDARN----FAAKH----ATGKWILAIDADECLEEESYRKLE 97
Cdd:PTZ00260 105 KFKYEIIIVNDGSKDKTLKVAKDFwRQNINPNIDIRLLSLLRNkgkgGAVRIgmlaSRGKYILMVDADGATDIDDFDKLE 184


                 ....*...
gi 489829408  98 KQLKSPTE 105
Cdd:PTZ00260 185 DIMLKIEQ 192
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
176-270 2.52e-04

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 40.54  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 176 EKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEALkEFSEAFRLRDHNHYIWaklsaYHIAELLEQEKRYD 255
Cdd:COG3063    3 LKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEAL-----LNLAELLLELGDYD 76

                         90
                 ....*....|....*
gi 489829408 256 ESLAIIEEARVIWPN 270
Cdd:COG3063   77 EALAYLERALELDPS 91
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 31-85 2.76e-04

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic 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. 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 42.08  E-value: 2.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489829408  31 EIIIVDTGSTDETKEIAQEFTDfvYDFEWTG-NFSdaRNF---AA-----KHATGKWILAIDAD 85
Cdd:cd04187   31 EIIFVDDGSTDRTLEILRELAA--RDPRVKViRLS--RNFgqqAAllaglDHARGDAVITMDAD 90
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 170-339 3.02e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 43.92  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  170 YMSEIVEKQDKSDRNLRLLE-KEVKNNKNSGFVHFNIGQEMNRLGNKKEALKEFSEAfrLRDHNHYIWAKLSAyhiAELL 248
Cdd:TIGR02917  95 LLARAYLLQGKFQQVLDELPgKTLLDDEGAAELLALRGLAYLGLGQLELAQKSYEQA--LAIDPRSLYAKLGL---AQLA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  249 EQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYqslleNAAIDYQPivlyeaTNFMPHKMLGTIYL 328
Cdd:TIGR02917 170 LAENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAY-----RKAIALRP------NNIAVLLALATILI 238

                         170
                  ....*....|.
gi 489829408  329 EEKDYTRAMTH 339
Cdd:TIGR02917 239 EAGEFEEAEKH 249
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 216-347 5.60e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 41.10  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 216 KEALKEFSEAFRLRDHNHYIWAKLSAYHIAELLEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIY 295
Cdd:COG5010   32 AGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYY 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489829408 296 QSLLENAaidyqpivlyeATNFMPHKMLGTIYLEEKDYTRAMTHFSKAYAEN 347
Cdd:COG5010  112 EKALALS-----------PDNPNAYSNLAALLLSLGQDDEAKAALQRALGTS 152
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 144-300 7.28e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.02  E-value: 7.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 144 IHEQL----EAIDKRPIAAGVAEVKIYHYGYMSEIVEKQDKSDRNLRLLEKEVKNNKNSGFVHFNIGQEMNRLGNKKEAL 219
Cdd:COG2956  119 IYEQEgdweKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAI 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 220 KEFSEAFRlRDHNHYIWaklsAYHIAELLEQEKRYDESLAIIEEARVIWPNVPEFpLKKANILYVNHQLEDAKEIYQSLL 299
Cdd:COG2956  199 AALERALE-QDPDYLPA----LPRLAELYEKLGDPEEALELLRKALELDPSDDLL-LALADLLERKEGLEAALALLERQL 272


                 .
gi 489829408 300 E 300
Cdd:COG2956  273 R 273
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 3-89 2.84e-03

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 39.49  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   3 PLISICMIVKN-EAHILRQSLASFRKFTE---EIIIVDTGSTD-ETKEIAQEFTD-----FVYDFEWTGNFSDARNFAAK 72
Cdd:cd04184    1 PLISIVMPVYNtPEKYLREAIESVRAQTYpnwELCIADDASTDpEVKRVLKKYAAqdpriKVVFREENGGISAATNSALE 80

                         90
                 ....*....|....*..
gi 489829408  73 HATGKWILAIDADECLE 89
Cdd:cd04184   81 LATGEFVALLDHDDELA 97
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 91-350 6.32e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 39.68  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408   91 ESYRKLEKQL-KSPTEPIQMAQIISFTGEKGRVTTTNQMARVYKNDGTICFRGVIheQLEAIDKRPIAAgvaeVKIYHYg 169
Cdd:TIGR02917 622 SSFKKLLALQpDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQIGLA--QLLLAAKRTESA----KKIAKS- 694

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  170 ymseiVEKQDKSDRNLRLLEKEV------------------KNNKNSGFVhFNIGQEMNRLGNKKEALKEFsEAFrLRDH 231
Cdd:TIGR02917 695 -----LQKQHPKAALGFELEGDLylrqkdypaaiqayrkalKRAPSSQNA-IKLHRALLASGNTAEAVKTL-EAW-LKTH 766

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408  232 NHYIWAKlsaYHIAELLEQEKRYDESlaiIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIYQSLLENAAIDYQPIVL 311
Cdd:TIGR02917 767 PNDAVLR---TALAELYLAQKDYDKA---IKHYQTVVKKAPDNAVVLNNLAWLYLELKDPRALEYAERALKLAPNIPAIL 840

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 489829408  312 yeatnfmphKMLGTIYLEEKDYTRAMTHFSKAYAENSSD 350
Cdd:TIGR02917 841 ---------DTLGWLLVEKGEADRALPLLRKAVNIAPEA 870
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
247-351 7.04e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 36.30  E-value: 7.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829408 247 LLEQEKRYDESLAIIEEARVIWPNVPEFPLKKANILYVNHQLEDAKEIyqslleNAAIDYQPivlyeaTNFMPHKMLGTI 326
Cdd:COG3063    1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL------EKALKLDP------NNAEALLNLAEL 68

                         90       100
                 ....*....|....*....|....*
gi 489829408 327 YLEEKDYTRAMTHFSKAYAENSSDY 351
Cdd:COG3063   69 LLELGDYDEALAYLERALELDPSAL 93
 
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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