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Conserved domains on  [gi|1057341137|ref|WP_068701709|]
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glucose-1-phosphate thymidylyltransferase RfbA [Paludibacter jiangxiensis]

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];
1-288 0e+00

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


:

Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 547.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  81 PSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 161 PAVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAANFISTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1057341137 241 ENRQGLMVACIEEIAFRMKFIDRDQLLQLAEPLKKNNYGQYLIKIANE 288
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-288 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 547.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  81 PSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 161 PAVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAANFISTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1057341137 241 ENRQGLMVACIEEIAFRMKFIDRDQLLQLAEPLKKNNYGQYLIKIANE 288
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
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 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  82 SPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 162 AVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAANFISTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1057341137 242 NRQGLMVACIEEIAFRMKFIDRDQLLQLAEPLKKNNYGQYLIKIA 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 3.24e-165

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: 458.19  E-value: 3.24e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  81 PSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 161 PAVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAANFISTI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-285 2.56e-147

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 414.84  E-value: 2.56e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  82 SPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 162 AVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAANFISTIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1057341137 242 NRQGLMVACIEEIAFRMKFIDRDQLLQLAEPLKKNNYGQYLIKI 285
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKM 288
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-237 9.29e-96

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: 282.22  E-value: 9.29e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNK-PMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  81 PSPDGLAQAFIIGEKFIGNDSV-CMVLGDNIFYGYNLSSQLQEAAQMKD--GATVFGYYVNDPERYGVAEFDPSGKVLSL 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 158 EEKPAVPK-SNYAVTGLYFYGNDVVAK-AKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAAN 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ..
gi 1057341137 236 FI 237
Cdd:pfam00483 241 FL 242
 
Name Accession Description Interval E-value
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-288 0e+00

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 547.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  81 PSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 161 PAVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAANFISTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1057341137 241 ENRQGLMVACIEEIAFRMKFIDRDQLLQLAEPLKKNNYGQYLIKIANE 288
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
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 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  82 SPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 162 AVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAANFISTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1057341137 242 NRQGLMVACIEEIAFRMKFIDRDQLLQLAEPLKKNNYGQYLIKIA 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 3.24e-165

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: 458.19  E-value: 3.24e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  81 PSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 161 PAVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAANFISTI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
2-285 2.56e-147

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 414.84  E-value: 2.56e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  82 SPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 162 AVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAANFISTIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1057341137 242 NRQGLMVACIEEIAFRMKFIDRDQLLQLAEPLKKNNYGQYLIKI 285
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKM 288
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-237 9.29e-96

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: 282.22  E-value: 9.29e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNK-PMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  81 PSPDGLAQAFIIGEKFIGNDSV-CMVLGDNIFYGYNLSSQLQEAAQMKD--GATVFGYYVNDPERYGVAEFDPSGKVLSL 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 158 EEKPAVPK-SNYAVTGLYFYGNDVVAK-AKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMAWLDTGTHDSLLEAAN 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240

                  ..
gi 1057341137 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 ...
1-233 1.76e-70

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: 217.82  E-value: 1.76e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDiDLYKRLFEDGSAYGLKIEYAIQ 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  81 PSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGyNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDpSGKVLSLEEK 160
Cdd:cd04189    80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQE-GISPLVRDFLEEDADASILLAEVEDPRRFGVAVVD-DGRIVRLVEK 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057341137 161 PAVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGR--LNVKLLGrgmAWLDTGTHDSLLEA 233
Cdd:cd04189   158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRrvGYSIVTG---WWKDTGTPEDLLEA 229
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-225 1.26e-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: 186.63  E-value: 1.26e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   3 GIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDiDLYKRLFEDGSAYGLKIEYAIQPS 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  83 PDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGyNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEKPA 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-DLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057341137 163 VPKSNYAVTGLYFYGNDVVakaKALKP-SPRGELEITDLNRIYLDEGRLNVKLLgrGMAWLDTG 225
Cdd:cd04181   159 LPESNLANAGIYIFEPEIL---DYIPEiLPRGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-233 7.39e-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: 7.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAIQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  82 SPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGyNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQD-GISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057341137 162 AVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGMaWLDTGTHDSLLEA 233
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDA 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-233 5.88e-46

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: 159.30  E-value: 5.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDiDLYKRLFEDGSAYGLKIEYAIQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  81 PSPDGLAQAFIIGEKFIgNDSVCMVLGDNIFygynlSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDpSGKVLSLEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLL-----DSDLLERLIRAEAPAIAVVEVDDPSDYGVVETD-GGRVTGIVEK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057341137 161 PAVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVKLLGRGmaWLDTGTHDSLLEA 233
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDA 223
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-233 8.91e-43

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: 146.45  E-value: 8.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEIlIIST---PQDIdlyKRLFEDGSAYGLKIEYA 78
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVgylAEQI---EEYFGDGSRFGVRITYV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  79 IQPSP----DGLAQAfiigEKFIGNDSVCMVLGDnIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKV 154
Cdd:COG1208    77 DEGEPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 155 LSLEEKPAVPKSNYAVTGLYFYGNDVVAKAkalkpsPRGE-LEITDLNRIYLDEGRLN-VKLLGRgmaWLDTGTHDSLLE 232
Cdd:COG1208   152 TRFVEKPEEPPSNLINAGIYVLEPEIFDYI------PEGEpFDLEDLLPRLIAEGRVYgYVHDGY---WLDIGTPEDLLE 222

                  .
gi 1057341137 233 A 233
Cdd:COG1208   223 A 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-233 1.30e-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: 126.11  E-value: 1.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTP----------QDIDLYKRLFEDG-- 68
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdRSYELEETLEKKGkt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  69 --------SAYGLKIEYAIQPSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYN-LSSQLQEAAQmKDGATVFGYYVND 139
Cdd:cd02541    81 dlleevriISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEpCLKQLIEAYE-KTGASVIAVEEVP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 140 PE---RYGVAEFDPSG----KVLSLEEKPAV--PKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRL 210
Cdd:cd02541   160 PEdvsKYGIVKGEKIDgdvfKVKGLVEKPKPeeAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239
                         250       260
                  ....*....|....*....|....
gi 1057341137 211 N-VKLLGRgmaWLDTGTHDSLLEA 233
Cdd:cd02541   240 YaYVFEGK---RYDCGNKLGYLKA 260
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-208 6.75e-23

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: 94.20  E-value: 6.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQE-ILIIS-TPQDIDLYKRLFEDgsAYGLKIEYA 78
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  79 IQPSPDGLAQAFIIGEKFIGNDSVC-MVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDP-SGKVLS 156
Cdd:cd06425    79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDEnTGRIER 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057341137 157 LEEKPAVPKSNYAVTGLYFYGNDVVAKAKaLKPS-----------PRGELEITDLNRIYLDEG 208
Cdd:cd06425   159 FVEKPKVFVGNKINAGIYILNPSVLDRIP-LRPTsiekeifpkmaSEGQLYAYELPGFWMDIG 220
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
4-210 1.08e-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: 90.69  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   4 IILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEIlIISTPQDIDLYKRLFEDGSAYGLKIEYAIQPSP 83
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  84 DGLAQAFIIGEKFIGNDSVCMVLGDNiFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSLEEKPAV 163
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQFLVLNGDT-YFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGPG 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1057341137 164 PKSNYAVTGLYFYGNDVVAKAKALKPSprgeLEiTDLNRIYLDEGRL 210
Cdd:cd06915   160 AAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL 201
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-233 1.98e-21

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 91.25  E-value: 1.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYplSV--LMLSGIQEILIISTP----------QDIDLYKRLFEDG- 68
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQY--VVeeAVAAGIEEIIFVTGRgkraiedhfdRSYELEATLEAKGk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  69 ---------SAYGLKIEYAIQPSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGY-NLSSQLQEAAQmKDGATVFGYYVN 138
Cdd:COG1210    83 eelleevrsISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEkPCLKQMIEVYE-ETGGSVIAVQEV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 139 DPE---RYGVAEFDPSG----KVLSLEEKPAVPK--SNYAVTGLYFYGNDVVAKAKALKPSPRGELEITD-LNRIYLDEG 208
Cdd:COG1210   162 PPEevsKYGIVDGEEIEggvyRVTGLVEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDaIAALAKEEP 241
                         250       260
                  ....*....|....*....|....*
gi 1057341137 209 RLNVKLLGRgmaWLDTGTHDSLLEA 233
Cdd:COG1210   242 VYAYEFEGK---RYDCGDKLGYLKA 263
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
4-233 6.51e-19

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: 82.94  E-value: 6.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   4 IILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEIlIIST---PQDIDLYkrlFEDGSAYGLKIEYAIQ 80
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVnylAEMIEDY---FGDGSKFGVNISYVRE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  81 PSPDGLAQAFIIGEKFIgNDSVCMVLGDnIFYGYNLSSQLQEAAQMKDGATVFG--YYVNDPerYGVAEFDpSGKVLSLE 158
Cdd:cd06426    78 DKPLGTAGALSLLPEKP-TDPFLVMNGD-ILTNLNYEHLLDFHKENNADATVCVreYEVQVP--YGVVETE-GGRITSIE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057341137 159 EKpavPKSNYAV-TGLYfygndvVAKAKALKPSPRGE-LEITDLNRIYLDEG-RLNV-KLLGRgmaWLDTGTHDSLLEA 233
Cdd:cd06426   153 EK---PTHSFLVnAGIY------VLEPEVLDLIPKNEfFDMPDLIEKLIKEGkKVGVfPIHEY---WLDIGRPEDYEKA 219
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-82 8.27e-17

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: 77.31  E-value: 8.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDID-LYKRLFEDGSAYGLKIEYAI 79
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAeISTYLRSFPLNLKQKLDEVT 80

                  ...
gi 1057341137  80 QPS 82
Cdd:cd04198    81 IVL 83
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-233 9.68e-14

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: 68.75  E-value: 9.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEIlIISTPQDIDLYKRLFEDgSAYGLKIEyaIQP 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNTHHLADQIEAHLGD-SRFGLRIT--ISD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  82 SPD-------GLAQAfiigEKFIGNDSVCMVLGDnIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEF--DPSG 152
Cdd:cd06422    77 EPDelletggGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFslDADG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 153 KVLSLEEKPAVPksnYAVTGLYfygndvVAKAKALKPSPRGELEITDLNRIYLDEGRLNVkLLGRGmAWLDTGTHDSLLE 232
Cdd:cd06422   152 RLRRGGGGAVAP---FTFTGIQ------ILSPELFAGIPPGKFSLNPLWDRAIAAGRLFG-LVYDG-LWFDVGTPERLLA 220

                  .
gi 1057341137 233 A 233
Cdd:cd06422   221 A 221
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-52 1.76e-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: 68.05  E-value: 1.76e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILII 52
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-199 7.72e-13

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 67.62  E-value: 7.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILII--STPQDID------------LYKR---- 63
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVthSSKNSIEnhfdtsfeleamLEKRvkrq 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  64 LFEDGSAY---GLKIEYAIQPSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGY-------NLSSQLQEAAQMKDgATVF 133
Cdd:PRK13389   90 LLDEVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYesdlsqdNLAEMIRRFDETGH-SQIM 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057341137 134 GYYVNDPERYGV-----AEFDP--SGKVLSLEEKPA--VPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITD 199
Cdd:PRK13389  169 VEPVADVTAYGVvdckgVELAPgeSVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-199 2.22e-12

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 66.07  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIIS------------TPQDID------LYK 62
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELEslleqrVKR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  63 RLFEDGSAY---GLKIEYAIQPSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYG-------YNLSSQLQEAAQMKDGATV 132
Cdd:PRK10122   84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDasadplrYNLAAMIARFNETGRSQVL 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057341137 133 FGYYVNDPERYGVAE----FDPSGKV---LSLEEKPAVPK---SNYAVTGLYFYGNDVVAKAKALKPSPRGELEITD 199
Cdd:PRK10122  164 AKRMPGDLSEYSVIQtkepLDREGKVsriVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-233 2.79e-10

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 60.47  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   3 GIILAGGSGTRLYPITKSISkqiipvynKPMIYY---------PLSVLMLSGIQEILIIsTPqdidlYK--RLFE---DG 68
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRA--------KPAVPFggkyriidfPLSNCVNSGIRRVGVL-TQ-----YKshSLNDhigSG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  69 SAYGLKIE---------YAIQPSPD---GLAQA------FIIGEKFignDSVCMVLGDNIfYGYNLSSQLQEAAQMKDGA 130
Cdd:COG0448    70 KPWDLDRKrggvfilppYQQREGEDwyqGTADAvyqnldFIERSDP---DYVLILSGDHI-YKMDYRQMLDFHIESGADI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 131 TVFGYYVNDPE--RYGVAEFDPSGKVLSLEEKPAVPKSNYAVTGLYFYgndvvaKAKALKpsprgELEITDLNRIYLDEG 208
Cdd:COG0448   146 TVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVF------NKDVLI-----ELLEEDAPNSSHDFG 214
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1057341137 209 RlNV--KLLGRG--MA------WLDTGTHDSLLEA 233
Cdd:COG0448   215 K-DIipRLLDRGkvYAyefdgyWRDVGTIDSYYEA 248
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-84 2.58e-08

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 53.32  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   2 KGIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDiDLYKRLFEDgsaYGLKIEYAIQP 81
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKA-ELIEEALAR---PGPDVTFVYNP 76

                  ...
gi 1057341137  82 SPD 84
Cdd:COG1213    77 DYD 79
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
4-75 4.29e-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: 52.53  E-value: 4.29e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057341137   4 IILAGGSGTRLypiTKSISKQIIPVYNKPMIYYPLSVLMLSG-IQEILIISTPQDIDLYKRLFEDGSAYGLKI 75
Cdd:cd02516     4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPPDDIDLAKELAKYGLSKVVKI 73
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
4-213 4.57e-08

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: 52.62  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   4 IILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDiDLYKRLFEDgsayGLKIEYAIQPSP 83
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKK-EQIEELLKK----YPNIKFVYNPDY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  84 D--GLAQAFIIGEKFIgNDSVCMVLGDNIFYGYNLSSQLQEAAqmKDGATVFGYYVNDPERYGVAeFDPSGKVLSLEEKP 161
Cdd:cd02523    77 AetNNIYSLYLARDFL-DEDFLLLEGDVVFDPSILERLLSSPA--DNAILVDKKTKEWEDEYVKD-LDDAGVLLGIISKA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1057341137 162 AVPKSNYAVT-GLYFY----GNDVVAKAKALKPSPRGELEITDLNRIYLDEGRLNVK 213
Cdd:cd02523   153 KNLEEIQGEYvGISKFspedADRLAEALEELIEAGRVNLYYEDALQRLISEEGVKVK 209
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-67 2.07e-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: 50.51  E-value: 2.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057341137   4 IILAGGSGTRLypiTKSISKQIIPVYNKPMIYYPLSVLMLSG-IQEILIISTPQDIDLYKRLFED 67
Cdd:COG1211     1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-210 2.37e-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: 50.72  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   3 GIILAGG--SGTRLYPITKSISKQIIPVYNKPMIYYPLSVL-MLSGIQEILIISTPQDIDLYKRLFEDGSAYGLKIEYAI 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  80 QPSPDGLAQAF-----IIGEkfiGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPE--RYGVAEFDPS- 151
Cdd:cd06428    81 EYKPLGTAGGLyhfrdQILA---GNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQasNYGCIVEDPSt 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1057341137 152 GKVLSLEEKPAVPKSNYAVTGLYFYGNDVVAKAKALKPSPRGELEITDLNRIYLDEGRL 210
Cdd:cd06428   158 GEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVI 216
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-200 5.61e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 50.53  E-value: 5.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLypitKS-ISKQIIPVYNKPMIYYPLSVlMLSGIQEILIIsTPQDIDLYKRLF-EDgsayglkIEYA 78
Cdd:PRK14357    1 MRALVLAAGKGTRM----KSkIPKVLHKISGKPMINWVIDT-AKKVAQKVGVV-LGHEAELVKKLLpEW-------VKIF 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  79 IQPSPDGLAQAFIIGEKFIG-NDSVCMVLGDNIFYGYNLSSQLQEAAQMKDG-ATVFGYYVNDPERYGVAEFDpSGKVLS 156
Cdd:PRK14357   68 LQEEQLGTAHAVMCARDFIEpGDDLLILYGDVPLISENTLKRLIEEHNRKGAdVTILVADLEDPTGYGRIIRD-GGKYRI 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1057341137 157 LEEKPAVPKSNYAV---TGLY-FYGNDVVAKAKALKP-SPRGELEITDL 200
Cdd:PRK14357  147 VEDKDAPEEEKKIKeinTGIYvFSGDFLLEVLPKIKNeNAKGEYYLTDA 195
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
4-209 1.28e-06

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: 48.28  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   4 IILAGGSGTRLypitKS-ISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLfedgsaYGLKIEYAIQPS 82
Cdd:cd02540     2 VILAAGKGTRM----KSdLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKAL------ANPNVEFVLQEE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  83 PDGLAQAFIIGEKFIGNDS-VCMVL-GDNIFygynLSSQ-----LQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVL 155
Cdd:cd02540    72 QLGTGHAVKQALPALKDFEgDVLVLyGDVPL----ITPEtlqrlLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVL 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 156 S-LEEKPAVP--KSNYAV-TGLY-FYGNDVVAKAKALKPSP-RGELEITDLNRIYLDEGR 209
Cdd:cd02540   148 RiVEEKDATEeeKAIREVnAGIYaFDAEFLFEALPKLTNNNaQGEYYLTDIIALAVADGL 207
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-53 2.99e-06

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: 46.77  E-value: 2.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1057341137   3 GIILAGGSGTRLYPITKSISKQIIPV---YNkpMIYYPLSVLMLSGIQEILIIS 53
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLT 52
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-67 3.12e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 47.05  E-value: 3.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057341137   4 IILAGGSGTRLypiTKSISKQIIPVYNKPMIYYPLSVLMLSG-IQEILIISTPQDIDLYKRLFED 67
Cdd:PRK00155    7 IIPAAGKGSRM---GADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELLLA 68
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
3-52 8.31e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 46.80  E-value: 8.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1057341137   3 GIILAGGSGTRLYPITKSISKQIIPVYNK-PMIYYPLSVLMLSGIQEILII 52
Cdd:PRK02862    6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
3-166 1.01e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 46.36  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   3 GIILAGGSGTRLYPITKSISKQIIP---VYNkpMIYYPLSVLMLSGIQEILI------------------ISTPQD--ID 59
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVltqykshsldrhisqtwrLSGLLGnyIT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  60 -------LYKRLFEdGSAyglkieyaiqpspDGLAQA--FIIGEKfigNDSVCMVLGDNIfYGYNLSSQLQEAAQMKDGA 130
Cdd:PRK00844   86 pvpaqqrLGKRWYL-GSA-------------DAIYQSlnLIEDED---PDYVVVFGADHV-YRMDPRQMVDFHIESGAGV 147
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1057341137 131 TVFGYYV--NDPERYGVAEFDPSGKVLSLEEKPAVPKS 166
Cdd:PRK00844  148 TVAAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPG 185
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-68 1.44e-05

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: 45.65  E-value: 1.44e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057341137   1 MKGIILAGGSGTRLYPI-TKSISKQIIPVY-NKPMIYYPLS-VLMLSGIQEILIISTPQDIDLYKRLFEDG 68
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVVTNEEYRFLVREQLPEG 71
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
1-174 1.77e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 45.63  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   1 MKGIILAGGSGTRLYPITKSISKQIIPVYNK-PMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLfEDGSAYGLKIE--- 76
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHI-GIGSPWDLDRIngg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  77 -YAIQPSPD--------GLAQAFIIGEKFIGN---DSVCMVLGDNIfYGYNLSSQLQEAAQMKDGAT--VFGYYVNDPER 142
Cdd:PRK05293   83 vTILPPYSEseggkwykGTAHAIYQNIDYIDQydpEYVLILSGDHI-YKMDYDKMLDYHKEKEADVTiaVIEVPWEEASR 161
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1057341137 143 YGVAEFDPSGKVLSLEEKPAVPKSNYAVTGLY 174
Cdd:PRK05293  162 FGIMNTDENMRIVEFEEKPKNPKSNLASMGIY 193
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
3-52 2.34e-05

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 45.23  E-value: 2.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1057341137   3 GIILAGGSGTRLYPITKSISKQIIPV---YNkpMIYYPLSVLMLSGIQEILII 52
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-264 3.74e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 44.73  E-value: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   4 IILAGGSGTRLypitKS-ISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLFEDGsayglKIEYAIQPS 82
Cdd:PRK14355    7 IILAAGKGTRM----KSdLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG-----DVSFALQEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  83 P--DGLAQAFIIGEKFIGNDSVCMVLGDN-IFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSL-E 158
Cdd:PRK14355   78 QlgTGHAVACAAPALDGFSGTVLILCGDVpLLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLRIvE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137 159 EKPAVPKS---NYAVTGLYFYGNDVVAKA-KALK-PSPRGELEITDLNRIYLDEGRLNVkllgrGMAWLD----TGTHD- 228
Cdd:PRK14355  158 EKDATPEErsiREVNSGIYCVEAAFLFDAiGRLGnDNAQGEYYLTDIVAMAAAEGLRCL-----AFPVADpdeiMGVNDr 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1057341137 229 -SLLEAANFISTIENRQgLMVACIEEIAFRMKFIDRD 264
Cdd:PRK14355  233 aQLAEAARVLRRRINRE-LMLAGVTLIDPETTYIDRG 268
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-176 8.91e-05

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: 43.01  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   4 IILAGGSGTRLYPITKSISKQIIPVYNKPMIYYplSVLMLSGIQE---ILIIstpqdidlykrLFEDGSAYGLKIE---- 76
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrfIFIC-----------RDEHNTKFHLDESlkll 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  77 ------YAIQPSPDGLAQAFIIGEKFIGNDSVCMVLGDNIFYGYNLSSQLQEAAQMKDGATVFGYYVNDPeRYGVAEFDP 150
Cdd:cd04183    69 apnatvVELDGETLGAACTVLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDE 147
                         170       180
                  ....*....|....*....|....*.
gi 1057341137 151 SGKVLSLEEKpaVPKSNYAVTGLYFY 176
Cdd:cd04183   148 NGRVIETAEK--EPISDLATAGLYYF 171
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-52 1.17e-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: 42.59  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1057341137   3 GIILAGGSGTRLYPITKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILII 52
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-208 1.16e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.20  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   4 IILAGGSGTRLypitKS-ISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTPQDIDLYKRLfedgsayGLKIEYAIQPS 82
Cdd:PRK14354    6 IILAAGKGTRM----KSkLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVL-------GDRSEFALQEE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137  83 PDGLAQAFIIGEKFIGN-DSVCMVL-GDN-IFYGYNLSSQLQEAAQMKDGATVFGYYVNDPERYGVAEFDPSGKVLSL-E 158
Cdd:PRK14354   75 QLGTGHAVMQAEEFLADkEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVEKIvE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1057341137 159 EKPAVP---KSNYAVTGLYFYGNDVVAKA-KALKP-SPRGELEITDLNRIYLDEG 208
Cdd:PRK14354  155 QKDATEeekQIKEINTGTYCFDNKALFEAlKKISNdNAQGEYYLTDVIEILKNEG 209
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
3-111 2.92e-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: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057341137   3 GIILAGGSGTRLypitksISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTpqDIDLYKRLFEdgsAYGLKIeYAIQPS 82
Cdd:pfam02348   2 AIIPARLGSKRL------PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVAT--DSEEIADVAK---EFGAGV-VMTSGS 69
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1057341137  83 -PDGLAQAFIIGEKFIG--NDSVCMVLGDNIF 111
Cdd:pfam02348  70 lSSGTDRFYEVVKAFLNdhDDIIVNIQGDNPL 101
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-52 3.24e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 38.51  E-value: 3.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1057341137   1 MKGIILAGGSGTRLYPI-TKSISKQIIPVY-NKPMIYypLSVLMLSGI---QEILII 52
Cdd:COG0836     3 IYPVILAGGSGTRLWPLsRESYPKQFLPLLgEKSLLQ--QTVERLAGLvppENILVV 57
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
4-52 4.11e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 38.28  E-value: 4.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1057341137   4 IILAGGSGTRLYPITKSISKQIIPVYNK-PMIYYPLSVLMLSGIQEILII 52
Cdd:PRK00725   19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVL 68
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-55 9.28e-03

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: 36.40  E-value: 9.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1057341137   6 LAGGSGTRLypitKSISKQIIPVYNKPMIYYPLSVLMLSGIQEILIISTP 55
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP 46
 
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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