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Conserved domains on  [gi|1756493346|gb|QFG01227|]
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glycosyltransferase [Psychrobacillus glaciei]

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

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  9445404|12691742
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 ...
 1-191 5.82e-51

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: 169.01  E-value: 5.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESVKGLVSEMIIIDTGSTDQTIDICKKHGAKVYpYMWKNDFADARNYGLSYATGDWILWLDADEEL 80
Cdd:cd02511     6 IITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVY-QRWWDGFGAQRNFALELATNDWVLSLDADERL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346  81 DATKKFLLQEILAHTNSYLLSLPILNYYgKTKPVNKDHVYLYYQLRVFRNYKDITFHNRIHETpllpAELTDKEIENISI 160
Cdd:cd02511    85 TPELADEILALLATDDYDGYYVPRRNFF-LGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQ----VVVDGGVGIVLKG 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1756493346 161 PIHHYGYlEDITETKQKGQRNLQLLQQEVAD 191
Cdd:cd02511   160 DILHYGY-KSLEEFLEKHNRYSSLEAKDLAA 189
Spy super family cl27809
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 138-337 1.61e-12

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


The actual alignment was detected with superfamily member COG3914:

Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 68.48  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 138 NRIHETPLLPAELTDKEIENISIPIHHYGYLEDITETKQKGQRNLQLLQQEVADPSHSPWIE--YHLASEYYRQGKYLQA 215
Cdd:COG3914    11 ALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAalLLLAALLELAALLLQA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 216 FQYVNESILLFLHQNQLPPSLLYKLKY--AMLIETNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFE 293
Cdd:COG3914    91 LGRYEEALALYRRALALNPDNAEALFNlgNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALR 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1756493346 294 KCLELGDHHTEYLILKGTgsfkagrykglCLEQLGRSEEAQEAF 337
Cdd:COG3914   171 RALELDPDNAEALNNLGN-----------ALQDLGRLEEAIAAY 203
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 1-191 5.82e-51

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: 169.01  E-value: 5.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESVKGLVSEMIIIDTGSTDQTIDICKKHGAKVYpYMWKNDFADARNYGLSYATGDWILWLDADEEL 80
Cdd:cd02511     6 IITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVY-QRWWDGFGAQRNFALELATNDWVLSLDADERL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346  81 DATKKFLLQEILAHTNSYLLSLPILNYYgKTKPVNKDHVYLYYQLRVFRNYKDITFHNRIHETpllpAELTDKEIENISI 160
Cdd:cd02511    85 TPELADEILALLATDDYDGYYVPRRNFF-LGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQ----VVVDGGVGIVLKG 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1756493346 161 PIHHYGYlEDITETKQKGQRNLQLLQQEVAD 191
Cdd:cd02511   160 DILHYGY-KSLEEFLEKHNRYSSLEAKDLAA 189
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-140 1.11e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 85.91  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESVK---GLVSEMIIIDTGSTDQTIDICKKHGA-----KVYPYMWKNDFADARNYGLSYATGDWIL 72
Cdd:COG0463     8 IPTYNEEEYLEEALESLLaqtYPDFEIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAAARGDYIA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346  73 WLDADEELDATKkflLQEILAH--TNSYLLSLPILNYYGKTKPVNKDHVYLYYQLRVFRNYKDITFHNRI 140
Cdd:COG0463    88 FLDADDQLDPEK---LEELVAAleEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRL 154
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 1-81 1.15e-15

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: 73.58  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESVK---GLVSEMIIIDTGSTDQTIDICKKH-----GAKVYPYMWKNDFADARNYGLSYATGDWIL 72
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLnqtYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAATGDYIA 83


                  ....*....
gi 1756493346  73 WLDADEELD 81
Cdd:pfam00535  84 FLDADDEVP 92
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 138-337 1.61e-12

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 68.48  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 138 NRIHETPLLPAELTDKEIENISIPIHHYGYLEDITETKQKGQRNLQLLQQEVADPSHSPWIE--YHLASEYYRQGKYLQA 215
Cdd:COG3914    11 ALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAalLLLAALLELAALLLQA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 216 FQYVNESILLFLHQNQLPPSLLYKLKY--AMLIETNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFE 293
Cdd:COG3914    91 LGRYEEALALYRRALALNPDNAEALFNlgNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALR 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1756493346 294 KCLELGDHHTEYLILKGTgsfkagrykglCLEQLGRSEEAQEAF 337
Cdd:COG3914   171 RALELDPDNAEALNNLGN-----------ALQDLGRLEEAIAAY 203
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 3-77 1.06e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 49.53  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   3 VKDEARSISNCLesVKGLVSEMIIIDTGSTDQTIDICKKHGAKVY----------PY------MWKndfadarnyGLSYA 66
Cdd:PRK13915   46 VGKVVDSIRPLL--MEPLVDELIVIDSGSTDATAERAAAAGARVVsreeilpelpPRpgkgeaLWR---------SLAAT 114

                          90
                  ....*....|.
gi 1756493346  67 TGDWILWLDAD 77
Cdd:PRK13915  115 TGDIVVFVDAD 125
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 233-319 2.83e-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: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 233 PPSLLYKLKYAMliETNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLILKGTG 312
Cdd:TIGR02917 159 LYAKLGLAQLAL--AENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATI 236


                  ....*..
gi 1756493346 313 SFKAGRY 319
Cdd:TIGR02917 237 LIEAGEF 243
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 269-298 1.77e-04

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 38.27  E-value: 1.77e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1756493346 269 VDLHFYKGDILYKMKNYREALQAFEKCLEL 298
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALEL 30
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 269-298 1.18e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 35.89  E-value: 1.18e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1756493346  269 VDLHFYKGDILYKMKNYREALQAFEKCLEL 298
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALEL 30
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 1-191 5.82e-51

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: 169.01  E-value: 5.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESVKGLVSEMIIIDTGSTDQTIDICKKHGAKVYpYMWKNDFADARNYGLSYATGDWILWLDADEEL 80
Cdd:cd02511     6 IITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVY-QRWWDGFGAQRNFALELATNDWVLSLDADERL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346  81 DATKKFLLQEILAHTNSYLLSLPILNYYgKTKPVNKDHVYLYYQLRVFRNYKDITFHNRIHETpllpAELTDKEIENISI 160
Cdd:cd02511    85 TPELADEILALLATDDYDGYYVPRRNFF-LGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQ----VVVDGGVGIVLKG 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1756493346 161 PIHHYGYlEDITETKQKGQRNLQLLQQEVAD 191
Cdd:cd02511   160 DILHYGY-KSLEEFLEKHNRYSSLEAKDLAA 189
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-140 1.11e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 85.91  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESVK---GLVSEMIIIDTGSTDQTIDICKKHGA-----KVYPYMWKNDFADARNYGLSYATGDWIL 72
Cdd:COG0463     8 IPTYNEEEYLEEALESLLaqtYPDFEIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAAARGDYIA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346  73 WLDADEELDATKkflLQEILAH--TNSYLLSLPILNYYGKTKPVNKDHVYLYYQLRVFRNYKDITFHNRI 140
Cdd:COG0463    88 FLDADDQLDPEK---LEELVAAleEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRL 154
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 1-81 1.15e-15

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: 73.58  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESVK---GLVSEMIIIDTGSTDQTIDICKKH-----GAKVYPYMWKNDFADARNYGLSYATGDWIL 72
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLnqtYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAATGDYIA 83


                  ....*....
gi 1756493346  73 WLDADEELD 81
Cdd:pfam00535  84 FLDADDEVP 92
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 1-137 8.43e-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: 71.00  E-value: 8.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESVKGL---VSEMIIIDTGSTDQTIDICKKHGAK-----VYPYMWKNDFADARNYGLSYATGDWIL 72
Cdd:cd00761     3 IPAYNEEPYLERCLESLLAQtypNFEVIVVDDGSTDGTLEILEEYAKKdprviRVINEENQGLAAARNAGLKAARGEYIL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756493346  73 WLDADEEL--DATKKFLLQE-------ILAHTNSYLLSLPILNYYGKTKPVNKDHVYLYYQLRVFRNYKDITFH 137
Cdd:cd00761    83 FLDADDLLlpDWLERLVAELladpeadAVGGPGNLLFRRELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAFR 156
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 138-337 1.61e-12

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 68.48  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 138 NRIHETPLLPAELTDKEIENISIPIHHYGYLEDITETKQKGQRNLQLLQQEVADPSHSPWIE--YHLASEYYRQGKYLQA 215
Cdd:COG3914    11 ALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAalLLLAALLELAALLLQA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 216 FQYVNESILLFLHQNQLPPSLLYKLKY--AMLIETNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFE 293
Cdd:COG3914    91 LGRYEEALALYRRALALNPDNAEALFNlgNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALR 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1756493346 294 KCLELGDHHTEYLILKGTgsfkagrykglCLEQLGRSEEAQEAF 337
Cdd:COG3914   171 RALELDPDNAEALNNLGN-----------ALQDLGRLEEAIAAY 203
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 197-337 7.90e-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: 59.44  E-value: 7.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 197 WIEYHLASEYYRQGKYLQAFQYVNEsillFLHQNQLPPSLLYKLKYaMLIETNSLDGAWPSIEKAILLYPDYVDLHFYKG 276
Cdd:COG4783     5 EALYALAQALLLAGDYDEAEALLEK----ALELDPDNPEAFALLGE-ILLQLGDLDEAIVLLHEALELDPDEPEARLNLG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1756493346 277 DILYKMKNYREALQAFEKCLELGDHHTEYLilkgtgsfkagRYKGLCLEQLGRSEEAQEAF 337
Cdd:COG4783    80 LALLKAGDYDEALALLEKALKLDPEHPEAY-----------LRLARAYRALGRPDEAIAAL 129
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 182-309 8.41e-11

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: 58.86  E-value: 8.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 182 LQLLQQEVA-DPSHSP-WIEyhLASEYYRQGKYLQAFQYVNESILLflhqnqLPPSLLYKLKYA-MLIETNSLDGAWPSI 258
Cdd:COG4235     3 IARLRQALAaNPNDAEgWLL--LGRAYLRLGRYDEALAAYEKALRL------DPDNADALLDLAeALLAAGDTEEAEELL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1756493346 259 EKAILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLILK 309
Cdd:COG4235    75 ERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARLLE 125
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 7-141 1.62e-10

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: 59.87  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   7 ARSISNCLESV-----KGLvsEMIIIDTGSTDQTIDICKKHGAKVYPYMWKNDF--ADARNYGLSYATGDWILWLDADEe 79
Cdd:cd06433    10 AETLEETIDSVlsqtyPNI--EYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKgiYDAMNKGIALATGDIIGFLNSDD- 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756493346  80 ldatkkFLLQEILAHTNSYLLSLPILNY-YGKTKPVNKDHVYLYYQLRVFRNYKDITFHNRIH 141
Cdd:cd06433    87 ------TLLPGALLAVVAAFAEHPEVDVvYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPIC 143
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-94 1.75e-10

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: 60.91  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   3 VKDEARSISNCLESVKGL-----VSEMIIIDTGSTDQTIDICKKHGAKVYP--YMWKND---FADARNYGLSYATGDWIL 72
Cdd:COG1215    37 AYNEEAVIEETLRSLLAQdypkeKLEVIVVDDGSTDETAEIARELAAEYPRvrVIERPEnggKAAALNAGLKAARGDIVV 116

                          90       100
                  ....*....|....*....|..
gi 1756493346  73 WLDADEELDATkkfLLQEILAH 94
Cdd:COG1215   117 FLDADTVLDPD---WLRRLVAA 135
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-96 2.39e-10

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 59.24  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESVKGLVS---EMIIIDTGSTDQTIDICKKH---GAKVYPYMWKNDFADARNYGLSYATGDWILWL 74
Cdd:COG1216     9 IPTYNRPELLRRCLESLLAQTYppfEVIVVDNGSTDGTAELLAALafpRVRVIRNPENLGFAAARNLGLRAAGGDYLLFL 88

                          90       100
                  ....*....|....*....|..
gi 1756493346  75 DADEELDATkkfLLQEILAHTN 96
Cdd:COG1216    89 DDDTVVEPD---WLERLLAAAC 107
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 5-77 2.76e-10

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: 59.51  E-value: 2.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   5 DEARSISNCLESVKGLVS---EMIIIDTGSTDQTIDICKKHGAKVYP-------YMwkndfadarNYGLSYATGDWILWL 74
Cdd:cd02522     9 NEAENLPRLLASLRRLNPlplEIIVVDGGSTDGTVAIARSAGVVVISspkgrarQM---------NAGAAAARGDWLLFL 79


                  ...
gi 1756493346  75 DAD 77
Cdd:cd02522    80 HAD 82
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 4-81 5.71e-10

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: 57.62  E-value: 5.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   4 KDEARSISNCLESVKGLVS---EMIIIDTGSTDQTIDICKKHGA-----KVYPYMWKNDF-ADARNYGLSYATGDWILWL 74
Cdd:cd06423     6 YNEEAVIERTIESLLALDYpklEVIVVDDGSTDDTLEILEELAAlyirrVLVVRDKENGGkAGALNAGLRHAKGDIVVVL 85


                  ....*..
gi 1756493346  75 DADEELD 81
Cdd:cd06423    86 DADTILE 92
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
200-337 6.13e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.86  E-value: 6.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 200 YHLASEYYRQGKYLQAFQYVNESILLFLHQnqlpPSLLYKLKYAmLIETNSLDGAWPSIEKAILLYPDYVDLHFYKGDIL 279
Cdd:COG0457    46 YNLGLAYLRLGRYEEALADYEQALELDPDD----AEALNNLGLA-LQALGRYEEALEDYDKALELDPDDAEALYNLGLAL 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1756493346 280 YKMKNYREALQAFEKCLELGDHHTEylilkgtgsfkAGRYKGLCLEQLGRSEEAQEAF 337
Cdd:COG0457   121 LELGRYDEAIEAYERALELDPDDAD-----------ALYNLGIALEKLGRYEEALELL 167
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
200-337 7.26e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 58.48  E-value: 7.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 200 YHLASEYYRQGKYLQAFQYVNESILLflhqNQLPPSLLYKLKYAmLIETNSLDGAWPSIEKAILLYPDYVDLHFYKGDIL 279
Cdd:COG0457    12 NNLGLAYRRLGRYEEAIEDYEKALEL----DPDDAEALYNLGLA-YLRLGRYEEALADYEQALELDPDDAEALNNLGLAL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1756493346 280 YKMKNYREALQAFEKCLELGDHHTEYLilkgtgsfkagRYKGLCLEQLGRSEEAQEAF 337
Cdd:COG0457    87 QALGRYEEALEDYDKALELDPDDAEAL-----------YNLGLALLELGRYDEAIEAY 133
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 6-77 2.36e-09

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: 56.04  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   6 EARSISNCLESVK-----GLVSEMIIIDTGSTDQTIDICKKHGAKVyPYMWKNDFadARNYG--------LSYATGDWIL 72
Cdd:cd04179     8 EEENIPELVERLLavleeGYDYEIIVVDDGSTDGTAEIARELAARV-PRVRVIRL--SRNFGkgaavragFKAARGDIVV 84


                  ....*
gi 1756493346  73 WLDAD 77
Cdd:cd04179    85 TMDAD 89
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 182-308 7.82e-09

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 56.93  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 182 LQLLQQEVADPSHSPWIEYHLASEYYRQGKYLQAFQYVNESIllflhqnQLPPSLL-YKLKYAM-LIETNSLDGAWPSIE 259
Cdd:COG3914    98 LALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRAL-------ALNPDFAeAYLNLGEaLRRLGRLEEAIAALR 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1756493346 260 KAILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLIL 308
Cdd:COG3914   171 RALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSN 219
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 244-321 8.91e-09

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: 53.09  E-value: 8.91e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1756493346 244 MLIETNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLILKGTGSFKAGRYKG 321
Cdd:COG4235    26 AYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAE 103
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 182-298 9.05e-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: 53.27  E-value: 9.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 182 LQLLQQEVADPSHSPWIEYHLASEYYRQGKYLQAFQYVNESILLFlhqnqlPPSLLYKLKYAM-LIETNSLDGAWPSIEK 260
Cdd:COG4783    24 EALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELD------PDEPEARLNLGLaLLKAGDYDEALALLEK 97

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1756493346 261 AILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLEL 298
Cdd:COG4783    98 ALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
251-337 3.77e-08

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 53.38  E-value: 3.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 251 LDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLilkgtgsfkagRYKGLCLEQLGRS 330
Cdd:COG4785    89 YDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAY-----------LNRGIALYYLGRY 157


                  ....*..
gi 1756493346 331 EEAQEAF 337
Cdd:COG4785   158 ELAIADL 164
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 202-337 2.21e-07

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: 49.96  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 202 LASEYYRQGKYLQAFQYVNESILLFLHQNQLPPSLLYKLKYAMLIETNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYK 281
Cdd:COG5010    21 RTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSR 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1756493346 282 MKNYREALQAFEKCLELGDHHTEylilkgtgsfkAGRYKGLCLEQLGRSEEAQEAF 337
Cdd:COG5010   101 SGDKDEAKEYYEKALALSPDNPN-----------AYSNLAALLLSLGQDDEAKAAL 145
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 1-81 4.20e-07

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: 50.31  E-value: 4.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESV------KGLVsEMIIIDTGSTDQTIDICKKHGAKVYPYMWKND----FADARNYGLSYATGDW 70
Cdd:cd02525     6 IPVRNEEKYIEELLESLlnqsypKDLI-EIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNpkriQSAGLNIGIRNSRGDI 84

                          90
                  ....*....|.
gi 1756493346  71 ILWLDADEELD 81
Cdd:cd02525    85 IIRVDAHAVYP 95
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 183-337 7.17e-07

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: 50.11  E-value: 7.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 183 QLLQQEVADPSHSPWIEYHLASEYYRQGKYLQAFQYVNEsillFLHQNQLPPSLLYKLKYAmLIETNSLDGAWPSIEKAI 262
Cdd:COG2956    97 ELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLER----LLKLGPENAHAYCELAEL-YLEQGDYDEAIEALEKAL 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1756493346 263 LLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLILKGTgsfkagrykglCLEQLGRSEEAQEAF 337
Cdd:COG2956   172 KLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAE-----------LYEKLGDPEEALELL 235
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 3-77 1.06e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 49.53  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   3 VKDEARSISNCLesVKGLVSEMIIIDTGSTDQTIDICKKHGAKVY----------PY------MWKndfadarnyGLSYA 66
Cdd:PRK13915   46 VGKVVDSIRPLL--MEPLVDELIVIDSGSTDATAERAAAAGARVVsreeilpelpPRpgkgeaLWR---------SLAAT 114

                          90
                  ....*....|.
gi 1756493346  67 TGDWILWLDAD 77
Cdd:PRK13915  115 TGDIVVFVDAD 125
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
264-337 1.79e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.46  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 264 LYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLILKGTGSFKAGRYK----------------------- 320
Cdd:COG0457     3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEealadyeqaleldpddaealnnl 82

                          90
                  ....*....|....*..
gi 1756493346 321 GLCLEQLGRSEEAQEAF 337
Cdd:COG0457    83 GLALQALGRYEEALEDY 99
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 168-335 1.88e-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: 48.57  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 168 LEDITETKQKGQRNLQLLQQEVADPSHSPWIEYHLASEYYRQGKYLQAFQYVNEsiLLFLHQNQLPPSLLYKLkyaMLIE 247
Cdd:COG2956   116 LAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEK--ALKLDPDCARALLLLAE---LYLE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 248 TNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLILkgtgsfkagrykGLCLEQL 327
Cdd:COG2956   191 QGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLAL------------ADLLERK 258


                  ....*...
gi 1756493346 328 GRSEEAQE 335
Cdd:COG2956   259 EGLEAALA 266
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 257-337 1.99e-06

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: 46.54  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 257 SIEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLILKGTgsfkagrykglCLEQLGRSEEAQEA 336
Cdd:COG4235     5 RLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAE-----------ALLAAGDTEEAEEL 73


                  .
gi 1756493346 337 F 337
Cdd:COG4235    74 L 74
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 233-319 2.83e-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: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 233 PPSLLYKLKYAMliETNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLILKGTG 312
Cdd:TIGR02917 159 LYAKLGLAQLAL--AENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATI 236


                  ....*..
gi 1756493346 313 SFKAGRY 319
Cdd:TIGR02917 237 LIEAGEF 243
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 3-77 6.01e-06

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: 45.93  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   3 VKDEARSISNCLESVK------GLVSEMIIIDTGSTDQTIDICKKHgAKVYP---YMwknDFAdaRNYG--------LSY 65
Cdd:cd04187     5 VYNEEENLPELYERLKavleslGYDYEIIFVDDGSTDRTLEILREL-AARDPrvkVI---RLS--RNFGqqaallagLDH 78

                          90
                  ....*....|..
gi 1756493346  66 ATGDWILWLDAD 77
Cdd:cd04187    79 ARGDAVITMDAD 90
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 14-77 7.17e-06

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: 46.41  E-value: 7.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1756493346  14 LESVKGLVSEMIIIDTGSTDQTIDICKKHGAKVypymwKNDFAD---ARNYG--------LSYATGDWILWLDAD 77
Cdd:cd04188    23 LEERPSFSYEIIVVDDGSKDGTAEVARKLARKN-----PALIRVltlPKNRGkggavragMLAARGDYILFADAD 92
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
182-337 9.68e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 46.15  E-value: 9.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 182 LQLLQQEVADPSHSPWIEYHLASEYYRQGKYLQAFQYVNESILLflhqNQLPPSLLYKLKYAmLIETNSLDGAWPSIEKA 261
Cdd:COG0457    62 LADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALEL----DPDDAEALYNLGLA-LLELGRYDEAIEAYERA 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1756493346 262 ILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLILKGTGSFKAGRYKGLCLEQLGRSEEAQEAF 337
Cdd:COG0457   137 LELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLA 212
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
245-320 1.05e-05

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 43.62  E-value: 1.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1756493346 245 LIETNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNYREALQaFEKCLELGDHHTEYLILKGTGSFKAGRYK 320
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYD 76
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 182-320 1.36e-05

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: 45.88  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 182 LQLLQQEVADPSHSPWIEYHLASEYYRQGKYLQAFQYvnesillflHQNQL---PPSLLYKLKYAML-IETNSLDGAWPS 257
Cdd:COG2956    28 IDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRI---------HQKLLerdPDRAEALLELAQDyLKAGLLDRAEEL 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756493346 258 IEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLILKGTGSFKAGRYK 320
Cdd:COG2956    99 LEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD 161
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 1-81 2.18e-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: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   1 MIVKDEARSISNCLESVKGLVS---EMIIIDTGSTDQTIDICKKHGAKV-YPYMWKN-DFADARNYGLSYATGDWILWLD 75
Cdd:cd04186     3 IVNYNSLEYLKACLDSLLAQTYpdfEVIVVDNASTDGSVELLRELFPEVrLIRNGENlGFGAGNNQGIREAKGDYVLLLN 82


                  ....*.
gi 1756493346  76 ADEELD 81
Cdd:cd04186    83 PDTVVE 88
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 23-81 2.20e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 45.81  E-value: 2.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756493346  23 EMIIIDTGSTDQTIDICKKHgAKVYPYM----WKNDFAD-ARNYGLSYATGDWILWLDADEELD 81
Cdd:PRK10073   37 EIIIVNDGSTDNSVEIAKHY-AENYPHVrllhQANAGVSvARNTGLAVATGKYVAFPDADDVVY 99
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 6-77 2.39e-05

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 44.83  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   6 EARSISNCLESVKGLVS----EMIIIDTGSTDQTIDICKKHgAKVYPYMW------KNDFADARNYGLSYATGDWILWLD 75
Cdd:cd06442     8 ERENIPELIERLDAALKgidyEIIVVDDNSPDGTAEIVREL-AKEYPRVRlivrpgKRGLGSAYIEGFKAARGDVIVVMD 86


                  ..
gi 1756493346  76 AD 77
Cdd:cd06442    87 AD 88
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 206-298 7.82e-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: 42.64  E-value: 7.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 206 YYRQGKYLQAFQYVNESILLFLHQnqlpPSLLYKLKYAmLIETNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNY 285
Cdd:COG5010    64 YNKLGDFEESLALLEQALQLDPNN----PELYYNLALL-YSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQD 138

                          90
                  ....*....|...
gi 1756493346 286 REALQAFEKCLEL 298
Cdd:COG5010   139 DEAKAALQRALGT 151
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 259-337 8.10e-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: 41.52  E-value: 8.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 259 EKAILLYPD---YVDLHFYKGDILYKMKNYREALQAFEKCLELGDHHTEYLilkgtgsfKAGRYKGLCLEQLGRSEEAQE 335
Cdd:COG1729    17 KAFLKRYPNsplAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAP--------DALLKLGLSYLELGDYDKARA 88


                  ..
gi 1756493346 336 AF 337
Cdd:COG1729    89 TL 90
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
200-337 1.02e-04

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 42.98  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 200 YHLASEYYRQGKYLQAFQYVNESILLFlhqnqlP--PSLLYKLKYAMLIETNsLDGAWPSIEKAILLYPDYVDLHFYKGD 277
Cdd:COG4785    77 YERGVAYDSLGDYDLAIADFDQALELD------PdlAEAYNNRGLAYLLLGD-YDAALEDFDRALELDPDYAYAYLNRGI 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1756493346 278 ILYKMKNYREALQAFEKCLELGDHHTE-----YLILKGTGSFKA----GRYKGLCLEQLGRSEEAQEAF 337
Cdd:COG4785   150 ALYYLGRYELAIADLEKALELDPNDPEralwlYLAERKLDPEKAlallLEDWATAYLLQGDTEEARELF 218
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 21-78 1.27e-04

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


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 40.31  E-value: 1.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1756493346  21 VSEMIIIDTGSTDQTIDICKKHGA-KVYPymWKNDFADARnYGL--------SYATGDWILWLDADE 78
Cdd:pfam13704  19 FDHIYVYDNGSDDGTAEILARLPDvSILR--SDLSYKDAR-FQVdwrnallaRYAEADWVLVVDADE 82
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 23-130 1.70e-04

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 42.65  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346  23 EMIIIDTGSTDQTID----ICKKHGAKVYPYMWKNDF--ADARNYGLSYATGDWILWLDAD-----EELDATKKFLLQEI 91
Cdd:pfam10111  31 ELIIINDGSTDKTLEevssIKDHNLQVYYPNAPDTTYslAASRNRGTSHAIGEYISFIDGDclwspDKFEKQLKIATSLA 110

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1756493346  92 LAHTNSYLLSLPILNYYGKTKPVNKDHVYLYYQLRVFRN 130
Cdd:pfam10111 111 LQENIQAAVVLPVTDLNDESSNFLRRGGDLTASGDVLRD 149
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 269-298 1.77e-04

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 38.27  E-value: 1.77e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1756493346 269 VDLHFYKGDILYKMKNYREALQAFEKCLEL 298
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALEL 30
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
206-298 2.16e-04

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.77  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 206 YYRQGKYLQAFQYVNESILLflhqNQLPPSLLYKLKYAmLIETNSLDGAWpSIEKAILLYPDYVDLHFYKGDILYKMKNY 285
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALEL----DPDNADALNNLGLL-LLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDY 75

                          90
                  ....*....|...
gi 1756493346 286 REALQAFEKCLEL 298
Cdd:COG3063    76 DEALAYLERALEL 88
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 13-77 2.39e-04

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 41.41  E-value: 2.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1756493346  13 CLESVKG---LVSEMIIIDTGSTDQTIDICKKHGAKV-YP--YMWKND--F--ADARNYGLSYATGDWILWLDAD 77
Cdd:cd06420    15 VLKSVLNqsiLPFEVIIADDGSTEETKELIEEFKSQFpIPikHVWQEDegFrkAKIRNKAIAAAKGDYLIFIDGD 89
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 3-77 3.34e-04

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: 41.51  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346   3 VKDEARSISNCLESVKGL-----VSEMIIIDTGSTDQTIDICKKHGAKVYPYMWKNDF--------ADARNYGLSYATGD 69
Cdd:cd04192     5 ARNEAENLPRLLQSLSALdypkeKFEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNsrvsisgkKNALTTAIKAAKGD 84


                  ....*...
gi 1756493346  70 WILWLDAD 77
Cdd:cd04192    85 WIVTTDAD 92
TPR_1 pfam00515
Tetratricopeptide repeat;
269-298 3.41e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.40  E-value: 3.41e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1756493346 269 VDLHFYKGDILYKMKNYREALQAFEKCLEL 298
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALEL 30
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 269-298 1.18e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 35.89  E-value: 1.18e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1756493346  269 VDLHFYKGDILYKMKNYREALQAFEKCLEL 298
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALEL 30
TPR_12 pfam13424
Tetratricopeptide repeat;
276-337 3.36e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 35.83  E-value: 3.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1756493346 276 GDILYKMKNYREALQAFEKCLEL------GDHHTEYLILKGTgsfkagrykGLCLEQLGRSEEAQEAF 337
Cdd:pfam13424  10 AAVLRRLGRYDEALELLEKALEIarrllgPDHPLTATTLLNL---------GRLYLELGRYEEALELL 68
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 217-337 5.45e-03

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: 37.25  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 217 QYVNESILLFLHQNQLPPSLLYKLKYAMLIETNSLDGAWPSIEKAILLYPDYVDLHFYKGDILYKMKNYREALQAFEKCL 296
Cdd:COG5010     2 RALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQAL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1756493346 297 ELGDHHTEYLilkgtgsfkagRYKGLCLEQLGRSEEAQEAF 337
Cdd:COG5010    82 QLDPNNPELY-----------YNLALLYSRSGDKDEAKEYY 111
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 14-77 6.43e-03

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: 37.61  E-value: 6.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1756493346  14 LESV---KGLVSEMIIIDTGSTDQTIDICKKHGAKvYPYMWKNDFAD-----ARNY--GLSYATGDWILWLDAD 77
Cdd:cd04196    17 LDSIlaqTYKNDELIISDDGSTDGTVEIIKEYIDK-DPFIIILIRNGknlgvARNFesLLQAADGDYVFFCDQD 89
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 23-77 7.06e-03

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 37.37  E-value: 7.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1756493346  23 EMIIIDTGSTDQTIDICKKHgAKVY--------PYMWKNDFADARNYGLSYATGDWILWLDAD 77
Cdd:PLN02726   42 EIIVVDDGSPDGTQDVVKQL-QKVYgedrillrPRPGKLGLGTAYIHGLKHASGDFVVIMDAD 103
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
276-337 7.33e-03

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 37.55  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 276 GDILYKMKNYREALQAFEKCLElGDHHTEYLILKGTGS--FKAGRYK-------------------------GLCLEQLG 328
Cdd:COG4700    96 ADALLELGRYDEAIELYEEALT-GIFADDPHILLGLAQalFELGRYAealetlekliaknpdfkssdahllyARALEALG 174


                  ....*....
gi 1756493346 329 RSEEAQEAF 337
Cdd:COG4700   175 DLEAAEAEL 183
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 205-297 9.87e-03

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: 35.35  E-value: 9.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1756493346 205 EYYRQGKYLQAFQYVNESILLFlHQNQLPPSLLYKLKYAmLIETNSLDGAWPSIEKAILLYPD---YVDLHFYKGDILYK 281
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRY-PNSPLAPDALYWLGEA-YYALGDYDEAAEAFEKLLKRYPDspkAPDALLKLGLSYLE 79

                          90
                  ....*....|....*.
gi 1756493346 282 MKNYREALQAFEKCLE 297
Cdd:COG1729    80 LGDYDKARATLEELIK 95
 
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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