|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
7-332 |
1.66e-121 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 351.83 E-value: 1.66e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 7 RDVGEQGLLPLLFHFCPPGV---VGDDAAVLAGLGTRSLVVTTDVLVEGVHFSDRTTPPDAVGWRAVAANLSDLAAMGAT 83
Cdd:PRK05731 1 MAMGEFDLIARLFARRPSSRelgIGDDAALLGPPPGQRLVVSTDMLVEGVHFRPDWSSPEDLGYKALAVNLSDLAAMGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 84 PLGMTIALAMPGEVPLAWVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTGL 163
Cdd:PRK05731 81 PAAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTTRGPDLSISVTAIGDVPGGRALRRSGAKPGDLVAVTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 164 HGASRLGLAILQEpslRGTVSSAEADRWRRAHQYPVPRLDVIEPLWQAIahtrcrsdIAAMDTSDGLADAIIQICRASGV 243
Cdd:PRK05731 161 LGDSAAGLALLLN---GLRVPDADAAALISRHLRPQPRVGLGQALAGLA--------SAAIDISDGLAADLGHIAEASGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 244 GAKVERERLRIPPEATAIVSPEQAITWVLYGGEDFELVLCLP---LAAAEELVQRLGGDAAIVGEVTSEPGVFlVDGreK 320
Cdd:PRK05731 230 GADIDLDALPISPALREAAEGEDALRWALSGGEDYELLFTFPpenRGALLAAAGHLGVGVTIIGRVTEGEGVV-VDG--E 306
|
330
....*....|..
gi 2331086371 321 KPLSLAQGFQHF 332
Cdd:PRK05731 307 PVTLDLKGYDHF 318
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
9-332 |
2.35e-120 |
|
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: 349.06 E-value: 2.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 9 VGEQGLLPLLFHFC---PPGVV---GDDAAVLAGLGTRsLVVTTDVLVEGVHFSDRTTPPDAVGWRAVAANLSDLAAMGA 82
Cdd:COG0611 1 MGEFGLIERLFKRLalrGPDVLlgiGDDAAVLDPPGGR-LVVTTDMLVEGVHFPLDWMSPEDLGWKAVAVNLSDLAAMGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 83 TPLGMTIALAMPGEVPLAWVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTG 162
Cdd:COG0611 80 RPLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPELTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 163 LHGASRLGLAILQEpslRGTVSSAEADRWRRAHQYPVPRLDviepLWQAIAHTRCRSdiAAMDTSDGLADAIIQICRASG 242
Cdd:COG0611 160 TLGDAAAGLALLLR---GLRVPLEAREYLLERHLRPEPRLA----LGRALAEAGLAT--AMIDISDGLAADLGHIAEASG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 243 VGAKVERERLRIPPEATAIVSPEQAITWVLYGGEDFELVLCLPLAAAEELVQRLGG-DAAIVGEVTSEPGVFLVDGREKK 321
Cdd:COG0611 231 VGAEIDLDALPLSPALREAALGLDPLELALTGGEDYELLFTVPPEALEALEAAALGvPLTVIGRVTEGEGVTLDDADGRP 310
|
330
....*....|.
gi 2331086371 322 PLSLAQGFQHF 332
Cdd:COG0611 311 IPLEARGWDHF 321
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
10-307 |
2.29e-107 |
|
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: 314.88 E-value: 2.29e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 10 GEQGLLPLLFHFCPPGV-----VGDDAAVLAGlGTRSLVVTTDVLVEGVHFsDRTTPPDAVGWRAVAANLSDLAAMGATP 84
Cdd:cd02194 1 GEFELIDRLFKRLGAGPgvllgIGDDAAVLKP-PGGRLVVTTDTLVEGVHF-PPDTTPEDIGWKALAVNLSDLAAMGARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 85 LGMTIALAMPGEVPLAWVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTGLH 164
Cdd:cd02194 79 LGFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 165 GASRLGLAILQEPslrGTVSSAEADRWRRAHQYPVPRLDVIEPLWQAIAHtrcrsdiAAMDTSDGLADAIIQICRASGVG 244
Cdd:cd02194 159 GDAAAGLALLLGG---LKLPEELYEELIERHLRPEPRLELGRALAEGLAT-------AMIDISDGLLADLGHIAEASGVG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2331086371 245 AKVERERLRIPPEATAIVSPEQAITWVLYGGEDFELVLCLPLAAAEELVQRLGGDAAIVGEVT 307
Cdd:cd02194 229 AVIDLDKLPLSPALRAAELGEDALELALSGGEDYELLFTVPPENAEAAAAKLGVPVTVIGRVT 291
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
8-332 |
4.64e-94 |
|
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: 282.30 E-value: 4.64e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 8 DVGEQGLLPLLFHFCPPGVVGDDAAVLAGLGTRSLVVTTDVLVEGVHFsDRTTPPDAVGWRAVAANLSDLAAMGATPLGM 87
Cdd:TIGR01379 4 ELIDRILRRLVQDPDVALGIGDDAALVSAPEGRDLVLTTDTLVEGVHF-PPDTTPEDLGWKAVAVNLSDLAAMGATPKWF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 88 TIALAMPGEVPLAWVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTGLHGAS 167
Cdd:TIGR01379 83 LLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPELVVTVTAIGEAPKGRALLRSGAKPGDLVFVTGTLGDS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 168 RLGLAILQEPslRGTVSSAEADRWRRAHQYPVPRLDVIEPLwQAIAHtrcrsdiAAMDTSDGLADAIIQICRASGVGAKV 247
Cdd:TIGR01379 163 AAGLALLLKG--KKEPDEEDDEALLQRHLRPEPRVEEGLAL-AGYAN-------AAIDVSDGLAADLGHIAEASGVGIVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 248 ERERLRIPPEATAIVSPEQAITWVLYGGEDFELVLCLPLAAAEELVQRLGGDAAIVGEVTSEPGVFLVDGREKKPLSLAQ 327
Cdd:TIGR01379 233 DLDRLPLSSELAAWAEGKNPLEWALSGGEDYELVFTVPPERREALLDAAKGPLTRIGRVTEGEGVVLLADGKTVELLDRL 312
|
....*
gi 2331086371 328 GFQHF 332
Cdd:TIGR01379 313 GWQHF 317
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
29-141 |
8.44e-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: 8.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 29 DDAAVlaglgtrslVVTTD-----VLVEGVHFsdrttppdaVGWRAVAANLSDLAAMGATPLGMTIALAMPGEVPLAW-V 102
Cdd:pfam00586 1 DDAAV---------AVTTDghgtpSLVDPYHF---------PGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvL 62
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2331086371 103 EHFYRGMTACLQASGGAILGGDLSQSPVR---SIAITALGQV 141
Cdd:pfam00586 63 EEIVEGIAEACREAGVPLVGGDTSFDPEGgkpTISVTAVGIV 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
7-332 |
1.66e-121 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 351.83 E-value: 1.66e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 7 RDVGEQGLLPLLFHFCPPGV---VGDDAAVLAGLGTRSLVVTTDVLVEGVHFSDRTTPPDAVGWRAVAANLSDLAAMGAT 83
Cdd:PRK05731 1 MAMGEFDLIARLFARRPSSRelgIGDDAALLGPPPGQRLVVSTDMLVEGVHFRPDWSSPEDLGYKALAVNLSDLAAMGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 84 PLGMTIALAMPGEVPLAWVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTGL 163
Cdd:PRK05731 81 PAAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTTRGPDLSISVTAIGDVPGGRALRRSGAKPGDLVAVTGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 164 HGASRLGLAILQEpslRGTVSSAEADRWRRAHQYPVPRLDVIEPLWQAIahtrcrsdIAAMDTSDGLADAIIQICRASGV 243
Cdd:PRK05731 161 LGDSAAGLALLLN---GLRVPDADAAALISRHLRPQPRVGLGQALAGLA--------SAAIDISDGLAADLGHIAEASGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 244 GAKVERERLRIPPEATAIVSPEQAITWVLYGGEDFELVLCLP---LAAAEELVQRLGGDAAIVGEVTSEPGVFlVDGreK 320
Cdd:PRK05731 230 GADIDLDALPISPALREAAEGEDALRWALSGGEDYELLFTFPpenRGALLAAAGHLGVGVTIIGRVTEGEGVV-VDG--E 306
|
330
....*....|..
gi 2331086371 321 KPLSLAQGFQHF 332
Cdd:PRK05731 307 PVTLDLKGYDHF 318
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
9-332 |
2.35e-120 |
|
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: 349.06 E-value: 2.35e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 9 VGEQGLLPLLFHFC---PPGVV---GDDAAVLAGLGTRsLVVTTDVLVEGVHFSDRTTPPDAVGWRAVAANLSDLAAMGA 82
Cdd:COG0611 1 MGEFGLIERLFKRLalrGPDVLlgiGDDAAVLDPPGGR-LVVTTDMLVEGVHFPLDWMSPEDLGWKAVAVNLSDLAAMGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 83 TPLGMTIALAMPGEVPLAWVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTG 162
Cdd:COG0611 80 RPLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPELTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 163 LHGASRLGLAILQEpslRGTVSSAEADRWRRAHQYPVPRLDviepLWQAIAHTRCRSdiAAMDTSDGLADAIIQICRASG 242
Cdd:COG0611 160 TLGDAAAGLALLLR---GLRVPLEAREYLLERHLRPEPRLA----LGRALAEAGLAT--AMIDISDGLAADLGHIAEASG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 243 VGAKVERERLRIPPEATAIVSPEQAITWVLYGGEDFELVLCLPLAAAEELVQRLGG-DAAIVGEVTSEPGVFLVDGREKK 321
Cdd:COG0611 231 VGAEIDLDALPLSPALREAALGLDPLELALTGGEDYELLFTVPPEALEALEAAALGvPLTVIGRVTEGEGVTLDDADGRP 310
|
330
....*....|.
gi 2331086371 322 PLSLAQGFQHF 332
Cdd:COG0611 311 IPLEARGWDHF 321
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
10-307 |
2.29e-107 |
|
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: 314.88 E-value: 2.29e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 10 GEQGLLPLLFHFCPPGV-----VGDDAAVLAGlGTRSLVVTTDVLVEGVHFsDRTTPPDAVGWRAVAANLSDLAAMGATP 84
Cdd:cd02194 1 GEFELIDRLFKRLGAGPgvllgIGDDAAVLKP-PGGRLVVTTDTLVEGVHF-PPDTTPEDIGWKALAVNLSDLAAMGARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 85 LGMTIALAMPGEVPLAWVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTGLH 164
Cdd:cd02194 79 LGFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 165 GASRLGLAILQEPslrGTVSSAEADRWRRAHQYPVPRLDVIEPLWQAIAHtrcrsdiAAMDTSDGLADAIIQICRASGVG 244
Cdd:cd02194 159 GDAAAGLALLLGG---LKLPEELYEELIERHLRPEPRLELGRALAEGLAT-------AMIDISDGLLADLGHIAEASGVG 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2331086371 245 AKVERERLRIPPEATAIVSPEQAITWVLYGGEDFELVLCLPLAAAEELVQRLGGDAAIVGEVT 307
Cdd:cd02194 229 AVIDLDKLPLSPALRAAELGEDALELALSGGEDYELLFTVPPENAEAAAAKLGVPVTVIGRVT 291
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
8-332 |
4.64e-94 |
|
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: 282.30 E-value: 4.64e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 8 DVGEQGLLPLLFHFCPPGVVGDDAAVLAGLGTRSLVVTTDVLVEGVHFsDRTTPPDAVGWRAVAANLSDLAAMGATPLGM 87
Cdd:TIGR01379 4 ELIDRILRRLVQDPDVALGIGDDAALVSAPEGRDLVLTTDTLVEGVHF-PPDTTPEDLGWKAVAVNLSDLAAMGATPKWF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 88 TIALAMPGEVPLAWVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTGLHGAS 167
Cdd:TIGR01379 83 LLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPELVVTVTAIGEAPKGRALLRSGAKPGDLVFVTGTLGDS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 168 RLGLAILQEPslRGTVSSAEADRWRRAHQYPVPRLDVIEPLwQAIAHtrcrsdiAAMDTSDGLADAIIQICRASGVGAKV 247
Cdd:TIGR01379 163 AAGLALLLKG--KKEPDEEDDEALLQRHLRPEPRVEEGLAL-AGYAN-------AAIDVSDGLAADLGHIAEASGVGIVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 248 ERERLRIPPEATAIVSPEQAITWVLYGGEDFELVLCLPLAAAEELVQRLGGDAAIVGEVTSEPGVFLVDGREKKPLSLAQ 327
Cdd:TIGR01379 233 DLDRLPLSSELAAWAEGKNPLEWALSGGEDYELVFTVPPERREALLDAAKGPLTRIGRVTEGEGVVLLADGKTVELLDRL 312
|
....*
gi 2331086371 328 GFQHF 332
Cdd:TIGR01379 313 GWQHF 317
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
26-315 |
4.10e-28 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 111.32 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 26 VVGDDAAVLAgLGTRSLVVTTDVLVegvhFSDRTTPPDAVGWRAVAANLSDLAAMGATPLGMTIALAMPGEVPLAWVEHF 105
Cdd:COG0309 28 VGGEDAAVLD-LGGGRLAFTTDSFV----VSPIFFPGGDIGKLAVHGTVNDLAVSGAKPLYLSVSLILEEGFPLEDLERI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 106 YRGMTACLQASGGAILGGDLSQSPVRS-----IAITALGQVDPDRVLRRSAAQKGDAIVVT---GLHG----ASRLGLAI 173
Cdd:COG0309 103 VESMAEAAREAGVSIVTGDTKVVERGGvdgpfINTTGIGVVPKGRLISPSGARPGDKIIVTggiGDHGtailAAREGLEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 174 LQEpslrgTVSSAEadrwrrahqypvPRLDVIEPLWQAiahtrCRSDIAAM-D-TSDGLADAIIQICRASGVGAKVERER 251
Cdd:COG0309 183 EGE-----LLSDAA------------PLNDLVSVLLEA-----APGGVHAMrDpTRGGLAGALNEIAEASGVGIEIDEDA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2331086371 252 LRIPPEATAIVSpeqaitwvLYGgedFE---------LVLCLPLAAAEELVQRL---GGDAAIVGEVTSEPGVFLV 315
Cdd:COG0309 241 IPVRPEVRGICE--------LLG---LDplylanegkLVAVVPPEDAEAVLEALrahGIDAAIIGEVTEGPPGRVV 305
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
29-141 |
8.44e-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: 8.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 29 DDAAVlaglgtrslVVTTD-----VLVEGVHFsdrttppdaVGWRAVAANLSDLAAMGATPLGMTIALAMPGEVPLAW-V 102
Cdd:pfam00586 1 DDAAV---------AVTTDghgtpSLVDPYHF---------PGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvL 62
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2331086371 103 EHFYRGMTACLQASGGAILGGDLSQSPVR---SIAITALGQV 141
Cdd:pfam00586 63 EEIVEGIAEACREAGVPLVGGDTSFDPEGgkpTISVTAVGIV 104
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
14-306 |
9.71e-22 |
|
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: 93.43 E-value: 9.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 14 LLPLLFHFCP----PGVVGDDAAVLAgLGTRSLVVTTDVLVEGVhfsdrttppDAVGWRAVAANLSDLAAMGATPLGMTI 89
Cdd:cd06061 14 ILKNLGADRDevlvGPGGGEDAAVVD-FGGKVLVVSTDPITGAG---------KDAGWLAVHIAANDIATSGARPRWLLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 90 ALAMPGEVPLAWVEHFYRGMTACLQASGGAILGGDLSQSPV--RSIA-ITALGQVDPDRVLRRSAAQKGDAIVVT---GL 163
Cdd:cd06061 84 TLLLPPGTDEEELKAIMREINEAAKELGVSIVGGHTEVTPGvtRPIIsVTAIGKGEKDKLVTPSGAKPGDDIVMTkgaGI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 164 HGASRlgLAILQEPSLRGTVSSAEADRWRRAHQYPVprldVIEPLWQAIAHtrcrsDIAAM-D-TSDGLADAIIQICRAS 241
Cdd:cd06061 164 EGTAI--LANDFEEELKKRLSEEELREAAKLFYKIS----VVKEALIAAEA-----GVTAMhDaTEGGILGALWEVAEAS 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2331086371 242 GVGAKVERERLRIPPEATAI-----VSPEQAItwvlygGEDFELVLClPLAAAEELVQRL---GGDAAIVGEV 306
Cdd:cd06061 233 GVGLRIEKDKIPIRQETKEIcealgIDPLRLI------SSGTLLITV-PPEKGDELVDALeeaGIPASVIGKI 298
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
41-305 |
1.72e-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: 85.53 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 41 SLVVTTDVLVEGVHFsdrttPPDAVGWRAVAANLSDLAAMGATPLGMTIALAMPGEVPLAWVEHFYRGMT-ACLQAsGGA 119
Cdd:cd00396 1 SLAMSTDGINPPLAI-----NPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAeACNQL-GVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 120 ILGGDLSQSPVR-----SIAITALGQVDPDRVLRRSAAQKGDAIVVTGlhgasrlglailqepslrgtvssaeadrwrra 194
Cdd:cd00396 75 IVGGHTSVSPGTmghklSLAVFAIGVVEKDRVIDSSGARPGDVLILTG-------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 195 hqypvprLDVIEPLWQAIahtrcrsDIAAM-DTSD-GLADAIIQICRASGVGAKVERERLRIPPEATAIVSpeQAITWVL 272
Cdd:cd00396 123 -------VDAVLELVAAG-------DVHAMhDITDgGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWLCV--EHIEEAL 186
|
250 260 270
....*....|....*....|....*....|....*.
gi 2331086371 273 YGGEDFELVLCLP---LAAAEELVQRLGGDAAIVGE 305
Cdd:cd00396 187 LFNSSGGLLIAVPaeeADAVLLLLNGNGIDAAVIGR 222
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
27-306 |
1.61e-16 |
|
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: 78.65 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 27 VGDDAAVLAGLGTRsLVVTTDVLVegvhfsdrTTPP-----DaVGWRAVAANLSDLAAMGATPLGMTIALAMPGEVPLAW 101
Cdd:cd02197 25 VLEDAAALLVGGGR-LAFTTDSFV--------VSPLffpggD-IGKLAVCGTVNDLAMMGAKPLYLSLGFILEEGFPLED 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 102 VEHFYRGMTACLQASGGAILGGDLSQSP---VRSIAI--TALGQVDPDRVLRRSAAQKGDAIVVTGL---HGAS----RL 169
Cdd:cd02197 95 LERIVKSMAEAAREAGVKIVTGDTKVVPkgkADGIFIntTGIGVIPRGVIISPSNIRPGDKIIVSGTigdHGAAilaaRE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 170 GLAIlqEPSLRGTVSsaeadrwrrahqypvPRLDVIEPLWQAIAHTRCRSDIaamdTSDGLADAIIQICRASGVGAKVER 249
Cdd:cd02197 175 GLGF--ETDIESDCA---------------PLNGLVEALLEAGPGIHAMRDP----TRGGLAAVLNEIARASGVGIEIEE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2331086371 250 ERLRIPPEATAIVSpeqaitwvLYGGEDFEL------VLCLPLAAAEELVQRL-----GGDAAIVGEV 306
Cdd:cd02197 234 EAIPVREEVRGACE--------MLGLDPLYLanegkfVAIVPPEDAEEVLEALrshplGKEAAIIGEV 293
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
27-323 |
3.33e-16 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 77.90 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 27 VGDDAAVLAgLGTRSLVVTTDVLVEGVHFSDrttpPDAVGWRAVAANLSDLAAMGATPLGMTIALAMPGEVPLAWVehfY 106
Cdd:COG2144 42 FGDDAAAIP-DGDGYLLLAAEGIWPKFVEAD----PWFAGYCSVLVNVSDIAAMGGRPLAVVDALWSSDEEAAAPV---L 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 107 RGMTACLQASGGAILGGDLS-QSPVRSIAITALGQVdpDRVLRRSAAQKGDAIVVtglhgasrlglAIlqepSLRGtvss 185
Cdd:COG2144 114 AGMRAASRKFGVPIVGGHTHpDTPYNALAVAILGRA--KKLLTSFTARPGDRLIA-----------AI----DLDG---- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 186 aeadRWRRAHqypvprldviePLWQAIAHT---RCRSDIAAMDT--SDGLADA------------IIQICRASGVGAKVE 248
Cdd:COG2144 173 ----RYHPPF-----------PYWDATTGKppeRLRAQLELLPElaEAGLVTAakdisnpgiigtLGMLLECSGVGATID 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2331086371 249 RERLRIPPEataiVSPEQaitWVL-YGGEDFelVLCLPLAAAEELVQRL---GGDAAIVGEVTSEPGVFLVDGREKKPL 323
Cdd:COG2144 238 LDAIPRPEG----VDLER---WLKaFPSFGF--LLTVPPENVDEVLARFaarGITAAVIGEVTDSRRLTLRDGGERATF 307
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
28-315 |
1.45e-15 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 76.27 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 28 GDDAAVLAGLGTRSLVVTTDvlvegvHFsdrtTP----PDAVGwRAVAAN-LSDLAAMGATPLgMTIA-LAMP-GEVPLA 100
Cdd:COG0709 47 SDDAAVYRLGDDQALVQTTD------FF----TPivddPYDFG-RIAAANaLSDVYAMGGRPL-TALAiVGFPiDKLPEE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 101 WVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTglhgaSRLGLailqepslr 180
Cdd:COG0709 115 VLAEILAGGADKCREAGAPLAGGHSIDDPEPKYGLAVTGLVHPDKVLRNAGARPGDVLILT-----KPLGT--------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 181 GTVSSAEadrwrrahqypvpRLDVIEPLWQAIAhtrcrsdIAAMDTSDGLADAIIQ---------------------ICR 239
Cdd:COG0709 181 GILTTAI-------------KAGLADGEDIAAA-------IASMTTLNKAAAELARlygvhactdvtgfgllghlleMAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 240 ASGVGAKVERERLRIPPEAT--------------------AIVSPEQAIT----WVLY-----GGedfeLVLCLPLAAAE 290
Cdd:COG0709 241 GSGVSAEIDLDAVPLLPGALelaeqgivpggtyrnrasygAKVEFAEGLDeaqrDLLFdpqtsGG----LLIAVPPEAAE 316
|
330 340
....*....|....*....|....*...
gi 2331086371 291 ELVQRL---GGDAAIVGEVTSEPGVFLV 315
Cdd:COG0709 317 ELLAALraaGYAAAIIGEVTAGEGGAIE 344
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
28-306 |
1.89e-14 |
|
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: 72.55 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 28 GDDAAVLAGLGTRSLVVTTDvlvegvHFsdrtTP----PDAVGwRAVAAN-LSDLAAMGATPLGMTIALAMP---GEVPL 99
Cdd:cd02195 41 GDDAAVYRLPGGLALVQTTD------FF----PPivddPYLFG-RIAAANaLSDIYAMGAKPLSALAIVTLPrklPALQE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 100 AWVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTGlhgasRLGLAILqepsl 179
Cdd:cd02195 110 EVLREILAGGKDKLREAGAVLVGGHTIEGPEPKYGLSVTGLVHPNKILRNSGAKPGDVLILTK-----PLGTGIL----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 180 rgtvsSAeADRWRRAHQYPVPR-LDVIEPLWQAIAHTRCRSDIAAM-D-TSDGLADAIIQICRASGVGAKVERErlRIPP 256
Cdd:cd02195 180 -----FA-AEMAGLARGEDIDAaLESMARLNRAAAELLRKYGAHACtDvTGFGLLGHLLEMARASGVSAEIDLD--KLPL 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2331086371 257 EATAivspeqaitwvlyGGedfeLVLCLPLAAAEELVQRL---GGDAAIVGEV 306
Cdd:cd02195 252 LQTS-------------GG----LLAAVPPEDAAALLALLkagGPPAAIIGEV 287
|
|
| selD |
TIGR00476 |
selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino ... |
27-252 |
6.88e-14 |
|
selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelD, known as selenophosphate synthetase, selenium donor protein, and selenide,water dikinase. SelD provides reduced selenium for the selenium transferase SelA. This protein itself contains selenocysteine in many species; any sequence scoring well but not aligning to the beginning of the model is likely to have a selenocysteine residue incorrectly interpreted as a stop codon upstream of the given sequence. The SelD protein also provides selenophosphate for the enzyme tRNA 2-selenouridine synthase, which catalyzes a tRNA base modification. It also contributes to selenium incorporation by selenium-dependent molybdenum hydroxylases (SDMH), in genomes with the marker TIGR03309. All genomes with SelD should make selenocysteine, selenouridine, SDMH, or some combination.
Pssm-ID: 273100 [Multi-domain] Cd Length: 301 Bit Score: 70.99 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 27 VGDDAAVLAGLGTRSLVVTTDvlvegvHFsdrttPP---DAVGW-RAVAAN-LSDLAAMGATPLGMTIALAMPGEV-PLA 100
Cdd:TIGR00476 41 TGDDAAVYKLNDGLALVSTTD------FF-----TPivdDPYDFgRIAATNaLSDIYAMGGTPLTALAILGWPRNKlPPE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 101 WVEHFYRGMTACLQASGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTGlhgasRLGLAILQePSLR 180
Cdd:TIGR00476 110 VLREILAGGADVCAEAGAPLAGGHSIDDPEPKYGLAVTGLVHPDKLKRNDGAQPGDVLILTK-----PLGVGVLT-AALK 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2331086371 181 GTVSSAEADRWRRAhqypvpRLDVIEPLWQAIAHTRcrsDIAAM-D-TSDGLADAIIQICRASGVGAKVERERL 252
Cdd:TIGR00476 184 KGGLAEEAYAAAIA------SMTTLNKQAAELAALA---GVHAMtDvTGFGLLGHLLEMCRGSGVSAEIDFDAV 248
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
23-259 |
1.82e-12 |
|
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: 66.47 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 23 PPGVVGDDAAVLAGLGTRSLVVTtdvlvEGVHFSDRTTPPDAVGWRAVAANLSDLAAMGATPLGMTIALAMPGEVPLAWV 102
Cdd:cd02192 30 VAADLGDDAAAIPDGDGYLLLAA-----DGIWPSLVEADPWWAGYCSVLVNVSDIAAMGGRPLAMVDALWSPSAEAAAQV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 103 ehfYRGMTACLQASGGAILGGDLS-QSPVRSIAITALGQVDPDrVLRRSAAQKGDAIVVtglhgASRLGLAILQEPSLR- 180
Cdd:cd02192 105 ---LEGMRDAAEKFGVPIVGGHTHpDSPYNALSVAILGRARKD-LLISFGAKPGDRLIL-----AIDLDGRVHPSPPPNw 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 181 GTVSSAEADRWRRahqypvpRLDVIEPLwqAIAHTRCrsdiAAMDTSD-GLADAIIQICRASGVGAKVERERLRIPPEAT 259
Cdd:cd02192 176 DATTMKSPALLRR-------QIALLPEL--AERGLVH----AAKDISNpGIIGTLGMLLEASGVGAEIDLDAIPRPEGVD 242
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
153-316 |
2.21e-10 |
|
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: 58.13 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 153 QKGDAIVVT---GLHGASRLGLAILQEPSLRGTVSSAEADRwRRAHQYPVPRLDVIEPLWQAIAHtrcrsdiaamDTSDG 229
Cdd:pfam02769 1 KPGDVLILLgssGLHGAGLSLSRKGLEDSGLAAVQLGDPLL-EPTLIYVKLLLAALGGLVKAMHD----------ITGGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 230 LADAIIQICRASGVGAKVErerLRIPPEATAIVSPEQAitwvLYGGEDFELVLCLP---LAAAEELVQRLGGDAAIVGEV 306
Cdd:pfam02769 70 LAGALAEMAPASGVGAEID---LDKVPIFEELMLPLEM----LLSENQGRGLVVVApeeAEAVLAILEKEGLEAAVIGEV 142
|
170
....*....|
gi 2331086371 307 TSEPGVFLVD 316
Cdd:pfam02769 143 TAGGRLTVIV 152
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
28-309 |
2.88e-10 |
|
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: 61.16 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 28 GDDAAVLA--GLGTRSLVVTTDVlvegvhfsdrtTP------PDAVGWRAVAANLSDLAAMGATPLGMTIAL--AMPGEV 97
Cdd:TIGR01736 417 GEDAAVLRikETGKLGLALTADC-----------NPryvyldPYAGAAGAVAEAYRNLAAVGAEPLAAVDCLnfGNPERP 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 98 PLAW-VEHFYRGMTACLQASGGAILGGDLS---QSPVRSIA----ITALGQV-DPDRVLRRSAAQKGDAIVVTGLHgasr 168
Cdd:TIGR01736 486 EVYWqFVEAVKGLGDACRALGTPVVGGNVSlynETNGVPIAptptIGMVGLVeDVEKLLTSNFKKEGDAIYLIGET---- 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 169 lglailqEPSLRGTVSSAEADRwRRAHQYPVPRLDVIEPLWQAIAHTRCRSDI-AAMDTSD-GLADAIIQICRASGVGAK 246
Cdd:TIGR01736 562 -------KDELGGSEYLRVIHG-IVSGQVPAVDLEEEKELADAVREAIRAGLVsAAHDVSRgGLAVALAEMAAASGIGAE 633
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2331086371 247 VERERLrippeataivsPEQAITWVLYGGEDFELVLCLPLAAAEELVQRLGGDAAIVGEVTSE 309
Cdd:TIGR01736 634 VDIDEI-----------ASARPDELLFSESNGRAIVAVPEEKAEEAVKSKGVPAKVIGKTGGD 685
|
|
| PRK00943 |
PRK00943 |
selenide, water dikinase SelD; |
29-308 |
2.41e-09 |
|
selenide, water dikinase SelD;
Pssm-ID: 234870 [Multi-domain] Cd Length: 347 Bit Score: 57.94 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 29 DDAAVLAGLGTRSLVVTTDVLVEGVhfSDrttpPDAVGwRAVAAN-LSDLAAMGATPLgMTIAL------AMPGEVPLAW 101
Cdd:PRK00943 50 DDAAVYDLNDGTGIISTTDFFMPIV--DD----PFDFG-RIAATNaISDIYAMGGKPI-MAIAIlgwpinKLPPEVAREV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 102 VEHfyrGMTACLQAsGGAILGGDLSQSPVRSIAITALGQVDPDRVLRRSAAQKGDAIVVTglhgaSRLGLAILqepslrg 181
Cdd:PRK00943 122 LEG---GRAACRQA-GIPLAGGHSIDAPEPIFGLAVTGVVPPERVKRNATAQAGDKLFLT-----KPLGIGIL------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 182 tvSSAEA-DRWRRAHQYpvprldvieplwQAIAHT----RCRSDIAAMD--------TSDGLADAIIQICRASGVGAKVE 248
Cdd:PRK00943 186 --TTAEKkSKLKPEHYG------------LAIEAMcqlnRPGADFAKLPgvhamtdvTGFGLLGHLLEMCQGAGLTARVD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 249 RERLRIPPEATAIVSpEQAIT------WVLYGGE--DFE----------------LVLCLPLAAAE--ELVQRLGGDAAI 302
Cdd:PRK00943 252 YAAVPLLPGVEEYIA-QGCVPggtgrnFASYGHLigELPdeqrallcdpqtsgglLVAVAPEAEAEvlAIAAEHGIELAA 330
|
....*.
gi 2331086371 303 VGEVTS 308
Cdd:PRK00943 331 IGELVE 336
|
|
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
28-324 |
6.49e-07 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 50.87 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 28 GDDAAVLAGLGT-RSLVVTTDVlvegvhfsdrtTP------PDAVGWRAVAANLSDLAAMGATPLGMTIAL--AMPgEVP 98
Cdd:PRK01213 427 GGDAAVLRIRGGgKGLALTTDC-----------NPryvyldPYEGAKLAVAEAARNLAAVGATPLAITDCLnfGNP-EKP 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 99 lawvEHFY------RGMT-AClQASGGAILGGDLS---QSPVRSI----AITALGQV-DPDRVLRRSAAQKGDAIVVTGL 163
Cdd:PRK01213 495 ----EVMWqfveavRGLAdAC-RALGTPVVGGNVSlynETGGTAIyptpVIGMVGLIdDVSKRTTSGFKKEGDLIYLLGE 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 164 HGASRLGLAILQEpsLRGTVssaeadrwrrAHQYPVPRLDVIEPLWQAIAHTRCRSDI-AAMDTSD-GLADAIIQICRAS 241
Cdd:PRK01213 570 TKDELGGSEYLKV--IHGHV----------GGRPPKVDLEAEKRLQELVREAIREGLVtSAHDVSEgGLAVALAEMAIAG 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 242 GVGAKVErerlrippeataiVSPEQAITWVLYgGEDFELVLCL----PLAAAEELVQRLGGDAAIVGEVTSepGVFLVDG 317
Cdd:PRK01213 638 GLGAEVD-------------LSDGLRPDALLF-SESQGRYVVSvppeNEEAFEALAEAAGVPATRIGVVGG--DALKVKG 701
|
....*..
gi 2331086371 318 REKKPLS 324
Cdd:PRK01213 702 NDTESLE 708
|
|
| PurM-like2 |
cd02691 |
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ... |
26-323 |
4.37e-06 |
|
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: 47.77 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 26 VVGDDAAVLAGLGTRSLVVTTDvlveGVHfSDRTTPPDAVGWRAVAANLSDLAAMGATPLGMT--IALAMPGEVplAWVE 103
Cdd:cd02691 33 VAQDDDAGVDAADVEYIVVAID----GIH-SRLSDFPFLAGFHATRAALRDVMVMGARPVALLsdIHLADDGDV--GKLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 104 HFYRGMTACLQASGGAIL-------GGDLSQSPVRSIAITALGQVDPDRvLRRSAAQKGDAIVVTGLHGAsrlglailqe 176
Cdd:cd02691 106 DFTAGVTAVSEATGVPLVagstlriGGDMVLGDRLVGGVGAVGRSKSDP-SRRKNAEPGDLILMTEGAGG---------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 177 pslrGTVSSAEAdrwrrAHQYPvprlDVIE--------PLWQAIAHTRCRSDIAAMD--TSDGLADAIIQICRASGVGAK 246
Cdd:cd02691 175 ----GTITTTAI-----YHGMP----DVVEetlnvdfiKACEALRDSGLVSKVHSMTdvTNGGIRGDALEISKTAGVSLV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 247 VERERLRippeatAIVSPEqaitwVLYGGEDFE----------LVLCLPLAAAEELVQRLGG---DAAIVGEVTSEPGVF 313
Cdd:cd02691 242 FDEEKVR------SLINPK-----VLKMLEELGidplgvsldsLMIIAPEEDAVDIIRTLREagvRADEVGRVEEGRGVP 310
|
330
....*....|
gi 2331086371 314 LVDGREKKPL 323
Cdd:cd02691 311 LVVTGEGREL 320
|
|
| PRK14105 |
PRK14105 |
selenide, water dikinase SelD; |
27-161 |
1.83e-05 |
|
selenide, water dikinase SelD;
Pssm-ID: 237611 [Multi-domain] Cd Length: 345 Bit Score: 45.92 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 27 VGDDAAVLAGLGTrSLVVTTDVlvegvhFSDRTTPPDAVGWRAVAANLSDLAAMGATP-LGMTIALAMPGEVPLAWVEHF 105
Cdd:PRK14105 46 LGDDAAVIIKNGL-AIVKTVDV------FTPIVDDPYIQGKIAACNSTSDVYAMGLSEiIGVLVILGIPPELPIEVAKEM 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2331086371 106 YRGMTACLQASGGAILGGDLSQSPVRSI--AITALGQvdPDRVLRRSAAQKGDAIVVT 161
Cdd:PRK14105 119 LQGFQDFCRENDTTIIGGHTILNPWPLIggAVTGVGK--EEDILTKAGAKEGDVLILT 174
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
63-307 |
6.83e-05 |
|
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: 44.00 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 63 DAVGWRAVAANLSDLAAMGATPLGM--TIALampGEVPLAWVEHFYRGMTACLQASGGAILGGDLSQSP--VRS----IA 134
Cdd:cd02196 43 DTIGIDLVAMCVNDILCQGAEPLFFldYIAT---GKLDPEVAAEIVKGIAEGCRQAGCALLGGETAEMPgvYAEgeydLA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 135 ITALGQVDPDRVLRRSAAQKGDAIV---VTGLH--GASrlgLA--ILQEPSLrgtvssaeadrwrrAHQYPVPRLD---- 203
Cdd:cd02196 120 GFAVGVVEKDKIIDGSKIKPGDVLIglpSSGLHsnGYS---LVrkILFEEGL--------------DYDDPEPGLGktlg 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 204 ------------VIEPLWQ-----AIAHtrcrsdIaamdTSDGLADAiiqICRA--SGVGAKVERERLRIPP-----EAT 259
Cdd:cd02196 183 eelltptriyvkPILPLLEkvlvkGMAH------I----TGGGLPEN---LPRVlpEGLGAVIDLGSWEIPPifkwiQKA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2331086371 260 AIVSPEQA-------ITWVLYGGEDFElvlclplAAAEELVQRLGGDAAIVGEVT 307
Cdd:cd02196 250 GNVSEEEMyrtfnmgIGMVLIVSEEDA-------DEVLEILEKLGEKAYVIGEVV 297
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
24-327 |
4.31e-03 |
|
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439816 [Multi-domain] Cd Length: 747 Bit Score: 38.88 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 24 PGVvgDDAAVLAGLGT-RSLVVTTDVlvegvhfsdrtTPP----DAV--GWRAVAANLSDLAAMGATPLGMTIAL----- 91
Cdd:COG0046 440 PGV--ADAAVVRVDGTyKGLAMSTGE-----------NPRyallDPYagARMAVAEAARNLAAVGAEPLAITDCLnwgnp 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 92 AMPGEvplAWveHFY---RGMT-AClQASGGAILGGDLS---QSPVRSIA------ITALGQV-DPDRVLRRSAAQKGDA 157
Cdd:COG0046 507 EKPEE---MA--QLVeavKGLAdAC-RALGIPVPSGNVSlynETKDGKVAipptpvIGAVGLVdDVRKTVTPDLKKEGDL 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 158 IVVTGlHGASRLGLAILQEpsLRGTVSSAeadrwrrahqypVPRLD------VIEPLWQAIAHTRCRsdiAAMDTSD-GL 230
Cdd:COG0046 581 LYLIG-ETKNELGGSEYAQ--VLGQLGGE------------PPDVDleaekaLFEAVQELIREGLIL---AAHDVSDgGL 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 231 ADAIIQICRASGVGAKVERERLRIPPEATAIVSPEQAitwvlyggedfELVLCLP---LAAAEELVQRLGGDAAIVGEVT 307
Cdd:COG0046 643 AVALAEMAFAGGLGADIDLDALGDLRPDAALFSESQG-----------RAVVQVApedAEAVEALLAEAGLPAHVIGTVT 711
|
330 340
....*....|....*....|.
gi 2331086371 308 SEPG-VFLVDGREKKPLSLAQ 327
Cdd:COG0046 712 GDDRlVIRRGGETLLSLSLAE 732
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
69-306 |
6.08e-03 |
|
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: 37.90 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 69 AVAANLSDLAAMGATPLGMTIAL----AMPGEVPLAwveHFYRGMTACLQAS---GGAILGGDLS---QSPVRSI----A 134
Cdd:cd02204 37 AVAEAVRNLVAVGADPLAITDCLnfgnPEKPEGEMG---QLVEAVLGLGDACralGTPVIGGKDSlynETEGVAIpptlV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 135 ITALGQVDPDRVLRRSAAQK-GDAIVVTGL----HGASRLGLAILQEPSlrGTVssaeadrwrrahqyPVPRLDVIEPLW 209
Cdd:cd02204 114 IGAVGVVDDVRKIVTLDFKKeGDLLYLIGEtkdeLGGSEYALAYHGLGG--GAP--------------PLVDLEREKALF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2331086371 210 QAIAHTRCRSDI-AAMDTSD-GLADAIIQICRASGVGAKVErerlrippeataiVSPEQAITWVLYgGEDFELVL--CLP 285
Cdd:cd02204 178 DAVQELIKEGLVlSAHDVSDgGLAVALAEMAFAGGLGAEVD-------------LSKDDAEDELLF-SESLGRVLveVKP 243
|
250 260
....*....|....*....|.
gi 2331086371 286 LAAAEELVQRLGGDAAIVGEV 306
Cdd:cd02204 244 ENEEVFEAEEAGVPATVIGTV 264
|
|
| |
