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Conserved domains on  [gi|1109516612|ref|NP_001334544|]
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ethanolamine-phosphate cytidylyltransferase isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00308 super family cl31425
ethanolamine-phosphate cytidylyltransferase; Provisional
15-372 4.64e-170

ethanolamine-phosphate cytidylyltransferase; Provisional


The actual alignment was detected with superfamily member PTZ00308:

Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 478.90  E-value: 4.64e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  15 KGPGDqriVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAP 94
Cdd:PTZ00308    7 KKPGT---IRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  95 YVTTLETLDKHNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSEy 170
Cdd:PTZ00308   84 YTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 171 reyadsfgkcpggQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLH 250
Cdd:PTZ00308  163 -------------LFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVH 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 251 FDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKT-EIVPDRDGSDPYQEPKRRG 329
Cdd:PTZ00308  228 EDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMG 307
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1109516612 330 IFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKELAFLE 372
Cdd:PTZ00308  308 IFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
15-372 4.64e-170

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 478.90  E-value: 4.64e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  15 KGPGDqriVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAP 94
Cdd:PTZ00308    7 KKPGT---IRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  95 YVTTLETLDKHNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSEy 170
Cdd:PTZ00308   84 YTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 171 reyadsfgkcpggQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLH 250
Cdd:PTZ00308  163 -------------LFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVH 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 251 FDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKT-EIVPDRDGSDPYQEPKRRG 329
Cdd:PTZ00308  228 EDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMG 307
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1109516612 330 IFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKELAFLE 372
Cdd:PTZ00308  308 IFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
21-163 2.57e-95

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: 280.99  E-value: 2.57e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  21 RIVRVWCDGCYDMVHYGHSNQLRQARAMG--DYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTT 98
Cdd:cd02174     1 RPVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109516612  99 LETLDKHNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSS 163
Cdd:cd02174    81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRR 145
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
23-150 2.74e-48

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 223688 [Multi-domain]  Cd Length: 140  Bit Score: 160.14  E-value: 2.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  23 VRVWCDGCYDMVHYGHSNQLRQARAMGDYLIV-GVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLET 101
Cdd:COG0615     2 KRVWADGTFDILHPGHIEFLRQAKKLGDELIVvVARDETVIKRKKRKPIMPEEQRAEVLESLRYVDEVILGAPWDIKFED 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1109516612 102 LDKHNCDFCVHGNDItlTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLV 150
Cdd:COG0615    82 IEEYKPDIVVLGDDQ--KFDEDDLKYELVKRGLFVEVKRTEGVSTCELI 128
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
26-152 4.29e-35

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: 125.51  E-value: 4.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  26 WCDGCYDMVHYGHSNQLRQARAMGDY-LIVGVHTDEEiAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDK 104
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1109516612 105 HNCDFCVHGNDITLTV--DGRDTYEEVKQAGRYR-----ECKRTQGVSTTDLVGR 152
Cdd:pfam01467  80 LNPDVLVIGADSLLDFwyELDEILGNVKLVVVVRpvffiPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
24-89 3.68e-24

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: 94.30  E-value: 3.68e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109516612  24 RVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEV 89
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
 
Name Accession Description Interval E-value
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
15-372 4.64e-170

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 478.90  E-value: 4.64e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  15 KGPGDqriVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAP 94
Cdd:PTZ00308    7 KKPGT---IRVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGPPVMHQEERYEALRACKWVDEVVEGYP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  95 YVTTLETLDKHNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHH----SSQEMSSEy 170
Cdd:PTZ00308   84 YTTRLEDLERLECDFVVHGDDISVDLNGRNSYQEIIDAGKFKVVKRTEGISTTDLVGRMLLCTKSHLlksvDEVQLESS- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 171 reyadsfgkcpggQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLH 250
Cdd:PTZ00308  163 -------------LFPYTPTSHCLTTSRKIVQFSNNRSPKPGDRIVYVDGSFDLFHIGHIRVLQKARELGD--YLIVGVH 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 251 FDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGKT-EIVPDRDGSDPYQEPKRRG 329
Cdd:PTZ00308  228 EDQVVNEQKGSNYPIMNLNERVLGVLSCRYVDEVVIGAPFDVTKEVIDSLHINVVVGGKFsDLVNEEGGSDPYEVPKAMG 307
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1109516612 330 IFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKELAFLE 372
Cdd:PTZ00308  308 IFKEVDSGCDLTTDSIVDRVVKNRLAFLKRQAKKRAKEIKSQE 350
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
14-367 7.03e-126

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 369.01  E-value: 7.03e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  14 LKGPGDQRIVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAA 93
Cdd:PLN02406   45 FKKKKKKKPVRVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  94 PYVTTLETL----DKHNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAH--HSSQEMS 167
Cdd:PLN02406  125 PYAITEEFMnklfNEYNIDYIIHGDDPCLLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERsiSDSHNHS 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 168 SEYREYADSFGKCPG-GQSPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVI 246
Cdd:PLN02406  205 SLQRQFSHGHSQFEDgGSGSGTRVSHFLPTSRRIVQFSNGKGPGPDARIVYIDGAFDLFHAGHVEILRLARALGD--FLL 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 247 AGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAELLNHFKVDLVCHGK-TEIVPDRDG-SDPYQE 324
Cdd:PLN02406  283 VGIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFNISLVVHGTvAENNDFLKGeDDPYAV 362
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1109516612 325 PKRRGIFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKEAKE 367
Cdd:PLN02406  363 PKSMGIFQVLESPLDITTSTIIRRIVANHEAYQKRNEKKAESE 405
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
21-163 2.57e-95

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: 280.99  E-value: 2.57e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  21 RIVRVWCDGCYDMVHYGHSNQLRQARAMG--DYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTT 98
Cdd:cd02174     1 RPVRVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGPPVMTEEERYEAVRHCKWVDEVVEGAPYVTT 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109516612  99 LETLDKHNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSS 163
Cdd:cd02174    81 PEFLDKYKCDYVAHGDDIYLDADGEDCYQEVKDAGRFKEVKRTEGVSTTDLIGRILLDYRDYHRR 145
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
212-364 1.47e-94

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: 279.14  E-value: 1.47e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 212 GETVIYVAGAFDLFHIGHVDFLQEVHKLakRPYVIAGLHFDQEVNRYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYS 291
Cdd:cd02173     1 GDKVVYVDGAFDLFHIGHIEFLEKAREL--GDYLIVGVHDDQTVNEYKGSNYPIMNLHERVLSVLACRYVDEVVIGAPYV 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109516612 292 VTAELLNHFKVDLVCHGKTEIVPD-RDGSDPYQEPKRRGIFYQIDSGSDLTTDLIVQRIIKNRLEYEARNQKKE 364
Cdd:cd02173    79 ITKELIEHFKIDVVVHGKTEETPDsLDGEDPYAVPKEMGIFKEIDSGSDLTTRDIVNRIIKNRLAYEARNKKKE 152
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
24-156 9.95e-53

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: 171.71  E-value: 9.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  24 RVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLD 103
Cdd:cd02170     3 RVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKPLEE 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1109516612 104 KHNcDFCVHGNDITLTVDGRDTYEEVKQAGRYREC--KRTQGVSTTDLVGRMLLV 156
Cdd:cd02170    83 LKP-DVIVLGDDQKNGVDEEEVYEELKKRGKVIEVprKKTEGISSSDIIKRILEL 136
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
23-150 2.74e-48

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 223688 [Multi-domain]  Cd Length: 140  Bit Score: 160.14  E-value: 2.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  23 VRVWCDGCYDMVHYGHSNQLRQARAMGDYLIV-GVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLET 101
Cdd:COG0615     2 KRVWADGTFDILHPGHIEFLRQAKKLGDELIVvVARDETVIKRKKRKPIMPEEQRAEVLESLRYVDEVILGAPWDIKFED 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1109516612 102 LDKHNCDFCVHGNDItlTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLV 150
Cdd:COG0615    82 IEEYKPDIVVLGDDQ--KFDEDDLKYELVKRGLFVEVKRTEGVSTCELI 128
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
8-154 4.22e-41

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 146.63  E-value: 4.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612   8 AASAAGLKGPGDQRIVRVWCDGCYDMVHYGHSNQLRQARAM--GDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKW 85
Cdd:PLN02413   13 SSGSATPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKW 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109516612  86 VDEVVPAAPYVTTLETLDKHNCDFCVHgnDITLTVD----GRDTYEEVKQAGRYRECKRTQGVSTTDLVGRML 154
Cdd:PLN02413   93 VDEVIPDAPWVITQEFLDKHRIDYVAH--DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIV 163
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
216-352 1.44e-35

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: 127.30  E-value: 1.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 216 IYVAGAFDLFHIGHVDFLQEVHKLAKRPYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYSVTAE 295
Cdd:cd02174     5 VYVDGCFDLFHYGHANALRQAKKLGPNDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 296 LLNHFKVDLVCHGKtEIVPDRDGSDPYQEPKRRGIFYQI---DSGSdlTTDlIVQRIIKN 352
Cdd:cd02174    83 FLDKYKCDYVAHGD-DIYLDADGEDCYQEVKDAGRFKEVkrtEGVS--TTD-LIGRILLD 138
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
26-152 4.29e-35

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: 125.51  E-value: 4.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  26 WCDGCYDMVHYGHSNQLRQARAMGDY-LIVGVHTDEEiAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDK 104
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEP-PHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1109516612 105 HNCDFCVHGNDITLTV--DGRDTYEEVKQAGRYR-----ECKRTQGVSTTDLVGR 152
Cdd:pfam01467  80 LNPDVLVIGADSLLDFwyELDEILGNVKLVVVVRpvffiPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
24-89 3.68e-24

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: 94.30  E-value: 3.68e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109516612  24 RVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEV 89
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
213-351 3.99e-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: 93.51  E-value: 3.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 213 ETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEVVIGAPYSV 292
Cdd:cd02170     1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGD--YLIVGVARDETVAKIKRR--PILPEEQRAEVVEALKYVDEVILGHPWSY 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109516612 293 TaELLNHFKVDLVCHGKTEIVPDrDGSDPYQEPKRRGIFYQIDSGSD--LTTDLIVQRIIK 351
Cdd:cd02170    77 F-KPLEELKPDVIVLGDDQKNGV-DEEEVYEELKKRGKVIEVPRKKTegISSSDIIKRILE 135
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
216-354 2.03e-21

Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 223688 [Multi-domain]  Cd Length: 140  Bit Score: 89.27  E-value: 2.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 216 IYVAGAFDLFHIGHVDFLQEVHKLAKRpYVIAGLHfDQEVNRYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYSVTAE 295
Cdd:COG0615     4 VWADGTFDILHPGHIEFLRQAKKLGDE-LIVVVAR-DETVIKRKKRK-PIMPEEQRAEVLESLRYVDEVILGAPWDIKFE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109516612 296 LLNHFKVDLVCHGkteivPDRDGSDPY--QEPKRRGIFYQIDSGSDL-TTDLIVQRIIKNRL 354
Cdd:COG0615    81 DIEEYKPDIVVLG-----DDQKFDEDDlkYELVKRGLFVEVKRTEGVsTCELISTSDIIKRI 137
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
204-360 2.71e-21

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 92.70  E-value: 2.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 204 ASGKEPQPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKRPYVIAGLHFDQEVNRYKGKNypIMNLHERTLSVLACRYVSE 283
Cdd:PLN02413   18 TPSSSPSDRPVRVYADGIYDLFHFGHARSLEQAKKLFPNTYLLVGCCNDELTHKYKGKT--VMTEDERYESLRHCKWVDE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 284 VVIGAPYSVTAELLNHFKVDLVCHgktEIVPDRD----GSDPYQEPKRRGIFYQIDSGSDLTTDLIVQRIIKNRLEYEAR 359
Cdd:PLN02413   96 VIPDAPWVITQEFLDKHRIDYVAH---DALPYADasgaGKDVYEFVKKIGKFKETKRTDGISTSDIIMRIVKDYNQYVMR 172

                  .
gi 1109516612 360 N 360
Cdd:PLN02413  173 N 173
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
29-149 1.14e-18

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: 81.38  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  29 GCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKHNCD 108
Cdd:cd02171     8 GTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIEDIKKYNVD 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1109516612 109 FCVHGNDITLTVDGRDTYEEVKqagrYREckRTQGVSTTDL 149
Cdd:cd02171    88 VFVMGDDWEGKFDFLKEYCEVV----YLP--RTKGISSTQL 122
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
25-115 2.85e-15

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: 72.06  E-value: 2.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  25 VWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVpAAPYVTTLETLDK 104
Cdd:cd02172     7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVNKGPGRPIFPEDLRAEVLAALGFVDYVV-LFDNPTALEIIDA 85
                          90
                  ....*....|.
gi 1109516612 105 HNCDFCVHGND 115
Cdd:cd02172    86 LQPNIYVKGGD 96
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
215-284 2.14e-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: 67.33  E-value: 2.14e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 215 VIYVAGAFDLFHIGHVDFLQEVHKLAkrPYVIAGLHFDQEVNRYKGKnyPIMNLHERTLSVLACRYVSEV 284
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELF--DELIVGVGSDQFVNPLKGE--PVFSLEERLEMLKALKYVDEV 66
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
25-153 4.21e-14

ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225425 [Multi-domain]  Cd Length: 467  Bit Score: 73.48  E-value: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612  25 VWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGP--PVFTQEERYKMVQAIKWVDEVVPAAPYvTTLETL 102
Cdd:COG2870   335 VFTNGCFDILHAGHVTYLAQARALGDRLIVGVNSDASVKRLKGEsrPINSEEDRAAVLAALESVDLVVIFDED-TPEELI 413
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1109516612 103 DKHNCDFCVHGNDITL-TVDGRdtyEEVKQA-GRYRECKRTQGVSTTDLVGRM 153
Cdd:COG2870   414 EAVKPDILVKGGDYKIeKIVGA---DIVEAYgGEVLLIPFEEGKSTTKIIEKI 463
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
217-308 4.78e-12

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: 62.72  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 217 YVAGAFDLFHIGHVDFLQEVHKLAKRPyVIAGLHFDQEVNRYKgknYPIMNLHERTLSVLACRYVSEVVIGAPYSVTAEL 296
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDED-LIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTREL 76
                          90
                  ....*....|..
gi 1109516612 297 LNHFKVDLVCHG 308
Cdd:pfam01467  77 LKELNPDVLVIG 88
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
210-317 5.94e-12

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: 62.82  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 210 QPGETVIYVAGAFDLFHIGHVDFLQEVHKLAKRpyVIAGLHFDQEVNryKGKNYPIMNLHERTLSVLACRYVSEVVIgAP 289
Cdd:cd02172     1 QRGKTVVLCHGVFDLLHPGHVRHLQAARSLGDI--LVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVL-FD 75
                          90       100
                  ....*....|....*....|....*...
gi 1109516612 290 YSVTAELLNHFKVDLVCHGKTEIVPDRD 317
Cdd:cd02172    76 NPTALEIIDALQPNIYVKGGDYENPEND 103
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
25-91 2.43e-11

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: 64.85  E-value: 2.43e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109516612  25 VWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGP--PVFTQEERYKMVQAIKWVDEVVP 91
Cdd:PRK11316  343 VMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEgrPVNPLEQRMAVLAALEAVDWVVP 411
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
212-277 3.69e-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: 3.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109516612 212 GETVIYVAGAFDLFHIGHVDFLQEVHKLAKRpyVIAGLHFDQEVNRYKGKNYPIMNLhERTLSVLA 277
Cdd:PRK11316  339 GEKIVMTNGCFDILHAGHVSYLANARKLGDR--LIVAVNSDASVKRLKGEGRPVNPL-EQRMAVLA 401
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
215-286 8.49e-07

ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 225425 [Multi-domain]  Cd Length: 467  Bit Score: 50.76  E-value: 8.49e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109516612 215 VIYVAGAFDLFHIGHVDFLQEVHKLAKRpyVIAGLHFDQEVNRYKGKNYPIMNLHER--TLSVLACryVSEVVI 286
Cdd:COG2870   334 VVFTNGCFDILHAGHVTYLAQARALGDR--LIVGVNSDASVKRLKGESRPINSEEDRaaVLAALES--VDLVVI 403
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
213-309 9.40e-07

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: 47.48  E-value: 9.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516612 213 ETVIYVAGAFDLFHIGHVDFLQEVHKLAKrpYVIAGLHFDqEVNRYKGKNyPIMNLHERTLSVLACRYVSEVVIGAPYSV 292
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGD--KLIVAVSTD-EFNAGKGKK-AVIPYEQRAEILESIRYVDLVIPETNWEQ 76
                          90
                  ....*....|....*..
gi 1109516612 293 TAELLNHFKVDLVCHGK 309
Cdd:cd02171    77 KIEDIKKYNVDVFVMGD 93
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
29-95 1.13e-04

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 42.13  E-value: 1.13e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109516612  29 GCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVqaIKWVDEVVPAAPY 95
Cdd:PRK00777    8 GTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNL--KKFLKAVEYDREY 72
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
29-81 5.63e-03

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 38.26  E-value: 5.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1109516612  29 GCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVfTQEERYKMVQ 81
Cdd:PRK01170    7 GTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVRKNKVYPI-PYEDRKRKLE 58
PRK07143 PRK07143
hypothetical protein; Provisional
199-271 7.85e-03

hypothetical protein; Provisional


Pssm-ID: 235946 [Multi-domain]  Cd Length: 279  Bit Score: 37.67  E-value: 7.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109516612 199 KIIQFAsgKEPQPGETVIYVAGAFDLFHIGHvdflQEVHKLAKRP-YVIAGLHFDQEVNRYKGKNYPIMNLHER 271
Cdd:PRK07143    3 KVYTFP--LKNFKFEKPTFVLGGFESFHLGH----LELFKKAKESnDEIVIVIFKNPENLPKNTNKKFSDLNSR 70
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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