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Conserved domains on  [gi|1391717868|emb|SPP93924|]
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Glucose-1-phosphate cytidylyltransferase [Bradyrhizobium vignae]

Protein Classification

glucose-1-phosphate cytidylyltransferase( domain architecture ID 10118576)

glucose-1-phosphate cytidylyltransferase catalyzes the transfer of a CMP moiety from CTP to glucose 1-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-254 4.69e-164

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


:

Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 453.95  E-value: 4.69e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   3 AVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYFLHQSNVTFDMREHK 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  83 MEVLENHSEPWKVTLIDTGEETMIGGRIKRILPYLGQDEAFCVTYGDGVSDINITESIAFHRREGRLATVTATQPPGRFG 162
Cdd:cd02524    81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 163 AINYVG-TRVTGFQEKPRGDGGWINGGFFVLSPKIGNYVEGDATIWEREPMINLAKDGQMSVFFHDGFWHPMDTLRDKRY 241
Cdd:cd02524   161 ELDLDDdGQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240
                         250
                  ....*....|...
gi 1391717868 242 LEDLWLSNKAPWK 254
Cdd:cd02524   241 LEELWNSGKAPWK 253
 
Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-254 4.69e-164

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 453.95  E-value: 4.69e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   3 AVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYFLHQSNVTFDMREHK 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  83 MEVLENHSEPWKVTLIDTGEETMIGGRIKRILPYLGQDEAFCVTYGDGVSDINITESIAFHRREGRLATVTATQPPGRFG 162
Cdd:cd02524    81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 163 AINYVG-TRVTGFQEKPRGDGGWINGGFFVLSPKIGNYVEGDATIWEREPMINLAKDGQMSVFFHDGFWHPMDTLRDKRY 241
Cdd:cd02524   161 ELDLDDdGQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240
                         250
                  ....*....|...
gi 1391717868 242 LEDLWLSNKAPWK 254
Cdd:cd02524   241 LEELWNSGKAPWK 253
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
2-256 4.63e-161

glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme glucose-1-phosphate cytidylyltransferase, also called CDP-glucose pyrophosphorylase, the product of the rfbF gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131672 [Multi-domain]  Cd Length: 254  Bit Score: 446.51  E-value: 4.63e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   2 KAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYFLHQSNVTFDMREH 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  82 KMEVLENHSEPWKVTLIDTGEETMIGGRIKRILPYLGqDEAFCVTYGDGVSDINITESIAFHRREGRLATVTATQPPGRF 161
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYLD-DEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 162 GAINYVGTRVTGFQEKPRGDGGWINGGFFVLSPKIGNYVEGDATIWEREPMINLAKDGQMSVFFHDGFWHPMDTLRDKRY 241
Cdd:TIGR02623 160 GALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNY 239
                         250
                  ....*....|....*
gi 1391717868 242 LEDLWLSNKAPWKKW 256
Cdd:TIGR02623 240 LEELWESGRAPWKVW 254
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-256 1.20e-92

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: 272.80  E-value: 1.20e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   2 KAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNyflhqsnvtfdmreh 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGD--------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  82 kmevleNHSEPWKVTLIDTGEETMIGGRIKRILPYLGqDEAFCVTYGDGVSDINITESIAFHRREGRLATVTAT--QPPG 159
Cdd:COG1208    66 ------GSRFGVRITYVDEGEPLGTGGALKRALPLLG-DEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpvPDPS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 160 RFGAINYVGT-RVTGFQEKPRGD-GGWINGGFFVLSPKIGNYVEGDATIWEREPMINLAKDGQMSVFFHDGFWHPMDTLR 237
Cdd:COG1208   139 RYGVVELDGDgRVTRFVEKPEEPpSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPE 218
                         250
                  ....*....|....*....
gi 1391717868 238 DKRYLEDLWLSNKAPWKKW 256
Cdd:COG1208   219 DLLEANALLLSGKAPVVIW 237
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-235 3.85e-14

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: 69.59  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   2 KAVLLAGGLGTRFAEETDIRPKPMIEIGGK-PILWHIMKIYSSHGINDFI-ICLGYKGYVIKEYFSnyflhqsnvtfdmR 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIvILTQEHRFMLNELLG-------------D 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  80 EHKMEVlenhsepwKVTLIDTGEETMIGGRIKRILPYLGQDEAFC-VTYGDGVSDINITESIAFHRREGRLATVT----A 154
Cdd:pfam00483  68 GSKFGV--------QITYALQPEGKGTAPAVALAADFLGDEKSDVlVLGGDHIYRMDLEQAVKFHIEKAADATVTfgivP 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 155 TQPPGRFGAINYVGT-RVTGFQEKPRGD--GGWINGGFFVLSPKIGNYVEGDAT-IWEREPMIN-----LAKDGQMSVFF 225
Cdd:pfam00483 140 VEPPTGYGVVEFDDNgRVIRFVEKPKLPkaSNYASMGIYIFNSGVLDFLAKYLEeLKRGEDEITdilpkALEDGKLAYAF 219
                         250
                  ....*....|
gi 1391717868 226 HDGFWHPMDT 235
Cdd:pfam00483 220 IFKGYAWLDV 229
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-82 5.38e-06

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 46.91  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   4 VLLAGGLGTRFAEETdirPKPMIEIGGKPILWHIMKiySSHGINDFI-ICLGYKGYVIKEYFSNYFlhqSNVTFDMREHK 82
Cdd:PRK14359    6 IILAAGKGTRMKSSL---PKVLHTICGKPMLFYILK--EAFAISDDVhVVLHHQKERIKEAVLEYF---PGVIFHTQDLE 77
 
Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-254 4.69e-164

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 453.95  E-value: 4.69e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   3 AVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYFLHQSNVTFDMREHK 82
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  83 MEVLENHSEPWKVTLIDTGEETMIGGRIKRILPYLGQDEAFCVTYGDGVSDINITESIAFHRREGRLATVTATQPPGRFG 162
Cdd:cd02524    81 IELHNSDIEDWKVTLVDTGLNTMTGGRLKRVRRYLGDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPPGRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 163 AINYVG-TRVTGFQEKPRGDGGWINGGFFVLSPKIGNYVEGDATIWEREPMINLAKDGQMSVFFHDGFWHPMDTLRDKRY 241
Cdd:cd02524   161 ELDLDDdGQVTSFTEKPQGDGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWQCMDTLRDKQT 240
                         250
                  ....*....|...
gi 1391717868 242 LEDLWLSNKAPWK 254
Cdd:cd02524   241 LEELWNSGKAPWK 253
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
2-256 4.63e-161

glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme glucose-1-phosphate cytidylyltransferase, also called CDP-glucose pyrophosphorylase, the product of the rfbF gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131672 [Multi-domain]  Cd Length: 254  Bit Score: 446.51  E-value: 4.63e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   2 KAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYFLHQSNVTFDMREH 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  82 KMEVLENHSEPWKVTLIDTGEETMIGGRIKRILPYLGqDEAFCVTYGDGVSDINITESIAFHRREGRLATVTATQPPGRF 161
Cdd:TIGR02623  81 TMEVHHKRVEPWRVTLVDTGESTQTGGRLKRVREYLD-DEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQPPGRF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 162 GAINYVGTRVTGFQEKPRGDGGWINGGFFVLSPKIGNYVEGDATIWEREPMINLAKDGQMSVFFHDGFWHPMDTLRDKRY 241
Cdd:TIGR02623 160 GALDLEGEQVTSFQEKPLGDGGWINGGFFVLNPSVLDLIDGDATVWEQEPLETLAQRGELSAYEHSGFWQPMDTLRDKNY 239
                         250
                  ....*....|....*
gi 1391717868 242 LEDLWLSNKAPWKKW 256
Cdd:TIGR02623 240 LEELWESGRAPWKVW 254
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-256 1.20e-92

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: 272.80  E-value: 1.20e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   2 KAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNyflhqsnvtfdmreh 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGD--------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  82 kmevleNHSEPWKVTLIDTGEETMIGGRIKRILPYLGqDEAFCVTYGDGVSDINITESIAFHRREGRLATVTAT--QPPG 159
Cdd:COG1208    66 ------GSRFGVRITYVDEGEPLGTGGALKRALPLLG-DEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpvPDPS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 160 RFGAINYVGT-RVTGFQEKPRGD-GGWINGGFFVLSPKIGNYVEGDATIWEREPMINLAKDGQMSVFFHDGFWHPMDTLR 237
Cdd:COG1208   139 RYGVVELDGDgRVTRFVEKPEEPpSNLINAGIYVLEPEIFDYIPEGEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPE 218
                         250
                  ....*....|....*....
gi 1391717868 238 DKRYLEDLWLSNKAPWKKW 256
Cdd:COG1208   219 DLLEANALLLSGKAPVVIW 237
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-234 1.32e-48

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: 159.67  E-value: 1.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   3 AVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYFLHQSNVTFdmrehk 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEY------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  83 mevlenhsepwkvtlIDTGEETMIGGRIKRILPYLGqDEAFCVTYGDGVSDINITESIAFHRREGRLATVTATQP--PGR 160
Cdd:cd04181    75 ---------------VVQEEPLGTAGAVRNAEDFLG-DDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVedPSR 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 161 FGAI--NYVGtRVTGFQEKPR-GDGGWINGGFFVLSPKIGNYVEGDAT---IWEREPMINLAKDGQMSVFFHDGFWHPMD 234
Cdd:cd04181   139 YGVVelDDDG-RVTRFVEKPTlPESNLANAGIYIFEPEILDYIPEILPrgeDELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
3-228 5.16e-40

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: 137.68  E-value: 5.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   3 AVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFsnyflhQSNVTFDMREHK 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYF------GDGYRGGIRIYY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  83 MEvlenhsEPwkvTLIDTgeetmiGGRIKRILPYLGQDEAFcVTYGDGVSDINITESIAFHRREGRLATVTATQPPG--R 160
Cdd:cd06915    75 VI------EP---EPLGT------GGAIKNALPKLPEDQFL-VLNGDTYFDVDLLALLAALRASGADATMALRRVPDasR 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 161 FGAINYV-GTRVTGFQEKPRGDG-GWINGGFFVLSPKIGNYVEGDATIWEREPMINLAKDGQMSVFFHDG 228
Cdd:cd06915   139 YGNVTVDgDGRVIAFVEKGPGAApGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDG 208
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-230 3.42e-30

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: 112.22  E-value: 3.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   3 AVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYFLHQSNVTFDMREHK 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  83 MevlenhsepwkvtlidtGeetmIGGRIKrILPYlGQDEAFCVTYGDGVSDINITESIAFHRREGRLATVTA----TQPP 158
Cdd:cd06426    81 L-----------------G----TAGALS-LLPE-KPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVreyeVQVP 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391717868 159 grFGAINYVGTRVTGFQEKPRGDgGWINGGFFVLSPKIGNYVEGDATIWEREPMINLAKDGQ-MSVFFHDGFW 230
Cdd:cd06426   138 --YGVVETEGGRITSIEEKPTHS-FLVNAGIYVLEPEVLDLIPKNEFFDMPDLIEKLIKEGKkVGVFPIHEYW 207
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-243 9.23e-25

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: 98.44  E-value: 9.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   1 MKAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYflhqsnvtfdmrE 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEY------------E 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  81 HKMEVlenhsepwKVTLIDTGEETMIGGRIKRILPYLGQD-EAFCVTYGDGVSDINITESIAFHRREGRLAT--VTATQP 157
Cdd:cd06425    69 KKLGI--------KITFSIETEPLGTAGPLALARDLLGDDdEPFFVLNSDVICDFPLAELLDFHKKHGAEGTilVTKVED 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 158 PGRFGAINY--VGTRVTGFQEKPRG-DGGWINGGFFVLSPKIGNYVEGDATIWEREPMINLAKDGQMSVFFHDGFWhpMD 234
Cdd:cd06425   141 PSKYGVVVHdeNTGRIERFVEKPKVfVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFW--MD 218

                  ....*....
gi 1391717868 235 TLRDKRYLE 243
Cdd:cd06425   219 IGQPKDFLK 227
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-76 8.05e-21

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 87.99  E-value: 8.05e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391717868   2 KAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYFLhqsNVTF 76
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGP---DVTF 72
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-238 1.90e-20

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: 86.47  E-value: 1.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   2 KAVLLAGGLGTRFAEETDIRPKPMIEIGGKP-ILWHIMKIYSShGINDFIICLGYKGYVIKEYFSNYFlHQSNVTFDMre 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPlIDHALDRLAAA-GIRRIVVNTHHLADQIEAHLGDSR-FGLRITISD-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  81 hkmevlenhsEPwkVTLIDTGeetmiGGrIKRILPYLGqDEAFCVTYGDGVSDINITESIAFH--RREGRLATVTATQPP 158
Cdd:cd06422    77 ----------EP--DELLETG-----GG-IKKALPLLG-DEPFLVVNGDILWDGDLAPLLLLHawRMDALLLLLPLVRNP 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 159 GRFGAINYV---GTRVTGfqEKPRGDGGWINGGFFVLSPKIGNYVEGDA----TIWERepminLAKDGQMSVFFHDGFWH 231
Cdd:cd06422   138 GHNGVGDFSldaDGRLRR--GGGGAVAPFTFTGIQILSPELFAGIPPGKfslnPLWDR-----AIAAGRLFGLVYDGLWF 210

                  ....*..
gi 1391717868 232 PMDTLRD 238
Cdd:cd06422   211 DVGTPER 217
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
3-76 4.97e-20

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: 85.36  E-value: 4.97e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391717868   3 AVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYFlhqsNVTF 76
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYP----NIKF 70
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-179 1.41e-18

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: 81.85  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   1 MKAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSnyflhqSNVTFDMRe 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALG------DGSRFGVR- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  81 hkmevlenhsepwkVTLIDTGEETMIGGRIKRILPYLGqDEAFCVTYGDGVSDINITESIAFHRREGRLAT--VTATQPP 158
Cdd:cd04189    74 --------------ITYILQEEPLGLAHAVLAARDFLG-DEPFVVYLGDNLIQEGISPLVRDFLEEDADASilLAEVEDP 138
                         170       180
                  ....*....|....*....|.
gi 1391717868 159 GRFGAINYVGTRVTGFQEKPR 179
Cdd:cd04189   139 RRFGVAVVDDGRIVRLVEKPK 159
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-235 3.85e-14

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: 69.59  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   2 KAVLLAGGLGTRFAEETDIRPKPMIEIGGK-PILWHIMKIYSSHGINDFI-ICLGYKGYVIKEYFSnyflhqsnvtfdmR 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIvILTQEHRFMLNELLG-------------D 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  80 EHKMEVlenhsepwKVTLIDTGEETMIGGRIKRILPYLGQDEAFC-VTYGDGVSDINITESIAFHRREGRLATVT----A 154
Cdd:pfam00483  68 GSKFGV--------QITYALQPEGKGTAPAVALAADFLGDEKSDVlVLGGDHIYRMDLEQAVKFHIEKAADATVTfgivP 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 155 TQPPGRFGAINYVGT-RVTGFQEKPRGD--GGWINGGFFVLSPKIGNYVEGDAT-IWEREPMIN-----LAKDGQMSVFF 225
Cdd:pfam00483 140 VEPPTGYGVVEFDDNgRVIRFVEKPKLPkaSNYASMGIYIFNSGVLDFLAKYLEeLKRGEDEITdilpkALEDGKLAYAF 219
                         250
                  ....*....|
gi 1391717868 226 HDGFWHPMDT 235
Cdd:pfam00483 220 IFKGYAWLDV 229
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-179 3.96e-14

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: 70.89  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   2 KAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYK-GYVIKEYFSNyflhqsNVTFDMre 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVtGEEIKEIVGE------GERFGA-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  81 hkmevlenhsepwKVTLIDTGEETMIGGRIKRILPYLGQDEaFCVTYGDGVSDINITESIAFHRREGRLATV--TATQPP 158
Cdd:TIGR01208  73 -------------KITYIVQGEPLGLAHAVYTARDFLGDDD-FVVYLGDNLIQDGISRFVKSFEEKDYDALIllTKVRDP 138
                         170       180
                  ....*....|....*....|..
gi 1391717868 159 GRFG-AINYVGTRVTGFQEKPR 179
Cdd:TIGR01208 139 TAFGvAVLEDGKRILKLVEKPK 160
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-154 1.23e-10

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: 59.59  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   1 MKAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGIND-FIICLGYKGYVIKEYFSNYFLHqsnvtfdmr 79
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDvIVVVPEEEQAEISTYLRSFPLN--------- 71
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391717868  80 eHKMEVLEnhsepwKVTLIDTGEETmiGGRIKRILPYLGQDeaFCVTYGDGVSDINITESIAFHRREGrlATVTA 154
Cdd:cd04198    72 -LKQKLDE------VTIVLDEDMGT--ADSLRHIRKKIKKD--FLVLSCDLITDLPLIELVDLHRSHD--ASLTV 133
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-156 2.17e-10

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: 58.80  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   1 MKAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGIND-FIICLGYKGYVIKEYFSNYFLHQSnvtfdmr 79
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEvFVVCCEHSQAIIEHLLKSKWSSLS------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  80 eHKMevlenhsepwKVTLIDTGEETMIGG--RIKRILPYLGQDeaFCVTYGDGVSDINITESIAFHRREGRL--ATVTAT 155
Cdd:cd02507    74 -SKM----------IVDVITSDLCESAGDalRLRDIRGLIRSD--FLLLSCDLVSNIPLSELLEERRKKDKNaiATLTVL 140

                  .
gi 1391717868 156 Q 156
Cdd:cd02507   141 L 141
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-230 3.07e-09

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: 56.11  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   3 AVLLAGG--LGTRFAEETDIRPKPMIEIGGKPILWHIM----KIYSSHGIndFIIclgykGYVIKEYFSNYflhqsnvtf 76
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIeacaKVPDLKEV--LLI-----GFYPESVFSDF--------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  77 dmrehkmevLENHSEPWKVTLIDTGEETMIG--GRI----KRILpyLGQDEAFCVTYGDGVSDINITESIAFHRREGRLA 150
Cdd:cd06428    65 ---------ISDAQQEFNVPIRYLQEYKPLGtaGGLyhfrDQIL--AGNPSAFFVLNADVCCDFPLQELLEFHKKHGASG 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868 151 TVTATQPPgRFGAINYvGT--------RVTGFQEKPrgdGGW----INGGFFVLSPKI---------------------G 197
Cdd:cd06428   134 TILGTEAS-REQASNY-GCivedpstgEVLHYVEKP---ETFvsdlINCGVYLFSPEIfdtikkafqsrqqeaqlgddnN 208
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1391717868 198 NYVEGDATIWEREPMINLAKDGQMSVFFHDGFW 230
Cdd:cd06428   209 REGRAEVIRLEQDVLTPLAGSGKLYVYKTDDFW 241
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-201 5.70e-09

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: 55.23  E-value: 5.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   1 MKAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYF-SNYFLhqsnVTFDMR 79
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFdRSYEL----EETLEK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868  80 EHKMEVLE---NHSEPWKVTLIDTGEETMIGGRIKRILPYLGqDEAFCVTYGDgvsDI------NITESIAFHRREGrlA 150
Cdd:cd02541    77 KGKTDLLEevrIISDLANIHYVRQKEPLGLGHAVLCAKPFIG-DEPFAVLLGD---DLidskepCLKQLIEAYEKTG--A 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391717868 151 TVTATQ--PP---GRFGAINYVGT-----RVTGFQEKPRGDGGWIN---GGFFVLSPKIGNYVE 201
Cdd:cd02541   151 SVIAVEevPPedvSKYGIVKGEKIdgdvfKVKGLVEKPKPEEAPSNlaiVGRYVLTPDIFDILE 214
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
3-51 1.11e-07

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: 50.99  E-value: 1.11e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1391717868   3 AVLLAGGLGTRFAEEtdiRPKPMIEIGGKPILWHIMKIYSSHGINDFII 51
Cdd:cd02516     3 AIILAAGSGSRMGAD---IPKQFLELGGKPVLEHTLEAFLAHPAIDEIV 48
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-64 1.60e-07

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 51.24  E-value: 1.60e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391717868   1 MKAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLG-YKGYVIKEYF 64
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLL 65
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-67 1.02e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 47.85  E-value: 1.02e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391717868   3 AVLLAGGLGTRFAeetdiRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNY 67
Cdd:COG2068     6 AIILAAGASSRMG-----RPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGL 65
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-72 3.38e-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: 46.86  E-value: 3.38e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   4 VLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFI-ICLgykgyviKEYFSNYFLHQS 72
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIfICR-------DEHNTKFHLDES 64
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
4-82 5.38e-06

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 46.91  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   4 VLLAGGLGTRFAEETdirPKPMIEIGGKPILWHIMKiySSHGINDFI-ICLGYKGYVIKEYFSNYFlhqSNVTFDMREHK 82
Cdd:PRK14359    6 IILAAGKGTRMKSSL---PKVLHTICGKPMLFYILK--EAFAISDDVhVVLHHQKERIKEAVLEYF---PGVIFHTQDLE 77
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-56 6.83e-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: 44.88  E-value: 6.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1391717868   3 AVLLAGGLGTRFAeetdiRPKPMIEIGGKPILWHIMKIYSSHGiNDFIICLGYK 56
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDE 48
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
1-38 6.99e-06

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 45.56  E-value: 6.99e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1391717868   1 MKAVLLAGGLGTRFAEEtdirPKPMIEIGGKPILWHIM 38
Cdd:PRK00317    4 ITGVILAGGRSRRMGGV----DKGLQELNGKPLIQHVI 37
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-71 9.44e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 45.51  E-value: 9.44e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391717868   3 AVLLAGGLGTRFAEEtdiRPKPMIEIGGKPILWHIMKIYSSHG-INDFIICL--GYKGYVIKEYFSNYFLHQ 71
Cdd:PRK00155    6 AIIPAAGKGSRMGAD---RPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVppDDRPDFAELLLAKDPKVT 74
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-67 1.41e-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: 44.47  E-value: 1.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391717868   3 AVLLAGGLGTRFAeetdiRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNY 67
Cdd:cd04182     3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGL 62
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-51 1.47e-05

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: 44.74  E-value: 1.47e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1391717868   4 VLLAGGLGTRFAEEtdiRPKPMIEIGGKPILWHIMKIYSSHGINDFII 51
Cdd:COG1211     1 IIPAAGSGSRMGAG---IPKQFLPLGGKPVLEHTLEAFLAHPRIDEIV 45
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
1-52 5.13e-05

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: 42.56  E-value: 5.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1391717868   1 MKAVLLAGGLGTRFAeetdiRPKPMIEIGGKPILWHIMKIYSSHGINDFIIC 52
Cdd:cd02503     1 ITGVILAGGKSRRMG-----GDKALLELGGKPLLEHVLERLKPLVDEVVISA 47
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
3-70 6.36e-05

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: 42.89  E-value: 6.36e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391717868   3 AVLLAGGLGTRFAEEtdiRPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNYFLH 70
Cdd:cd02540     1 AVILAAGKGTRMKSD---LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVE 65
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
1-67 1.09e-04

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 43.09  E-value: 1.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391717868   1 MKAVLLAGGLGTRFAEETdirPKPMIEIGGKPILWHIMKIYSSHGINDFIICLGYKGYVIKEYFSNY 67
Cdd:COG1207     3 LAVVILAAGKGTRMKSKL---PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADL 66
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-37 1.63e-04

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: 41.33  E-value: 1.63e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1391717868   1 MKAVLLAGGLGTRFAeetdiRPKPMIEIGGKPILWHI 37
Cdd:COG0746     5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERV 36
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-145 9.30e-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: 39.51  E-value: 9.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391717868   3 AVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGIND-FIICLGYKGYvIKEYFSNyflhqsnvtFDMREH 81
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEvFVFCCSHSDQ-IKEYIEK---------SKWSKP 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391717868  82 KmevlenhSEPWKVTLIdTGEETMIGGRIKRILPYLG---QDeaFCVTYGDGVSDINITESIAFHRR 145
Cdd:cd04197    73 K-------SSLMIVIII-MSEDCRSLGDALRDLDAKGlirGD--FILVSGDVVSNIDLKEILEEHKE 129
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
6-37 1.10e-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: 38.72  E-value: 1.10e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1391717868   6 LAGGLGTRFaeetDIRPKPMIEIGGKPILWHI 37
Cdd:COG2266     1 MAGGKGTRL----GGGEKPLLEICGKPMIDRV 28
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
3-31 1.36e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 39.44  E-value: 1.36e-03
                          10        20
                  ....*....|....*....|....*....
gi 1391717868   3 AVLLAGGLGTRFAEETDIRPKPMIEIGGK 31
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKPAVYFGGK 46
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
3-39 2.67e-03

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 38.58  E-value: 2.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1391717868   3 AVLLAGGLGTRFAEetdiRPKPMIEIGGKPILWHIMK 39
Cdd:PRK14489    8 GVILAGGLSRRMNG----RDKALILLGGKPLIERVVD 40
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-51 5.86e-03

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: 37.17  E-value: 5.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1391717868   1 MKAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMKIYSSHGINDFII 51
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILI 51
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-64 8.24e-03

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 36.93  E-value: 8.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391717868   2 KAVLLAGGLGTRFAEETDIRPKPMIEIGGKPILWHIMK-IYSShGINDFIICLGYKGYVIKEYF 64
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEeAVAA-GIEEIIFVTGRGKRAIEDHF 67
 
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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