|
Name |
Accession |
Description |
Interval |
E-value |
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
21-354 |
0e+00 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 518.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 21 MGHGAGGRAASQLIEELFLAAFDNEWLRQGDDGAVFTPPplppGARLVMATDGHVVSPLFFPGGDVGCLSVHGTVNDVAM 100
Cdd:COG0309 1 LAHGSGGKLMRELIEELFLPALGNEVLVGGEDAAVLDLG----GGRLAFTTDSFVVSPIFFPGGDIGKLAVHGTVNDLAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 101 SGATPLYLTASFVLEEGFALAELKRIVDSMARAAREAGVPVITGDTKVVERGKGDGVFISTTGLGVVAAGVHISGRNARP 180
Cdd:COG0309 77 SGAKPLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGIGVVPKGRLISPSGARP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 181 GDVLLLSGTLGEHGVAVLSQRESLAFETTITSDTAALHTLVAAMLAAAPGGVRVLRDPTRGGLATTLNEVARQSGVGMVL 260
Cdd:COG0309 157 GDKIIVTGGIGDHGTAILAAREGLELEGELLSDAAPLNDLVSVLLEAAPGGVHAMRDPTRGGLAGALNEIAEASGVGIEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 261 EEAAIPVLPQVDAACELLGLDPLYIANEGKLIAVCAPEAAEAVLAAMRAHplGQAAARIGEVCQDPQNFVQMNTRFGGRR 340
Cdd:COG0309 237 DEDAIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVLEALRAH--GIDAAIIGEVTEGPPGRVVLKTAIGGER 314
|
330
....*....|....
gi 2444578437 341 VVDWLSGEQLPRIC 354
Cdd:COG0309 315 ILDPPEGDPLPRIC 328
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
25-322 |
5.27e-175 |
|
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: 487.34 E-value: 5.27e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 25 AGGRAASQLIEELFLAAFDNEWLRQGDDGAVFtpppLPPGARLVMATDGHVVSPLFFPGGDVGCLSVHGTVNDVAMSGAT 104
Cdd:cd02197 1 SGGKLMQELIEELFLKAFDNPILEVLEDAAAL----LVGGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDLAMMGAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 105 PLYLTASFVLEEGFALAELKRIVDSMARAAREAGVPVITGDTKVVERGKGDGVFISTTGLGVVAAGVHISGRNARPGDVL 184
Cdd:cd02197 77 PLYLSLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIPRGVIISPSNIRPGDKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 185 LLSGTLGEHGVAVLSQRESLAFETTITSDTAALHTLVAAMLAAAPgGVRVLRDPTRGGLATTLNEVARQSGVGMVLEEAA 264
Cdd:cd02197 157 IVSGTIGDHGAAILAAREGLGFETDIESDCAPLNGLVEALLEAGP-GIHAMRDPTRGGLAAVLNEIARASGVGIEIEEEA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2444578437 265 IPVLPQVDAACELLGLDPLYIANEGKLIAVCAPEAAEAVLAAMRAHPLGQAAARIGEV 322
Cdd:cd02197 236 IPVREEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRSHPLGKEAAIIGEV 293
|
|
| hypE |
TIGR02124 |
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ... |
32-354 |
1.98e-170 |
|
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: 477.13 E-value: 1.98e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 32 QLIEELFLAAFDNEWLRQGDDGAVFTPPplppGARLVMATDGHVVSPLFFPGGDVGCLSVHGTVNDVAMSGATPLYLTAS 111
Cdd:TIGR02124 3 QLIQELFLKAFGNEILAAMEDAAVLELS----GGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYLSCG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 112 FVLEEGFALAELKRIVDSMARAAREAGVPVITGDTKVVERGKGDGVFISTTGLGVVAAGVHISGRNARPGDVLLLSGTLG 191
Cdd:TIGR02124 79 FILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPISAHNLQPGDKIIVSGTIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 192 EHGVAVLSQRESLAFETTITSDTAALHTLVAAMLAAAPgGVRVLRDPTRGGLATTLNEVARQSGVGMVLEEAAIPVLPQV 271
Cdd:TIGR02124 159 DHGAAILAVREGLGFETNLESDCAPLNGLVETLLNAGP-AVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKEEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 272 DAACELLGLDPLYIANEGKLIAVCAPEAAEAVLAAMRAHPLGQAAARIGEVCQDPQNFVQMNTRFGGRRVVDWLSGEQLP 351
Cdd:TIGR02124 238 KGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERKEGRVVLKTAYGGKRILDMPSGELLP 317
|
...
gi 2444578437 352 RIC 354
Cdd:TIGR02124 318 RIC 320
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
50-322 |
5.28e-53 |
|
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: 177.02 E-value: 5.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 50 GDDGAVFtpppLPPGARLVMATDghvvsPLFFPGGDVGCLSVHGTVNDVAMSGATPLYLTASFVLEEGFALAELKRIVDS 129
Cdd:cd06061 32 GEDAAVV----DFGGKVLVVSTD-----PITGAGKDAGWLAVHIAANDIATSGARPRWLLVTLLLPPGTDEEELKAIMRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 130 MARAAREAGVPVITGDTKVvergkGDGVF---ISTTGLGVVAAGVHISGRNARPGDVLLLSGTLGEHGVAVLSQRESLAF 206
Cdd:cd06061 103 INEAAKELGVSIVGGHTEV-----TPGVTrpiISVTAIGKGEKDKLVTPSGAKPGDDIVMTKGAGIEGTAILANDFEEEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 207 ETTITSDTAA-------LHTLVAAMLAAAPGGVRVLRDPTRGGLATTLNEVARQSGVGMVLEEAAIPVLPQVDAACELLG 279
Cdd:cd06061 178 KKRLSEEELReaaklfyKISVVKEALIAAEAGVTAMHDATEGGILGALWEVAEASGVGLRIEKDKIPIRQETKEICEALG 257
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2444578437 280 LDPLYIANEGKLIAVCAPEAAEAVLAAMRAHplGQAAARIGEV 322
Cdd:cd06061 258 IDPLRLISSGTLLITVPPEKGDELVDALEEA--GIPASVIGKI 298
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
67-321 |
2.99e-46 |
|
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: 157.17 E-value: 2.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 67 LVMATDGHVvSPLFFPGGDVGCLSVHGTVNDVAMSGATPLYLTASFVLEEGFALAELKRIVDSMARAAREAGVPVITGDT 146
Cdd:cd00396 2 LAMSTDGIN-PPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAEACNQLGVPIVGGHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 147 KVVERGKGDGVFISTTGLGVVAAGVHISGRNARPGDVLLLSGTLgehgvAVLSQRESlafettitsdtaalhtlvaamla 226
Cdd:cd00396 81 SVSPGTMGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTGVD-----AVLELVAA----------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 227 aapGGVRVLRDPTRGGLATTLNEVARQSGVGMVLEEAAIPVLPQVDAACELLGLDPLYIANEGKLIAVCAPEAAEAVLAA 306
Cdd:cd00396 133 ---GDVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWLCVEHIEEALLFNSSGGLLIAVPAEEADAVLLL 209
|
250
....*....|....*
gi 2444578437 307 MRAHplGQAAARIGE 321
Cdd:cd00396 210 LNGN--GIDAAVIGR 222
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
50-322 |
7.40e-36 |
|
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: 132.58 E-value: 7.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 50 GDDGAVFTPPplppGARLVMATDGHVVSPLFFPGG----DVGCLSVhgTVN--DVAMSGATPLYLTASFVLEEGFALAEL 123
Cdd:COG0611 26 GDDAAVLDPP----GGRLVVTTDMLVEGVHFPLDWmspeDLGWKAV--AVNlsDLAAMGARPLAALLSLALPPDTDVEWL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 124 KRIVDSMARAAREAGVPVITGDTkvverGKGDGVFISTTGLGVVAAGVHISGRNARPGDVLLLSGTLGE--HGVAVLSQR 201
Cdd:COG0611 100 EEFARGLAEAADRYGVDLVGGDT-----TRSPELTISVTAIGEVPGGRPLLRSGARPGDLVYVTGTLGDaaAGLALLLRG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 202 ESLAFEttitSDTAALHTL------VAAMLAAAPGGVRV----LRDptrgGLATTLNEVARQSGVGMVLEEAAIPVLPQV 271
Cdd:COG0611 175 LRVPLE----AREYLLERHlrpeprLALGRALAEAGLATamidISD----GLAADLGHIAEASGVGAEIDLDALPLSPAL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2444578437 272 DAACelLGLDPL-YIANEG---KLIAVCAPEAAEAVLAAMrahpLGQAAARIGEV 322
Cdd:COG0611 247 REAA--LGLDPLeLALTGGedyELLFTVPPEALEALEAAA----LGVPLTVIGRV 295
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
33-322 |
2.66e-32 |
|
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: 122.28 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 33 LIEELF--LAAFDNEWLRQGDDGAVFTPPplppGARLVMATDGHVVS---PLFFPGGDVGCLSVhgTVN--DVAMSGATP 105
Cdd:cd02194 5 LIDRLFkrLGAGPGVLLGIGDDAAVLKPP----GGRLVVTTDTLVEGvhfPPDTTPEDIGWKAL--AVNlsDLAAMGARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 106 LYLTASFVLEEGFALAELKRIVDSMARAAREAGVPVITGDTKvvergKGDGVFISTTGLGVVAAGVHISGRNARPGDVLL 185
Cdd:cd02194 79 LGFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTT-----SGSELVISVTALGEVEKGKPLRRSGAKPGDLLY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 186 LSGTLGEHGVAVLSQRESLAFETTITSDTAALHTLVAAMLAAAPGGVRVLR-------DptrgGLATTLNEVARQSGVGM 258
Cdd:cd02194 154 VTGTLGDAAAGLALLLGGLKLPEELYEELIERHLRPEPRLELGRALAEGLAtamidisD----GLLADLGHIAEASGVGA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2444578437 259 VLEEAAIPVLPQVDAacELLGLDPLYIANEG----KLIAVCAPEAAEAvlaamRAHPLGQAAARIGEV 322
Cdd:cd02194 230 VIDLDKLPLSPALRA--AELGEDALELALSGgedyELLFTVPPENAEA-----AAAKLGVPVTVIGRV 290
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
33-322 |
2.71e-30 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 117.63 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 33 LIEELFLAAFDNEWLRQGDDGAVFTPPPlppGARLVMATDGHVVSPLFFPGG----DVGCLSVhgTVN--DVAMSGATPL 106
Cdd:PRK05731 8 LIARLFARRPSSRELGIGDDAALLGPPP---GQRLVVSTDMLVEGVHFRPDWsspeDLGYKAL--AVNlsDLAAMGARPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 107 YLTASFVLEEGFALAELKRIVDSMARAAREAGVPVITGDTKvvergKGDGVFISTTGLGVVAAGVHISGRNARPGDVLLL 186
Cdd:PRK05731 83 AFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT-----RGPDLSISVTAIGDVPGGRALRRSGAKPGDLVAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 187 SGTLGEH--GVAVLSQRESLafettitsDTAALHTLVAAMLAAAP--GGVRVLRDPTRG------GLATTLNEVARQSGV 256
Cdd:PRK05731 158 TGTLGDSaaGLALLLNGLRV--------PDADAAALISRHLRPQPrvGLGQALAGLASAaidisdGLAADLGHIAEASGV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 257 GMVLEEAAIPVLPQVDAAceLLGLDPLYIANEG----KLIAVCAPEAAEAVLAAMRAHPLGqaAARIGEV 322
Cdd:PRK05731 230 GADIDLDALPISPALREA--AEGEDALRWALSGgedyELLFTFPPENRGALLAAAGHLGVG--VTIIGRV 295
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
29-330 |
7.10e-30 |
|
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: 116.28 E-value: 7.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 29 AASQLIEELFLAAF--DNEWLRQGDDGAVFTPPPlppGARLVMATDGHVVSPLFFPG---GDVGCLSVHGTVNDVAMSGA 103
Cdd:TIGR01379 1 GEFELIDRILRRLVqdPDVALGIGDDAALVSAPE---GRDLVLTTDTLVEGVHFPPDttpEDLGWKAVAVNLSDLAAMGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 104 TPLYLTASFVLEEGFALAELKRIVDSMARAAREAGVPVITGDTKvvergKGDGVFISTTGLGVVAAGVHISGRNARPGDV 183
Cdd:TIGR01379 78 TPKWFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTV-----SSPELVVTVTAIGEAPKGRALLRSGAKPGDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 184 LLLSGTLGEhGVAVLSQRESLAFETTITSDTAALHTL------VAAMLAAApGGVRVLRDPTrGGLATTLNEVARQSGVG 257
Cdd:TIGR01379 153 VFVTGTLGD-SAAGLALLLKGKKEPDEEDDEALLQRHlrpeprVEEGLALA-GYANAAIDVS-DGLAADLGHIAEASGVG 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2444578437 258 MVLEEAAIPVLPQVDAACEllGLDPLYIANEG----KLIAVCAPEAAEAVLAAMrahplGQAAARIGEVCQDPQNFV 330
Cdd:TIGR01379 230 IVIDLDRLPLSSELAAWAE--GKNPLEWALSGgedyELVFTVPPERREALLDAA-----KGPLTRIGRVTEGEGVVL 299
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
179-331 |
7.01e-29 |
|
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: 109.36 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 179 RPGDVLLLSGTLGEHGVAVLSQRESLAFETTIT---SDTAALHTLVAAM--LAAAPGGVRVLRDPTRGGLATTLNEVARQ 253
Cdd:pfam02769 1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSGLAAvqlGDPLLEPTLIYVKllLAALGGLVKAMHDITGGGLAGALAEMAPA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2444578437 254 SGVGMVLEEAAIPVLpqvdaaCEL-LGLDPLYIANEGKLIAVCAPEAAEAVLAAMRAHPLgqAAARIGEVCQDPQNFVQ 331
Cdd:pfam02769 81 SGVGAEIDLDKVPIF------EELmLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGL--EAAVIGEVTAGGRLTVI 151
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
67-167 |
1.20e-21 |
|
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: 88.27 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 67 LVMATDGH----VVSPLFFPGgdvgCLSVHGTVNDVAMSGATPLYLTASFVLEEGFALAE-LKRIVDSMARAAREAGVPV 141
Cdd:pfam00586 5 VAVTTDGHgtpsLVDPYHFPG----AKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvLEEIVEGIAEACREAGVPL 80
|
90 100
....*....|....*....|....*.
gi 2444578437 142 ITGDTKVVERgkGDGVFISTTGLGVV 167
Cdd:pfam00586 81 VGGDTSFDPE--GGKPTISVTAVGIV 104
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
31-322 |
1.21e-16 |
|
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: 79.10 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 31 SQLIEELFLAAFDNEW--LRQGDDGAVFtppPLPPGARLVMATDghvvsplFFPG-----GDVGCLSVHGTVNDV-AMsG 102
Cdd:cd02195 20 SQLLAGLPLPTDPNLLvgLGTGDDAAVY---RLPGGLALVQTTD-------FFPPivddpYLFGRIAAANALSDIyAM-G 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 103 ATPLYLTASFVL-EEGFALAE--LKRIVDSMARAAREAGVPVITGDTkvverGKGDGVFISTTGLGVVAAGVHISGRNAR 179
Cdd:cd02195 89 AKPLSALAIVTLpRKLPALQEevLREILAGGKDKLREAGAVLVGGHT-----IEGPEPKYGLSVTGLVHPNKILRNSGAK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 180 PGDVLLLSGTLGEhGVAVLSQRESLAFETTITsdtAALHTLV----AAMLAAAPGGVRVLRDPTRGGLATTLNEVARQSG 255
Cdd:cd02195 164 PGDVLILTKPLGT-GILFAAEMAGLARGEDID---AALESMArlnrAAAELLRKYGAHACTDVTGFGLLGHLLEMARASG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2444578437 256 VGMVLEEAAIPVLpQvdaacellgldplyiaNEGKLIAVCAPEAAEAVLAAMRAhpLGQAAARIGEV 322
Cdd:cd02195 240 VSAEIDLDKLPLL-Q----------------TSGGLLAAVPPEDAAALLALLKA--GGPPAAIIGEV 287
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
47-330 |
2.10e-10 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 61.24 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 47 LRQGDDGAVFTpppLPPGARLVMATDghvvsplFFPG-----GDVGCLSVHGTVNDV-AMsGATPLYLTASFvleeGF-- 118
Cdd:COG0709 44 LETSDDAAVYR---LGDDQALVQTTD-------FFTPivddpYDFGRIAAANALSDVyAM-GGRPLTALAIV----GFpi 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 119 -ALAE--LKRIVDSMARAAREAGVPVITGDTkvVErgkgDGVFI---STTGLgvvaagVHISG--RN--ARPGDVLLLSG 188
Cdd:COG0709 109 dKLPEevLAEILAGGADKCREAGAPLAGGHS--ID----DPEPKyglAVTGL------VHPDKvlRNagARPGDVLILTK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 189 TLGehgVAVLS--QRESLAFETTITSDTAALHTL--VAAMLAAAPGgVRVLRDPTRGGLATTLNEVARQSGVGMVLEEAA 264
Cdd:COG0709 177 PLG---TGILTtaIKAGLADGEDIAAAIASMTTLnkAAAELARLYG-VHACTDVTGFGLLGHLLEMARGSGVSAEIDLDA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 265 IPVLPQV-------------------------------DAACELL-------GLdplyianegkLIAVcAPEAAEAVLAA 306
Cdd:COG0709 253 VPLLPGAlelaeqgivpggtyrnrasygakvefaegldEAQRDLLfdpqtsgGL----------LIAV-PPEAAEELLAA 321
|
330 340
....*....|....*....|....
gi 2444578437 307 MRAHplGQAAARIGEVCQDPQNFV 330
Cdd:COG0709 322 LRAA--GYAAAIIGEVTAGEGGAI 343
|
|
| PurM-like2 |
cd02691 |
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ... |
94-350 |
4.48e-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: 60.10 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 94 TVNDVAMSGATPLYLTASFVLEEGfalAELKRIVDSMA--RAAREA-GVPVITGDTKvveRGKGDGVFISTTGLGVVAAG 170
Cdd:cd02691 75 ALRDVMVMGARPVALLSDIHLADD---GDVGKLFDFTAgvTAVSEAtGVPLVAGSTL---RIGGDMVLGDRLVGGVGAVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 171 VHISG----RNARPGDVLLLsgTLGEHG-----VAVLSQRESLAFETTITSDTAALHTLVAAMLAaapGGVRVLRDPTRG 241
Cdd:cd02691 149 RSKSDpsrrKNAEPGDLILM--TEGAGGgtittTAIYHGMPDVVEETLNVDFIKACEALRDSGLV---SKVHSMTDVTNG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 242 GLATTLNEVARQSGVGMVLEEAAIPVL--PQVDAACELLGLDPLYIANEGKLIaVCAPEAAEAVLAAMRAHPLGqaAARI 319
Cdd:cd02691 224 GIRGDALEISKTAGVSLVFDEEKVRSLinPKVLKMLEELGIDPLGVSLDSLMI-IAPEEDAVDIIRTLREAGVR--ADEV 300
|
250 260 270
....*....|....*....|....*....|.
gi 2444578437 320 GEVcqdpqnfvqmnTRFGGRRVVDWLSGEQL 350
Cdd:cd02691 301 GRV-----------EEGRGVPLVVTGEGREL 320
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
98-344 |
3.79e-08 |
|
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: 55.06 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 98 VAMSGATPLYLTASF-----VLEEGFAlaELKRIVDSMARAAREAGVPVITGdtKV---VERGKGDG-VFISTTglgVVA 168
Cdd:COG0046 487 LAAVGAEPLAITDCLnwgnpEKPEEMA--QLVEAVKGLADACRALGIPVPSG--NVslyNETKDGKVaIPPTPV---IGA 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 169 AGVHISGRNA------RPGDVL-LLSGTLGEHGVAVLSQRESLAFETTITSDTAALHTLVAAMLAAAPGGvRVL--RDPT 239
Cdd:COG0046 560 VGLVDDVRKTvtpdlkKEGDLLyLIGETKNELGGSEYAQVLGQLGGEPPDVDLEAEKALFEAVQELIREG-LILaaHDVS 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 240 RGGLATTLNEVARQSGVGMVLEeaaIPVLPQVDAACELLGLDPlyianeGKLIAVCAPEAAEAVLAAMRAHplGQAAARI 319
Cdd:COG0046 639 DGGLAVALAEMAFAGGLGADID---LDALGDLRPDAALFSESQ------GRAVVQVAPEDAEAVEALLAEA--GLPAHVI 707
|
250 260
....*....|....*....|....*
gi 2444578437 320 GEVCQDPqnfvQMNTRFGGRRVVDW 344
Cdd:COG0046 708 GTVTGDD----RLVIRRGGETLLSL 728
|
|
| PRK00943 |
PRK00943 |
selenide, water dikinase SelD; |
125-322 |
9.84e-08 |
|
selenide, water dikinase SelD;
Pssm-ID: 234870 [Multi-domain] Cd Length: 347 Bit Score: 52.93 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 125 RIVDSMARAAREAGVPVITGDT-KVVErgkgdGVFisttglGVVAAG-VHIS--GRN--ARPGDVLLLSGTLGehgVAVL 198
Cdd:PRK00943 120 EVLEGGRAACRQAGIPLAGGHSiDAPE-----PIF------GLAVTGvVPPErvKRNatAQAGDKLFLTKPLG---IGIL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 199 S--QRESLAFETTITSDTAALHTL--VAAMLAAAPGgVRVLRDPTRGGLATTLNEVARQSGVGMVLEEAAIPVLPQV--- 271
Cdd:PRK00943 186 TtaEKKSKLKPEHYGLAIEAMCQLnrPGADFAKLPG-VHAMTDVTGFGLLGHLLEMCQGAGLTARVDYAAVPLLPGVeey 264
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2444578437 272 --------------DAACELLG-LDPLYIA------NEGKLIAVCAPEAAEAVLAAMRAHplGQAAARIGEV 322
Cdd:PRK00943 265 iaqgcvpggtgrnfASYGHLIGeLPDEQRAllcdpqTSGGLLVAVAPEAEAEVLAIAAEH--GIELAAIGEL 334
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
50-321 |
1.26e-07 |
|
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: 52.21 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 50 GDDGAVftpppLP-PGARLVMATDGHV-----VSPLFfpggdVGCLSVHGTVNDVAMSGATPLYLTASFVLEEGFALAEl 123
Cdd:cd02192 35 GDDAAA-----IPdGDGYLLLAADGIWpslveADPWW-----AGYCSVLVNVSDIAAMGGRPLAMVDALWSPSAEAAAQ- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 124 krIVDSMARAAREAGVPVITGDTKV-VERGKgdgvfISTTGLGVvAAGVHISGRNARPGDVLLLSGTLGEHgvavLSQRE 202
Cdd:cd02192 104 --VLEGMRDAAEKFGVPIVGGHTHPdSPYNA-----LSVAILGR-ARKDLLISFGAKPGDRLILAIDLDGR----VHPSP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 203 SLAFETTITSDTAALHTLVAAMLAAAPGG-VRVLRDPTRGGLATTLNEVARQSGVGMVLEEAAIPVLPQVDAAcELLGLD 281
Cdd:cd02192 172 PPNWDATTMKSPALLRRQIALLPELAERGlVHAAKDISNPGIIGTLGMLLEASGVGAEIDLDAIPRPEGVDLE-RWLKCF 250
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2444578437 282 PLYianeGKLIAVcAPEAAEAVLAAMRAHPLgqAAARIGE 321
Cdd:cd02192 251 PGF----GFLLTA-RPENADEVVAVFAAVGI--TAAVIGE 283
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
67-185 |
3.94e-06 |
|
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: 47.85 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 67 LVMATDGhvvsplffpggdVGC-------LSVHGT---------VNDVAMSGATPLyltasFVLEEgFALAEL-----KR 125
Cdd:cd02196 22 LVSGTDG------------VGTklklaqeMGKHDTigidlvamcVNDILCQGAEPL-----FFLDY-IATGKLdpevaAE 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2444578437 126 IVDSMARAAREAGVPVITGDT----KVVERGKGDgvfISTTGLGVVAAGVHISGRNARPGDVLL 185
Cdd:cd02196 84 IVKGIAEGCRQAGCALLGGETaempGVYAEGEYD---LAGFAVGVVEKDKIIDGSKIKPGDVLI 144
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
98-322 |
6.85e-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: 43.68 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 98 VAMSGATPLYLTASfvLE------EGFALAELKRIVDSMARAAREAGVPVITG------DTKVVergkgdGVF----IST 161
Cdd:cd02204 45 LVAVGADPLAITDC--LNfgnpekPEGEMGQLVEAVLGLGDACRALGTPVIGGkdslynETEGV------AIPptlvIGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 162 TGLgVVAAGVHISGRNARPGDVLLLSGTLGEHgvavLSQRESLAFETTITSDTA-------------ALHTLVAAMLAAA 228
Cdd:cd02204 117 VGV-VDDVRKIVTLDFKKEGDLLYLIGETKDE----LGGSEYALAYHGLGGGAPplvdlerekalfdAVQELIKEGLVLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 229 pggvrvLRDPTRGGLATTLNEVARQSGVGMvleEAAIPVLPQVDAAceLLGLDPlyianeGKLIAVCAPEAAEAVLAAMR 308
Cdd:cd02204 192 ------AHDVSDGGLAVALAEMAFAGGLGA---EVDLSKDDAEDEL--LFSESL------GRVLVEVKPENEEVFEAEEA 254
|
250
....*....|....
gi 2444578437 309 AHPlgqaAARIGEV 322
Cdd:cd02204 255 GVP----ATVIGTV 264
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
71-310 |
8.17e-05 |
|
Formylglycinamide ribonucleotide amidotransferase (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: 100029 [Multi-domain] Cd Length: 272 Bit Score: 43.82 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 71 TDGHVVSPLFFPGGDVGclsVHGTVNDVAMSG--ATPLYLTASFVLEEGF--ALAELKRIVDSMARAAREAGVPVITGDT 146
Cdd:cd02193 9 EHNHPAAIDPAAGAATG---VGGAIRDIAATGidAKPIALSANWMASAGHpgEDAILYDAVKGVAELCNQLGLPIPVGKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 147 KV----------VERGKGDGVFISTTGLGVVAAGVHISGRNARPGDVLLL----SGTLGEHGVAVLSQRES---LAFETT 209
Cdd:cd02193 86 RMsmktrwqegnEQREMTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLLigggKGHNGLGGTALASVALSyrqLGDKSA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 210 ITSDTAALHTLVAAMLA-AAPGGVRVLRDPTRGGLATTLNEVARQSGVGMVLEEAAIPVLPQVDAACELLgldpLYIANE 288
Cdd:cd02193 166 QVRDPAQEKGFYEAMQAlVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAALGDDEPDMEPLEIA----LFESQE 241
|
250 260
....*....|....*....|..
gi 2444578437 289 GKLIAVcAPEAAEAVLAAMRAH 310
Cdd:cd02193 242 RGVIQV-RAEDRDAVEEAQYGL 262
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
47-322 |
5.70e-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: 41.90 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 47 LRQGDDGAVFTPPPLPPGArLVMATDG---HV-VSPlfFPGGDvgcLSVHGTVNDVAMSGATPLYLTASFVL---EEGFA 119
Cdd:TIGR01736 414 VKPGEDAAVLRIKETGKLG-LALTADCnprYVyLDP--YAGAA---GAVAEAYRNLAAVGAEPLAAVDCLNFgnpERPEV 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 120 LAELKRIVDSMARAAREAGVPVITGDTKVVERGKGDGVFISTT--GLGVVAAGVHI-SGRNARPGDVLLLSG-TLGEHGV 195
Cdd:TIGR01736 488 YWQFVEAVKGLGDACRALGTPVVGGNVSLYNETNGVPIAPTPTigMVGLVEDVEKLlTSNFKKEGDAIYLIGeTKDELGG 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 196 AVLSQR----ESLAFETTitsDTAALHTLVAAMLAAAPGG-VRVLRDPTRGGLATTLNEVARQSGVGMvleEAAIPVLPQ 270
Cdd:TIGR01736 568 SEYLRVihgiVSGQVPAV---DLEEEKELADAVREAIRAGlVSAAHDVSRGGLAVALAEMAAASGIGA---EVDIDEIAS 641
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2444578437 271 VDAACELLGLdplyiANEGKLIAVCAPEAAEAVLAamrahpLGQAAARIGEV 322
Cdd:TIGR01736 642 ARPDELLFSE-----SNGRAIVAVPEEKAEEAVKS------KGVPAKVIGKT 682
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
28-322 |
7.12e-04 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 40.92 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 28 RAASQLIEELFLAAFDNEWLRQGDDGAVFtppPLPPGArLVMATDGHV-----VSPLFfpggdVGCLSVHGTVNDVAMSG 102
Cdd:COG2144 21 RDIADVVRALGLASSGGTAAAFGDDAAAI---PDGDGY-LLLAAEGIWpkfveADPWF-----AGYCSVLVNVSDIAAMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 103 ATPLYLTASFvLEEGFALAELkrIVDSMARAAREAGVPVITGDTKVVERGKGDGVFIsttgLGVVAAgvHISGRNARPGD 182
Cdd:COG2144 92 GRPLAVVDAL-WSSDEEAAAP--VLAGMRAASRKFGVPIVGGHTHPDTPYNALAVAI----LGRAKK--LLTSFTARPGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 183 VLL----LSGTLGEHgvavlsqreSLAFETTITSDTAAL--HTLVAAMLAAApGGVRVLRDPTRGGLATTLNEVARQSGV 256
Cdd:COG2144 163 RLIaaidLDGRYHPP---------FPYWDATTGKPPERLraQLELLPELAEA-GLVTAAKDISNPGIIGTLGMLLECSGV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2444578437 257 GMVLEEAAIPVLPQVDAAcELLGLDPLYianeGKLIAVcAPEAAEAVLAAMRAHplGQAAARIGEV 322
Cdd:COG2144 233 GATIDLDAIPRPEGVDLE-RWLKAFPSF----GFLLTV-PPENVDEVLARFAAR--GITAAVIGEV 290
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
138-343 |
2.77e-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: 39.59 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 138 GVPVITGDTKVVERgkgdgvFISTTGLGVVAAGVH-----ISGRNARPGDVLLLSGTL----GEHGVAVLSqrESLAfET 208
Cdd:TIGR01736 144 GVPTVGGEVEFDES------YNGNPLVNVMCVGLVrkddiVTGKAKGPGNKLVLVGGKtgrdGIGGATFAS--EELS-EE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2444578437 209 TITSDTAALHT--------LVAAMLAAAP-GGVRVLRDPTRGGLATTLNEVARQSGVGMVLEEAAIPVLPQVDAACELLg 279
Cdd:TIGR01736 215 AEEEDRPAVQVgdpfteklLIEATLEAVDtGLVKGIKDLGAAGLTSASSEMAAKGGLGAEIYLDKVPLREPGMTPYEIM- 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2444578437 280 ldpLYIANEgKLIAVCAPEAAEAVLAAMRAHPLGqaAARIGEVCQDPqnfvQMNTRFGGRRVVD 343
Cdd:TIGR01736 294 ---LSESQE-RMLLVVAPEDVEEVLEIFEKYELP--ASVIGEVTDEG----RIRLYYKGEVVAD 347
|
|
| |
