|
Name |
Accession |
Description |
Interval |
E-value |
| hypE |
TIGR02124 |
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ... |
26-345 |
2.48e-147 |
|
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein required for expression of catalytically active hydrogenase in many systems. It appears to be an accessory protein involved in maturation rather than a regulatory protein involved in expression. HypE shows considerable homology to the thiamine-monophosphate kinase ThiL (TIGR01379) and other enzymes.
Pssm-ID: 273984 [Multi-domain] Cd Length: 320 Bit Score: 418.20 E-value: 2.48e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 26 SRELV-ELIAEILGDTYLGTMEDSALLELPSRQIAFTTDSFVVTPLIFGNGDIGKIAVCGTVNDLAVSGARPLYLTLSLI 104
Cdd:TIGR02124 1 MQQLIqELFLKAFGNEILAAMEDAAVLELSGGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYLSCGFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 105 IEDGMPISELSAIIESVRDTAIAADVKIVAGDTKVVGKGEADRLFINTAGVGVIER-APVSIKNVRPGQKIILSGFIGNH 183
Cdd:TIGR02124 81 LEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSgIPISAHNLQPGDKIIVSGTIGDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 184 SIHLLSLREGLGFERNILSDCAPLNAMIHQLIDAVPagKIASMRDVTRGGLSAVLHEHARAAKHEMRCERQSLPIQPETA 263
Cdd:TIGR02124 161 GAAILAVREGLGFETNLESDCAPLNGLVETLLNAGP--AVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKEEVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 264 MAANMLGVDVINLANEGCLCLFVEPDSAEDVLRLLKTHPLGQKAAIIGEVLATPEVRVSMLEQDGTVSTIEELYGAELPR 343
Cdd:TIGR02124 239 GACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERKEGRVVLKTAYGGKRILDMPSGELLPR 318
|
..
gi 1476636193 344 LC 345
Cdd:TIGR02124 319 IC 320
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
21-313 |
1.59e-145 |
|
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: 412.61 E-value: 1.59e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 21 TGARLSRELVE-LIAEILGDTYLGTMEDSALLELPSRQIAFTTDSFVVTPLIFGNGDIGKIAVCGTVNDLAVSGARPLYL 99
Cdd:cd02197 1 SGGKLMQELIEeLFLKAFDNPILEVLEDAAALLVGGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDLAMMGAKPLYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 100 TLSLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTKVVGKGEADRLFINTAGVGVIER-APVSIKNVRPGQKIILSG 178
Cdd:cd02197 81 SLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIPRgVIISPSNIRPGDKIIVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 179 FIGNHSIHLLSLREGLGFERNILSDCAPLNAMIHQLIDAVPagKIASMRDVTRGGLSAVLHEHARAAKHEMRCERQSLPI 258
Cdd:cd02197 161 TIGDHGAAILAAREGLGFETDIESDCAPLNGLVEALLEAGP--GIHAMRDPTRGGLAAVLNEIARASGVGIEIEEEAIPV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1476636193 259 QPETAMAANMLGVDVINLANEGCLCLFVEPDSAEDVLRLLKTHPLGQKAAIIGEV 313
Cdd:cd02197 239 REEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRSHPLGKEAAIIGEV 293
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
17-345 |
9.71e-139 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 396.75 E-value: 9.71e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 17 LDHGTGARLSRELVE-LIAEILGDTYLGTMEDSALLELPSRQIAFTTDSFVVTPLIFGNGDIGKIAVCGTVNDLAVSGAR 95
Cdd:COG0309 1 LAHGSGGKLMRELIEeLFLPALGNEVLVGGEDAAVLDLGGGRLAFTTDSFVVSPIFFPGGDIGKLAVHGTVNDLAVSGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 96 PLYLTLSLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTKVVGKGEADRLFINTAGVGVIER-APVSIKNVRPGQKI 174
Cdd:COG0309 81 PLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGIGVVPKgRLISPSGARPGDKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 175 ILSGFIGNHSIHLLSLREGLGFERNILSDCAPLNAMIHQLIDAVPAGkIASMRDVTRGGLSAVLHEHARAAKHEMRCERQ 254
Cdd:COG0309 161 IVTGGIGDHGTAILAAREGLELEGELLSDAAPLNDLVSVLLEAAPGG-VHAMRDPTRGGLAGALNEIAEASGVGIEIDED 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 255 SLPIQPETAMAANMLGVDVINLANEGCLCLFVEPDSAEDVLRLLKTHplGQKAAIIGEVLATPEVRVSMLEQDGTVSTIE 334
Cdd:COG0309 240 AIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVLEALRAH--GIDAAIIGEVTEGPPGRVVLKTAIGGERILD 317
|
330
....*....|.
gi 1476636193 335 ELYGAELPRLC 345
Cdd:COG0309 318 PPEGDPLPRIC 328
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
58-158 |
3.56e-20 |
|
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: 84.03 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 58 IAFTTDSFVVTPLIFGNGDIGKIAVCGTVNDLAVSGARPLYLTLSLIIEDGMPISE-LSAIIESVRDTAIAADVKIVAGD 136
Cdd:pfam00586 5 VAVTTDGHGTPSLVDPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvLEEIVEGIAEACREAGVPLVGGD 84
|
90 100
....*....|....*....|..
gi 1476636193 137 TKVVgkGEADRLFINTAGVGVI 158
Cdd:pfam00586 85 TSFD--PEGGKPTISVTAVGIV 104
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
23-321 |
1.16e-15 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 76.41 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 23 ARLSRELVELIAEILGDtylgtmeDSALLELPS-RQIAFTTDSFV---------VTPLifgngDIGKIAVcgTVN--DLA 90
Cdd:PRK05731 10 ARLFARRPSSRELGIGD-------DAALLGPPPgQRLVVSTDMLVegvhfrpdwSSPE-----DLGYKAL--AVNlsDLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 91 VSGARPLYLTLSLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTKvvgkgEADRLFIN-TAgVG-VIERAPVSIKNV 168
Cdd:PRK05731 76 AMGARPAAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT-----RGPDLSISvTA-IGdVPGGRALRRSGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 169 RPGQKIILSGFIGNHSIHLLSLREGLGFERNILSDCapLNAMIH-QL-IDAVPA--GKIASMRDVTrGGLSAVLHEHARA 244
Cdd:PRK05731 150 KPGDLVAVTGTLGDSAAGLALLLNGLRVPDADAAAL--ISRHLRpQPrVGLGQAlaGLASAAIDIS-DGLAADLGHIAEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 245 AKHEMRCERQSLPIQPetAMAANMLGVDVINLAneGC------LCLFVEPDSAEDVLRLLKTHplGQKAAIIGEVLATPE 318
Cdd:PRK05731 227 SGVGADIDLDALPISP--ALREAAEGEDALRWA--LSggedyeLLFTFPPENRGALLAAAGHL--GVGVTIIGRVTEGEG 300
|
...
gi 1476636193 319 VRV 321
Cdd:PRK05731 301 VVV 303
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| hypE |
TIGR02124 |
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ... |
26-345 |
2.48e-147 |
|
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein required for expression of catalytically active hydrogenase in many systems. It appears to be an accessory protein involved in maturation rather than a regulatory protein involved in expression. HypE shows considerable homology to the thiamine-monophosphate kinase ThiL (TIGR01379) and other enzymes.
Pssm-ID: 273984 [Multi-domain] Cd Length: 320 Bit Score: 418.20 E-value: 2.48e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 26 SRELV-ELIAEILGDTYLGTMEDSALLELPSRQIAFTTDSFVVTPLIFGNGDIGKIAVCGTVNDLAVSGARPLYLTLSLI 104
Cdd:TIGR02124 1 MQQLIqELFLKAFGNEILAAMEDAAVLELSGGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYLSCGFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 105 IEDGMPISELSAIIESVRDTAIAADVKIVAGDTKVVGKGEADRLFINTAGVGVIER-APVSIKNVRPGQKIILSGFIGNH 183
Cdd:TIGR02124 81 LEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSgIPISAHNLQPGDKIIVSGTIGDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 184 SIHLLSLREGLGFERNILSDCAPLNAMIHQLIDAVPagKIASMRDVTRGGLSAVLHEHARAAKHEMRCERQSLPIQPETA 263
Cdd:TIGR02124 161 GAAILAVREGLGFETNLESDCAPLNGLVETLLNAGP--AVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKEEVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 264 MAANMLGVDVINLANEGCLCLFVEPDSAEDVLRLLKTHPLGQKAAIIGEVLATPEVRVSMLEQDGTVSTIEELYGAELPR 343
Cdd:TIGR02124 239 GACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERKEGRVVLKTAYGGKRILDMPSGELLPR 318
|
..
gi 1476636193 344 LC 345
Cdd:TIGR02124 319 IC 320
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
21-313 |
1.59e-145 |
|
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: 412.61 E-value: 1.59e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 21 TGARLSRELVE-LIAEILGDTYLGTMEDSALLELPSRQIAFTTDSFVVTPLIFGNGDIGKIAVCGTVNDLAVSGARPLYL 99
Cdd:cd02197 1 SGGKLMQELIEeLFLKAFDNPILEVLEDAAALLVGGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDLAMMGAKPLYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 100 TLSLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTKVVGKGEADRLFINTAGVGVIER-APVSIKNVRPGQKIILSG 178
Cdd:cd02197 81 SLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIPRgVIISPSNIRPGDKIIVSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 179 FIGNHSIHLLSLREGLGFERNILSDCAPLNAMIHQLIDAVPagKIASMRDVTRGGLSAVLHEHARAAKHEMRCERQSLPI 258
Cdd:cd02197 161 TIGDHGAAILAAREGLGFETDIESDCAPLNGLVEALLEAGP--GIHAMRDPTRGGLAAVLNEIARASGVGIEIEEEAIPV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1476636193 259 QPETAMAANMLGVDVINLANEGCLCLFVEPDSAEDVLRLLKTHPLGQKAAIIGEV 313
Cdd:cd02197 239 REEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRSHPLGKEAAIIGEV 293
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
17-345 |
9.71e-139 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 396.75 E-value: 9.71e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 17 LDHGTGARLSRELVE-LIAEILGDTYLGTMEDSALLELPSRQIAFTTDSFVVTPLIFGNGDIGKIAVCGTVNDLAVSGAR 95
Cdd:COG0309 1 LAHGSGGKLMRELIEeLFLPALGNEVLVGGEDAAVLDLGGGRLAFTTDSFVVSPIFFPGGDIGKLAVHGTVNDLAVSGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 96 PLYLTLSLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTKVVGKGEADRLFINTAGVGVIER-APVSIKNVRPGQKI 174
Cdd:COG0309 81 PLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGIGVVPKgRLISPSGARPGDKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 175 ILSGFIGNHSIHLLSLREGLGFERNILSDCAPLNAMIHQLIDAVPAGkIASMRDVTRGGLSAVLHEHARAAKHEMRCERQ 254
Cdd:COG0309 161 IVTGGIGDHGTAILAAREGLELEGELLSDAAPLNDLVSVLLEAAPGG-VHAMRDPTRGGLAGALNEIAEASGVGIEIDED 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 255 SLPIQPETAMAANMLGVDVINLANEGCLCLFVEPDSAEDVLRLLKTHplGQKAAIIGEVLATPEVRVSMLEQDGTVSTIE 334
Cdd:COG0309 240 AIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVLEALRAH--GIDAAIIGEVTEGPPGRVVLKTAIGGERILD 317
|
330
....*....|.
gi 1476636193 335 ELYGAELPRLC 345
Cdd:COG0309 318 PPEGDPLPRIC 328
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
35-313 |
4.83e-30 |
|
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: 116.16 E-value: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 35 EILGDTYLGtmEDSALLELPSRQIAFTTDsfvvtpLIFGNG-DIGKIAVCGTVNDLAVSGARPLYLTLSLIIEDGMPISE 113
Cdd:cd06061 24 EVLVGPGGG--EDAAVVDFGGKVLVVSTD------PITGAGkDAGWLAVHIAANDIATSGARPRWLLVTLLLPPGTDEEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 114 LSAIIESVRDTAIAADVKIVAGDTKVVGKgeADRLFINTAGVGVIERA-PVSIKNVRPGQKIILSGFIGNHSIHLLS--- 189
Cdd:cd06061 96 LKAIMREINEAAKELGVSIVGGHTEVTPG--VTRPIISVTAIGKGEKDkLVTPSGAKPGDDIVMTKGAGIEGTAILAndf 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 190 ---LREGLGfERNILSDCAPLNAMI--HQLIDAVPAGkIASMRDVTRGGLSAVLHEHARAAKHEMRCERQSLPIQPETAM 264
Cdd:cd06061 174 eeeLKKRLS-EEELREAAKLFYKISvvKEALIAAEAG-VTAMHDATEGGILGALWEVAEASGVGLRIEKDKIPIRQETKE 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1476636193 265 AANMLGVDVINLANEGCLCLFVEPDSAEDVLRLLKTHplGQKAAIIGEV 313
Cdd:cd06061 252 ICEALGIDPLRLISSGTLLITVPPEKGDELVDALEEA--GIPASVIGKI 298
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
58-312 |
5.70e-29 |
|
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: 111.33 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 58 IAFTTDSFVvTPLIFGNGDIGKIAVCGTVNDLAVSGARPLYLTLSLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDT 137
Cdd:cd00396 2 LAMSTDGIN-PPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAEACNQLGVPIVGGHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 138 KVVGKGEADRLFINTAGVGVIERAPV-SIKNVRPGQKIILSGfignhsihllslreglgfernilsdcapLNAMIHqlid 216
Cdd:cd00396 81 SVSPGTMGHKLSLAVFAIGVVEKDRViDSSGARPGDVLILTG----------------------------VDAVLE---- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 217 AVPAGKIASMRDVTRGGLSAVLHEHARAAKHEMRCERQSLPIQPETAMAANMLGVDVINLANEGCLCLFVEPDSAEDVLR 296
Cdd:cd00396 129 LVAAGDVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWLCVEHIEEALLFNSSGGLLIAVPAEEADAVLL 208
|
250
....*....|....*.
gi 1476636193 297 LLKTHplGQKAAIIGE 312
Cdd:cd00396 209 LLNGN--GIDAAVIGR 222
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
27-334 |
9.16e-23 |
|
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: 96.75 E-value: 9.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 27 RELVELIAEILG----DTYLGTMEDSALLELPSRQIAFTTDSFV---------VTPlifgnGDIGKIAVCGTVNDLAVSG 93
Cdd:COG0611 4 FGLIERLFKRLAlrgpDVLLGIGDDAAVLDPPGGRLVVTTDMLVegvhfpldwMSP-----EDLGWKAVAVNLSDLAAMG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 94 ARPLYLTLSLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTkvvgkGEADRLFINTAGVG-VIERAPVSIKNVRPGQ 172
Cdd:COG0611 79 ARPLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDT-----TRSPELTISVTAIGeVPGGRPLLRSGARPGD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 173 KIILSGFIGNHSIHLLSLREGLGFERNILSDCapLNAM------IHQLIDAVPAGKIASMRDVTrGGLSAVLHEHARAAK 246
Cdd:COG0611 154 LVYVTGTLGDAAAGLALLLRGLRVPLEAREYL--LERHlrpeprLALGRALAEAGLATAMIDIS-DGLAADLGHIAEASG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 247 HEMRCERQSLPIQPETAMAAnmLGVDVINLA-NEG---CLCLFVEPDSAEDVLRLLkthpLGQKAAIIGEVLATPEVRVs 322
Cdd:COG0611 231 VGAEIDLDALPLSPALREAA--LGLDPLELAlTGGedyELLFTVPPEALEALEAAA----LGVPLTVIGRVTEGEGVTL- 303
|
330
....*....|..
gi 1476636193 323 mLEQDGTVSTIE 334
Cdd:COG0611 304 -DDADGRPIPLE 314
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
58-158 |
3.56e-20 |
|
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: 84.03 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 58 IAFTTDSFVVTPLIFGNGDIGKIAVCGTVNDLAVSGARPLYLTLSLIIEDGMPISE-LSAIIESVRDTAIAADVKIVAGD 136
Cdd:pfam00586 5 VAVTTDGHGTPSLVDPYHFPGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvLEEIVEGIAEACREAGVPLVGGD 84
|
90 100
....*....|....*....|..
gi 1476636193 137 TKVVgkGEADRLFINTAGVGVI 158
Cdd:pfam00586 85 TSFD--PEGGKPTISVTAVGIV 104
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
31-313 |
9.08e-19 |
|
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: 84.91 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 31 ELIAEILG------DTYLGTMEDSALLELPSRQIAFTTDSFVVT---PLIFGNGDIGKIAVCGTVNDLAVSGARPLYLTL 101
Cdd:cd02194 4 ELIDRLFKrlgagpGVLLGIGDDAAVLKPPGGRLVVTTDTLVEGvhfPPDTTPEDIGWKALAVNLSDLAAMGARPLGFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 102 SLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTKvvgkgEADRLFINTAGVGVIER-APVSIKNVRPGQKIILSGFI 180
Cdd:cd02194 84 SLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTT-----SGSELVISVTALGEVEKgKPLRRSGAKPGDLLYVTGTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 181 GNHSIHLLSLREGLgferniLSDCAPLNAMIHQL------IDAVPA---GKIASMRDVTrGGLSAVLHEHARAAKHEMRC 251
Cdd:cd02194 159 GDAAAGLALLLGGL------KLPEELYEELIERHlrpeprLELGRAlaeGLATAMIDIS-DGLLADLGHIAEASGVGAVI 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1476636193 252 ERQSLPIQPEtaMAANMLGVDVINLANEG----CLCLFVEPDSAEDVLrllktHPLGQKAAIIGEV 313
Cdd:cd02194 232 DLDKLPLSPA--LRAAELGEDALELALSGgedyELLFTVPPENAEAAA-----AKLGVPVTVIGRV 290
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
169-321 |
2.94e-17 |
|
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: 77.77 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 169 RPGQKIILSGFIGNHSIHLLSLREGLGFER---NILSDCAPLNAMIH-QLIDAVPAGKIASMRDVTRGGLSAVLHEHARA 244
Cdd:pfam02769 1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSGlaaVQLGDPLLEPTLIYvKLLLAALGGLVKAMHDITGGGLAGALAEMAPA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1476636193 245 AKHEMRCERQSLPIqpetaMAANMLGVDVINLANEGCLCLFVEPDSAEDVLRLLKTHPLgqKAAIIGEVLATPEVRV 321
Cdd:pfam02769 81 SGVGAEIDLDKVPI-----FEELMLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGL--EAAVIGEVTAGGRLTV 150
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
23-332 |
3.54e-16 |
|
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: 78.14 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 23 ARLSRELVELIAEILGdtyLGtmEDSALLELP-SRQIAFTTDSFV--------VTPlifgnGDIGKIAVCGTVNDLAVSG 93
Cdd:TIGR01379 7 DRILRRLVQDPDVALG---IG--DDAALVSAPeGRDLVLTTDTLVegvhfppdTTP-----EDLGWKAVAVNLSDLAAMG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 94 ARPLYLTLSLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTKvvgkgEADRLFINTAGVGVIE-RAPVSIKNVRPGQ 172
Cdd:TIGR01379 77 ATPKWFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTV-----SSPELVVTVTAIGEAPkGRALLRSGAKPGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 173 KIILSGFIGNhSIHLLSLREGLGFERNILSDCAPLNAmiHQL----IDAVP--AGKIASMRDVTrGGLSAVLHEHARAAK 246
Cdd:TIGR01379 152 LVFVTGTLGD-SAAGLALLLKGKKEPDEEDDEALLQR--HLRpeprVEEGLalAGYANAAIDVS-DGLAADLGHIAEASG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 247 HEMRCERQSLPIQPEtaMAANMLGVDVINLANEGC----LCLFVEPDSAEDVLRLLKthplgQKAAIIGEVlaTPEVRVS 322
Cdd:TIGR01379 228 VGIVIDLDRLPLSSE--LAAWAEGKNPLEWALSGGedyeLVFTVPPERREALLDAAK-----GPLTRIGRV--TEGEGVV 298
|
330
....*....|
gi 1476636193 323 MLEQDGTVST 332
Cdd:TIGR01379 299 LLADGKTVEL 308
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
23-321 |
1.16e-15 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 76.41 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 23 ARLSRELVELIAEILGDtylgtmeDSALLELPS-RQIAFTTDSFV---------VTPLifgngDIGKIAVcgTVN--DLA 90
Cdd:PRK05731 10 ARLFARRPSSRELGIGD-------DAALLGPPPgQRLVVSTDMLVegvhfrpdwSSPE-----DLGYKAL--AVNlsDLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 91 VSGARPLYLTLSLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTKvvgkgEADRLFIN-TAgVG-VIERAPVSIKNV 168
Cdd:PRK05731 76 AMGARPAAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT-----RGPDLSISvTA-IGdVPGGRALRRSGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 169 RPGQKIILSGFIGNHSIHLLSLREGLGFERNILSDCapLNAMIH-QL-IDAVPA--GKIASMRDVTrGGLSAVLHEHARA 244
Cdd:PRK05731 150 KPGDLVAVTGTLGDSAAGLALLLNGLRVPDADAAAL--ISRHLRpQPrVGLGQAlaGLASAAIDIS-DGLAADLGHIAEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 245 AKHEMRCERQSLPIQPetAMAANMLGVDVINLAneGC------LCLFVEPDSAEDVLRLLKTHplGQKAAIIGEVLATPE 318
Cdd:PRK05731 227 SGVGADIDLDALPISP--ALREAAEGEDALRWA--LSggedyeLLFTFPPENRGALLAAAGHL--GVGVTIIGRVTEGEG 300
|
...
gi 1476636193 319 VRV 321
Cdd:PRK05731 301 VVV 303
|
|
| PurM-like2 |
cd02691 |
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ... |
85-313 |
6.45e-10 |
|
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: 59.71 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 85 TVNDLAVSGARPLYLTLSLIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTKVVGkGEA---DRLFINTAGVGVIERA 161
Cdd:cd02691 75 ALRDVMVMGARPVALLSDIHLADDGDVGKLFDFTAGVTAVSEATGVPLVAGSTLRIG-GDMvlgDRLVGGVGAVGRSKSD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 162 PVSIKNVRPGQKIILSGFIGNHSIHLLSLREGLgfeRNILSDCAPLNAM--IHQLIDAVPAGKIASMRDVTRGGLSAVLH 239
Cdd:cd02691 154 PSRRKNAEPGDLILMTEGAGGGTITTTAIYHGM---PDVVEETLNVDFIkaCEALRDSGLVSKVHSMTDVTNGGIRGDAL 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1476636193 240 EHARAAKHEMRCERQSL--PIQPETAMAANMLGVDVINLANEGcLCLFVEPDSAEDVLRLLKTHplGQKAAIIGEV 313
Cdd:cd02691 231 EISKTAGVSLVFDEEKVrsLINPKVLKMLEELGIDPLGVSLDS-LMIIAPEEDAVDIIRTLREA--GVRADEVGRV 303
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
80-313 |
4.60e-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: 53.63 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 80 IAVCgtVNDLAVSGARPL----YLTLSLIIEDgmpisELSAIIESVRDTAIAADVKIVAGDT----KVVGKGEADrlfin 151
Cdd:cd02196 50 VAMC--VNDILCQGAEPLffldYIATGKLDPE-----VAAEIVKGIAEGCRQAGCALLGGETaempGVYAEGEYD----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 152 TAG--VGVIERAPV-SIKNVRPGQKII-L--SGFignHS-----IHLLSLREGLGFERNILSDCAPL-NAMI-------H 212
Cdd:cd02196 118 LAGfaVGVVEKDKIiDGSKIKPGDVLIgLpsSGL---HSngyslVRKILFEEGLDYDDPEPGLGKTLgEELLtptriyvK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 213 QLIDAVPAGKIASMRDVTRGGLSA----VLHEHARAakhemRCERQSLPIQP------------ETAMAA--NMlGVdvi 274
Cdd:cd02196 195 PILPLLEKVLVKGMAHITGGGLPEnlprVLPEGLGA-----VIDLGSWEIPPifkwiqkagnvsEEEMYRtfNM-GI--- 265
|
250 260 270
....*....|....*....|....*....|....*....
gi 1476636193 275 nlaneGcLCLFVEPDSAEDVLRLLKTHplGQKAAIIGEV 313
Cdd:cd02196 266 -----G-MVLIVSEEDADEVLEILEKL--GEKAYVIGEV 296
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
19-313 |
2.16e-06 |
|
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: 48.67 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 19 HGTGARLSR-ELVELIAEILGDTY------LGTMEDSALLELPS-RQIAFTTD---SFVVTPLIFGngdigKIAVCGTVN 87
Cdd:cd02195 8 AGCGAKVGPgVLSQLLAGLPLPTDpnllvgLGTGDDAAVYRLPGgLALVQTTDffpPIVDDPYLFG-----RIAAANALS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 88 DLAVSGARPLY----LTLSlIIEDGMPISELSAIIESVRDTAIAADVKIVAGDTkvvgkGEADRLFINTAGVGVIERAPV 163
Cdd:cd02195 83 DIYAMGAKPLSalaiVTLP-RKLPALQEEVLREILAGGKDKLREAGAVLVGGHT-----IEGPEPKYGLSVTGLVHPNKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 164 SIKN-VRPGQKIILSGFIGNhSIHLLSLREGLGFERNILsdcAPLNAMI---HQLIDAVPAGKIASMRDVTRGGLSAVLH 239
Cdd:cd02195 157 LRNSgAKPGDVLILTKPLGT-GILFAAEMAGLARGEDID---AALESMArlnRAAAELLRKYGAHACTDVTGFGLLGHLL 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1476636193 240 EHARAAKHEMRCERQSLPIQpETAmaanmlgvdvinlaneGCLCLFVEPDSAEDVLRLLKThpLGQKAAIIGEV 313
Cdd:cd02195 233 EMARASGVSAEIDLDKLPLL-QTS----------------GGLLAAVPPEDAAALLALLKA--GGPPAAIIGEV 287
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
78-344 |
1.22e-04 |
|
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: 43.88 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 78 GKIAVCGTVNDLAVSGARPLYLTLSLI-------IEDGmpisELSAIIESVRDTAIAADVKIVAG------DTK------ 138
Cdd:COG0046 476 ARMAVAEAARNLAAVGAEPLAITDCLNwgnpekpEEMA----QLVEAVKGLADACRALGIPVPSGnvslynETKdgkvai 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 139 ----VVGkgeadrlfintaGVGVIE--RAPVSIKNVRPGQKIILsgfIGNHsihllslREGLG-----FERNILSDCAP- 206
Cdd:COG0046 552 pptpVIG------------AVGLVDdvRKTVTPDLKKEGDLLYL---IGET-------KNELGgseyaQVLGQLGGEPPd 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 207 -----LNAMIHQLIDAVPAGKIASMRDVTRGGLSAVLhehAraakhEMrcerqslpiqpetAMAANmLGVDvINLANEGC 281
Cdd:COG0046 610 vdleaEKALFEAVQELIREGLILAAHDVSDGGLAVAL---A-----EM-------------AFAGG-LGAD-IDLDALGD 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 282 L----CLF----------VEPDSAEDVLRLLKTHplGQKAAIIGEVLATPEVRVSMLEQ---DGTVSTIEELYGAELPRL 344
Cdd:COG0046 667 LrpdaALFsesqgravvqVAPEDAEAVEALLAEA--GLPAHVIGTVTGDDRLVIRRGGEtllSLSLAELRDAWEETLPRL 744
|
|
| PRK14105 |
PRK14105 |
selenide, water dikinase SelD; |
9-299 |
3.01e-04 |
|
selenide, water dikinase SelD;
Pssm-ID: 237611 [Multi-domain] Cd Length: 345 Bit Score: 42.07 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 9 MKPTDTVVLdHGTGARL-SRELVELIAEI-----LGDTYLGTMEDSALLELPSRQIAFTTDSFvvTPLIFGNGDIGKIAV 82
Cdd:PRK14105 6 IKLTEMVKL-HGUACKLpSTELENLVKGIileedLKHTKVGLGDDAAVIIKNGLAIVKTVDVF--TPIVDDPYIQGKIAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 83 CGTVNDLAVSGARPLYLTLSLI-IEDGMPISELSAIIESVRDTAIAADVKIVAGDT-----KVVGKGeadrlfinTAGVG 156
Cdd:PRK14105 83 CNSTSDVYAMGLSEIIGVLVILgIPPELPIEVAKEMLQGFQDFCRENDTTIIGGHTilnpwPLIGGA--------VTGVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 157 VIERApVSIKNVRPGQKIILSGFIGNHSIHLLSlREGLGFERNILSDCAPLNAMIHQLIDAVPAG--------------- 221
Cdd:PRK14105 155 KEEDI-LTKAGAKEGDVLILTKPLGTQSAMALS-RVPEEFEDLIDITKEEKEYIINKAIELMTTSnryallalreaeeev 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 222 --KIA-SMRDVTRGGLSAvlHEHARAAKHEMRCERQSLPIQPETAMAANMLG---VDVINLANEGCLCLFVEPDSAEDVL 295
Cdd:PRK14105 233 geKIAnAMTDVTGFGILG--HSQEMAEQSNVEIEISTLPVIKGTPELSSLFGhalLDGYGAETAGGLLISVKPEYKDKLI 310
|
....
gi 1476636193 296 RLLK 299
Cdd:PRK14105 311 DKLE 314
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
42-321 |
3.75e-04 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 41.98 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 42 LGTMEDSALLELPSRQ-IAFTTDSFvvTPLI---FgngDIGKIAVCGTVNDLAVSGARPLyLTLSLIiedGMPISELSA- 116
Cdd:COG0709 44 LETSDDAAVYRLGDDQaLVQTTDFF--TPIVddpY---DFGRIAAANALSDVYAMGGRPL-TALAIV---GFPIDKLPEe 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 117 ----IIESVRDTAIAADVKIVAGDTkvvgkGEADRLFINTAGVGVIERAPVsIKN--VRPGQKIILSGFIGNhsihllsl 190
Cdd:COG0709 115 vlaeILAGGADKCREAGAPLAGGHS-----IDDPEPKYGLAVTGLVHPDKV-LRNagARPGDVLILTKPLGT-------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 191 reGL---GFERNILSDcaplnAMIHQLIDAV-----PAGKIA------SMRDVTRGGLSAVLHEHARAAKHEMRCERQSL 256
Cdd:COG0709 181 --GIlttAIKAGLADG-----EDIAAAIASMttlnkAAAELArlygvhACTDVTGFGLLGHLLEMARGSGVSAEIDLDAV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 257 PIQPETAMAANMlGV-------------DVINLANE---------------GCLCLFVEPDSAEDVLRLLKTHplGQKAA 308
Cdd:COG0709 254 PLLPGALELAEQ-GIvpggtyrnrasygAKVEFAEGldeaqrdllfdpqtsGGLLIAVPPEAAEELLAALRAA--GYAAA 330
|
330
....*....|...
gi 1476636193 309 IIGEVLATPEVRV 321
Cdd:COG0709 331 IIGEVTAGEGGAI 343
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
78-244 |
7.86e-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: 37.51 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 78 GKIAVCGTVNDLAVSGARPLYLTLSL------IIEDGMpiSELSAIIESVRDTAIAADVKIVAGdtKVVGKGEADRLFIN 151
Cdd:cd02204 34 AALAVAEAVRNLVAVGADPLAITDCLnfgnpeKPEGEM--GQLVEAVLGLGDACRALGTPVIGG--KDSLYNETEGVAIP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 152 ----TAGVGVIE--RAPVSIKNVRPGQKIILSGFIGNHSIHLLSLREGLGFERNILS--DCAPLNAMIHQLIDAVPAGKI 223
Cdd:cd02204 110 ptlvIGAVGVVDdvRKIVTLDFKKEGDLLYLIGETKDELGGSEYALAYHGLGGGAPPlvDLEREKALFDAVQELIKEGLV 189
|
170 180
....*....|....*....|.
gi 1476636193 224 ASMRDVTRGGLSAVLHEHARA 244
Cdd:cd02204 190 LSAHDVSDGGLAVALAEMAFA 210
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
82-321 |
8.52e-03 |
|
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: 38.05 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 82 VCGTVNDLAVSGARPLYLTLSLI---IEDGMPISELSAIIESVRDTAIAADVKIVAGDTkvvgkgEADRLF-----INTA 153
Cdd:TIGR01736 94 VGGILRDILSMGARPIALLDSLRfgpLDDPKNRYLFEGVVAGISDYGNRIGVPTVGGEV------EFDESYngnplVNVM 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 154 GVGVIER-APVSIKNVRPGQKIILSGfignhsihLLSLREGLG---FERNILSDCAPLNA--------------MIHQLI 215
Cdd:TIGR01736 168 CVGLVRKdDIVTGKAKGPGNKLVLVG--------GKTGRDGIGgatFASEELSEEAEEEDrpavqvgdpfteklLIEATL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476636193 216 DAVPAGKIASMRDVTRGGLSAVLHEHARAAKHEMRCERQSLPIQPEtamaaNMLGVDVINLANEGCLCLFVEPDSAEDVL 295
Cdd:TIGR01736 240 EAVDTGLVKGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREP-----GMTPYEIMLSESQERMLLVVAPEDVEEVL 314
|
250 260
....*....|....*....|....*.
gi 1476636193 296 RLLKTHPLGqkAAIIGEVLATPEVRV 321
Cdd:TIGR01736 315 EIFEKYELP--ASVIGEVTDEGRIRL 338
|
|
| |
