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Conserved domains on  [gi|563344529|gb|AHB48552|]
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thiamine-monophosphate kinase [Hyphomicrobium nitrativorans NL23]

Protein Classification

thiamine-monophosphate kinase( domain architecture ID 11427471)

thiamine-monophosphate kinase catalyzes the formation of thiamine pyrophosphate (TPP) from thiamine monophosphate in an ATP- and Mg2+-dependent manner

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiL COG0611
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 8-333 1.32e-97

Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


:

Pssm-ID: 440376 [Multi-domain]  Cd Length: 321  Bit Score: 291.28  E-value: 1.32e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   8 GEDALIQATFAPLA-SGFPGAFGLKDDCALLTPPaGMDLVLTTDAVAEGVHFFAD-DAAHDIAWKALAVNVSDLVAKGAR 85
Cdd:COG0611    2 GEFGLIERLFKRLAlRGPDVLLGIGDDAAVLDPP-GGRLVVTTDMLVEGVHFPLDwMSPEDLGWKAVAVNLSDLAAMGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  86 PLAYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGpLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSG 165
Cdd:COG0611   81 PLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPE-LTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 166 TLGDAALGLLLRQDRARAaqmglDDVSARALVGRYLRPQPKLSLAPAILE--FASAAMDVSDGLVKDCGRLARASGVSAR 243
Cdd:COG0611  160 TLGDAAAGLALLLRGLRV-----PLEAREYLLERHLRPEPRLALGRALAEagLATAMIDISDGLAADLGHIAEASGVGAE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 244 IEGVRVPLSEPARtAVEHSPDLFQVVLSGGDDYEVLAAVPPDRADAFRDAAAksGVAVAEVGQCGDGQDVTVAGRDGRAL 323
Cdd:COG0611  235 IDLDALPLSPALR-EAALGLDPLELALTGGEDYELLFTVPPEALEALEAAAL--GVPLTVIGRVTEGEGVTLDDADGRPI 311

                        330
                 ....*....|
gi 563344529 324 DVAGGGWDHF 333
Cdd:COG0611  312 PLEARGWDHF 321
 
Name Accession Description Interval E-value
ThiL COG0611
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 8-333 1.32e-97

Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440376 [Multi-domain]  Cd Length: 321  Bit Score: 291.28  E-value: 1.32e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   8 GEDALIQATFAPLA-SGFPGAFGLKDDCALLTPPaGMDLVLTTDAVAEGVHFFAD-DAAHDIAWKALAVNVSDLVAKGAR 85
Cdd:COG0611    2 GEFGLIERLFKRLAlRGPDVLLGIGDDAAVLDPP-GGRLVVTTDMLVEGVHFPLDwMSPEDLGWKAVAVNLSDLAAMGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  86 PLAYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGpLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSG 165
Cdd:COG0611   81 PLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPE-LTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 166 TLGDAALGLLLRQDRARAaqmglDDVSARALVGRYLRPQPKLSLAPAILE--FASAAMDVSDGLVKDCGRLARASGVSAR 243
Cdd:COG0611  160 TLGDAAAGLALLLRGLRV-----PLEAREYLLERHLRPEPRLALGRALAEagLATAMIDISDGLAADLGHIAEASGVGAE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 244 IEGVRVPLSEPARtAVEHSPDLFQVVLSGGDDYEVLAAVPPDRADAFRDAAAksGVAVAEVGQCGDGQDVTVAGRDGRAL 323
Cdd:COG0611  235 IDLDALPLSPALR-EAALGLDPLELALTGGEDYELLFTVPPEALEALEAAAL--GVPLTVIGRVTEGEGVTLDDADGRPI 311

                        330
                 ....*....|
gi 563344529 324 DVAGGGWDHF 333
Cdd:COG0611  312 PLEARGWDHF 321
ThiL cd02194
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
 8-307 2.53e-90

ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).


Pssm-ID: 100030 [Multi-domain]  Cd Length: 291  Bit Score: 271.73  E-value: 2.53e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   8 GEDALIQATFAPLASGFPGAFGLKDDCALLTPPaGMDLVLTTDAVAEGVHFFADDAAHDIAWKALAVNVSDLVAKGARPL 87
Cdd:cd02194    1 GEFELIDRLFKRLGAGPGVLLGIGDDAAVLKPP-GGRLVVTTDTLVEGVHFPPDTTPEDIGWKALAVNLSDLAAMGARPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  88 AYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPgPLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSGTL 167
Cdd:cd02194   80 GFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGS-ELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 168 GdaalglllrqdRARAA----QMGLDDVSA--RALVGRYLRPQPKLSLAPAILE-FASAAMDVSDGLVKDCGRLARASGV 240
Cdd:cd02194  159 G-----------DAAAGlallLGGLKLPEElyEELIERHLRPEPRLELGRALAEgLATAMIDISDGLLADLGHIAEASGV 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 563344529 241 SARIEGVRVPLSEPARTAVEHsPDLFQVVLSGGDDYEVLAAVPPdraDAFRDAAAKSGVAVAEVGQC 307
Cdd:cd02194  228 GAVIDLDKLPLSPALRAAELG-EDALELALSGGEDYELLFTVPP---ENAEAAAAKLGVPVTVIGRV 290
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
 8-333 3.74e-88

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 267.08  E-value: 3.74e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   8 GEDALIQATFAPLASgfPGAFGLKDDCALLTPPAGMDLVLTTDAVAEGVHFFADDA-AHDIAWKALAVNVSDLVAKGARP 86
Cdd:PRK05731   4 GEFDLIARLFARRPS--SRELGIGDDAALLGPPPGQRLVVSTDMLVEGVHFRPDWSsPEDLGYKALAVNLSDLAAMGARP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  87 LAYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGpLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSGT 166
Cdd:PRK05731  82 AAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTTRGPD-LSISVTAIGDVPGGRALRRSGAKPGDLVAVTGT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 167 LGDAALGLLLRQDRARAaqmglDDVSARALVGRYLRPQPKLSLAPAILEFASAAMDVSDGLVKDCGRLARASGVSARIEG 246
Cdd:PRK05731 161 LGDSAAGLALLLNGLRV-----PDADAAALISRHLRPQPRVGLGQALAGLASAAIDISDGLAADLGHIAEASGVGADIDL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 247 VRVPLSEPARTAVEHSpDLFQVVLSGGDDYEVLAAVPPDRADAFRDAAAKSGVAVAEVGQCGDGQDVTvagRDGRALDVA 326
Cdd:PRK05731 236 DALPISPALREAAEGE-DALRWALSGGEDYELLFTFPPENRGALLAAAGHLGVGVTIIGRVTEGEGVV---VDGEPVTLD 311


                 ....*..
gi 563344529 327 GGGWDHF 333
Cdd:PRK05731 312 LKGYDHF 318
thiL TIGR01379
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ...
 8-333 1.00e-77

thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that converts thiamine monophosphate into thiamine pyrophosphate (TPP, coenzyme B1), an enzyme cofactor. Thiamine monophosphate may be derived from de novo synthesis or from unphosphorylated thiamine, known as vitamin B1. Proteins scoring between the trusted and noise cutoff for this model include short forms from the Thermoplasmas (which lack the N-terminal region) and a highly derived form from Campylobacter jejuni. Eukaryotes lack this enzyme, and add pyrophosphate from ATP to unphosphorylated thiamine in a single step. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273589 [Multi-domain]  Cd Length: 317  Bit Score: 240.70  E-value: 1.00e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529    8 GEDALIQATFAPLASGFPGAFGLKDDCALLTPPAGMDLVLTTDAVAEGVHFFADDAAHDIAWKALAVNVSDLVAKGARPL 87
Cdd:TIGR01379   1 GEFELIDRILRRLVQDPDVALGIGDDAALVSAPEGRDLVLTTDTLVEGVHFPPDTTPEDLGWKAVAVNLSDLAAMGATPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   88 AYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGpLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSGTL 167
Cdd:TIGR01379  81 WFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPE-LVVTVTAIGEAPKGRALLRSGAKPGDLVFVTGTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  168 GDAALGLLLRQDRARAAQMGLDDvsarALVGRYLRPQPKLSLAPAILEFASAAMDVSDGLVKDCGRLARASGVSARIEGV 247
Cdd:TIGR01379 160 GDSAAGLALLLKGKKEPDEEDDE----ALLQRHLRPEPRVEEGLALAGYANAAIDVSDGLAADLGHIAEASGVGIVIDLD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  248 RVPLSEPARTAVEhSPDLFQVVLSGGDDYEVLAAVPPDRADAFRDAAAKSgvaVAEVGQCGDGQDVtVAGRDGRALDVAG 327
Cdd:TIGR01379 236 RLPLSSELAAWAE-GKNPLEWALSGGEDYELVFTVPPERREALLDAAKGP---LTRIGRVTEGEGV-VLLADGKTVELLD 310


                  ....*..
gi 563344529  328 G-GWDHF 333
Cdd:TIGR01379 311 RlGWQHF 317
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
 32-144 9.49e-23

AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 459859 [Multi-domain]  Cd Length: 104  Bit Score: 90.97  E-value: 9.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   32 DDCALltppagmdlVLTTDAVAegvHFFADDAAHDIAWKALAVNVSDLVAKGARPLAYLLALSFPDRPDDAW-LAGFQAG 110
Cdd:pfam00586   1 DDAAV---------AVTTDGHG---TPSLVDPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvLEEIVEG 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 563344529  111 LADAQAAFGLSLAGGDT--DRRPGPLSIGVTAVGAV 144
Cdd:pfam00586  69 IAEACREAGVPLVGGDTsfDPEGGKPTISVTAVGIV 104
 
Name Accession Description Interval E-value
ThiL COG0611
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 8-333 1.32e-97

Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440376 [Multi-domain]  Cd Length: 321  Bit Score: 291.28  E-value: 1.32e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   8 GEDALIQATFAPLA-SGFPGAFGLKDDCALLTPPaGMDLVLTTDAVAEGVHFFAD-DAAHDIAWKALAVNVSDLVAKGAR 85
Cdd:COG0611    2 GEFGLIERLFKRLAlRGPDVLLGIGDDAAVLDPP-GGRLVVTTDMLVEGVHFPLDwMSPEDLGWKAVAVNLSDLAAMGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  86 PLAYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGpLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSG 165
Cdd:COG0611   81 PLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPE-LTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 166 TLGDAALGLLLRQDRARAaqmglDDVSARALVGRYLRPQPKLSLAPAILE--FASAAMDVSDGLVKDCGRLARASGVSAR 243
Cdd:COG0611  160 TLGDAAAGLALLLRGLRV-----PLEAREYLLERHLRPEPRLALGRALAEagLATAMIDISDGLAADLGHIAEASGVGAE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 244 IEGVRVPLSEPARtAVEHSPDLFQVVLSGGDDYEVLAAVPPDRADAFRDAAAksGVAVAEVGQCGDGQDVTVAGRDGRAL 323
Cdd:COG0611  235 IDLDALPLSPALR-EAALGLDPLELALTGGEDYELLFTVPPEALEALEAAAL--GVPLTVIGRVTEGEGVTLDDADGRPI 311

                        330
                 ....*....|
gi 563344529 324 DVAGGGWDHF 333
Cdd:COG0611  312 PLEARGWDHF 321
ThiL cd02194
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
 8-307 2.53e-90

ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).


Pssm-ID: 100030 [Multi-domain]  Cd Length: 291  Bit Score: 271.73  E-value: 2.53e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   8 GEDALIQATFAPLASGFPGAFGLKDDCALLTPPaGMDLVLTTDAVAEGVHFFADDAAHDIAWKALAVNVSDLVAKGARPL 87
Cdd:cd02194    1 GEFELIDRLFKRLGAGPGVLLGIGDDAAVLKPP-GGRLVVTTDTLVEGVHFPPDTTPEDIGWKALAVNLSDLAAMGARPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  88 AYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPgPLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSGTL 167
Cdd:cd02194   80 GFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGS-ELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 168 GdaalglllrqdRARAA----QMGLDDVSA--RALVGRYLRPQPKLSLAPAILE-FASAAMDVSDGLVKDCGRLARASGV 240
Cdd:cd02194  159 G-----------DAAAGlallLGGLKLPEElyEELIERHLRPEPRLELGRALAEgLATAMIDISDGLLADLGHIAEASGV 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 563344529 241 SARIEGVRVPLSEPARTAVEHsPDLFQVVLSGGDDYEVLAAVPPdraDAFRDAAAKSGVAVAEVGQC 307
Cdd:cd02194  228 GAVIDLDKLPLSPALRAAELG-EDALELALSGGEDYELLFTVPP---ENAEAAAAKLGVPVTVIGRV 290
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
 8-333 3.74e-88

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 267.08  E-value: 3.74e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   8 GEDALIQATFAPLASgfPGAFGLKDDCALLTPPAGMDLVLTTDAVAEGVHFFADDA-AHDIAWKALAVNVSDLVAKGARP 86
Cdd:PRK05731   4 GEFDLIARLFARRPS--SRELGIGDDAALLGPPPGQRLVVSTDMLVEGVHFRPDWSsPEDLGYKALAVNLSDLAAMGARP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  87 LAYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGpLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSGT 166
Cdd:PRK05731  82 AAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTTRGPD-LSISVTAIGDVPGGRALRRSGAKPGDLVAVTGT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 167 LGDAALGLLLRQDRARAaqmglDDVSARALVGRYLRPQPKLSLAPAILEFASAAMDVSDGLVKDCGRLARASGVSARIEG 246
Cdd:PRK05731 161 LGDSAAGLALLLNGLRV-----PDADAAALISRHLRPQPRVGLGQALAGLASAAIDISDGLAADLGHIAEASGVGADIDL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 247 VRVPLSEPARTAVEHSpDLFQVVLSGGDDYEVLAAVPPDRADAFRDAAAKSGVAVAEVGQCGDGQDVTvagRDGRALDVA 326
Cdd:PRK05731 236 DALPISPALREAAEGE-DALRWALSGGEDYELLFTFPPENRGALLAAAGHLGVGVTIIGRVTEGEGVV---VDGEPVTLD 311


                 ....*..
gi 563344529 327 GGGWDHF 333
Cdd:PRK05731 312 LKGYDHF 318
thiL TIGR01379
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ...
 8-333 1.00e-77

thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that converts thiamine monophosphate into thiamine pyrophosphate (TPP, coenzyme B1), an enzyme cofactor. Thiamine monophosphate may be derived from de novo synthesis or from unphosphorylated thiamine, known as vitamin B1. Proteins scoring between the trusted and noise cutoff for this model include short forms from the Thermoplasmas (which lack the N-terminal region) and a highly derived form from Campylobacter jejuni. Eukaryotes lack this enzyme, and add pyrophosphate from ATP to unphosphorylated thiamine in a single step. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273589 [Multi-domain]  Cd Length: 317  Bit Score: 240.70  E-value: 1.00e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529    8 GEDALIQATFAPLASGFPGAFGLKDDCALLTPPAGMDLVLTTDAVAEGVHFFADDAAHDIAWKALAVNVSDLVAKGARPL 87
Cdd:TIGR01379   1 GEFELIDRILRRLVQDPDVALGIGDDAALVSAPEGRDLVLTTDTLVEGVHFPPDTTPEDLGWKAVAVNLSDLAAMGATPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   88 AYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGpLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSGTL 167
Cdd:TIGR01379  81 WFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPE-LVVTVTAIGEAPKGRALLRSGAKPGDLVFVTGTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  168 GDAALGLLLRQDRARAAQMGLDDvsarALVGRYLRPQPKLSLAPAILEFASAAMDVSDGLVKDCGRLARASGVSARIEGV 247
Cdd:TIGR01379 160 GDSAAGLALLLKGKKEPDEEDDE----ALLQRHLRPEPRVEEGLALAGYANAAIDVSDGLAADLGHIAEASGVGIVIDLD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  248 RVPLSEPARTAVEhSPDLFQVVLSGGDDYEVLAAVPPDRADAFRDAAAKSgvaVAEVGQCGDGQDVtVAGRDGRALDVAG 327
Cdd:TIGR01379 236 RLPLSSELAAWAE-GKNPLEWALSGGEDYELVFTVPPERREALLDAAKGP---LTRIGRVTEGEGV-VLLADGKTVELLD 310


                  ....*..
gi 563344529  328 G-GWDHF 333
Cdd:TIGR01379 311 RlGWQHF 317
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
 32-144 9.49e-23

AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 459859 [Multi-domain]  Cd Length: 104  Bit Score: 90.97  E-value: 9.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   32 DDCALltppagmdlVLTTDAVAegvHFFADDAAHDIAWKALAVNVSDLVAKGARPLAYLLALSFPDRPDDAW-LAGFQAG 110
Cdd:pfam00586   1 DDAAV---------AVTTDGHG---TPSLVDPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvLEEIVEG 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 563344529  111 LADAQAAFGLSLAGGDT--DRRPGPLSIGVTAVGAV 144
Cdd:pfam00586  69 IAEACREAGVPLVGGDTsfDPEGGKPTISVTAVGIV 104
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
 45-306 2.45e-19

AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM (formylglycinamidine ribonucleotide) synthase and Selenophosphate synthetase (SelD). The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 100027 [Multi-domain]  Cd Length: 222  Bit Score: 85.14  E-value: 2.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  45 LVLTTDAVAEGVHFFADDaahdIAWKALAVNVSDLVAKGARPLAYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAG 124
Cdd:cd00396    2 LAMSTDGINPPLAINPWA----GGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAEACNQLGVPIVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 125 GDTDRRPG----PLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSGTLGDAalglllrqdraraaqmglddvSARALVGry 200
Cdd:cd00396   78 GHTSVSPGtmghKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTGVDAVL---------------------ELVAAGD-- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 201 lrpqpklslapailefASAAMDVSD-GLVKDCGRLARASGVSARIEGVRVPLSEPARTAVEHSPDLFqvvLSGGDDYEVL 279
Cdd:cd00396  135 ----------------VHAMHDITDgGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWLCVEHIEEA---LLFNSSGGLL 195

                        250       260
                 ....*....|....*....|....*..
gi 563344529 280 AAVPPDRADAFRDAAAKSGVAVAEVGQ 306
Cdd:cd00396  196 IAVPAEEADAVLLLLNGNGIDAAVIGR 222
PurM-like1 cd06061
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ...
 32-305 2.13e-11

AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.


Pssm-ID: 100037 [Multi-domain]  Cd Length: 298  Bit Score: 63.77  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  32 DDCALLTPpAGMDLVLTTDAVaegvhFFADDaahDIAWKALAVNVSDLVAKGARPLAYLLALSFPDRPDDAWLAGFQAGL 111
Cdd:cd06061   33 EDAAVVDF-GGKVLVVSTDPI-----TGAGK---DAGWLAVHIAANDIATSGARPRWLLVTLLLPPGTDEEELKAIMREI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 112 ADAQAAFGLSLAGGDTDRRPG--PLSIGVTAVGAVPHGRFVQRGTAQPGDLLFLSGTLGDAALGLLLRQDRARAAQMGLD 189
Cdd:cd06061  104 NEAAKELGVSIVGGHTEVTPGvtRPIISVTAIGKGEKDKLVTPSGAKPGDDIVMTKGAGIEGTAILANDFEEELKKRLSE 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 190 DVSARALvgRYLRpqpKLSLAP----AILEFASAAMDVSDGLVKdcGRL---ARASGVSARIEGVRVPLSEPARTAVEH- 261
Cdd:cd06061  184 EELREAA--KLFY---KISVVKealiAAEAGVTAMHDATEGGIL--GALwevAEASGVGLRIEKDKIPIRQETKEICEAl 256

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 563344529 262 SPDLFQVVLSGGddyeVLAAVPPDRADAFRDAAAKSGVAVAEVG 305
Cdd:cd06061  257 GIDPLRLISSGT----LLITVPPEKGDELVDALEEAGIPASVIG 296
SelD cd02195
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ...
 28-306 1.34e-10

Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate which is required by a number of bacterial, archaeal and eukaryotic organisms for synthesis of Secys-tRNA, the precursor of selenocysteine in selenoenzymes. The N-terminal domain of SelD is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100031 [Multi-domain]  Cd Length: 287  Bit Score: 61.00  E-value: 1.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  28 FGLKDDCALLTPPAGMDLVLTTDavaegvHFFA--DD--------AAHdiawkALavnvSDLVAKGARPLAYLLALSFP- 96
Cdd:cd02195   38 LGTGDDAAVYRLPGGLALVQTTD------FFPPivDDpylfgriaAAN-----AL----SDIYAMGAKPLSALAIVTLPr 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  97 --DRPDDAWL----AGFQAGLADAQAAfglsLAGGDTDRRPGPlSIGVTAVGAVPHGRFVQRGTAQPGDLLFLS---GTL 167
Cdd:cd02195  103 klPALQEEVLreilAGGKDKLREAGAV----LVGGHTIEGPEP-KYGLSVTGLVHPNKILRNSGAKPGDVLILTkplGTG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 168 GdaalglllrqdrARAAQMGLDDVSA--RALVGRYLRPQPKLSLApAILEFASAAMDVSD-GLVKDCGRLARASGVSARI 244
Cdd:cd02195  178 I------------LFAAEMAGLARGEdiDAALESMARLNRAAAEL-LRKYGAHACTDVTGfGLLGHLLEMARASGVSAEI 244

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 563344529 245 EGVRVPlsepartavehspdLFQVvlSGGddyeVLAAVPPDRADAFRDAAAKSGVAVAEVGQ 306
Cdd:cd02195  245 DLDKLP--------------LLQT--SGG----LLAAVPPEDAAALLALLKAGGPPAAIIGE 286
PurM cd02196
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ...
 23-161 1.99e-08

PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for purine biosynthesis, catalyzes the conversion of formylglycinamide ribonucleotide (FGAM) and ATP to AIR, ADP, and Pi, the fifth step in de novo purine biosynthesis. The N-terminal domain of PurM is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100032 [Multi-domain]  Cd Length: 297  Bit Score: 54.79  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  23 GFPGAFGlkddcALLTPPAGMD----LVLTTDAVaeG----VHFFADDaaHD-IAWKALAVNVSDLVAKGARPLAYL--L 91
Cdd:cd02196    1 GGIGGFA-----GLFDLGLGGYkdpvLVSGTDGV--GtklkLAQEMGK--HDtIGIDLVAMCVNDILCQGAEPLFFLdyI 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 563344529  92 ALSfpdRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGPLSIGV-----TAVGAVPHGRFVQRGTAQPGDLL 161
Cdd:cd02196   72 ATG---KLDPEVAAEIVKGIAEGCRQAGCALLGGETAEMPGVYAEGEydlagFAVGVVEKDKIIDGSKIKPGDVL 143
PurM-like3 cd02192
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ...
 21-250 6.67e-08

AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.


Pssm-ID: 100028 [Multi-domain]  Cd Length: 283  Bit Score: 52.98  E-value: 6.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  21 ASGFPGAFGlkDDCALLtpPAGMDLVLttdAVAEGVH--------FFAddaahdiAWKALAVNVSDLVAKGARPLAYLLA 92
Cdd:cd02192   27 SLGVAADLG--DDAAAI--PDGDGYLL---LAADGIWpslveadpWWA-------GYCSVLVNVSDIAAMGGRPLAMVDA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  93 LSfpdRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGPLSIGVTAVGAVpHGRFVQRGTAQPGDLLFLsgtlgdaal 172
Cdd:cd02192   93 LW---SPSAEAAAQVLEGMRDAAEKFGVPIVGGHTHPDSPYNALSVAILGRA-RKDLLISFGAKPGDRLIL--------- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 173 GLLLRQDRARAAQMGLDDVSARAlvGRYLRPQpkLSLAPAILE--FASAAMDVSD-GLVKDCGRLARASGVSARIEGVRV 249
Cdd:cd02192  160 AIDLDGRVHPSPPPNWDATTMKS--PALLRRQ--IALLPELAErgLVHAAKDISNpGIIGTLGMLLEASGVGAEIDLDAI 235


                 .
gi 563344529 250 P 250
Cdd:cd02192  236 P 236
COG2144 COG2144
Selenophosphate synthetase-related protein [General function prediction only];
25-323 3.31e-07

Selenophosphate synthetase-related protein [General function prediction only];


Pssm-ID: 441747 [Multi-domain]  Cd Length: 323  Bit Score: 51.32  E-value: 3.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  25 PGAFGlkDDCALLtPPAGMDLVLTTD----AVAEGVHFFAddaahdiAWKALAVNVSDLVAKGARPLAYLLALSFPDrPD 100
Cdd:COG2144   39 AAAFG--DDAAAI-PDGDGYLLLAAEgiwpKFVEADPWFA-------GYCSVLVNVSDIAAMGGRPLAVVDALWSSD-EE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 101 DAwlAGFQAGLADAQAAFGLSLAGGDTDRRPGPLSIGVTAVGAVPHgrfVQRG-TAQPGDLLFlsgtlgdaalglllrqd 179
Cdd:COG2144  108 AA--APVLAGMRAASRKFGVPIVGGHTHPDTPYNALAVAILGRAKK---LLTSfTARPGDRLI----------------- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 180 raraaqMGLDdvsaraLVGRYLRPQP---------------KLSLAPAILE--FASAAMDVSD-GLVKDCGRLARASGVS 241
Cdd:COG2144  166 ------AAID------LDGRYHPPFPywdattgkpperlraQLELLPELAEagLVTAAKDISNpGIIGTLGMLLECSGVG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 242 ARIEGVRVPLsePARTAVEHSPDLFQvvlsggdDYEVLAAVPPDRADAFRDAAAKSGVAVAEVGQCGDGQDVTVAGRDGR 321
Cdd:COG2144  234 ATIDLDAIPR--PEGVDLERWLKAFP-------SFGFLLTVPPENVDEVLARFAARGITAAVIGEVTDSRRLTLRDGGER 304


                 ..
gi 563344529 322 AL 323
Cdd:COG2144  305 AT 306
SelD COG0709
Selenophosphate synthase [Amino acid transport and metabolism];
28-315 2.40e-06

Selenophosphate synthase [Amino acid transport and metabolism];


Pssm-ID: 440473 [Multi-domain]  Cd Length: 346  Bit Score: 48.53  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  28 FGLKDDCALLTPPAGMDLVLTTDavaegvHF--FADD--------AAHdiawkALavnvSDLVAKGARPLAYLLALSFP- 96
Cdd:COG0709   44 LETSDDAAVYRLGDDQALVQTTD------FFtpIVDDpydfgriaAAN-----AL----SDVYAMGGRPLTALAIVGFPi 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  97 DRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGPlSIGVTAVGAVPHGRFVQRGTAQPGDLLFL-----SGTLGdaa 171
Cdd:COG0709  109 DKLPEEVLAEILAGGADKCREAGAPLAGGHSIDDPEP-KYGLAVTGLVHPDKVLRNAGARPGDVLILtkplgTGILT--- 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 172 lglllrqdrarAAQMG--LDDVSARALVGRYLRPQpklSLAPAILEF--ASAAMDVSD-GLVKDCGRLARASGVSARIEG 246
Cdd:COG0709  185 -----------TAIKAglADGEDIAAAIASMTTLN---KAAAELARLygVHACTDVTGfGLLGHLLEMARGSGVSAEIDL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 247 VRVPLSEPARTAVEH-----------------------SPDLFQVVL-----SGGddyeVLAAVPPDRADAFRDAAAKSG 298
Cdd:COG0709  251 DAVPLLPGALELAEQgivpggtyrnrasygakvefaegLDEAQRDLLfdpqtSGG----LLIAVPPEAAEELLAALRAAG 326

                        330
                 ....*....|....*..
gi 563344529 299 VAVAEVGQCGDGQDVTV 315
Cdd:COG0709  327 YAAAIIGEVTAGEGGAI 343
PurL_repeat2 cd02204
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ...
 71-163 4.12e-05

PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.


Pssm-ID: 100035 [Multi-domain]  Cd Length: 264  Bit Score: 44.45  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  71 ALAV--NVSDLVAKGARPLAYLLALSF--PDRPDDAWLAGFQA--GLADAQAAFGLSLAGG------DTDRRPGPLSIGV 138
Cdd:cd02204   35 ALAVaeAVRNLVAVGADPLAITDCLNFgnPEKPEGEMGQLVEAvlGLGDACRALGTPVIGGkdslynETEGVAIPPTLVI 114

                         90       100
                 ....*....|....*....|....*.
gi 563344529 139 TAVGAVPHGRF-VQRGTAQPGDLLFL 163
Cdd:cd02204  115 GAVGVVDDVRKiVTLDFKKEGDLLYL 140
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
 4-166 9.21e-05

HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase biosynthesis. HypE dehydrates its own carbamoyl moiety in an ATP-dependent process to yield the enzyme thiocyanate. The N-terminal domain of HypE is related to the ATP-binding domains of the AIR synthases, selenophosphate synthetase (SelD), and FGAM synthase and is thought to bind ATP.


Pssm-ID: 100033 [Multi-domain]  Cd Length: 293  Bit Score: 43.59  E-value: 9.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   4 RETRgedALIQATFAPLasgFPGAFGLKDDCALLTPPAGMDLVLTTDA-VaegVH--FFADDaahDIAwkALAVN--VSD 78
Cdd:cd02197    4 KLMQ---ELIEELFLKA---FDNPILEVLEDAAALLVGGGRLAFTTDSfV---VSplFFPGG---DIG--KLAVCgtVND 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  79 LVAKGARPLAYLLAL----SFPdrpddawLAGFQ---AGLADAQAAFGLSLAGGDT--------DRrpgpLSIGVTAVGA 143
Cdd:cd02197   70 LAMMGAKPLYLSLGFileeGFP-------LEDLErivKSMAEAAREAGVKIVTGDTkvvpkgkaDG----IFINTTGIGV 138

                        170       180
                 ....*....|....*....|...
gi 563344529 144 VPHGRFVQRGTAQPGDLLFLSGT 166
Cdd:cd02197  139 IPRGVIISPSNIRPGDKIIVSGT 161
PurM-like2 cd02691
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ...
 76-164 1.06e-04

AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.


Pssm-ID: 100036  Cd Length: 346  Bit Score: 43.53  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  76 VSDLVAKGARPLAYLLALSFPDRPDDAWLAGFQAGLADAQAAFGLSLAGGDTDRRPGPLSIG---VTAVGAVphGRFVQ- 151
Cdd:cd02691   76 LRDVMVMGARPVALLSDIHLADDGDVGKLFDFTAGVTAVSEATGVPLVAGSTLRIGGDMVLGdrlVGGVGAV--GRSKSd 153

                         90
                 ....*....|....*.
gi 563344529 152 ---RGTAQPGDLLFLS 164
Cdd:cd02691  154 psrRKNAEPGDLILMT 169
FGAM_synth_II TIGR01736
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ...
 76-165 5.93e-04

phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a single, long polypeptide in most Proteobacteria and eukarotes. Three proteins are required in Bacillus subtilis and many other species. This is the longest of the three and is designated PurL, phosphoribosylformylglycinamidine synthase II, or FGAM synthase II. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273781 [Multi-domain]  Cd Length: 715  Bit Score: 41.52  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529   76 VSDLVAKGARPLAYLLALSF--PDRPDDAWLA-GFQAGLADAQAAFGLSLAGGDTDRRPG----PLsIGVTAVGAVPHGR 148
Cdd:TIGR01736  98 LRDILSMGARPIALLDSLRFgpLDDPKNRYLFeGVVAGISDYGNRIGVPTVGGEVEFDESyngnPL-VNVMCVGLVRKDD 176

                          90
                  ....*....|....*...
gi 563344529  149 fVQRGTAQ-PGDLLFLSG 165
Cdd:TIGR01736 177 -IVTGKAKgPGNKLVLVG 193
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
 156-315 2.27e-03

AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The function of the C-terminal domain of AIR synthase is unclear, but the cleft formed between N and C domains is postulated as a sulphate binding site.


Pssm-ID: 460684 [Multi-domain]  Cd Length: 152  Bit Score: 38.10  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  156 QPGDLLFLSGTLGDAALglllrqdrARAAQMGLDDVSARALV--GRYLRPQPKLSLAPAILEF---ASAAMDVSD-GLVK 229
Cdd:pfam02769   1 KPGDVLILLGSSGLHGA--------GLSLSRKGLEDSGLAAVqlGDPLLEPTLIYVKLLLAALgglVKAMHDITGgGLAG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  230 DCGRLARASGVSARIEGVRVPLSEPARTAVEhspdlfqvVLSGGDDYEVLAAVPPDRADAFRDAAAKSGVAVAEVGQCGD 309
Cdd:pfam02769  73 ALAEMAPASGVGAEIDLDKVPIFEELMLPLE--------MLLSENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEVTA 144


                  ....*.
gi 563344529  310 GQDVTV 315
Cdd:pfam02769 145 GGRLTV 150
PRK01213 PRK01213
phosphoribosylformylglycinamidine synthase subunit PurL;
71-324 4.30e-03

phosphoribosylformylglycinamidine synthase subunit PurL;


Pssm-ID: 234921 [Multi-domain]  Cd Length: 724  Bit Score: 38.93  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529  71 ALAVNVSDLVAKGARPLAYLLALSF--PDRPDDAW-LAGFQAGLADAQAAFGLSLAGG------DTDRR---PGPlSIGV 138
Cdd:PRK01213 464 AVAEAARNLAAVGATPLAITDCLNFgnPEKPEVMWqFVEAVRGLADACRALGTPVVGGnvslynETGGTaiyPTP-VIGM 542

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 139 taVGAVPH-GRFVQRGTAQPGDLLFLSGTLGdaalglllrqdraraaqmglDDVSARAlvgrYLR----------PQPKL 207
Cdd:PRK01213 543 --VGLIDDvSKRTTSGFKKEGDLIYLLGETK--------------------DELGGSE----YLKvihghvggrpPKVDL 596

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563344529 208 SLAPAILEF---------ASAAMDVSDG-----LVKdcgrLARASGVsarieGVRVPLSEPARTAVEhspdLFQVvlSGG 273
Cdd:PRK01213 597 EAEKRLQELvreaireglVTSAHDVSEGglavaLAE----MAIAGGL-----GAEVDLSDGLRPDAL----LFSE--SQG 661

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 563344529 274 ddyEVLAAVPPDRADAFRDAAAKSGVAVAEVGQCGDGQdVTVAGRDGRALD 324
Cdd:PRK01213 662 ---RYVVSVPPENEEAFEALAEAAGVPATRIGVVGGDA-LKVKGNDTESLE 708
 
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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