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Conserved domains on  [gi|2524717045|ref|WP_286738624|]
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Gfo/Idh/MocA family oxidoreductase [Bacteroides sp. 44_46]

Protein Classification

Gfo/Idh/MocA family oxidoreductase; nucleotidyl transferase family protein( domain architecture ID 11617401)

Gfo/Idh/MocA family oxidoreductase belonging to the NAD(P)(+)-binding Rossmann-fold superfamily catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant| nucleotidyl transferase (NT) family protein contains a conserved dinucleotide-binding domain; the NT superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and cytidylyltransferases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-126 5.61e-53

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


:

Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 173.75  E-value: 5.61e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   2 KRVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLDRGKLNVrNNVMERIENVRKTGLADEIIIEEYLGqKIDD 81
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPI-IPEEQRKEIVEALKYVDEVILGEEWD-KFED 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2524717045  82 IQRYNVDIFAIGSDWEGHFDYLKEY-------CEVVYLERTEGISSTQLRNE 126
Cdd:COG0615    79 IEEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKR 130
MviM COG0673
Predicted dehydrogenase [General function prediction only];
127-369 2.49e-39

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 143.14  E-value: 2.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 127 DIVRLGIIGTGRIANRFFPEVQHVNGVRVTAVYNPaNPTEADAFADTYSIPVSTvEPEEFLNS--VDAVYVASPHLTHYS 204
Cdd:COG0673     2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADR-DPERAEAFAEEYGVRVYT-DYEELLADpdIDAVVIATPNHLHAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 205 YVKWLLENDKHVLCETPLTLVSTEAVSLIELARERYLTLMEANKTAHFPAFNHLISLIKSGLIGTIVDIDASLSTLRQEG 284
Cdd:COG0673    80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 285 LRE--MDPSQAGGSVTEN-----ISFVLLpifkFLGTGYKDLMFFSSF----RGGVDIYTKGILQYSS-AVASFKIGL-- 350
Cdd:COG0673   160 PADwrFDPELAGGGALLDlgihdIDLARW----LLGSEPESVSATGGRlvpdRVEVDDTAAATLRFANgAVATLEASWva 235

                         250       260
                  ....*....|....*....|
gi 2524717045 351 -GVKTEGNLVISGTRGYAYV 369
Cdd:COG0673   236 pGGERDERLEVYGTKGTLFV 255
 
Name Accession Description Interval E-value
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-126 5.61e-53

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 173.75  E-value: 5.61e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   2 KRVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLDRGKLNVrNNVMERIENVRKTGLADEIIIEEYLGqKIDD 81
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPI-IPEEQRKEIVEALKYVDEVILGEEWD-KFED 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2524717045  82 IQRYNVDIFAIGSDWEGHFDYLKEY-------CEVVYLERTEGISSTQLRNE 126
Cdd:COG0615    79 IEEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKR 130
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-126 1.81e-51

glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.


Pssm-ID: 173922 [Multi-domain]  Cd Length: 129  Bit Score: 169.97  E-value: 1.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   1 MKRVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLDRGKLNVRNnVMERIENVRKTGLADEIIIEEYLGQKID 80
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIP-YEQRAEILESIRYVDLVIPETNWEQKIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2524717045  81 DIQRYNVDIFAIGSDWEGHFDYLKEYCEVVYLERTEGISSTQLRNE 126
Cdd:cd02171    80 DIKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEM 125
MviM COG0673
Predicted dehydrogenase [General function prediction only];
127-369 2.49e-39

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 143.14  E-value: 2.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 127 DIVRLGIIGTGRIANRFFPEVQHVNGVRVTAVYNPaNPTEADAFADTYSIPVSTvEPEEFLNS--VDAVYVASPHLTHYS 204
Cdd:COG0673     2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADR-DPERAEAFAEEYGVRVYT-DYEELLADpdIDAVVIATPNHLHAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 205 YVKWLLENDKHVLCETPLTLVSTEAVSLIELARERYLTLMEANKTAHFPAFNHLISLIKSGLIGTIVDIDASLSTLRQEG 284
Cdd:COG0673    80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 285 LRE--MDPSQAGGSVTEN-----ISFVLLpifkFLGTGYKDLMFFSSF----RGGVDIYTKGILQYSS-AVASFKIGL-- 350
Cdd:COG0673   160 PADwrFDPELAGGGALLDlgihdIDLARW----LLGSEPESVSATGGRlvpdRVEVDDTAAATLRFANgAVATLEASWva 235

                         250       260
                  ....*....|....*....|
gi 2524717045 351 -GVKTEGNLVISGTRGYAYV 369
Cdd:COG0673   236 pGGERDERLEVYGTKGTLFV 255
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 129-246 5.35e-23

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 93.43  E-value: 5.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 129 VRLGIIGTGRIANRFFPEVQ-HVNGVRVTAVYNPaNPTEADAFADTYSIPVSTvEPEEFLNS--VDAVYVASPHLTHYSY 205
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNaSQPGAELVAILDP-NSERAEAVAESFGVEVYS-DLEELLNDpeIDAVIVATPNGLHYDL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2524717045 206 VKWLLENDKHVLCETPLTLVSTEAVSLIELARERYLTLMEA 246
Cdd:pfam01408  79 AIAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVG 119
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-124 1.28e-19

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 84.68  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   5 ITYGTYDLLHQGHINLLRRAKALGDY-LIVGVTTDNFDlDRGKLNVrNNVMERIENVRKTGLADEIIIEEYLGQKIDDIQ 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPP-HKLKRPL-FSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2524717045  84 RYNVDIFAIGSDW----EGHFDYLKEYCEVV---------YLERTEGISSTQLR 124
Cdd:pfam01467  79 ELNPDVLVIGADSlldfWYELDEILGNVKLVvvvrpvffiPLKPTNGISSTDIR 132
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 3-61 3.41e-14

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 66.95  E-value: 3.41e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717045   3 RVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLDRGKLNVrNNVMERIENVR 61
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPV-FSLEERLEMLK 58
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 3-123 3.06e-13

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 70.58  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   3 RVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNfDLDRGKLNVRNNVMERIENVRKTGLADEIIIEEYLGQKIDDI 82
Cdd:PTZ00308   13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDE-EIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2524717045  83 QRYNVDIFAIGSDWEGHFDYLKEYCEVV------YLERTEGISSTQL 123
Cdd:PTZ00308   92 ERLECDFVVHGDDISVDLNGRNSYQEIIdagkfkVVKRTEGISTTDL 138
PRK10206 PRK10206
putative oxidoreductase; Provisional
 134-281 3.68e-08

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 54.83  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 134 IGTGRIANRF-FPEVQH-VNGVRVTAVYN-PANPTEAdafADTYSIPVSTVEPEEFLN--SVDAVYVASPHLTHYSYVKW 208
Cdd:PRK10206    7 IGFGKSTTRYhLPYVLNrKDSWHVAHIFRrHAKPEEQ---APIYSHIHFTSDLDEVLNdpDVKLVVVCTHADSHFEYAKR 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717045 209 LLENDKHVLCETPLTLVSTEAVSLIELARERYLTLMEANKTAHFPAFNHLISLIKSGLIGTIVDIDASLSTLR 281
Cdd:PRK10206   84 ALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKKAIESGKLGEIVEVESHFDYYR 156
 
Name Accession Description Interval E-value
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 2-126 5.61e-53

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis]; Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440380 [Multi-domain]  Cd Length: 131  Bit Score: 173.75  E-value: 5.61e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   2 KRVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLDRGKLNVrNNVMERIENVRKTGLADEIIIEEYLGqKIDD 81
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPI-IPEEQRKEIVEALKYVDEVILGEEWD-KFED 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2524717045  82 IQRYNVDIFAIGSDWEGHFDYLKEY-------CEVVYLERTEGISSTQLRNE 126
Cdd:COG0615    79 IEEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKR 130
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-126 1.81e-51

glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase,(CDP-glycerol pyrophosphorylase). Glycerol-3-phosphate cytidyltransferase acts in pathways of teichoic acid biosynthesis. Teichoic acids are substituted polymers, linked by phosphodiester bonds, of glycerol, ribitol, etc. An example is poly(glycerol phosphate), the major teichoic acid of the Bacillus subtilis cell wall. Most, but not all, species encoding proteins in this family are Gram-positive bacteria. A closely related protein assigned a different function experimentally is a human ethanolamine-phosphate cytidylyltransferase.


Pssm-ID: 173922 [Multi-domain]  Cd Length: 129  Bit Score: 169.97  E-value: 1.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   1 MKRVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLDRGKLNVRNnVMERIENVRKTGLADEIIIEEYLGQKID 80
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIP-YEQRAEILESIRYVDLVIPETNWEQKIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2524717045  81 DIQRYNVDIFAIGSDWEGHFDYLKEYCEVVYLERTEGISSTQLRNE 126
Cdd:cd02171    80 DIKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEM 125
MviM COG0673
Predicted dehydrogenase [General function prediction only];
127-369 2.49e-39

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 143.14  E-value: 2.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 127 DIVRLGIIGTGRIANRFFPEVQHVNGVRVTAVYNPaNPTEADAFADTYSIPVSTvEPEEFLNS--VDAVYVASPHLTHYS 204
Cdd:COG0673     2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADR-DPERAEAFAEEYGVRVYT-DYEELLADpdIDAVVIATPNHLHAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 205 YVKWLLENDKHVLCETPLTLVSTEAVSLIELARERYLTLMEANKTAHFPAFNHLISLIKSGLIGTIVDIDASLSTLRQEG 284
Cdd:COG0673    80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 285 LRE--MDPSQAGGSVTEN-----ISFVLLpifkFLGTGYKDLMFFSSF----RGGVDIYTKGILQYSS-AVASFKIGL-- 350
Cdd:COG0673   160 PADwrFDPELAGGGALLDlgihdIDLARW----LLGSEPESVSATGGRlvpdRVEVDDTAAATLRFANgAVATLEASWva 235

                         250       260
                  ....*....|....*....|
gi 2524717045 351 -GVKTEGNLVISGTRGYAYV 369
Cdd:COG0673   236 pGGERDERLEVYGTKGTLFV 255
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 1-126 1.84e-23

cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.


Pssm-ID: 173921 [Multi-domain]  Cd Length: 136  Bit Score: 95.44  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   1 MKRVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLDRGKLNVrNNVMERIENVRKTGLADEIIIEEYLGQKID 80
Cdd:cd02170     1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPI-LPEEQRAEVVEALKYVDEVILGHPWSYFKP 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2524717045  81 DIQRYNvDIFAIGSDWEGH------FDYLKEYCEVVYLER--TEGISSTQLRNE 126
Cdd:cd02170    80 LEELKP-DVIVLGDDQKNGvdeeevYEELKKRGKVIEVPRkkTEGISSSDIIKR 132
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 129-246 5.35e-23

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 93.43  E-value: 5.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 129 VRLGIIGTGRIANRFFPEVQ-HVNGVRVTAVYNPaNPTEADAFADTYSIPVSTvEPEEFLNS--VDAVYVASPHLTHYSY 205
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNaSQPGAELVAILDP-NSERAEAVAESFGVEVYS-DLEELLNDpeIDAVIVATPNGLHYDL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2524717045 206 VKWLLENDKHVLCETPLTLVSTEAVSLIELARERYLTLMEA 246
Cdd:pfam01408  79 AIAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVG 119
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-124 1.28e-19

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 84.68  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   5 ITYGTYDLLHQGHINLLRRAKALGDY-LIVGVTTDNFDlDRGKLNVrNNVMERIENVRKTGLADEIIIEEYLGQKIDDIQ 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPP-HKLKRPL-FSAEERLEMLELAKWVDEVIVVAPWELTRELLK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2524717045  84 RYNVDIFAIGSDW----EGHFDYLKEYCEVV---------YLERTEGISSTQLR 124
Cdd:pfam01467  79 ELNPDVLVIGADSlldfWYELDEILGNVKLVvvvrpvffiPLKPTNGISSTDIR 132
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 3-61 3.41e-14

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 66.95  E-value: 3.41e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717045   3 RVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLDRGKLNVrNNVMERIENVR 61
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPV-FSLEERLEMLK 58
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 3-123 3.06e-13

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 70.58  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   3 RVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNfDLDRGKLNVRNNVMERIENVRKTGLADEIIIEEYLGQKIDDI 82
Cdd:PTZ00308   13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDE-EIMRNKGPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2524717045  83 QRYNVDIFAIGSDWEGHFDYLKEYCEVV------YLERTEGISSTQL 123
Cdd:PTZ00308   92 ERLECDFVVHGDDISVDLNGRNSYQEIIdagkfkVVKRTEGISTTDL 138
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 3-123 1.50e-11

CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) catalyzes the condensation of CTP and phosphocholine to form CDP-choline as the rate-limiting and regulatory step in the CDP-choline pathway. CCT is unique in that its enzymatic activity is regulated by the extent of its association with membrane structures. A current model posts that the elastic stress of the bilayer curvature is sensed by CCT and this governs the degree of membrane association, thus providing a mechanism for both positive and negative regulation of activity.


Pssm-ID: 173925  Cd Length: 150  Bit Score: 62.20  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   3 RVITYGTYDLLHQGHINLLRRAKALG--DYLIVGVTTDnFDLDRGKLNVRNNVMERIENVRKTGLADEIII-------EE 73
Cdd:cd02174     4 RVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSD-EEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEgapyvttPE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717045  74 YLGQ-KIDdiqrYNV--DIFAIGSDWEGHFDYLKE---YCEVvylERTEGISSTQL 123
Cdd:cd02174    83 FLDKyKCD----YVAhgDDIYLDADGEDCYQEVKDagrFKEV---KRTEGVSTTDL 131
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
1-103 2.75e-11

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 61.39  E-value: 2.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   1 MKRVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLDRGKLNVRnNVMERIENVRKTgLADEIIIEEYLGQKID 80
Cdd:PRK00777    1 MMKVAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVR-PYEVRLKNLKKF-LKAVEYDREYEIVKID 78

                          90       100
                  ....*....|....*....|...
gi 2524717045  81 DiqrynvdifAIGSDWEGHFDYL 103
Cdd:PRK00777   79 D---------PYGPALEDDFDAI 92
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 4-121 3.25e-11

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


Pssm-ID: 173912 [Multi-domain]  Cd Length: 105  Bit Score: 59.86  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   4 VITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLDRGKLNvrnnvmERIENVRktgladeiIIEEylgqkiddiq 83
Cdd:cd02156     2 ARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPPVKVWQDPH------ELEERKE--------SIEE---------- 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2524717045  84 rynvDIFAIGSDWEGHFDY---------LKEYCEVVYLER----TEGISST 121
Cdd:cd02156    58 ----DISVCGEDFQQNRELyrwvkdnitLPVDPEQVELPRlnleTTVMSKR 104
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 3-129 4.29e-10

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 61.24  E-value: 4.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   3 RVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNfDLDRGKLNVRNNVMERIENVRKTGLADEI-------IIEEYL 75
Cdd:PLN02406   55 RVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDE-EIIANKGPPVTPMHERMIMVSGVKWVDEVipdapyaITEEFM 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717045  76 GQKIDdiqRYNVD---------IFAIGSDWEGHFDYLKEYCEVvylERTEGISSTqlrneDIV 129
Cdd:PLN02406  134 NKLFN---EYNIDyiihgddpcLLPDGTDAYALAKKAGRYKQI---KRTEGVSST-----DIV 185
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 5-95 7.48e-10

CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine cytidylyltransferase (ECT) catalyzes the conversion of phosphoethanolamine to CDP-ethanolamine as part of the CDP-ethanolamine biosynthesis pathway. ECT expression in hepatocytes is localized predominantly to areas of the cytoplasm that are rich in rough endoplasmic reticulum. Several ECTs, including yeast and human ECT, have large repetitive sequences located within their N- and C-termini.


Pssm-ID: 173924  Cd Length: 152  Bit Score: 57.27  E-value: 7.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   5 ITY--GTYDLLHQGHINLLRRAKALGDYLIVGVTTDN-FDLDRGKLNVRNNVMERIENVRKTGLADEIIIEEYLGQKIDD 81
Cdd:cd02173     4 VVYvdGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQtVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYVITKEL 83

                          90
                  ....*....|....
gi 2524717045  82 IQRYNVDIFAIGSD 95
Cdd:cd02173    84 IEHFKIDVVVHGKT 97
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 4-99 1.91e-09

N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .


Pssm-ID: 173923 [Multi-domain]  Cd Length: 144  Bit Score: 55.89  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   4 VITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFdLDRGKLNVRNNVMERIENVRKTGLADEIIIEEYlGQKIDDIQ 83
Cdd:cd02172     7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRY-VNKGPGRPIFPEDLRAEVLAALGFVDYVVLFDN-PTALEIID 84

                          90
                  ....*....|....*.
gi 2524717045  84 RYNVDIFAIGSDWEGH 99
Cdd:cd02172    85 ALQPNIYVKGGDYENP 100
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 3-125 3.26e-09

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 55.14  E-value: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   3 RVITYGTYDLLHQGHINLLRRAKALG-DYLIVGVTTDNFDLDRGKLNVRNNvmERIENVRKTGLA-DEIIIEEYLGQKID 80
Cdd:cd02039     1 VGIIIGRFEPFHLGHLKLIKEALEEAlDEVIIIIVSNPPKKKRNKDPFSLH--ERVEMLKEILKDrLKVVPVDFPEVKIL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2524717045  81 DIQR--------YNVDIFAIGSDWEGHFDY--------LKEYCEVVYLERTEG---ISSTQLRN 125
Cdd:cd02039    79 LAVVfilkillkVGPDKVVVGEDFAFGKNAsynkdlkeLFLDIEIVEVPRVRDgkkISSTLIRE 142
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 8-152 8.44e-09

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 57.38  E-value: 8.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   8 GTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFDLD-RGKLNVRNNVMERIENVRKTGLADEIIIEEYLGQKIDDIQRYN 86
Cdd:PLN02406  258 GAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAhRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFN 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045  87 VDIFAIGSDWEGHfDYLKEYCEVVYLERTEGISSTQLRNEDIVRLGIIgTGRIAN----------------RFFPEVQHV 150
Cdd:PLN02406  338 ISLVVHGTVAENN-DFLKGEDDPYAVPKSMGIFQVLESPLDITTSTII-RRIVANheayqkrnekkaesekRYYESKSFV 415


                  ..
gi 2524717045 151 NG 152
Cdd:PLN02406  416 SG 417
PRK10206 PRK10206
putative oxidoreductase; Provisional
 134-281 3.68e-08

putative oxidoreductase; Provisional


Pssm-ID: 182305 [Multi-domain]  Cd Length: 344  Bit Score: 54.83  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 134 IGTGRIANRF-FPEVQH-VNGVRVTAVYN-PANPTEAdafADTYSIPVSTVEPEEFLN--SVDAVYVASPHLTHYSYVKW 208
Cdd:PRK10206    7 IGFGKSTTRYhLPYVLNrKDSWHVAHIFRrHAKPEEQ---APIYSHIHFTSDLDEVLNdpDVKLVVVCTHADSHFEYAKR 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2524717045 209 LLENDKHVLCETPLTLVSTEAVSLIELARERYLTLMEANKTAHFPAFNHLISLIKSGLIGTIVDIDASLSTLR 281
Cdd:PRK10206   84 ALEAGKNVLVEKPFTPTLAEAKELFALAKSKGLTVTPYQNRRFDSCFLTAKKAIESGKLGEIVEVESHFDYYR 156
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 4-71 1.31e-07

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 53.25  E-value: 1.31e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717045   4 VITY--GTYDLLHQGHINLLRRAKALGDYLIVGVTTDN-FDLDRGKLNVRNNVMERIENVRKTGLADEIII 71
Cdd:PTZ00308  193 RIVYvdGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQvVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVI 263
PRK11579 PRK11579
putative oxidoreductase; Provisional
 127-271 2.95e-07

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 52.03  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045 127 DIVRLGIIGTGRIANRFF-PEVQHVNGVRVTAVynpanpTEADA---FADTYSIPVSTvEPEEFLN--SVDAVYVASPHL 200
Cdd:PRK11579    3 DKIRVGLIGYGYASKTFHaPLIAGTPGLELAAV------SSSDAtkvKADWPTVTVVS-EPQHLFNdpNIDLIVIPTPND 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2524717045 201 THYSYVKWLLENDKHVLCETPLTLVSTEAVSLIELARERYLTLMEANKTAHFPAFNHLISLIKSGLIGTIV 271
Cdd:PRK11579   76 THFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFLTLKALLAEGVLGEVA 146
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 2-39 5.02e-07

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 51.75  E-value: 5.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2524717045   2 KRVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDN 39
Cdd:PRK11316  341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDA 378
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
2-81 6.25e-06

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 47.89  E-value: 6.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   2 KRVITYGTYDLLHQGHINLLRRAKALGDYLIVGVTTDNFdldrgklnVRNNVMERIE-NVRKTGLADEII--IEEYLGQK 78
Cdd:PRK01170    1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEY--------VRKNKVYPIPyEDRKRKLENFIKkfTNKFRIRP 72


                  ...
gi 2524717045  79 IDD 81
Cdd:PRK01170   73 IDD 75
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 3-123 4.34e-05

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 45.32  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   3 RVITYGTYDLLHQGHINLLRRAKAL--GDYLIVGVTTDNF-DLDRGKlnvrnNVM---ERIENVRKTGLADEII------ 70
Cdd:PLN02413   29 RVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELtHKYKGK-----TVMtedERYESLRHCKWVDEVIpdapwv 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2524717045  71 -IEEYLGQ-KID----DIQRYnVDIFAIGSDWeghFDYLKEYCEVVYLERTEGISSTQL 123
Cdd:PLN02413  104 iTQEFLDKhRIDyvahDALPY-ADASGAGKDV---YEFVKKIGKFKETKRTDGISTSDI 158
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 8-82 5.05e-04

phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; The PPAT domain of the bifunctional enzyme with PPAT and DPCK functions. The final two steps of the CoA biosynthesis pathway are catalyzed by phosphopantetheine adenylyltransferase (PPAT) and dephospho-CoA (dPCoA) kinase (DPCK). The PPAT reaction involves the reversible adenylation of 4'-phosphopantetheine to form 3'-dPCoA and PPi, and DPCK catalyses phosphorylation of the 3'-hydroxy group of the ribose moiety of dPCoA. In eukaryotes the two enzymes are part of a large multienzyme complex . Studies in Corynebacterium ammoniagenes suggested that separate enzymes were present, and this was confirmed through identification of the bacterial PPAT/CoAD.


Pssm-ID: 173915  Cd Length: 143  Bit Score: 40.34  E-value: 5.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717045   8 GTYDLLHQGHINLLRRAKALG-DYLIVGVTTDNFDLDRGKLNVRNNVMERIENVRKTgLADEIIIEEYLGQKIDDI 82
Cdd:cd02164     6 GTFDRLHDGHKILLSVAFLLAgEKLIIGVTSDELLKNKSLKELIEPYEERIANLHEF-LVDLKPTLKYEIVPIDDP 80
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
1-125 9.55e-04

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 41.09  E-value: 9.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524717045   1 MKRVITYGTYDLLHQGHINLLRRA-KALG-DYLIVGVTTDNFDLDRGKLNVRNNVMERIENVRKtgLADEIIIEEY-LGQ 77
Cdd:PRK07152    1 MKIAIFGGSFDPIHKGHINIAKKAiKKLKlDKLFFVPTYINPFKKKQKASNGEHRLNMLKLALK--NLPKMEVSDFeIKR 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2524717045  78 K-----IDDI----QRY-NVDI-FAIGSD-------WEgHFDYLKEYCEVVYLERTEGISSTQLRN 125
Cdd:PRK07152   79 QnvsytIDTIkyfkKKYpNDEIyFIIGSDnlekfkkWK-NIEEILKKVQIVVFKRKKNINKKNLKK 143
 
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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