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Conserved domains on  [gi|1395859111|gb|AWR49762|]
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glucose-1-phosphate thymidylyltransferase [Escherichia coli]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-286 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: 558.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  82 SPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 162 LKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASHFIHTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1395859111 242 KRQGMKVACLEEIGYRNQWLSAEGVAAQAERLKKTEYGAYLKRLL 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
 
Name Accession Description Interval E-value
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: 558.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  82 SPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 162 LKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASHFIHTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1395859111 242 KRQGMKVACLEEIGYRNQWLSAEGVAAQAERLKKTEYGAYLKRLL 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
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: 554.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  81 PSPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 161 PLKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASHFIHTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1395859111 241 EKRQGMKVACLEEIGYRNQWLSAEGVAAQAERLKKTEYGAYLKRLLNER 289
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 9.54e-172

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


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 474.37  E-value: 9.54e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  81 PSPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 161 PLKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASHFIHTI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-286 1.12e-151

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 425.63  E-value: 1.12e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  82 SPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 162 LKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASHFIHTIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1395859111 242 KRQGMKVACLEEIGYRNQWLSAEGVAAQAERLKKTEYGAYLKRLL 286
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-238 2.40e-95

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: 281.06  E-value: 2.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDK-PMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  81 PSPDGLAQAFIIGEKFIGNDAC-ALVLGDNIYFGQSFGKKLEAAAAKTS--GATVFGYQVLDPERFGVVEFDENFKALSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 158 EEKPLKPK-SDWAVTGLYFYDNNVVEM-AKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASH 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ...
gi 1395859111 236 FIH 238
Cdd:pfam00483 241 FLL 243
 
Name Accession Description Interval E-value
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: 558.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQP 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  82 SPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEKP 161
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 162 LKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASHFIHTIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1395859111 242 KRQGMKVACLEEIGYRNQWLSAEGVAAQAERLKKTEYGAYLKRLL 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
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: 554.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQ 80
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  81 PSPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEK 160
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 161 PLKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASHFIHTI 240
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1395859111 241 EKRQGMKVACLEEIGYRNQWLSAEGVAAQAERLKKTEYGAYLKRLLNER 289
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDSN 289
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-240 9.54e-172

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


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 474.37  E-value: 9.54e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQ 80
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  81 PSPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEK 160
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 161 PLKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASHFIHTI 240
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-286 1.12e-151

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 425.63  E-value: 1.12e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQP 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  82 SPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 162 LKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASHFIHTIE 241
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1395859111 242 KRQGMKVACLEEIGYRNQWLSAEGVAAQAERLKKTEYGAYLKRLL 286
Cdd:PRK15480  245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKMI 289
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-238 2.40e-95

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: 281.06  E-value: 2.40e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDK-PMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQ 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  81 PSPDGLAQAFIIGEKFIGNDAC-ALVLGDNIYFGQSFGKKLEAAAAKTS--GATVFGYQVLDPERFGVVEFDENFKALSI 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 158 EEKPLKPK-SDWAVTGLYFYDNNVVEM-AKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFAWLDTGTHDSLMDASH 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFlAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240


                  ...
gi 1395859111 236 FIH 238
Cdd:pfam00483 241 FLL 243
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-237 6.72e-67

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: 208.19  E-value: 6.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILII--STPDDmpsFQRLLGDGSQFGVNFSYA 78
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVvgPTGEE---IKEALGDGSRFGVRITYI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  79 IQPSPDGLAQAFIIGEKFIGNDACALVLGDNIyFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENfKALSIE 158
Cdd:cd04189    78 LQEEPLGLAHAVLAARDFLGDEPFVVYLGDNL-IQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 159 EKPLKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGdLHVEL-LGRGFaWLDTGTHDSLMDASHFI 237
Cdd:cd04189   156 EKPKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRG-RRVGYsIVTGW-WKDTGTPEDLLEANRLL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-225 2.77e-60

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: 190.87  E-value: 2.77e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   3 GIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDmPSFQRLLGDGSQFGVNFSYAIQPS 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  83 PDGLAQAFIIGEKFIGNDACALVLGDNIyFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEKPL 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVL-TDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395859111 163 KPKSDWAVTGLYFYDNNVVEMAKDVKPseRGELEITTLNQMYLEQGDLHVELLgrGFAWLDTG 225
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-249 8.34e-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: 186.07  E-value: 8.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAIQP 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  82 SPDGLAQAFIIGEKFIGNDACALVLGDNIyFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNL-IQDGISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 162 LKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGFaWLDTGTHDSLMDASHFI-HTI 240
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLIlDEV 238

                         250
                  ....*....|
gi 1395859111 241 EKR-QGMKVA 249
Cdd:TIGR01208 239 EREvQGVDDE 248
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-225 3.14e-44

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: 154.67  E-value: 3.14e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDmPSFQRLLGDGSQFGVNFSYAIQ 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGK-EKVREYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  81 PSPDGLAQAFIIGEKFIgNDACALVLGDNIYFGQSFGKKLEAaaaktSGATVFGYQVLDPERFGVVEFDENfKALSIEEK 160
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLIRA-----EAPAIAVVEVDDPSDYGVVETDGG-RVTGIVEK 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395859111 161 PLKPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDLHVELLGRGfaWLDTG 225
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVG 215
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-233 9.56e-41

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


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 141.06  E-value: 9.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDIlIIST---PDDMPSFqrlLGDGSQFGVNFSYA 78
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVgylAEQIEEY---FGDGSRFGVRITYV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  79 IQPSP----DGLAQAfiigEKFIGNDACALVLGDnIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKA 154
Cdd:COG1208    77 DEGEPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRV 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395859111 155 LSIEEKPLKPKSDWAVTGLYFYDNNVVEmakDVKPSERGELEiTTLNQMyLEQGDLHVELLgRGFaWLDTGTHDSLMDA 233
Cdd:COG1208   152 TRFVEKPEEPPSNLINAGIYVLEPEIFD---YIPEGEPFDLE-DLLPRL-IAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-234 1.26e-31

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: 118.02  E-value: 1.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTP------------------------D 56
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdrsyeleetlekkgkT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  57 DMPSFQRLLGDGsqfgVNFSYAIQPSPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFG-KKLEAAAAKTsGATVFGY 135
Cdd:cd02541    81 DLLEEVRIISDL----ANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPClKQLIEAYEKT-GASVIAV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 136 QVLDPE---RFGVVEF----DENFKALSIEEKPlKPK---SDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYL 205
Cdd:cd02541   156 EEVPPEdvsKYGIVKGekidGDVFKVKGLVEKP-KPEeapSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLL 234

                         250       260       270
                  ....*....|....*....|....*....|
gi 1395859111 206 EQGDLH-VELLGRgfaWLDTGTHDSLMDAS 234
Cdd:cd02541   235 EEEPVYaYVFEGK---RYDCGNKLGYLKAT 261
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-226 1.10e-20

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 89.32  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTP---------DDMPSFQRLL---GD-- 67
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraiedhfDRSYELEATLeakGKee 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  68 ------GSQFGVNFSYAIQPSPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFG-KKLEAAAAKTsGATVFGYQVLDP 140
Cdd:COG1210    85 lleevrSISPLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPClKQMIEVYEET-GGSVIAVQEVPP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 141 E---RFGVVEFDEN----FKALSIEEKPlKPK---SDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYLEQGDL 210
Cdd:COG1210   164 EevsKYGIVDGEEIeggvYRVTGLVEKP-APEeapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEEPV 242

                         250
                  ....*....|....*..
gi 1395859111 211 H-VELLGRgfaWLDTGT 226
Cdd:COG1210   243 YaYEFEGK---RYDCGD 256
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-226 5.58e-20

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: 86.11  E-value: 5.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRD-ILIIS-TPDDMPSFQRLLGDgsQFGVNFSYA 78
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  79 IQPSPDGLAQAFIIGEKFI-GNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKAL-S 156
Cdd:cd06425    79 IETEPLGTAGPLALARDLLgDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIeR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 157 IEEKPLKPKSDWAVTGLYFYDNNVVemakDVKPSERGELEITTLNQMyLEQGDLHVELLgRGFaWLDTGT 226
Cdd:cd06425   159 FVEKPKVFVGNKINAGIYILNPSVL----DRIPLRPTSIEKEIFPKM-ASEGQLYAYEL-PGF-WMDIGQ 221
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-230 4.67e-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: 83.33  E-value: 4.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   4 IVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDIlIIST---PDDMPSFqrlLGDGSQFGVNFSYAIQ 80
Cdd:cd06426     2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVnylAEMIEDY---FGDGSKFGVNISYVRE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  81 PSPDGLAQAFIIGEKFIGNDacALVLGDNIYFGQSFGKKLEAAAAKTSGATV----FGYQVldPerFGVVEFDENFkALS 156
Cdd:cd06426    78 DKPLGTAGALSLLPEKPTDP--FLVMNGDILTNLNYEHLLDFHKENNADATVcvreYEVQV--P--YGVVETEGGR-ITS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 157 IEEkplKPKSDWAV-TGLYFYDNNVVEMakdVKPSERgeLEITTLNQMYLEQGD------LHVEllgrgfaWLDTGTHDS 229
Cdd:cd06426   151 IEE---KPTHSFLVnAGIYVLEPEVLDL---IPKNEF--FDMPDLIEKLIKEGKkvgvfpIHEY-------WLDIGRPED 215


                  .
gi 1395859111 230 L 230
Cdd:cd06426   216 Y 216
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-233 5.45e-17

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: 77.98  E-value: 5.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   4 IVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDIL---------IIstpddmpsfqRLLGDGSQFGVN 74
Cdd:cd06915     2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVlsvgylaeqIE----------EYFGDGYRGGIR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  75 FSYAIQPSPDGLAQAFIIGEKFIGNDACALVLGDNiYFGQSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFKA 154
Cdd:cd06915    72 IYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDT-YFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 155 LSIEEKPLKPKSDWAVTGLYFYDNNVVEMAKDVKPSergeleittlnqmyLEQGDLHVELLG---RGFA----WLDTGTH 227
Cdd:cd06915   151 IAFVEKGPGAAPGLINGGVYLLRKEILAEIPADAFS--------------LEADVLPALVKRgrlYGFEvdgyFIDIGIP 216


                  ....*.
gi 1395859111 228 DSLMDA 233
Cdd:cd06915   217 EDYARA 222
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-65 6.08e-16

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 74.62  E-value: 6.08e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLL 65
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYL 65
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-58 3.48e-12

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: 64.20  E-value: 3.48e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDM 58
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQ 58
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-177 9.04e-10

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 58.55  E-value: 9.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   3 GIVLAGGSGTRLYPITQGVSKQLLPI---Y---DkpmiFyPVSVLMLAGIRDILIIsTPDDMPSFQRLLGDGSQFGVNfs 76
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPAVPFggkYriiD----F-PLSNCVNSGIRRVGVL-TQYKSHSLNDHIGSGKPWDLD-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  77 yaiqPSPDGL----AQAFIIGEKFIGNDACA----------------LVL-GDNIY---FGQSFgkkleaAAAKTSGA-- 130
Cdd:COG0448    76 ----RKRGGVfilpPYQQREGEDWYQGTADAvyqnldfiersdpdyvLILsGDHIYkmdYRQML------DFHIESGAdi 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1395859111 131 TVFGYQVLDPE--RFGVVEFDENFKALSIEEKPLKPKSDWAVTGLYFYD 177
Cdd:COG0448   146 TVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFN 194
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-52 7.41e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 54.86  E-value: 7.41e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILII 52
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-198 7.78e-09

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 55.66  E-value: 7.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIIS------------TPDDMPSF------Q 62
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvkR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  63 RLLGDGSQF---GVNFSYAIQPSPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQS---FGKKLEAAAAK---TSGATVF 133
Cdd:PRK10122   84 QLLAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASadpLRYNLAAMIARfneTGRSQVL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395859111 134 GYQVL-DPERFGVVEFDENFKA-------LSIEEKPLKPK---SDWAVTGLYFYDNNVVEMAKDVKPSERGELEIT 198
Cdd:PRK10122  164 AKRMPgDLSEYSVIQTKEPLDRegkvsriVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-207 3.68e-08

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 53.37  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILII--STPDDM-----PSF----------QRL 64
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVthSSKNSIenhfdTSFeleamlekrvKRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  65 LGDGSQF----GVNFSYAIQPSPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAA------KTSGATVFG 134
Cdd:PRK13389   90 LLDEVQSicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEmirrfdETGHSQIMV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 135 YQVLDPERFGVVEFD-------ENFKALSIEEKPL--KPKSDWAVTGLYFYDNNVVEMAKDVKPSERGELEITTLNQMYL 205
Cdd:PRK13389  170 EPVADVTAYGVVDCKgvelapgESVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDMLI 249


                  ..
gi 1395859111 206 EQ 207
Cdd:PRK13389  250 EK 251
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-233 5.24e-08

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: 52.19  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   2 KGIVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDIlIIST---PDDMPSFqrlLGDgSQFGVN--FS 76
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlADQIEAH---LGD-SRFGLRitIS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  77 Y---AIQPSPDGLAQAfiigEKFIGNDACALVLGDNIYFGqSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENfK 153
Cdd:cd06422    76 DepdELLETGGGIKKA----LPLLGDEPFLVVNGDILWDG-DLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLD-A 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 154 ALSIEEKPLKPKSDWAVTGLYFYDNNVVEMAKDVKPSergeleittLNQMY---LEQGDLHVELLgRGFaWLDTGTHDSL 230
Cdd:cd06422   150 DGRLRRGGGGAVAPFTFTGIQILSPELFAGIPPGKFS---------LNPLWdraIAAGRLFGLVY-DGL-WFDVGTPERL 218


                  ...
gi 1395859111 231 MDA 233
Cdd:cd06422   219 LAA 221
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-52 7.34e-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: 51.85  E-value: 7.34e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1395859111   4 IVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILII 52
Cdd:cd02523     2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIV 50
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-67 7.87e-08

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: 7.87e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395859111   4 IVLAGGSGTRLypiTQGVSKQLLPIYDKPMIFYPVSVLMLAG-IRDILIISTPDDMPSFQRLLGD 67
Cdd:COG1211     1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAK 62
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-65 5.28e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 49.36  E-value: 5.28e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395859111   4 IVLAGGSGTRLYPitqGVSKQLLPIYDKPMIFYPVSVLMLAG-IRDILIISTPDDMPSFQRLL 65
Cdd:PRK00155    7 IIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-132 1.23e-06

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: 47.19  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   3 GIVLAGGSGTRLypitqGVSKQLLPIYDKPMIFYpvSVLMLAGIRDILIISTPDDmpsfqRLLGDGSQFGVNFsyAIQPS 82
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLER--VLERLRPAGDEVVVVANDE-----EVLAALAGLGVPV--VPDPD 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1395859111  83 PD-----GLAQAFiigEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATV 132
Cdd:pfam12804  67 PGqgplaGLLAAL---RAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIV 118
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 4-208 2.16e-06

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 48.82  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   4 IVLAGGSGTRLypiTQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFgvnfsyAIQPSP 83
Cdd:PRK14358   11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAF------ARQEQQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  84 DGLAQAFIIGEKFIGN-DACALVL-GDNIYFGQSFGKKLEAA-AAKTSGATVFGYQVLDPERFGVVEFDENFKALSIEEK 160
Cdd:PRK14358   82 LGTGDAFLSGASALTEgDADILVLyGDTPLLRPDTLRALVADhRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVEQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1395859111 161 PLKPKSDWAV----TGLYFYDNNVVEMAKDV-KPSERGELEITTLNQMYLEQG 208
Cdd:PRK14358  162 KDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-68 2.44e-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: 2.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395859111   4 IVLAGGSGTRLypiTQGVSKQLLPIYDKPMIFYPVSVLM-LAGIRDILIISTPDDMPSFQRLLGDG 68
Cdd:cd02516     4 IILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYG 66
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-65 3.64e-06

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 46.42  E-value: 3.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   6 LAGGSGTRLypitQGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPdDMPSFQRLL 65
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP-NTPKTREYL 55
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-217 9.98e-06

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: 45.71  E-value: 9.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   4 IVLAGGSGTRLYPITQGVSKQLLPIYDKPMIFYpvSVLMLAGIRD---ILIIS----TPDDMPSFQRLLGDGSQFgvnfs 76
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrfIFICRdehnTKFHLDESLKLLAPNATV----- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  77 YAIQPSPDGLAQAFIIGEKFIGNDACALVLGDNIYFGQSFGKKLEAAAAKTSGATVFGYQVLDPeRFGVVEFDENFKALS 156
Cdd:cd04183    75 VELDGETLGAACTVLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGRVIE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395859111 157 IEEKplKPKSDWAVTGLYFYDNN--VVEMAKDVKP---SERGELEIT-TLNQMYLEQGDLHVELLGR 217
Cdd:cd04183   154 TAEK--EPISDLATAGLYYFKSGslFVEAAKKMIRkddSVNGEFYISpLYNELILDGKKVGIYLIDK 218
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-74 1.61e-05

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: 44.84  E-value: 1.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395859111   3 GIVLAGGSGTRLYPITQGVSKQLLPI---YDkpMIFYPVSVLMLAGIRDILIIsTPDDMPSFQRLLGDGSQFGVN 74
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVL-TQYKSRSLNDHLGSGKEWDLD 72
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 4-69 2.06e-05

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


Pssm-ID: 460075  Cd Length: 219  Bit Score: 44.75  E-value: 2.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395859111   4 IVLAGGSGTRLypiTQGVSKQLLPIYDKPMIFYPVSVLMLAGIRD-ILIISTPDDMPSFQRLLGDGS 69
Cdd:pfam01128   2 VIPAAGSGKRM---GAGVPKQFLQLLGQPLLEHTVDAFLASPVVDrIVVAVSPDDTPEFRQLLGDPS 65
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-108 3.77e-05

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 43.32  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   3 GIVLAGGSGTRLypitqGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNfsyaiqps 82
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVIN-------- 69

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1395859111  83 PD---GLAQAFIIGEKFIGN--DACALVLGD 108
Cdd:cd04182    70 PDweeGMSSSLAAGLEALPAdaDAVLILLAD 100
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-150 3.81e-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: 44.10  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPI-TQGVSKQLLPIY-DKPMIFYPVS-VLMLAGIRDILIISTPDDMPSFQRLLGDGSQfGVNFSy 77
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLLQQTLDrLKGLVPPDRILVVTNEEYRFLVREQLPEGLP-EENII- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  78 aIQPSPDGLAQAFIIGEKFI---GNDACALVL------GDNIYFGQSFGKKLEAAAAK---------TSGATVFGY---- 135
Cdd:cd02509    79 -LEPEGRNTAPAIALAALYLakrDPDAVLLVLpsdhliEDVEAFLKAVKKAVEAAEEGylvtfgikpTRPETGYGYieag 157

                         170
                  ....*....|....*
gi 1395859111 136 QVLDPERFGVVEFDE 150
Cdd:cd02509   158 EKLGGGVYRVKRFVE 172
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-87 3.92e-05

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: 44.17  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   3 GIVLAGG--SGTRLYPITQGVSKQLLPIYDKPMIFYPVSVL-MLAGIRDILIISTPDDMPsFQRLLGDGSQ-FGVNFSYA 78
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESV-FSDFISDAQQeFNVPIRYL 79


                  ....*....
gi 1395859111  79 IQPSPDGLA 87
Cdd:cd06428    80 QEYKPLGTA 88
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-108 5.51e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 43.23  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   3 GIVLAGGSGTRLypitqGVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTPDDMPSFQRLLGDGSQFGVNFSYAiqps 82
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWE---- 76

                          90       100
                  ....*....|....*....|....*...
gi 1395859111  83 pDGLAQAFIIGEKFIGN--DACALVLGD 108
Cdd:COG2068    77 -EGMSSSLRAGLAALPAdaDAVLVLLGD 103
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-57 8.05e-05

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 42.49  E-value: 8.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1395859111   1 MKGIVLAGGSGTRLypitqGVSKQLLPIYDKPMIFYPVSVlmLAGIRDILIISTPDD 57
Cdd:COG0746     5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLER--LRPQVDEVVIVANRP 54
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 4-67 1.15e-04

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


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 42.91  E-value: 1.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395859111   4 IVLAGGSGTRLypiTQGVSKQLLPIYDKPMIFYPVSVLMLAG-IRDILIISTPDDMPSFQRLLGD 67
Cdd:PRK09382    9 VIVAAGRSTRF---SAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPE 70
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-52 2.94e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 41.76  E-value: 2.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1395859111   3 GIVLAGGSGTRLYPITQGVSKQLLPI---YDkpMIFYPVSVLMLAGIRDILII 52
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-34 4.43e-04

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 41.20  E-value: 4.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1395859111   1 MKGIVLAGGSGTRLYPitqgVS-----KQLLPIY-DKPMI 34
Cdd:COG0836     3 IYPVILAGGSGTRLWP----LSresypKQFLPLLgEKSLL 38
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 1-52 4.46e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 41.41  E-value: 4.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1395859111   1 MK---GIVLAGGSGTRLYPITQGVSKQLLPIYDK-PMIFYPVSVLMLAGIRDILII 52
Cdd:PRK02862    1 MKrvlAIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVL 56
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-64 6.32e-04

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 39.78  E-value: 6.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395859111   1 MKGIVLAGGSGTRLypitQGVSKQLLPIYDKPMIFYpvsVLM-LAGIRDILIISTPDDMPSFQRL 64
Cdd:PRK00317    4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQH---VIErLAPQVDEIVINANRNLARYAAF 61
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 104-234 7.20e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 40.62  E-value: 7.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111 104 LVL-GDNIYfGQSFGKKLEAAAAKTSGATVFGYQVLDPE--RFGVVEFDENFKALSIEEKPLKPKSDWAVTGLYFY---- 176
Cdd:PRK05293  121 LILsGDHIY-KMDYDKMLDYHKEKEADVTIAVIEVPWEEasRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFnwkr 199

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395859111 177 -----------DNNVVEMAKDVKPSergeleittlnqmYLEQGdlhvellGRGFA------WLDTGTHDSLMDAS 234
Cdd:PRK05293  200 lkeyliedeknPNSSHDFGKNVIPL-------------YLEEG-------EKLYAypfkgyWKDVGTIESLWEAN 254
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 3-58 5.18e-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: 37.32  E-value: 5.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1395859111   3 GIVLAGGSGTRLypitqgVSKQLLPIYDKPMIFYPVSVLMLAGIRDILIISTpDDM 58
Cdd:pfam02348   2 AIIPARLGSKRL------PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVAT-DSE 50
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-23 6.23e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 37.88  E-value: 6.23e-03
                          10        20
                  ....*....|....*....|.
gi 1395859111   3 GIVLAGGSGTRLYPITQGVSK 23
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAK 28
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-160 7.09e-03

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 37.11  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111   4 IVLAGGSGTRL---YPitqgvsKQLLPIYDKPMIFYPVSVLMLAGIRDILIIsTPDDMPSFQRLLGDGsqfgvNFSYAIQ 80
Cdd:cd02540     2 VILAAGKGTRMksdLP------KVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALANP-----NVEFVLQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395859111  81 PSPDGLAQAFIIGEKFIGNDaCALVLgdnIYFG-------QSFGKKLEAAAAKTSGATVFGYQVLDPERFGVVEFDENFK 153
Cdd:cd02540    70 EEQLGTGHAVKQALPALKDF-EGDVL---VLYGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGK 145


                  ....*...
gi 1395859111 154 ALSI-EEK 160
Cdd:cd02540   146 VLRIvEEK 153
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-64 9.52e-03

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 36.40  E-value: 9.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395859111   1 MKGIVLAGGSGTRLypitqGVSKQLLPIYDKPMIFYPVSvlMLAGIRDILIISTPDDMPSFQRL 64
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYALL 57
 
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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