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Conserved domains on  [gi|518330561|ref|WP_019500768|]
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glucose-1-phosphate thymidylyltransferase RfbA [Pseudanabaena sp. PCC 6802]

Protein Classification

sugar nucleotidyltransferase( domain architecture ID 11440264)

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

CATH:  3.90.550.10
EC:  2.7.7.-
Gene Ontology:  GO:0016779|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
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 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 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  81 PSPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 161 PKQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAATFIQTL 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 518330561 241 EQRQGLKVACIEEIAYSEGYITRSQLLELAAPMAKSSYGEYLHRVAHES 289
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 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 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  81 PSPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 161 PKQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAATFIQTL 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 518330561 241 EQRQGLKVACIEEIAYSEGYITRSQLLELAAPMAKSSYGEYLHRVAHES 289
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-286 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: 527.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561    2 KGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   82 SPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  162 KQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAATFIQTLE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 518330561  242 QRQGLKVACIEEIAYSEGYITRSQLLELAAPMAKSSYGEYLHRVA 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 8.48e-168

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: 464.74  E-value: 8.48e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  81 PSPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 161 PKQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAATFIQTL 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-282 2.76e-145

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 409.83  E-value: 2.76e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   2 KGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQP 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  82 SPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEKP 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 162 KQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAATFIQTLE 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 518330561 242 QRQGLKVACIEEIAYSEGYITRSQLLELAAPMAKSSYGEYL 282
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYL 285
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 4.34e-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: 285.69  E-value: 4.34e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561    2 KGIILAGGSGTRLYPITRALSKQLMPVYDK-PMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   81 PSPDGLAQAFILGKDFIGSDPV-CLVLGDNIFYGHGFKDVLRSAAQLKSGGLV--FGYRVTDPQRYGVIEFDRDGIAISL 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAADATVtfGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  158 EEKPKQPK-SNYAVPGIYFYDAQVVEK-ASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAAT 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 518330561  236 FI 237
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-289 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 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQ 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  81 PSPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEK 160
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 161 PKQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAATFIQTL 240
Cdd:COG1209  161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 518330561 241 EQRQGLKVACIEEIAYSEGYITRSQLLELAAPMAKSSYGEYLHRVAHES 289
Cdd:COG1209  241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-286 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: 527.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561    2 KGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   82 SPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  162 KQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAATFIQTLE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 518330561  242 QRQGLKVACIEEIAYSEGYITRSQLLELAAPMAKSSYGEYLHRVA 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 8.48e-168

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: 464.74  E-value: 8.48e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQ 80
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  81 PSPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEK 160
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 161 PKQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAATFIQTL 240
Cdd:cd02538  161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-282 2.76e-145

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 409.83  E-value: 2.76e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   2 KGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQP 81
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  82 SPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEKP 161
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 162 KQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAATFIQTLE 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 518330561 242 QRQGLKVACIEEIAYSEGYITRSQLLELAAPMAKSSYGEYL 282
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYL 285
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-237 4.34e-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: 285.69  E-value: 4.34e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561    2 KGIILAGGSGTRLYPITRALSKQLMPVYDK-PMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   81 PSPDGLAQAFILGKDFIGSDPV-CLVLGDNIFYGHGFKDVLRSAAQLKSGGLV--FGYRVTDPQRYGVIEFDRDGIAISL 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAADATVtfGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  158 EEKPKQPK-SNYAVPGIYFYDAQVVEK-ASQLKPSARNELEITDLNLAYLREGHLKVEILGRGYAWLDTGTHESLHQAAT 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ..
gi 518330561  236 FI 237
Cdd:pfam00483 241 FL 242
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-230 4.99e-68

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: 211.66  E-value: 4.99e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDlPLFQTLLQDGSQWGLKFSYTAQ 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  81 PSPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGhGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDrDGIAISLEEK 160
Cdd:cd04189   80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLVEK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518330561 161 PKQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREG-HLKVEILgRGYaWLDTGTHESL 230
Cdd:cd04189  158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGrRVGYSIV-TGW-WKDTGTPEDL 226
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-233 1.99e-59

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: 193.39  E-value: 1.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561    2 KGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTAQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   82 SPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGhGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518330561  162 KQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLnLAYLREGHLKVEILGRGYAWLDTGTHESLHQA 233
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDA-IQWLIEKGYKVGGSKVTGWWKDTGKPEDLLDA 230
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-225 2.27e-58

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: 186.25  E-value: 2.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   3 GIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDlPLFQTLLQDGSQWGLKFSYTAQPS 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  83 PDGLAQAFILGKDFIGSDPVCLVLGDNIFYGhGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEKPK 162
Cdd:cd04181   80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518330561 163 QPKSNYAVPGIYFYDAQVVEKASQLKPsaRNELEITDLNLAYLREGHLKVeILGRGYaWLDTG 225
Cdd:cd04181  159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG-YPVDGY-WLDIG 217
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-233 1.55e-42

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: 146.07  E-value: 1.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   2 KGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDIlIISTpNDLP-LFQTLLQDGSQWGLKFSYTAQ 80
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINV-GYLAeQIEEYFGDGSRFGVRITYVDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  81 PSPDGLAQAFILGKDFIGSDPVCLVLGDnIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEK 160
Cdd:COG1208   79 GEPLGTGGALKRALPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518330561 161 PKQPKSNYAVPGIYFYDAQVVEKAsqlkpSARNELEITDLNLAYLREGHLKVEILgRGYaWLDTGTHESLHQA 233
Cdd:COG1208  158 PEEPPSNLINAGIYVLEPEIFDYI-----PEGEPFDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-225 9.96e-42

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: 148.13  E-value: 9.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561    1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDlPLFQTLLQDGSQWGLKFSYTAQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   81 PSPDGLAQAFILGKDFIgSDPVCLVLGDNIFYGHGFKDVLRSaaqlkSGGLVFGYRVTDPQRYGVIEFDrDGIAISLEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLIRA-----EAPAIAVVEVDDPSDYGVVETD-GGRVTGIVEK 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518330561  161 PKQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGRGyaWLDTG 225
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVG 215
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-233 1.37e-33

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: 123.41  E-value: 1.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPN----------DLPLFQTLLQDGSQ 70
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfdrSYELEETLEKKGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  71 WGLK----------FSYTAQPSPDGLAQAFILGKDFIGSDPVCLVLGDNIFYghGFKDVLRSAAQL--KSGGLVFGYRVT 138
Cdd:cd02541   81 DLLEevriisdlanIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLID--SKEPCLKQLIEAyeKTGASVIAVEEV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 139 DP---QRYGVIEFDRDGIAI----SLEEKPKQ--PKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITD-LNLAYLREG 208
Cdd:cd02541  159 PPedvSKYGIVKGEKIDGDVfkvkGLVEKPKPeeAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDaIAKLLEEEP 238

                        250       260
                 ....*....|....*....|....*
gi 518330561 209 HLKVEILGRGYawlDTGTHESLHQA 233
Cdd:cd02541  239 VYAYVFEGKRY---DCGNKLGYLKA 260
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-233 2.63e-26

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: 103.02  E-value: 2.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   4 IILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDIlIISTPNDLPLFQTLLQDGSQWGLKFSYTAQPSP 83
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  84 DGLAQAFILGKDFIgSDPVCLVL-GDNIFYGhGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEKPK 162
Cdd:cd06915   81 LGTGGAIKNALPKL-PEDQFLVLnGDTYFDV-DLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGP 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518330561 163 QPKSNYAVPGIYFYDAQVVEKASQLKPSarneLEiTDLNLAYLREGHLKVEIlGRGYaWLDTGTHESLHQA 233
Cdd:cd06915  159 GAAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRLYGFE-VDGY-FIDIGIPEDYARA 222
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-195 1.18e-22

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: 93.43  E-value: 1.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRD-ILIIS-TPNDLPLFQTLLQDgsQWGLKFSYT 78
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  79 AQPSPDGLAQAFILGKDFIGSDPVC-LVLGDNIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRD-GIAIS 156
Cdd:cd06425   79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIER 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 518330561 157 LEEKPKQPKSNYAVPGIYFYDAQVVEKAsQLKP-SARNEL 195
Cdd:cd06425  159 FVEKPKVFVGNKINAGIYILNPSVLDRI-PLRPtSIEKEI 197
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-233 1.59e-22

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: 92.96  E-value: 1.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   4 IILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDIlIISTpNDLP-LFQTLLQDGSQWGLKFSYTAQPS 82
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISV-NYLAeMIEDYFGDGSKFGVNISYVREDK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  83 PDGLAQAFILGKDFIgSDPVCLVLGD---NIFYGHGFKDVLRSAAQLKSGGLVFGYRVtdPqrYGVIEFDrDGIAISLEE 159
Cdd:cd06426   80 PLGTAGALSLLPEKP-TDPFLVMNGDiltNLNYEHLLDFHKENNADATVCVREYEVQV--P--YGVVETE-GGRITSIEE 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518330561 160 KPKQpksNYAV-PGIYFYDAQVVEkasQLKPSARneLEITDLNLAYLREGHlKVEILG-RGYaWLDTGTHESLHQA 233
Cdd:cd06426  154 KPTH---SFLVnAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEGK-KVGVFPiHEY-WLDIGRPEDYEKA 219
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-199 1.96e-22

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 94.33  E-value: 1.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   2 KGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYplSV--LMLAGIRDILIISTPN----------DLPLFQTLLQDG- 68
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRGkraiedhfdrSYELEATLEAKGk 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  69 ---------SQWGLKFSYTAQPSPDGLAQAFILGKDFIGSDPVCLVLGDNIFYGHgfKDVLrsaAQL-----KSGGLVFG 134
Cdd:COG1210   83 eelleevrsISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE--KPCL---KQMievyeETGGSVIA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518330561 135 -YRV--TDPQRYGVI---EFDRDGIAIS-LEEKPKQPK--SNYAVPGIYFYDAQVVEKASQLKPSARNELEITD 199
Cdd:COG1210  158 vQEVppEEVSKYGIVdgeEIEGGVYRVTgLVEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTD 231
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-65 1.16e-15

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: 74.23  E-value: 1.16e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLPLFQTLL 65
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYL 65
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-233 4.88e-14

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 71.64  E-value: 4.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   3 GIILAGGSGTRLYPIT--RAlskqlmpvydKPMIYY---------PLSVLMLAGIRDILIIsTPNdlpLFQTL---LQDG 68
Cdd:COG0448    4 AIILAGGRGSRLGPLTkdRA----------KPAVPFggkyriidfPLSNCVNSGIRRVGVL-TQY---KSHSLndhIGSG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  69 SQWGLK------FSYTAQPSPD------GLAQAFILGKDFI-GSDP--VCLVLGDNIF---YghgfKDVLRSAAQLKSGG 130
Cdd:COG0448   70 KPWDLDrkrggvFILPPYQQREgedwyqGTADAVYQNLDFIeRSDPdyVLILSGDHIYkmdY----RQMLDFHIESGADI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 131 LVFGYRVTDPQ--RYGVIEFDRDGIAISLEEKPKQPKSNYAVPGIYFYDAQVVEKAsqLKPSARNELE--ITDLNLAYLR 206
Cdd:COG0448  146 TVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVLIEL--LEEDAPNSSHdfGKDIIPRLLD 223

                        250       260
                 ....*....|....*....|....*...
gi 518330561 207 EGHLKV-EIlgRGYaWLDTGTHESLHQA 233
Cdd:COG0448  224 RGKVYAyEF--DGY-WRDVGTIDSYYEA 248
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-233 1.56e-13

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: 68.37  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   2 KGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDIL---------IISTpndlplfqtlLQDgSQWG 72
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVvnthhladqIEAH----------LGD-SRFG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  73 LK--FSY-------TAqpspDGLAQAFilgkDFIGSDPVCLVLGDnIFYGHGFKDVLRSAAQLKSGGLVFGYRVTDP--Q 141
Cdd:cd06422   70 LRitISDepdelleTG----GGIKKAL----PLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPghN 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 142 RYGVIEFDRDGIaISLEEKPKQPKSNYAvpGIYFYDAQVVEKASQLKPSarneleITDLNLAYLREGHLKVEILgRGYaW 221
Cdd:cd06422  141 GVGDFSLDADGR-LRRGGGGAVAPFTFT--GIQILSPELFAGIPPGKFS------LNPLWDRAIAAGRLFGLVY-DGL-W 209

                        250
                 ....*....|..
gi 518330561 222 LDTGTHESLHQA 233
Cdd:cd06422  210 FDVGTPERLLAA 221
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-199 4.71e-13

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 67.99  E-value: 4.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILII--STPN----------------DLPLFQ 62
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVthASKNavenhfdtsyelesllEQRVKR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  63 TLL---QDGSQWGLKFSYTAQPSPDGLAQAFILGKDFIGSDPVCLVLGDnIFYGHGFKDVLR-----SAAQLKSGG--LV 132
Cdd:PRK10122  84 QLLaevQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPD-VVIDDASADPLRynlaaMIARFNETGrsQV 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518330561 133 FGYRVT-DPQRYGVIE----FDRDG-IAISLE--EKPKQPK---SNYAVPGIYFYDAQVVEKASQLKPSARNELEITD 199
Cdd:PRK10122 163 LAKRMPgDLSEYSVIQtkepLDREGkVSRIVEfiEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-52 1.40e-11

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: 62.66  E-value: 1.40e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILII 52
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-199 5.47e-11

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 62.23  E-value: 5.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   2 KGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILII--STPNDLP-LFQT--------------- 63
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVthSSKNSIEnHFDTsfeleamlekrvkrq 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  64 LLQDGSQW---GLKFSYTAQPSPDGLAQAFILGKDFIGSDPVCLVLGDNI---FYGHGFKDVLRSAAQ-LKSGGL--VFG 134
Cdd:PRK13389  90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVIldeYESDLSQDNLAEMIRrFDETGHsqIMV 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518330561 135 YRVTDPQRYGVIefDRDGIA---------ISLEEKPK--QPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITD 199
Cdd:PRK13389 170 EPVADVTAYGVV--DCKGVElapgesvpmVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-233 6.49e-11

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: 61.09  E-value: 6.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   4 IILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDlPLFQTLLQDgsqwGLKFSYTAQPSP 83
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKK-EQIEELLKK----YPNIKFVYNPDY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  84 D--GLAQAFILGKDFIGSDpvCLVL-GDNIFYghgfKDVLRSAAQLKSGGLVFGYRVTDP--QRYGVIEFDRDGIAISlE 158
Cdd:cd02523   77 AetNNIYSLYLARDFLDED--FLLLeGDVVFD----PSILERLLSSPADNAILVDKKTKEweDEYVKDLDDAGVLLGI-I 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 159 EKPKQPKSNYAVP-GIYFYDAQ----VVEKASQLKPSARNELEITDLNLAYLREGHLKVEILGrGYAWLDTGTHESLHQA 233
Cdd:cd02523  150 SKAKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-233 9.48e-11

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 61.81  E-value: 9.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   1 MKGIILAGGSGTRLYPITRALSKQLMPVYDK-PMIYYPLSVLMLAGIRDILIISTPNDLPLfQTLLQDGSQWGLKF---- 75
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQYQPLEL-NNHIGIGSPWDLDRingg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  76 -----SYTAQPSPD---GLAQAFILGKDFIGS-DP-VCLVL-GDNIfYGHGFKDVLRSAAQLKSGGLVFGYRV--TDPQR 142
Cdd:PRK05293  83 vtilpPYSESEGGKwykGTAHAIYQNIDYIDQyDPeYVLILsGDHI-YKMDYDKMLDYHKEKEADVTIAVIEVpwEEASR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 143 YGVIEFDRDGIAISLEEKPKQPKSNYAVPGIYFYDAQVVEKAsqLKPSARNELEITDL--NL--AYLREGHLKVEILGRG 218
Cdd:PRK05293 162 FGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLKEY--LIEDEKNPNSSHDFgkNVipLYLEEGEKLYAYPFKG 239

                        250
                 ....*....|....*
gi 518330561 219 YaWLDTGTHESLHQA 233
Cdd:PRK05293 240 Y-WKDVGTIESLWEA 253
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-213 3.88e-10

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: 59.19  E-value: 3.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   3 GIILAGG--SGTRLYPITRALSKQLMPVYDKPMIYYPLSVL-MLAGIRDILIISTPNDLPLFQTLLQDGSQWGLKFSYTA 79
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  80 QPSPDGLAQAFILGKDFIGSDPVclvlgDNIFYGHG-------FKDVLRSAAQLKSGGLVFGYRVTDPQ--RYGVIEFDR 150
Cdd:cd06428   81 EYKPLGTAGGLYHFRDQILAGNP-----SAFFVLNAdvccdfpLQELLEFHKKHGASGTILGTEASREQasNYGCIVEDP 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518330561 151 D-GIAISLEEKPKQPKSNYAVPGIYFYDAQVVEKASQLKPSARNELEITDLNLAYLREGHLKVE 213
Cdd:cd06428  156 StGEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLE 219
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-52 1.88e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 56.79  E-value: 1.88e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518330561   2 KGIILAGGSGTRLYPITRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILII 52
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-213 4.90e-08

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: 52.52  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   4 IILAGGSGTRLYpitRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIIsTPNDLPLFQTLLQDgsqwgLKFSYTAQPSP 83
Cdd:cd02540    2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALAN-----PNVEFVLQEEQ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  84 DGLAQAFILGKDFIG--SDPVcLVLgdnifYG-------HGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDG-- 152
Cdd:cd02540   73 LGTGHAVKQALPALKdfEGDV-LVL-----YGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGkv 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518330561 153 IAIsLEEK---PKQPKSNYAVPGIYFYDAQVVEKA-SQLKPS-ARNELEITDLnLAYLREGHLKVE 213
Cdd:cd02540  147 LRI-VEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDI-IALAVADGLKVA 210
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-67 1.06e-07

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: 51.67  E-value: 1.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518330561   4 IILAGGSGTRLypiTRALSKQLMPVYDKPMIYYPLSVLMLAG-IRDILIISTPNDLPLFQTLLQD 67
Cdd:COG1211    1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-196 1.59e-07

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: 51.42  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   1 MKGIILAGGSGTRLYPITR-ALSKQLMPVY-DKPMIYYPLS-VLMLAGIRDILIISTPNDLPLFQTLLQDGsqwGLKFSY 77
Cdd:cd02509    1 IYPVILAGGSGTRLWPLSReSYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVVTNEEYRFLVREQLPEG---LPEENI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  78 TAQPSPDGLAQAFILGKDFI---GSDPVCLVL------GDNifygHGFKDVLRSAAQL-KSGGLV-FGYRVTDPQ-RYGV 145
Cdd:cd02509   78 ILEPEGRNTAPAIALAALYLakrDPDAVLLVLpsdhliEDV----EAFLKAVKKAVEAaEEGYLVtFGIKPTRPEtGYGY 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518330561 146 IEF-DRDGIAISLE----EKPKQPKSNYAV--------PGIYFYDAQVV-EKASQLKPSARNELE 196
Cdd:cd02509  154 IEAgEKLGGGVYRVkrfvEKPDLETAKEYLesgnylwnSGIFLFRAKTFlEELKKHAPDIYEALE 218
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-208 1.83e-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: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   4 IILAGGSGTRLypiTRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIIsTPNDLPLFQTLLQdgsQWGLKFSYTAQPSp 83
Cdd:PRK14358  11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVV-TGHGAEQVEAALQ---GSGVAFARQEQQL- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  84 dGLAQAFILGKDFIGS-DPVCLVL-GDN-IFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISLEEK 160
Cdd:PRK14358  83 -GTGDAFLSGASALTEgDADILVLyGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQ 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518330561 161 PKQPKSNYAV----PGIYFYDAQVVEKASQL-KPSARNELEITDLNLAYLREG 208
Cdd:PRK14358 162 KDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-111 6.77e-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: 48.69  E-value: 6.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   3 GIILAGGSGTRLYPITRALSKQLMPV---YDkpMIYYPLSVLMLAGIRDILIISTPNDLPLFQTlLQDGSQWGLK----- 74
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLTQYKSRSLNDH-LGSGKEWDLDrkngg 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 518330561  75 ---FSYTAQPSPD---GLAQAFILGKDFI-GSDP--VCLVLGDNIF 111
Cdd:cd02508   78 lfiLPPQQRKGGDwyrGTADAIYQNLDYIeRSDPeyVLILSGDHIY 123
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-68 2.58e-06

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: 47.52  E-value: 2.58e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518330561   4 IILAGGSGTRLypiTRALSKQLMPVYDKPMIYYPLSVLM-LAGIRDILIISTPNDLPLFQTLLQDG 68
Cdd:cd02516    4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYG 66
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-233 3.15e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 47.90  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   3 GIILAGGSGTRLYPITRALSKQLMP---VYDkpMIYYPLSVLMLAGIRDILI------------------ISTPND---- 57
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVltqykshsldrhisqtwrLSGLLGnyit 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  58 -LPLFQTLlqdGSQWglkFSYTAqpspDGLAQAFILGKDFigsDP--VCLVLGDNIfYGHGFKDVLRSAAQLKSGGLVFG 134
Cdd:PRK00844  86 pVPAQQRL---GKRW---YLGSA----DAIYQSLNLIEDE---DPdyVVVFGADHV-YRMDPRQMVDFHIESGAGVTVAA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 135 YRV--TDPQRYGVIEFDRDGIAISLEEKPKQPKS-------NYAVPGIYFYDAQVVEKAsqLKPSARNELEITDLN---L 202
Cdd:PRK00844 152 IRVprEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDALVDA--LRRDAADEDSSHDMGgdiI 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 518330561 203 AYL-REGHLKV------EILG-----RGYaWLDTGTHESLHQA 233
Cdd:PRK00844 230 PRLvERGRAYVydfstnEVPGaterdRGY-WRDVGTIDAYYDA 271
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-52 1.44e-05

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 45.83  E-value: 1.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 518330561   1 MKGIILAGGSGTRLYPITRALS-KQLMPVY-DKPMIYypLSVLMLAGI---RDILII 52
Cdd:COG0836    3 IYPVILAGGSGTRLWPLSRESYpKQFLPLLgEKSLLQ--QTVERLAGLvppENILVV 57
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-70 1.58e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 45.12  E-value: 1.58e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518330561   4 IILAGGSGTRLYPitrALSKQLMPVYDKPMIYYPLSVLMLAG-IRDILIISTPNDLPLFQTLLQDGSQ 70
Cdd:PRK00155   7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELLLAKDP 71
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 4-180 3.42e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 44.83  E-value: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   4 IILAGGSGTRLYPIT--RAlskqlmpvydKPMIY---------YPLSVLMLAGIRDILIIST-----------------P 55
Cdd:PRK00725  19 LILAGGRGSRLKELTdkRA----------KPAVYfggkfriidFALSNCINSGIRRIGVLTQykahslirhiqrgwsffR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  56 NDLPLFQTLL-----QDGSQWglkFSYTAqpspDGLAQAFilgkDFIGS-DP-VCLVL-GDNIF---YGHGFKDVLRSAA 124
Cdd:PRK00725  89 EELGEFVDLLpaqqrVDEENW---YRGTA----DAVYQNL----DIIRRyDPkYVVILaGDHIYkmdYSRMLADHVESGA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518330561 125 QLKSGGL-VfgyRVTDPQRYGVIEFDRDGIAISLEEKPKQPKsnyAVP----------GIYFYDAQV 180
Cdd:PRK00725 158 DCTVACLeV---PREEASAFGVMAVDENDRITAFVEKPANPP---AMPgdpdkslasmGIYVFNADY 218
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-200 1.51e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.81  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   4 IILAGGSGTRLypiTRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIIsTPNDLPLFQTLLQDgsQWGLKFSYTAQPSP 83
Cdd:PRK14355   7 IILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLV-VGHQAEKVREHFAG--DGDVSFALQEEQLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  84 DGLAQAFILGKDFIGSDPVCLVLGDN-IFYGHGFKDVLRSAAQLKSGGLVFGYRVTDPQRYGVIEFDRDGIAISL-EEK- 160
Cdd:PRK14355  81 TGHAVACAAPALDGFSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvEEKd 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 518330561 161 --PKQPKSNYAVPGIYFYDAQVVEKA-SQLK-PSARNELEITDL 200
Cdd:PRK14355 161 atPEERSIREVNSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDI 204
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 3-52 1.85e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 42.56  E-value: 1.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518330561   3 GIILAGGSGTRLYPITRALSKQLMPVYDK-PMIYYPLSVLMLAGIRDILII 52
Cdd:PRK02862   6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-56 3.85e-04

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: 40.64  E-value: 3.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518330561   6 LAGGSGTRLypitRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPN 56
Cdd:COG2266    1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPN 47
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-52 6.87e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 40.99  E-value: 6.87e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518330561   3 GIILAGGSGTRLYPITRALSKQLMPV---YDkpMIYYPLSVLMLAGIRDILII 52
Cdd:PLN02241   6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-216 1.22e-03

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 40.01  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   4 IILAGGSGTRLYpitRALSKQLMPVYDKPMIYYPLSVLMLAGIRDILII---------STPNDLPLfQTLLQDgSQWGlk 74
Cdd:COG1207    6 VILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVvghgaeqvrAALADLDV-EFVLQE-EQLG-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561  75 fsyTAqpspDGLAQAfilgKDFIGSDP-VCLVLgdnifYGhgfkDV--LRSA--AQLKSGGLVFGYRVT-------DPQR 142
Cdd:COG1207   79 ---TG----HAVQQA----LPALPGDDgTVLVL-----YG----DVplIRAEtlKALLAAHRAAGAAATvltaeldDPTG 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561 143 YGVIEFDRDG--IAIsLEEK---PKQPKSNYAVPGIYFYDAQVVEKA-SQLKPS-ARNELEITDLnLAYLREGHLKV--- 212
Cdd:COG1207  139 YGRIVRDEDGrvLRI-VEEKdatEEQRAIREINTGIYAFDAAALREAlPKLSNDnAQGEYYLTDV-IAIARADGLKVaav 216

                        250
                 ....*....|
gi 518330561 213 ------EILG 216
Cdd:COG1207  217 qpedpwEVLG 226
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 3-208 2.99e-03

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 38.09  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561    3 GIILAGGSGTRLypitraLSKQLMPVYDKPMIYYPLSVLMLAGIRDILIISTPNDLplfqtLLQDGSQWGLKFSYTAQPS 82
Cdd:pfam02348   2 AIIPARLGSKRL------PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEE-----IADVAKEFGAGVVMTSGSL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518330561   83 PDGLAQAFILGKDFIGSDP--VCLVLGDNIFYGHgfKDVLRSAAQLKSGGLVF----------GYRVTDPQRYGVIeFDR 150
Cdd:pfam02348  71 SSGTDRFYEVVKAFLNDHDdiIVNIQGDNPLLQP--EVILKAIETLLNNGEPYmstlvvpvgsAEEVLNANALKVV-LDD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518330561  151 DGIAISLEEKP----KQPKSNYAVP-----GIY-FYDAQVVEKASQLKPSARNELEitDL-NLAYLREG 208
Cdd:pfam02348 148 DGYALYFSRSVipyiREHPAELYYVylrhiGIYtFRKNMPLIELVIDTPTALEYIE--KLeQLRVLYNG 214
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-57 8.07e-03

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: 36.40  E-value: 8.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 518330561    3 GIILAGGSGTRLypitrALSKQLMPVYDKPMIYYplSVLMLAGIRDILIISTPND 57
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLER--VLERLRPAGDEVVVVANDE 48
 
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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