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Conserved domains on  [gi|488972388|ref|WP_002883307|]
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MULTISPECIES: glucose-1-phosphate thymidylyltransferase RfbA [Klebsiella]

Protein Classification

glucose-1-phosphate thymidylyltransferase( domain architecture ID 11492097)

glucose-1-phosphate thymidylyltransferase catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis

EC:  2.7.7.24
Gene Ontology:  GO:0008879|GO:0046872|GO:0000271
PubMed:  9445404|12691742
SCOP:  4000694

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-287 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


:

Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 570.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   82 TPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  162 KQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASMFVQTVE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 488972388  242 KRQGFKIACLEEIGWRNGWLDDDGVKRAAKRLEKTGYGQYLLDLLR 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
 
Name Accession Description Interval E-value
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-287 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 570.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   82 TPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  162 KQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASMFVQTVE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 488972388  242 KRQGFKIACLEEIGWRNGWLDDDGVKRAAKRLEKTGYGQYLLDLLR 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-293 0e+00

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 552.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  81 PTPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 161 PKQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASMFVQTV 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488972388 241 EKRQGFKIACLEEIGWRNGWLDDDGVKRAAKRLEKTGYGQYLLDLLRARPRQY 293
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRARV 293
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 2.00e-172

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 476.30  E-value: 2.00e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  81 PTPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 161 PKQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASMFVQTV 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-288 4.23e-139

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 394.04  E-value: 4.23e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQP 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  82 TPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFsPKLRSVAARTE-GATIFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDL-PKLMEAAVNKEsGATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 161 PKQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASMFVQTV 240
Cdd:PRK15480 164 PLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATI 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 488972388 241 EKRQGFKIACLEEIGWRNGWLDDDGVKRAAKRLEKTGYGQYLLDLLRA 288
Cdd:PRK15480 244 EERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKG 291
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 6.51e-97

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 285.30  E-value: 6.51e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   81 PTPDGLAQAFIIGEAFLNGEPA-CLVLGDNIFFGQSFSPKLRSVAARTE--GATIFGYQVMDPERFGVVEFDDNFRALSL 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  158 EEKPKQPK-SNWAVTGLYFYDGKVTEY-AKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASM 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 488972388  236 FV 237
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-287 0e+00

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 570.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   82 TPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  162 KQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASMFVQTVE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 488972388  242 KRQGFKIACLEEIGWRNGWLDDDGVKRAAKRLEKTGYGQYLLDLLR 287
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLLE 286
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-293 0e+00

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 552.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  81 PTPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 161 PKQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASMFVQTV 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488972388 241 EKRQGFKIACLEEIGWRNGWLDDDGVKRAAKRLEKTGYGQYLLDLLRARPRQY 293
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSNRARV 293
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 2.00e-172

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 476.30  E-value: 2.00e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  81 PTPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 161 PKQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASMFVQTV 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-288 4.23e-139

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 394.04  E-value: 4.23e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQP 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  82 TPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFsPKLRSVAARTE-GATIFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDL-PKLMEAAVNKEsGATVFAYHVNDPERYGVVEFDQNGTAISLEEK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 161 PKQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASMFVQTV 240
Cdd:PRK15480 164 PLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATI 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 488972388 241 EKRQGFKIACLEEIGWRNGWLDDDGVKRAAKRLEKTGYGQYLLDLLRA 288
Cdd:PRK15480 244 EERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMIKG 291
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 6.51e-97

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 285.30  E-value: 6.51e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   81 PTPDGLAQAFIIGEAFLNGEPA-CLVLGDNIFFGQSFSPKLRSVAARTE--GATIFGYQVMDPERFGVVEFDDNFRALSL 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  158 EEKPKQPK-SNWAVTGLYFYDGKVTEY-AKRVKPSERGELEITSINQMYLEDGALTVELLGRGFAWLDTGTHDSLIEASM 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 488972388  236 FV 237
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-237 3.88e-71

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 219.36  E-value: 3.88e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIT--TPDDLRDFqrlLGDGSEFGIALHYA 78
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVgpTGEEIKEA---LGDGSRFGVRITYI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  79 VQPTPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGqSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNfRALSLE 158
Cdd:cd04189   78 LQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488972388 159 EKPKQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFaWLDTGTHDSLIEASMFV 237
Cdd:cd04189  156 EKPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-225 6.69e-59

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 187.40  E-value: 6.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   3 GIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDlRDFQRLLGDGSEFGIALHYAVQPT 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  83 PDGLAQAFIIGEAFLNGEPACLVLGDNIFFGqSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRALSLEEKPK 162
Cdd:cd04181   80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488972388 163 QPKSNWAVTGLYFYDGKVTEYAKRVKPseRGELEITSINQMYLEDGALTVELLgrGFAWLDTG 225
Cdd:cd04181  159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-249 8.06e-57

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 186.45  E-value: 8.06e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388    2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAVQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   82 TPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGqSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRALSLEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  162 KQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGFaWLDTGTHDSLIEAS-MFVQTV 240
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANrLILDEV 238

                         250
                  ....*....|
gi 488972388  241 EKR-QGFKIA 249
Cdd:TIGR01208 239 EREvQGVDDE 248
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-234 3.40e-48

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 165.07  E-value: 3.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388    1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTP--DDLRDFqrlLGDGSEFGIALHYA 78
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYgkEKVREY---FGDGSRGGVPIEYV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   79 VQPTPDGLAQAFIIGEAFLNGEpaCLVL-GDNIFfgqsfSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNfRALSL 157
Cdd:TIGR03992  78 VQEEQLGTADALGSAKEYVDDE--FLVLnGDVLL-----DSDLLERLIRAEAPAIAVVEVDDPSDYGVVETDGG-RVTGI 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488972388  158 EEKPKQPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYLEDGALTVELLGRGfaWLDTGTHDSLIEAS 234
Cdd:TIGR03992 150 VEKPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDAN 224
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-233 5.57e-41

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 141.83  E-value: 5.57e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITT--PDDLRDFqrlLGDGSEFGIALHYAV 79
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGylAEQIEEY---FGDGSRFGVRITYVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  80 QPTP----DGLAQAfiigEAFLNGEPACLVLGDnIFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRAL 155
Cdd:COG1208   78 EGEPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVT 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488972388 156 SLEEKPKQPKSNWAVTGLYFYDGKVTEYakrVKPSERGELEiTSINQMyLEDGALTVELLgRGFaWLDTGTHDSLIEA 233
Cdd:COG1208  153 RFVEKPEEPPSNLINAGIYVLEPEIFDY---IPEGEPFDLE-DLLPRL-IAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-234 5.53e-34

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 124.57  E-value: 5.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTP------------------------D 56
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdrsyeleetlekkgkT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  57 DLRDFQRLLGDGsefgIALHYAVQPTPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSF-SPKLRSVAARTeGATIFGY 135
Cdd:cd02541   81 DLLEEVRIISDL----ANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPcLKQLIEAYEKT-GASVIAV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 136 QVMDPE---RFGVVEF----DDNFRALSLEEKPKQ--PKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEIT-SINQMYL 205
Cdd:cd02541  156 EEVPPEdvsKYGIVKGekidGDVFKVKGLVEKPKPeeAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTdAIAKLLE 235

                        250       260
                 ....*....|....*....|....*....
gi 488972388 206 EDGALTVELLGRgfaWLDTGTHDSLIEAS 234
Cdd:cd02541  236 EEPVYAYVFEGK---RYDCGNKLGYLKAT 261
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 1.59e-21

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 91.63  E-value: 1.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYplSV--LMLAGIREILIITTP------------------------ 55
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRgkraiedhfdrsyeleatleakgk 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  56 -DDLRDFQRLLGDGSefgiaLHYAVQPTPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQsfSPKLRSV--AARTEGATI 132
Cdd:COG1210   83 eELLEEVRSISPLAN-----IHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCLKQMieVYEETGGSV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 133 FGYQVMDPE---RFGVVE----FDDNFRALSLEEKPKQPK--SNWAVTGLYFYDGKVTEYAKRVKPSERGELEIT-SINQ 202
Cdd:COG1210  156 IAVQEVPPEevsKYGIVDgeeiEGGVYRVTGLVEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTdAIAA 235

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488972388 203 MYLEDGALTVELLGRgfaWLDTGTHDSLIEA 233
Cdd:COG1210  236 LAKEEPVYAYEFEGK---RYDCGDKLGYLKA 263
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-233 2.74e-21

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 89.53  E-value: 2.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   4 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIT--TPDDLRDFqrlLGDGSEFGIALHYAVQP 81
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVgyLAEQIEEY---FGDGYRGGIRIYYVIEP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  82 TPDGLAQAFIIGEAFLnGEPACLVL-GDNiFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNFRALSLEEK 160
Cdd:cd06915   79 EPLGTGGAIKNALPKL-PEDQFLVLnGDT-YFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488972388 161 PKQPKSNWAVTGLYFYDGKVTEYAKRVKPS-ERGELEItsinqmYLEDGALtvellgRGFA----WLDTGTHDSLIEA 233
Cdd:cd06915  157 GPGAAPGLINGGVYLLRKEILAEIPADAFSlEADVLPA------LVKRGRL------YGFEvdgyFIDIGIPEDYARA 222
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-226 5.33e-21

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 89.19  E-value: 5.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITT--PDDLRDFQRLLGDgsEFGIALHYA 78
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNyrPEDMVPFLKEYEK--KLGIKITFS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  79 VQPTPDGLAQAFIIGEAFLNGEPAC-LVLGDNIFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFD-DNFRALS 156
Cdd:cd06425   79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDeNTGRIER 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488972388 157 LEEKPKQPKSNWAVTGLYFYDGKVTeyakrvkpsERGELEITSINQ----MYLEDGALTVELLgRGFaWLDTGT 226
Cdd:cd06425  159 FVEKPKVFVGNKINAGIYILNPSVL---------DRIPLRPTSIEKeifpKMASEGQLYAYEL-PGF-WMDIGQ 221
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-233 1.97e-18

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 81.79  E-value: 1.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   4 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITT--PDDLRDFqrlLGDGSEFGIALHYAVQP 81
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNylAEMIEDY---FGDGSKFGVNISYVRED 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  82 TPDGLAQAFIIGEAFLNgEPACLVLGD---NIFFGQSFSPKLRSVAARTEGATIFGYQVmdPerFGVVEFDDNfRALSLE 158
Cdd:cd06426   79 KPLGTAGALSLLPEKPT-DPFLVMNGDiltNLNYEHLLDFHKENNADATVCVREYEVQV--P--YGVVETEGG-RITSIE 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488972388 159 EKPKQpksNWAV-TGLYFYDGKVTEYakrVKPSERgeLEITSINQMYLEDGALTVELLGRGFaWLDTGTHDSLIEA 233
Cdd:cd06426  153 EKPTH---SFLVnAGIYVLEPEVLDL---IPKNEF--FDMPDLIEKLIKEGKKVGVFPIHEY-WLDIGRPEDYEKA 219
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-57 2.45e-16

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 75.77  E-value: 2.45e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488972388   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDD 57
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-57 3.22e-13

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 67.28  E-value: 3.22e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488972388   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDD 57
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHS 57
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-198 1.35e-12

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 66.84  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   1 MKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPD------------------DLRDFQ 62
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASknavenhfdtsyelesllEQRVKR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  63 RLLGDGSEF---GIALHYAVQPTPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFSPKLRSVAARTEGATIFGY-QVM 138
Cdd:PRK10122  84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNETGRsQVL 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488972388 139 ------DPERFGVVEFDDNF-------RALSLEEKPKQPK---SNWAVTGLYFYDGKVTEYAKRVKPSERGELEIT 198
Cdd:PRK10122 164 akrmpgDLSEYSVIQTKEPLdregkvsRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-53 9.41e-11

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 60.64  E-value: 9.41e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488972388   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIT 53
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT 52
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-206 1.05e-10

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 61.08  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIT------------TPDDL-----RDFQRL 64
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThssknsienhfdTSFELeamleKRVKRQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  65 LGDGSEFGIALHYAV----QPTPDGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFSPKLRSVAA------RTEGATIFG 134
Cdd:PRK13389  90 LLDEVQSICPPHVTImqvrQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEmirrfdETGHSQIMV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 135 YQVMDPERFGVVEFD-------DNFRALSLEEKPK--QPKSNWAVTGLYFYDGKVTEYAKRVKPSERGELEITSINQMYL 205
Cdd:PRK13389 170 EPVADVTAYGVVDCKgvelapgESVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDMLI 249


                 .
gi 488972388 206 E 206
Cdd:PRK13389 250 E 250
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-233 6.12e-10

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 57.97  E-value: 6.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   2 KGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREIlIITT---PDDLRDFqrlLGDgSEFGIALHYA 78
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlADQIEAH---LGD-SRFGLRITIS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  79 VQP-----TPDGLAQAfiigEAFLNGEPACLVLGDNIFFGqSFSPKLRSVAARTEGATIFGYQVMDPERFGVVEFDDNfR 153
Cdd:cd06422   76 DEPdelleTGGGIKKA----LPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLD-A 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 154 ALSLEEKPKQPKSNWAVTGLYFYDGKVTeyakrvkpsERGELEITSINQMY---LEDGALTVELLgRGFaWLDTGTHDSL 230
Cdd:cd06422  150 DGRLRRGGGGAVAPFTFTGIQILSPELF---------AGIPPGKFSLNPLWdraIAAGRLFGLVY-DGL-WFDVGTPERL 218


                 ...
gi 488972388 231 IEA 233
Cdd:cd06422  219 LAA 221
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-180 6.18e-10

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 59.32  E-value: 6.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   3 GIILAGGSGTRLHPITRGVSKqllpiydkPMIYY---------PLSVLMLAGIREILIITtpddlrdfQRL-------LG 66
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVLT--------QYKshslndhIG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  67 DGSEFGIA--------LHYAVQPTPD----GLAQAFIIGEAFLNGEPACLVL---GDNIF---FGQSFSpklrsvAARTE 128
Cdd:COG0448   68 SGKPWDLDrkrggvfiLPPYQQREGEdwyqGTADAVYQNLDFIERSDPDYVLilsGDHIYkmdYRQMLD------FHIES 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488972388 129 GA--TIFGYQV--MDPERFGVVEFDDNFRALSLEEKPKQPKSNWAVTGLYFYDGKV 180
Cdd:COG0448  142 GAdiTVACIEVprEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDV 197
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-67 7.36e-10

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 57.83  E-value: 7.36e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488972388   4 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPLSVLMLAG-IREILIITTPDDLRDFQRLLGD 67
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 2.17e-09

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 56.30  E-value: 2.17e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488972388   4 IILAGGSGTRLHPitrGVSKQLLPIYDKPMIYYPLSVLMLAG-IREILIITTPDDLRDFQRLL 65
Cdd:PRK00155   7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-53 3.64e-09

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 55.70  E-value: 3.64e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488972388   4 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIT 53
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVT 51
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-70 2.82e-08

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 53.30  E-value: 2.82e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488972388   4 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPLSVLM-LAGIREILIITTPDDLRDFQRLLGDGSE 70
Cdd:cd02516    4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLS 68
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-108 5.43e-08

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with 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: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 51.79  E-value: 5.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   3 GIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTPDDLRDFQRLLGDGSEFGIALHYAvqpt 82
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWE---- 73

                         90       100
                 ....*....|....*....|....*...
gi 488972388  83 pDGLAQAFIIG-EAFLNGEPACLV-LGD 108
Cdd:cd04182   74 -EGMSSSLAAGlEALPADADAVLIlLAD 100
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-87 1.43e-07

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 51.49  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   3 GIILAGG--SGTRLHPITRGVSKQLLPIYDKPMIYYPLSVL-MLAGIREILIITTPDDlRDFQRLLGDGS-EFGIALHYA 78
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPE-SVFSDFISDAQqEFNVPIRYL 79


                 ....*....
gi 488972388  79 VQPTPDGLA 87
Cdd:cd06428   80 QEYKPLGTA 88
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-209 2.17e-07

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 51.90  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   4 IILAGGSGTRLHpitRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITtpddlrdfqrllGDGSE------FGIALHY 77
Cdd:PRK14358  11 VILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVT------------GHGAEqveaalQGSGVAF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  78 AVQPTPDGLAQAFIIG-EAFLNGEPACLVL-GDN-IFFGQSFSPKLRSVAARTEGATIFGYQVMDPERFG-VVEFDDNFR 153
Cdd:PRK14358  76 ARQEQQLGTGDAFLSGaSALTEGDADILVLyGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGrIVRGADGAV 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488972388 154 ALSLEEKPKQPKSNwAV----TGLYFYDGKVTEYAKRV-KPSERGELEITSINQMYLEDGA 209
Cdd:PRK14358 156 ERIVEQKDATDAEK-AIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGGA 215
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-132 2.60e-07

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 49.50  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388    3 GIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPLSVLMLAGiREILIITTPDDLRDFQRLLGdgsefgiaLHYAVQPT 82
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLG--------VPVVPDPD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488972388   83 PD-GLAQAFIIGEAFLNGEPACLVL-GDNIFFGQSFSPKLRSVAARTEGATI 132
Cdd:pfam12804  67 PGqGPLAGLLAALRAAPGADAVLVLaCDMPFLTPELLRRLLAAAEESGADIV 118
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 142-235 6.03e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 50.25  E-value: 6.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388 142 RFGVVEFDDNFRALSLEEKPKQPKSNWAVTGLYFYDGKV-TEYAkrvkpsERGELEITSINQ-------MYLEDGaltve 213
Cdd:PRK05293 161 RFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRlKEYL------IEDEKNPNSSHDfgknvipLYLEEG----- 229

                         90       100
                 ....*....|....*....|....*...
gi 488972388 214 llGRGFA------WLDTGTHDSLIEASM 235
Cdd:PRK05293 230 --EKLYAypfkgyWKDVGTIESLWEANM 255
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-53 9.70e-07

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 48.31  E-value: 9.70e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488972388   3 GIILAGGSGTRLHPITRGVSKQLLPI---YDkpMIYYPLSVLMLAGIREILIIT 53
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLT 52
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-55 2.67e-06

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 46.81  E-value: 2.67e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488972388   6 LAGGSGTRLhpitRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITTP 55
Cdd:COG2266    1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-53 7.03e-06

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 46.42  E-value: 7.03e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488972388   1 MKGIILAGGSGTRLHPITR-GVSKQLLPIY-DKPMIYYPLS-VLMLAGIREILIIT 53
Cdd:cd02509    1 IYPVILAGGSGTRLWPLSReSYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVVT 56
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-53 2.42e-05

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 44.00  E-value: 2.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488972388   3 GIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIIT 53
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVL 51
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-53 3.83e-05

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 44.85  E-value: 3.83e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488972388   3 GIILAGGSGTRLHPITRGVSKQLLPI---YDkpMIYYPLSVLMLAGIREILIIT 53
Cdd:PLN02241   6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVLT 57
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-57 3.92e-05

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 43.64  E-value: 3.92e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488972388   1 MKGIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPLSVLMLAgIREILIITTPDD 57
Cdd:COG0746    5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANRPE 55
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 4-166 4.87e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 44.45  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   4 IILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPLSVLMLAGIREILIITTPDD---LRDFQR----LLGDGSEFgIAL 75
Cdd:PRK00725  19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLTQYKAhslIRHIQRgwsfFREELGEF-VDL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  76 HYAVQP---------TPDGLAQAFIIGEAFlngEPA-CLVL-GDNIfFGQSFSPKLRSVAARteGA--TIFGYQV--MDP 140
Cdd:PRK00725  98 LPAQQRvdeenwyrgTADAVYQNLDIIRRY---DPKyVVILaGDHI-YKMDYSRMLADHVES--GAdcTVACLEVprEEA 171

                        170       180
                 ....*....|....*....|....*.
gi 488972388 141 ERFGVVEFDDNFRALSLEEKPKQPKS 166
Cdd:PRK00725 172 SAFGVMAVDENDRITAFVEKPANPPA 197
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 5.92e-05

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 43.90  E-value: 5.92e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488972388   1 MKGIILAGGSGTRLHPITRGVS-KQLLPIY-DKPMIYypLSVLMLAGI---REILIIT 53
Cdd:COG0836    3 IYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLLQ--QTVERLAGLvppENILVVT 58
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-209 1.02e-04

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 42.63  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   4 IILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYplSVLMLAGIR--EILIITTPDDLRDFQrllGDGSEFGIALHYAVQP 81
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFdsRFIFICRDEHNTKFH---LDESLKLLAPNATVVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  82 TP---DGLAQAFIIGEAFLNGEPACLVLGDNIFFGQSFSPKLRSVAARTEGATIFGYQVMDPeRFGVVEFDDNFRALSLE 158
Cdd:cd04183   77 LDgetLGAACTVLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGRVIETA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488972388 159 EKpkQPKSNWAVTGLYFYD--GKVTEYAKRVKP---SERGELEITS-INQMyLEDGA 209
Cdd:cd04183  156 EK--EPISDLATAGLYYFKsgSLFVEAAKKMIRkddSVNGEFYISPlYNEL-ILDGK 209
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-53 2.26e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 42.12  E-value: 2.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488972388   3 GIILAGGSGTRLHPITRGVSKQLLP---IYDkpMIYYPLSVLMLAGIREILIIT 53
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLT 59
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-53 3.51e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 41.79  E-value: 3.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488972388   3 GIILAGGSGTRLHPITRGVSKQLLPIYDK-PMIYYPLSVLMLAGIREILIIT 53
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT 57
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-54 4.97e-04

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 40.67  E-value: 4.97e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488972388   3 GIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREILIITT 54
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCC 54
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 4-67 5.23e-04

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 40.99  E-value: 5.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488972388   4 IILAGGSGTRLhpiTRGVSKQLLPIYDKPMIYYPLSVLMLAG-IREILIITTPDDLRDFQRLLGD 67
Cdd:PRK09382   9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 4-69 1.33e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 39.36  E-value: 1.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488972388    4 IILAGGSGTRLHPitrGVSKQLLPIYDKPMIYYPLSVLMLAG-IREILIITTPDDLRDFQRLLGDGS 69
Cdd:pfam01128   2 VIPAAGSGKRMGA---GVPKQFLQLLGQPLLEHTVDAFLASPvVDRIVVAVSPDDTPEFRQLLGDPS 65
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-208 2.56e-03

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 38.27  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388   4 IILAGGSGTRLH---PitrgvsKQLLPIYDKPMIYYPLSVLMLAGIREILIIttpddlrdfqrlLGDGSEF------GIA 74
Cdd:cd02540    2 VILAAGKGTRMKsdlP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGAEQvkkalaNPN 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488972388  75 LHYAVQPTPDGLAQAFIIGEAFLNGEPA-CLVL-GDNIFF-GQSFSPKLRSVAARTEGATIFGYQVMDPERFG--VVEFD 149
Cdd:cd02540   64 VEFVLQEEQLGTGHAVKQALPALKDFEGdVLVLyGDVPLItPETLQRLLEAHREAGADVTVLTAELEDPTGYGriIRDGN 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488972388 150 DNFRALsLEEK---PKQPKSNWAVTGLY-FYDGKVTEYAKRVKPS-ERGELEITSINQMYLEDG 208
Cdd:cd02540  144 GKVLRI-VEEKdatEEEKAIREVNAGIYaFDAEFLFEALPKLTNNnAQGEYYLTDIIALAVADG 206
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-62 6.40e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 37.09  E-value: 6.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488972388   1 MKGIILAGGSGTRLHpitrGVSKQLLPIYDKPMIYYPLSVLmLAGIREILIITT--------------PDDLRDFQ 62
Cdd:PRK00317   4 ITGVILAGGRSRRMG----GVDKGLQELNGKPLIQHVIERL-APQVDEIVINANrnlaryaafglpviPDSLADFP 74
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-61 9.45e-03

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 36.40  E-value: 9.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488972388   1 MKGIILAGGSGTRLhpitrGVSKQLLPIYDKPMIYYPLSVLMLAgIREILIITTPDDLRDF 61
Cdd:cd02503    1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVISANRDQERYA 55
 
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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