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Conserved domains on  [gi|446074129|ref|WP_000151984|]
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MULTISPECIES: hydroxymethylglutaryl-CoA synthase [Staphylococcus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HMG-CoA-S_prok super family cl33300
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 3-384 2.04e-170

3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of hydroxymethylglutaryl-CoA (HMG-CoA) synthases is found in a limited spectrum of mostly gram-positive bacteria which make isopentenyl pyrophosphate (IPP) via the mevalonate pathway. This pathway is found primarily in eukaryotes and archaea, but the bacterial homologs are distinct, having aparrently diverged after being laterally transferred from an early eukaryote. HMG-CoA synthase is the first step in the pathway and joins acetyl-CoA with acetoacetyl-CoA with the release of one molecule of CoA. The Borellia sequence may have resulted from a separate lateral transfer event.


The actual alignment was detected with superfamily member TIGR01835:

Pssm-ID: 213655 [Multi-domain]  Cd Length: 379  Bit Score: 480.78  E-value: 2.04e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDIITDEDKKKIGMVIVATESAV 82
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQKIDMVIFGTESGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   83 DAAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYLATRPNEKVLVIATDTARYGLNSGGEPTQGAGAVAMVI 162
Cdd:TIGR01835  81 DQSKAAAVYVHGLLGLQPFCRSFELKQACYGATAALQMAKGHVALSPDRKVLVIASDIAKYGLESPGEPTQGAGAVAMLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  163 AHNPSILALNEDAVAYTEDVYDFWRPTGHKYPLVDGALSKDAYIRSFQQSWNEYAKRQGKSLADFASLCFHVPFTKMGKK 242
Cdd:TIGR01835 161 SADPKLLAINEDSVLYTDDIMDFWRPNYSTTALVDGQYSNEQYLNAFENAWNDYAKRTGLSLADFAAFCFHVPFTKMGLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  243 ALESIIDNADETTQERLRSGYEDAVDYNRYVGNIYTGSLYLSLISLLEN-RDLQAGETIGLFSYGSGSVGEFYSATLVEG 321
Cdd:TIGR01835 241 ALRHILKKNYEDEDESVQNAYLESIIYNREVGNLYTGSLYLGLASLLENaFEDTTGDKIGLFSYGSGAVAEFFSGTLVAG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446074129  322 YKDHLDQAAHKTLLNNRTEVSVDAYETFFKRFDDVDfdeqQDAVHEDRHIFYLSNIENNVREY 384
Cdd:TIGR01835 321 YRDHLKKERHLALLKNRTNLSYAEYEALFEETLPTD----GDQPGEDRGFFRLAGINDHKRIY 379
 
Name Accession Description Interval E-value
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 3-384 2.04e-170

3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of hydroxymethylglutaryl-CoA (HMG-CoA) synthases is found in a limited spectrum of mostly gram-positive bacteria which make isopentenyl pyrophosphate (IPP) via the mevalonate pathway. This pathway is found primarily in eukaryotes and archaea, but the bacterial homologs are distinct, having aparrently diverged after being laterally transferred from an early eukaryote. HMG-CoA synthase is the first step in the pathway and joins acetyl-CoA with acetoacetyl-CoA with the release of one molecule of CoA. The Borellia sequence may have resulted from a separate lateral transfer event.


Pssm-ID: 213655 [Multi-domain]  Cd Length: 379  Bit Score: 480.78  E-value: 2.04e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDIITDEDKKKIGMVIVATESAV 82
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQKIDMVIFGTESGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   83 DAAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYLATRPNEKVLVIATDTARYGLNSGGEPTQGAGAVAMVI 162
Cdd:TIGR01835  81 DQSKAAAVYVHGLLGLQPFCRSFELKQACYGATAALQMAKGHVALSPDRKVLVIASDIAKYGLESPGEPTQGAGAVAMLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  163 AHNPSILALNEDAVAYTEDVYDFWRPTGHKYPLVDGALSKDAYIRSFQQSWNEYAKRQGKSLADFASLCFHVPFTKMGKK 242
Cdd:TIGR01835 161 SADPKLLAINEDSVLYTDDIMDFWRPNYSTTALVDGQYSNEQYLNAFENAWNDYAKRTGLSLADFAAFCFHVPFTKMGLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  243 ALESIIDNADETTQERLRSGYEDAVDYNRYVGNIYTGSLYLSLISLLEN-RDLQAGETIGLFSYGSGSVGEFYSATLVEG 321
Cdd:TIGR01835 241 ALRHILKKNYEDEDESVQNAYLESIIYNREVGNLYTGSLYLGLASLLENaFEDTTGDKIGLFSYGSGAVAEFFSGTLVAG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446074129  322 YKDHLDQAAHKTLLNNRTEVSVDAYETFFKRFDDVDfdeqQDAVHEDRHIFYLSNIENNVREY 384
Cdd:TIGR01835 321 YRDHLKKERHLALLKNRTNLSYAEYEALFEETLPTD----GDQPGEDRGFFRLAGINDHKRIY 379
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 1-384 1.68e-167

3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 442651 [Multi-domain]  Cd Length: 382  Bit Score: 473.51  E-value: 1.68e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   1 MTIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDIITDE--DKKKIGMVIVAT 78
Cdd:COG3425    1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAgiDPSDIGAVYVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  79 ESAVDAAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYLATRPNEKVLVIATDTARYGLNSGGEPTQGAGAV 158
Cdd:COG3425   81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 159 AMVIAHNPSILALNEDAVAYTEDVYDFWRPTGHKYPLVDGALSKDAYIRSFQQSWNEYAKRQGKSLADFASLCFHVPFTK 238
Cdd:COG3425  161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 239 MGKKALESIIDNADETTQERLRSGYEDAVDYNRYVGNIYTGSLYLSLISLLENRDLQAGETIGLFSYGSGSVGEFYSATL 318
Cdd:COG3425  241 MPKKAAKKLGRKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTV 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446074129 319 VEGYKDHLDQAAHKTLLNNRTEVSVDAYETFFKRFDDVDFDEqqdavHEDRHIFYLSNIENNVREY 384
Cdd:COG3425  321 TPGIEERLRRPGVEEQLANRRYLSYAEYEKLRGKILPEDAED-----VTLPGEFVLTGIKDHERIY 381
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 2-316 2.97e-73

"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.


Pssm-ID: 238423 [Multi-domain]  Cd Length: 324  Bit Score: 231.17  E-value: 2.97e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   2 TIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSpvNQDIVSMGANAAKDII--TDEDKKKIGMVIVATE 79
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGD--DEDVPTMAVEAARRALerAGIDPDDIGLLIVATE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  80 SAVDAAKAAAVQIHNLLGIQpFARCFEMKEACYAATPAIQLAKDYLATRPNEKVLVIATDTARYGL--NSGGEPTQGAGA 157
Cdd:cd00827   79 SPIDKGKSAATYLAELLGLT-NAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLdeGSALEPTLGDGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 158 VAMVIAHNPSILALNEDAVAYTED---------VYDFWRPTGHKYPLVDGALSKDAYIRSFQQSWNEYAKRQGKSLADFA 228
Cdd:cd00827  158 AAMLVSRNPGILAAGIVSTHSTSDpgydfspypVMDGGYPKPCKLAYAIRLTAEPAGRAVFEAAHKLIAKVVRKALDRAG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 229 S---LCFHVPFTKMGKKALESIIDNADETTqERLRSGYEDavdYNRYVGNIYTGSLYLSLISLLENRDLQAGETIGLFSY 305
Cdd:cd00827  238 LsedIDYFVPHQPNGKKILEAVAKKLGGPP-EKASQTRWI---LLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSY 313

                        330
                 ....*....|.
gi 446074129 306 GSGSVGEFYSA 316
Cdd:cd00827  314 GSGFTAEAFVL 324
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
 3-385 9.30e-33

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 127.94  E-value: 9.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDIIT--DEDKKKIGMVIVATES 80
Cdd:PLN02577   5 VGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEkyNIDPKQIGRLEVGSET 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  81 avdaAKAAAVQIHNLLgIQPFARC-------FEMKEACYAATPAIQLAKDYLATRP--NEKVLVIATDTARYGlNSGGEP 151
Cdd:PLN02577  85 ----VIDKSKSIKTFL-MQLFEESgntdiegVDSTNACYGGTAALLNCVNWVESSSwdGRYGLVVAADSAVYA-EGPARP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 152 TQGAGAVAMVIAHNPSILALNEDAVAYTEDVYDFWRPTG-HKYPLVDGALSKDAYIRS----FQQSWNEYAKRQGK--SL 224
Cdd:PLN02577 159 TGGAGAVAMLVGPNAPIVFESKYRGSHMAHVYDFYKPDLaSEYPVVDGKLSQTCYLMAldscYKRFCEKYEKLEGKqfSI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 225 ADFASLCFHVPFTKMGKKALESIIDN--------ADETTQERLR-----SGYE-------DAV-------DYN------- 270
Cdd:PLN02577 239 SDADYFVFHAPYNKLVQKSFARLVYNdfqrnassVDEDAKEKLApfaglSSDEsyqnrdlEKVsqqvakpLYDakvqptt 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 271 ---RYVGNIYTGSLYLSLISLLEN-RDLQAGETIGLFSYGSGSVGEFYSATLVEGYKDHLDQAAHKTL-----LNNRTEV 341
Cdd:PLN02577 319 lipKQVGNMYTASLYAALASLVHNkHSELAGKRILMFSYGSGLTATMFSLRLHEGQHPFSLSNIAKVMdvsekLKSRHEV 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 446074129 342 S----VDAYETFFKRFDDVDFDEQQDAVHEDRHIFYLSNIENNVREYH 385
Cdd:PLN02577 399 SpekfVETLKLMEHRYGAKDFVPSKDVSLLAPGTYYLTEVDSLYRRFY 446
HMG_CoA_synt_N pfam01154
Hydroxymethylglutaryl-coenzyme A synthase N terminal;
3-165 1.74e-13

Hydroxymethylglutaryl-coenzyme A synthase N terminal;


Pssm-ID: 307348 [Multi-domain]  Cd Length: 173  Bit Score: 68.03  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDII--TDEDKKKIGMVIVATES 80
Cdd:pfam01154   4 VGILALEIYFPAQYVDQTELEKFDGVEAGKYTIGLGQTRMGFCSDREDINSLCLTVVQKLMerYNLPWDKIGRLEVGTET 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   81 AVDAAKAAAVQIHNLLGIQPFA--RCFEMKEACYAATPAIQLAKDYLATRP--NEKVLVIATDTARYGlNSGGEPTQGAG 156
Cdd:pfam01154  84 IIDKSKSVKSVLMQLFQESGNTdiEGIDTTNACYGGTAALFNAANWIESSSwdGRYALVVCGDIAIYP-SGNARPTGGAG 162


                  ....*....
gi 446074129  157 AVAMVIAHN 165
Cdd:pfam01154 163 AVAMLIGPK 171
 
Name Accession Description Interval E-value
HMG-CoA-S_prok TIGR01835
3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of ...
 3-384 2.04e-170

3-hydroxy-3-methylglutaryl CoA synthase, prokaryotic clade; This clade of hydroxymethylglutaryl-CoA (HMG-CoA) synthases is found in a limited spectrum of mostly gram-positive bacteria which make isopentenyl pyrophosphate (IPP) via the mevalonate pathway. This pathway is found primarily in eukaryotes and archaea, but the bacterial homologs are distinct, having aparrently diverged after being laterally transferred from an early eukaryote. HMG-CoA synthase is the first step in the pathway and joins acetyl-CoA with acetoacetyl-CoA with the release of one molecule of CoA. The Borellia sequence may have resulted from a separate lateral transfer event.


Pssm-ID: 213655 [Multi-domain]  Cd Length: 379  Bit Score: 480.78  E-value: 2.04e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDIITDEDKKKIGMVIVATESAV 82
Cdd:TIGR01835   1 IGIDKISFFTPQNYLDMTALAEARGVDPEKFHIGIGQKKMAVPPIDEDIVTMAASAAKPILDRNDKQKIDMVIFGTESGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   83 DAAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYLATRPNEKVLVIATDTARYGLNSGGEPTQGAGAVAMVI 162
Cdd:TIGR01835  81 DQSKAAAVYVHGLLGLQPFCRSFELKQACYGATAALQMAKGHVALSPDRKVLVIASDIAKYGLESPGEPTQGAGAVAMLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  163 AHNPSILALNEDAVAYTEDVYDFWRPTGHKYPLVDGALSKDAYIRSFQQSWNEYAKRQGKSLADFASLCFHVPFTKMGKK 242
Cdd:TIGR01835 161 SADPKLLAINEDSVLYTDDIMDFWRPNYSTTALVDGQYSNEQYLNAFENAWNDYAKRTGLSLADFAAFCFHVPFTKMGLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  243 ALESIIDNADETTQERLRSGYEDAVDYNRYVGNIYTGSLYLSLISLLEN-RDLQAGETIGLFSYGSGSVGEFYSATLVEG 321
Cdd:TIGR01835 241 ALRHILKKNYEDEDESVQNAYLESIIYNREVGNLYTGSLYLGLASLLENaFEDTTGDKIGLFSYGSGAVAEFFSGTLVAG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446074129  322 YKDHLDQAAHKTLLNNRTEVSVDAYETFFKRFDDVDfdeqQDAVHEDRHIFYLSNIENNVREY 384
Cdd:TIGR01835 321 YRDHLKKERHLALLKNRTNLSYAEYEALFEETLPTD----GDQPGEDRGFFRLAGINDHKRIY 379
PksG COG3425
3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; ...
 1-384 1.68e-167

3-hydroxy-3-methylglutaryl CoA synthase [Lipid transport and metabolism]; 3-hydroxy-3-methylglutaryl CoA synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 442651 [Multi-domain]  Cd Length: 382  Bit Score: 473.51  E-value: 1.68e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   1 MTIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDIITDE--DKKKIGMVIVAT 78
Cdd:COG3425    1 MKVGIDAIGFYIPRYRLDLEELAEARGVDPEKYTKGLGQEEKSVPPPDEDAVTMAANAARRALDRAgiDPSDIGAVYVGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  79 ESAVDAAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYLATRPNEKVLVIATDTARYGLNSGGEPTQGAGAV 158
Cdd:COG3425   81 ESGPDASKPIATYVHGALGLPPNCRAFELKFACYAGTAALQAALGWVASGPNKKALVIASDIARYGPGSAGEYTQGAGAV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 159 AMVIAHNPSILALNEDAVAYTEDVYDFWRPTGHKYPLVDGALSKDAYIRSFQQSWNEYAKRQGKSLADFASLCFHVPFTK 238
Cdd:COG3425  161 AMLVGADPRIAEIEGGSGSYTTDVMDFWRPNGSDYPLVDGRFSEPAYLDHLEEAVKDYKEKTGLKPDDFDYFVFHQPFGK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 239 MGKKALESIIDNADETTQERLRSGYEDAVDYNRYVGNIYTGSLYLSLISLLENRDLQAGETIGLFSYGSGSVGEFYSATL 318
Cdd:COG3425  241 MPKKAAKKLGRKAGREIQEDFEEQVEPSLIYSRRIGNTYTGSLYLGLASLLDNAKDLPGDRIGLFSYGSGAGSEFFSGTV 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446074129 319 VEGYKDHLDQAAHKTLLNNRTEVSVDAYETFFKRFDDVDFDEqqdavHEDRHIFYLSNIENNVREY 384
Cdd:COG3425  321 TPGIEERLRRPGVEEQLANRRYLSYAEYEKLRGKILPEDAED-----VTLPGEFVLTGIKDHERIY 381
init_cond_enzymes cd00827
"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 2-316 2.97e-73

"initiating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type III and polyketide synthases, type III, which include chalcone synthase and related enzymes. They are characterized by the utlization of CoA substrate primers, as well as the nature of their active site residues.


Pssm-ID: 238423 [Multi-domain]  Cd Length: 324  Bit Score: 231.17  E-value: 2.97e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   2 TIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSpvNQDIVSMGANAAKDII--TDEDKKKIGMVIVATE 79
Cdd:cd00827    1 DVGIEAIGAYLPRYRVDNEELAEGLGVDPGKYTTGIGQRHMAGD--DEDVPTMAVEAARRALerAGIDPDDIGLLIVATE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  80 SAVDAAKAAAVQIHNLLGIQpFARCFEMKEACYAATPAIQLAKDYLATRPNEKVLVIATDTARYGL--NSGGEPTQGAGA 157
Cdd:cd00827   79 SPIDKGKSAATYLAELLGLT-NAEAFDLKQACYGGTAALQLAANLVESGPWRYALVVASDIASYLLdeGSALEPTLGDGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 158 VAMVIAHNPSILALNEDAVAYTED---------VYDFWRPTGHKYPLVDGALSKDAYIRSFQQSWNEYAKRQGKSLADFA 228
Cdd:cd00827  158 AAMLVSRNPGILAAGIVSTHSTSDpgydfspypVMDGGYPKPCKLAYAIRLTAEPAGRAVFEAAHKLIAKVVRKALDRAG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 229 S---LCFHVPFTKMGKKALESIIDNADETTqERLRSGYEDavdYNRYVGNIYTGSLYLSLISLLENRDLQAGETIGLFSY 305
Cdd:cd00827  238 LsedIDYFVPHQPNGKKILEAVAKKLGGPP-EKASQTRWI---LLRRVGNMYAASILLGLASLLESGKLKAGDRVLLFSY 313

                        330
                 ....*....|.
gi 446074129 306 GSGSVGEFYSA 316
Cdd:cd00827  314 GSGFTAEAFVL 324
PLN02577 PLN02577
hydroxymethylglutaryl-CoA synthase
 3-385 9.30e-33

hydroxymethylglutaryl-CoA synthase


Pssm-ID: 178189 [Multi-domain]  Cd Length: 459  Bit Score: 127.94  E-value: 9.30e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDIIT--DEDKKKIGMVIVATES 80
Cdd:PLN02577   5 VGILAMEVYFPPTCVQQEALEAHDGVSKGKYTIGLGQDCMAFCTDVEDVISMSLTVVKSLLEkyNIDPKQIGRLEVGSET 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  81 avdaAKAAAVQIHNLLgIQPFARC-------FEMKEACYAATPAIQLAKDYLATRP--NEKVLVIATDTARYGlNSGGEP 151
Cdd:PLN02577  85 ----VIDKSKSIKTFL-MQLFEESgntdiegVDSTNACYGGTAALLNCVNWVESSSwdGRYGLVVAADSAVYA-EGPARP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 152 TQGAGAVAMVIAHNPSILALNEDAVAYTEDVYDFWRPTG-HKYPLVDGALSKDAYIRS----FQQSWNEYAKRQGK--SL 224
Cdd:PLN02577 159 TGGAGAVAMLVGPNAPIVFESKYRGSHMAHVYDFYKPDLaSEYPVVDGKLSQTCYLMAldscYKRFCEKYEKLEGKqfSI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 225 ADFASLCFHVPFTKMGKKALESIIDN--------ADETTQERLR-----SGYE-------DAV-------DYN------- 270
Cdd:PLN02577 239 SDADYFVFHAPYNKLVQKSFARLVYNdfqrnassVDEDAKEKLApfaglSSDEsyqnrdlEKVsqqvakpLYDakvqptt 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 271 ---RYVGNIYTGSLYLSLISLLEN-RDLQAGETIGLFSYGSGSVGEFYSATLVEGYKDHLDQAAHKTL-----LNNRTEV 341
Cdd:PLN02577 319 lipKQVGNMYTASLYAALASLVHNkHSELAGKRILMFSYGSGLTATMFSLRLHEGQHPFSLSNIAKVMdvsekLKSRHEV 398

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 446074129 342 S----VDAYETFFKRFDDVDFDEQQDAVHEDRHIFYLSNIENNVREYH 385
Cdd:PLN02577 399 SpekfVETLKLMEHRYGAKDFVPSKDVSLLAPGTYYLTEVDSLYRRFY 446
HMG-CoA-S_euk TIGR01833
3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA ...
 3-347 3.39e-32

3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic clade; Hydroxymethylglutaryl(HMG)-CoA synthase is the first step of isopentenyl pyrophosphate (IPP) biosynthesis via the mevalonate pathway. This pathway is found mainly in eukaryotes, but also in archaea and some bacteria. This model is specific for eukaryotes.


Pssm-ID: 273826 [Multi-domain]  Cd Length: 457  Bit Score: 126.04  E-value: 3.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDIITDE--DKKKIGMVIVATES 80
Cdd:TIGR01833   5 VGILALEIYFPSQYVDQAELEKYDGVSAGKYTIGLGQTKMGFCTDREDINSLCLTVVSKLMERYniDYDQIGRLEVGTET 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   81 avdaAKAAAVQIHNLLgIQPFARC-------FEMKEACYAATPAIQLAKDYLATRP--NEKVLVIATDTARYGLNSgGEP 151
Cdd:TIGR01833  85 ----IIDKSKSVKTVL-MQLFEESgntdvegIDTTNACYGGTAALFNAINWIESSSwdGRYALVVAGDIAVYAKGN-ARP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  152 TQGAGAVAMVIAHNPSILALNEDAVAYTEDVYDFWRPT-GHKYPLVDGALSKDAYIRSFQQSWNEYAKR---QGK----- 222
Cdd:TIGR01833 159 TGGAGAVAMLIGPNAPIVFERGLRGSHMQHAYDFYKPDlASEYPVVDGKLSIQCYLSALDRCYKSYCKKiekQWGksgsd 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  223 ---SLADFASLCFHVPFTKMGKKALESIIDN----ADETTQERLRSG--------YED------------AVDYNRY--- 272
Cdd:TIGR01833 239 rkfTLDDFDYMIFHSPYCKLVQKSLARLLYNdflrNPSSTDTSLYEGlealsglkLEDtytdrdlekafmKASKELFdkk 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  273 ----------VGNIYTGSLYLSLI---SLLENRDLqAGETIGLFSYGSGSVGEFYSATLVE--GYKDHLDQAAHKTL--- 334
Cdd:TIGR01833 319 tkpsllvptqVGNMYTASLYGCLAsllSSKSAQEL-AGKRVGMFSYGSGLAASMFSLRVSQdaSPGSALDKLIASLSdlk 397

                         410
                  ....*....|....*
gi 446074129  335 --LNNRTEVSVDAYE 347
Cdd:TIGR01833 398 nrLDSRHCVAPEEFE 412
PRK04262 PRK04262
hypothetical protein; Provisional
 1-325 4.97e-24

hypothetical protein; Provisional


Pssm-ID: 235266 [Multi-domain]  Cd Length: 347  Bit Score: 101.52  E-value: 4.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   1 MTIGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDIITDE--DKKKIGMVIVAT 78
Cdd:PRK04262   1 MMVGIVGYGAYIPRYRIKVEEIARVWGDDPEAIKRGLGVEEKSVPGPDEDTATIAVEAARNALKRAgiDPKEIGAVYVGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  79 ESAVDAAKAAAVQIHNLLGIQPFARCFEMKEACYAATPAIQLAKDYLATRPNEKVLVIATDTARyglnsgGEP------T 152
Cdd:PRK04262  81 ESHPYAVKPTATIVAEALGATPDLTAADLEFACKAGTAALQAAMGLVKSGMIKYALAIGADTAQ------GAPgdaleyT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 153 QGAGAVAMVIAHNPSIlALNEDAVAYTEDVYDFWRPTGHKYPLVDGALSKD-AYIRSFQQSWNEYAKRQGKSLADFASLC 231
Cdd:PRK04262 155 AAAGGAAFIIGKEEVI-AEIEATYSYTTDTPDFWRREGEPYPRHGGRFTGEpAYFKHIISAAKGLMEKLGLKPSDYDYAV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 232 FHVP---F-TKMGKKAlesiidnadETTQERLRSGYedavdYNRYVGNIYTGSLYLSLISLLENRdlQAGETIGLFSYGS 307
Cdd:PRK04262 234 FHQPngkFpLRVAKML---------GFTKEQVKPGL-----LTPYIGNTYSGSALLGLAAVLDVA--KPGDRILVVSFGS 297

                        330       340
                 ....*....|....*....|.
gi 446074129 308 GSVGEFYSATL---VEGYKDH 325
Cdd:PRK04262 298 GAGSDAFSITVtdaIEEKRDL 318
HMG_CoA_synt_N pfam01154
Hydroxymethylglutaryl-coenzyme A synthase N terminal;
3-165 1.74e-13

Hydroxymethylglutaryl-coenzyme A synthase N terminal;


Pssm-ID: 307348 [Multi-domain]  Cd Length: 173  Bit Score: 68.03  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129    3 IGIDKINFYVPKYYVDMAKLAEARQVDPNKFLIGIGQTEMAVSPVNQDIVSMGANAAKDII--TDEDKKKIGMVIVATES 80
Cdd:pfam01154   4 VGILALEIYFPAQYVDQTELEKFDGVEAGKYTIGLGQTRMGFCSDREDINSLCLTVVQKLMerYNLPWDKIGRLEVGTET 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   81 AVDAAKAAAVQIHNLLGIQPFA--RCFEMKEACYAATPAIQLAKDYLATRP--NEKVLVIATDTARYGlNSGGEPTQGAG 156
Cdd:pfam01154  84 IIDKSKSVKSVLMQLFQESGNTdiEGIDTTNACYGGTAALFNAANWIESSSwdGRYALVVCGDIAIYP-SGNARPTGGAG 162


                  ....*....
gi 446074129  157 AVAMVIAHN 165
Cdd:pfam01154 163 AVAMLIGPK 171
HMG_CoA_synt_C pfam08540
Hydroxymethylglutaryl-coenzyme A synthase C terminal;
178-382 6.22e-13

Hydroxymethylglutaryl-coenzyme A synthase C terminal;


Pssm-ID: 400722  Cd Length: 280  Bit Score: 68.66  E-value: 6.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  178 YTEDVYDFWRPT-GHKYPLVDGALSKDAYIRSFQQSWNEYAKR---------QGKSLADFASLCFHVPFTKMGKKAL--- 244
Cdd:pfam08540  11 HMEHAYDFYKPDlTSEYPVVDGKLSLSCYLKALDRCYKNYRKKinritkdgdKIFGLNDFDYMIFHSPTCKLVQKSLarl 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  245 --------------ESIIDNADETTQERLRSGYED---------------------AVDYNRYVGNIYTGSLYLSLIS-- 287
Cdd:pfam08540  91 lyndflsnpssdkfNGVDEKLTAFGGLTLDESYTDkdlekafmklskpffkkkvqpSLLVPTNNGNMYTASLYAALASll 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  288 LLENRDLQAGETIGLFSYGSGSVGEFYSATLVEGYKDHLDQAAHKTL-----LNNRTEVSVDAYETFFKRFDD----VDF 358
Cdd:pfam08540 171 SHVSADDLAGKRIGAFSYGSGLAATLFSLRVKQDVSPGSILDIASVLdlgkrLDSRICVTPEEFTEAMELREQahlkKNF 250

                         250       260
                  ....*....|....*....|....
gi 446074129  359 DEQQDAVHEDRHIFYLSNIENNVR 382
Cdd:pfam08540 251 KPQGSIDSLFPGTYYLTNVDDKFR 274
FabH COG0332
3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl- ...
 44-308 2.88e-07

3-oxoacyl-[acyl-carrier-protein] synthase III [Lipid transport and metabolism]; 3-oxoacyl-[acyl-carrier-protein] synthase III is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440101 [Multi-domain]  Cd Length: 323  Bit Score: 51.65  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  44 VSPVNQDIVSMGANAAKDIITDE--DKKKIGMVIVATESAVDAAKAAAVQIHNLLGIQPfARCFEMKEAC----YAatpa 117
Cdd:COG0332   44 IAAPDETTSDLAVEAARKALEAAgiDPEDIDLIIVATVTPDYLFPSTACLVQHKLGAKN-AAAFDINAACsgfvYA---- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 118 IQLAKDYLATRPNEKVLVIATDTARYGLNsggePTQ-------GAGAVAMVIAH---NPSILA--LNEDAvAYTEDVY-- 183
Cdd:COG0332  119 LSVAAALIRSGQAKNVLVVGAETLSRIVD----WTDrstcvlfGDGAGAVVLEAseeGPGILGsvLGSDG-SGADLLVvp 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129 184 -------DFWRPTGHKYPLVDG-ALSKDAyIRSFQQSWNEYAKRQGKSLADFASLCFHvpftkmgkKALESIIdnadETT 255
Cdd:COG0332  194 aggsrnpPSPVDEGDHYLRMDGrEVFKFA-VRNLPEVIREALEKAGLTLDDIDWFIPH--------QANLRII----EAV 260

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446074129 256 QERLRSGYEDAVDYNRYVGNI---------YTGSlylslisllENRDLQAGETIGLFSYGSG 308
Cdd:COG0332  261 AKRLGLPEEKVVVNIDRYGNTsaasiplalDEAL---------REGRIKPGDLVLLAGFGAG 313
KAS_III cd00830
Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty ...
 48-172 1.11e-05

Ketoacyl-acyl carrier protein synthase III (KASIII) initiates the elongation in type II fatty acid synthase systems. It is found in bacteria and plants. Elongation of fatty acids in the type II systems occurs by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP. KASIII initiates this process by specifically using acetyl-CoA over acyl-CoA.


Pssm-ID: 238426 [Multi-domain]  Cd Length: 320  Bit Score: 46.76  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  48 NQDIVSMGANAAKDIITDE--DKKKIGMVIVATESAVDAAKAAAVQIHNLLGIQPfARCFEMKEACYAATPAIQLAKDYL 125
Cdd:cd00830   47 GETTSDLAVEAAKKALEDAgiDADDIDLIIVATSTPDYLFPATACLVQARLGAKN-AAAFDINAACSGFLYGLSTAAGLI 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446074129 126 ATRPNEKVLVIATDTARYGLN---SGGEPTQGAGAVAMVI---AHNPSILALN 172
Cdd:cd00830  126 RSGGAKNVLVVGAETLSRILDwtdRSTAVLFGDGAGAVVLeatEEDPGILDSV 178
PRK12879 PRK12879
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 8-140 3.38e-05

3-oxoacyl-(acyl carrier protein) synthase III; Reviewed


Pssm-ID: 237245 [Multi-domain]  Cd Length: 325  Bit Score: 45.24  E-value: 3.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   8 INFYVPKYYVDMAKLAeaRQVDPNKFLI----GIgqTEMAVSPVNQDIVSMGANAAKDIITDEDK--KKIGMVIVATESA 81
Cdd:PRK12879  10 IGTYVPPRVLTNDDLE--TFIDTSDEWIvqrtGI--KERRIAHVEEYTSDLAIKAAERALARAGLdaEDIDLIIVATTTP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446074129  82 VDAAKAAAVQIHNLLGIqPFARCFEMKEACYAATPAIQLAKDYLATRPNEKVLVIATDT 140
Cdd:PRK12879  86 DYLFPSTASQVQARLGI-PNAAAFDINAACAGFLYGLETANGLITSGLYKKVLVIGAER 143
PRK07515 PRK07515
3-oxoacyl-(acyl carrier protein) synthase III; Reviewed
 54-136 3.47e-05

3-oxoacyl-(acyl carrier protein) synthase III; Reviewed


Pssm-ID: 236037  Cd Length: 372  Bit Score: 45.64  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  54 MGANAAKDIITDEDKK--KIGMVIVATESAVDAAKAAAVQIHNLLGIQPFArcFEMKEACYAATPAIQLAKDYLATRPNE 131
Cdd:PRK07515  98 MGVAAARQALARAGRTaeDIDAVIVACSNMQRAYPAMAIEIQQALGIEGFA--FDMNVACSSATFGIQTAANAIRSGSAR 175


                 ....*
gi 446074129 132 KVLVI 136
Cdd:PRK07515 176 RVLVV 180
CHS_like cd00831
Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, ...
 111-138 4.23e-04

Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.


Pssm-ID: 238427 [Multi-domain]  Cd Length: 361  Bit Score: 42.21  E-value: 4.23e-04
                         10        20
                 ....*....|....*....|....*...
gi 446074129 111 CYAATPAIQLAKDYLATRPNEKVLVIAT 138
Cdd:cd00831  147 CSAGAIALDLAKDLLEANPGARVLVVST 174
Chal_sti_synt_N pfam00195
Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase ...
 47-166 1.51e-03

Chalcone and stilbene synthases, N-terminal domain; The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain.


Pssm-ID: 395142  Cd Length: 225  Bit Score: 39.84  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129   47 VNQDIVSMGANAAKDIITD--EDKKKIGMVIVATESAVDAAKAAAvQIHNLLGIQPFARCFEM-KEACYAATPAIQLAKD 123
Cdd:pfam00195  95 ANAEVPELGAEAALKAIKEwgQPKSKITHLVFCTTSGVRMPGADY-QLAKLLGLRPSVKRVMLyFQGCYGGATVLRTAKD 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446074129  124 YLATRPNEKVLVIATDTARYGLNSG---------GEPTQGAGAVAMVIAHNP 166
Cdd:pfam00195 174 IAENNPGARVLVVCSEITVLGFRGPskdrldslvGAALFGDGAAAVIIGADP 225
PLN03173 PLN03173
chalcone synthase; Provisional
 50-168 7.17e-03

chalcone synthase; Provisional


Pssm-ID: 178717 [Multi-domain]  Cd Length: 391  Bit Score: 38.13  E-value: 7.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  50 DIVSMGANAAKDIITD--EDKKKIGMVIVATESAVDAAKAAAvQIHNLLGIQPFARCFEM-KEACYAATPAIQLAKDYLA 126
Cdd:PLN03173 101 EVPKLGKEAAAKAIKEwgQPKSKITHLVFCTTSGVDMPGADY-QLTKLLGLRSSVKRFMMyQQGCFAGGTVLRLAKDLAE 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446074129 127 TRPNEKVLVIATDTARYGLNSG---------GEPTQGAGAVAMVIAHNPSI 168
Cdd:PLN03173 180 NNKGARVLVVCSEITAVTFRGPsdthldslvGQALFGDGAAAIIIGSDPVL 230
PRK09352 PRK09352
beta-ketoacyl-ACP synthase 3;
48-170 9.45e-03

beta-ketoacyl-ACP synthase 3;


Pssm-ID: 236475 [Multi-domain]  Cd Length: 319  Bit Score: 37.75  E-value: 9.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446074129  48 NQDIVSMGANAAKDIITDE--DKKKIGMVIVATESAVDAAKAAAVQIHNLLGIQ-PFArcFEMKEAC----YaatpAIQL 120
Cdd:PRK09352  49 DETTSDLATEAAKKALEAAgiDPEDIDLIIVATTTPDYAFPSTACLVQARLGAKnAAA--FDLSAACsgfvY----ALST 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446074129 121 AKDYLATRPNEKVLVIATDTarygLNSGGEPTQ---------GAGAVAMVIAHNPSILA 170
Cdd:PRK09352 123 ADQFIRSGAYKNVLVIGAEK----LSRIVDWTDrstcvlfgdGAGAVVLGASEEPGILS 177
 
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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