|
Name |
Accession |
Description |
Interval |
E-value |
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
7-341 |
2.06e-145 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 413.31 E-value: 2.06e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 7 LAHGAGGRETGEIIEKFFVNLFKikrvgeGIGLDDLEDSATIPLsDGGHLAFTIDSYTVNPIFFPGGNIGKLAATGTIND 86
Cdd:COG0309 1 LAHGSGGKLMRELIEELFLPALG------NEVLVGGEDAAVLDL-GGGRLAFTTDSFVVSPIFFPGGDIGKLAVHGTVND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 87 LAVMGAKPLAAMDSMVIEEGFSIEDLEKILSSMKGVLEKYNIALIGGDFKVMPKDQVDKIVLTMAGIGLIPKGRLIKDSY 166
Cdd:COG0309 74 LAVSGAKPLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGIGVVPKGRLISPSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 167 VKPGDKIVVTGPIGEHGAAIMIAQAGLEAEApNIKSDCAPIIDAMEAAF--TIGGIHAAKDPTRGGLAMALNDWAKKAKV 244
Cdd:COG0309 154 ARPGDKIIVTGGIGDHGTAILAAREGLELEG-ELLSDAAPLNDLVSVLLeaAPGGVHAMRDPTRGGLAGALNEIAEASGV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 245 SIIIWEEKVPLREEVRIYSEMLGIDPFTLASEGIALIAVKQDKAEELVNKLKNMGyKKAEIIGEVRKEREGYVLVETISG 324
Cdd:COG0309 233 GIEIDEDAIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVLEALRAHG-IDAAIIGEVTEGPPGRVVLKTAIG 311
|
330
....*....|....*..
gi 1491196573 325 GLRILEPPVGEIVPRIC 341
Cdd:COG0309 312 GERILDPPEGDPLPRIC 328
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
11-309 |
2.98e-136 |
|
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: 388.73 E-value: 2.98e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 11 AGGRETGEIIEKFFVNLFKikrvgeGIGLDDLEDSATIPLsDGGHLAFTIDSYTVNPIFFPGGNIGKLAATGTINDLAVM 90
Cdd:cd02197 1 SGGKLMQELIEELFLKAFD------NPILEVLEDAAALLV-GGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDLAMM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 91 GAKPLAAMDSMVIEEGFSIEDLEKILSSMKGVLEKYNIALIGGDFKVMPKDQVDKIVLTMAGIGLIPKGRLIKDSYVKPG 170
Cdd:cd02197 74 GAKPLYLSLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIPRGVIISPSNIRPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 171 DKIVVTGPIGEHGAAIMIAQAGLEAEApNIKSDCAPIIDAMEAAF-TIGGIHAAKDPTRGGLAMALNDWAKKAKVSIIIW 249
Cdd:cd02197 154 DKIIVSGTIGDHGAAILAAREGLGFET-DIESDCAPLNGLVEALLeAGPGIHAMRDPTRGGLAAVLNEIARASGVGIEIE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196573 250 EEKVPLREEVRIYSEMLGIDPFTLASEGIALIAVKQDKAEELVNKLKNMGY-KKAEIIGEV 309
Cdd:cd02197 233 EEAIPVREEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRSHPLgKEAAIIGEV 293
|
|
| hypE |
TIGR02124 |
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ... |
16-341 |
3.02e-126 |
|
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: 364.65 E-value: 3.02e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 16 TGEIIEKFFVNLFKikrvgeGIGLDDLEDSATIPLSdGGHLAFTIDSYTVNPIFFPGGNIGKLAATGTINDLAVMGAKPL 95
Cdd:TIGR02124 1 MQQLIQELFLKAFG------NEILAAMEDAAVLELS-GGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 96 AAMDSMVIEEGFSIEDLEKILSSMKGVLEKYNIALIGGDFKVMPKDQVDKIVLTMAGIGLIPKGRLIKDSYVKPGDKIVV 175
Cdd:TIGR02124 74 YLSCGFILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPISAHNLQPGDKIIV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 176 TGPIGEHGAAIMIAQAGLEAEApNIKSDCAPIIDAMEAAFTIG-GIHAAKDPTRGGLAMALNDWAKKAKVSIIIWEEKVP 254
Cdd:TIGR02124 154 SGTIGDHGAAILAVREGLGFET-NLESDCAPLNGLVETLLNAGpAVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 255 LREEVRIYSEMLGIDPFTLASEGIALIAVKQDKAEELVNKLKNMGY-KKAEIIGEVRKEREGYVLVETISGGLRILEPPV 333
Cdd:TIGR02124 233 VKEEVKGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYgKDAAIIGEVVERKEGRVVLKTAYGGKRILDMPS 312
|
....*...
gi 1491196573 334 GEIVPRIC 341
Cdd:TIGR02124 313 GELLPRIC 320
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
15-309 |
8.89e-44 |
|
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: 152.37 E-value: 8.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 15 ETGEIIEKFFVNLFKI----KRVGEGIGLDDLEDSATIpLSDGGHLAFTIDsytvnPIFFPGGNIGKLAATGTINDLAVM 90
Cdd:cd06061 1 KIGKLPPEFLKRLILKnlgaDRDEVLVGPGGGEDAAVV-DFGGKVLVVSTD-----PITGAGKDAGWLAVHIAANDIATS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 91 GAKPLAAMDSMVIEEGFSIEDLEKILSSMKGVLEKYNIALIGGDFKVMPKdqVDKIVLTMAGIGLIPKGRLIKDSYVKPG 170
Cdd:cd06061 75 GARPRWLLVTLLLPPGTDEEELKAIMREINEAAKELGVSIVGGHTEVTPG--VTRPIISVTAIGKGEKDKLVTPSGAKPG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 171 DKIVVTGPIGEHGAAIMIAQAGLEAEAPNIKSD---CAPIIDAM----EAAFTIG-GIHAAKDPTRGGLAMALNDWAKKA 242
Cdd:cd06061 153 DDIVMTKGAGIEGTAILANDFEEELKKRLSEEElreAAKLFYKIsvvkEALIAAEaGVTAMHDATEGGILGALWEVAEAS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196573 243 KVSIIIWEEKVPLREEVRIYSEMLGIDPFTLASEGIALIAVKQDKAEELVNKLKNMGYkKAEIIGEV 309
Cdd:cd06061 233 GVGLRIEKDKIPIRQETKEICEALGIDPLRLISSGTLLITVPPEKGDELVDALEEAGI-PASVIGKI 298
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
55-305 |
1.41e-37 |
|
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: 134.06 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 55 HLAFTIDSYTVnPIFFPGGNIGKLAATGTINDLAVMGAKPLAAMDSMVIEEGFSIEDLEKILSSMKGVLEKYNIALIGGD 134
Cdd:cd00396 1 SLAMSTDGINP-PLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAEACNQLGVPIVGGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 135 FKVMPKDQVDKIVLTMAGIGLIPKGRLIKDSYVKPGDKIVVTGpigehgaaimiaqagleaeapniksdcapiIDAMEAA 214
Cdd:cd00396 80 TSVSPGTMGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTG------------------------------VDAVLEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 215 FTIGGIHAAKDPTRGGLAMALNDWAKKAKVSIIIWEEKVPLREEVRIYSEMLGIDPFTLASEGIALIAVKQDKAEELVNK 294
Cdd:cd00396 130 VAAGDVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWLCVEHIEEALLFNSSGGLLIAVPAEEADAVLLL 209
|
250
....*....|.
gi 1491196573 295 LKNMGYKKAEI 305
Cdd:cd00396 210 LNGNGIDAAVI 220
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
18-331 |
1.94e-32 |
|
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: 122.95 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 18 EIIEKFFvNLFKIKRVGEGIGLDDleDSATIPLSdGGHLAFTIDSYTVNPIFFPGG----NIGKLAATGTINDLAVMGAK 93
Cdd:COG0611 5 GLIERLF-KRLALRGPDVLLGIGD--DAAVLDPP-GGRLVVTTDMLVEGVHFPLDWmspeDLGWKAVAVNLSDLAAMGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 94 PLAAMDSMVIEEGFSIEDLEKILSSMKGVLEKYNIALIGGDFKVMPkdqvdKIVLTMAGIGLIPKGRLIKDSYVKPGDKI 173
Cdd:COG0611 81 PLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSP-----ELTISVTAIGEVPGGRPLLRSGARPGDLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 174 VVTGPIGEHGAAIMIAQAGLEAEAPNIKSDCA------PIIDAMEAAFTIGGIHAA---KDptrgGLAMALNDWAKKAKV 244
Cdd:COG0611 156 YVTGTLGDAAAGLALLLRGLRVPLEAREYLLErhlrpePRLALGRALAEAGLATAMidiSD----GLAADLGHIAEASGV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 245 SIIIWEEKVPLREEVRIYSemLGIDPFTLASEG----IALIAVKQDKAEELVNKLKNMGYKkaeIIGEVRKEREgyVLVE 320
Cdd:COG0611 232 GAEIDLDALPLSPALREAA--LGLDPLELALTGgedyELLFTVPPEALEALEAAALGVPLT---VIGRVTEGEG--VTLD 304
|
330
....*....|.
gi 1491196573 321 TISGGLRILEP 331
Cdd:COG0611 305 DADGRPIPLEA 315
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
18-260 |
1.88e-29 |
|
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: 115.12 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 18 EIIEKFFVNLFKIKRVGEGIGlddlEDSATIPLSDGGHLAFTIDSYTVNPIFFPG---GNIGKLAATGTINDLAVMGAKP 94
Cdd:TIGR01379 4 ELIDRILRRLVQDPDVALGIG----DDAALVSAPEGRDLVLTTDTLVEGVHFPPDttpEDLGWKAVAVNLSDLAAMGATP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 95 LAAMDSMVIEEGFSIEDLEKILSSMKGVLEKYNIALIGGDFkvmpkDQVDKIVLTMAGIGLIPKGRLIKDSYVKPGDKIV 174
Cdd:TIGR01379 80 KWFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDT-----VSSPELVVTVTAIGEAPKGRALLRSGAKPGDLVF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 175 VTGPIGEHGAAIMIAQAGLEAEAPNIKSDCA-------PIIDAMEAAftIGGIHAAKDPTrGGLAMALNDWAKKAKVSII 247
Cdd:TIGR01379 155 VTGTLGDSAAGLALLLKGKKEPDEEDDEALLqrhlrpePRVEEGLAL--AGYANAAIDVS-DGLAADLGHIAEASGVGIV 231
|
250
....*....|...
gi 1491196573 248 IWEEKVPLREEVR 260
Cdd:TIGR01379 232 IDLDRLPLSSELA 244
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
18-274 |
3.36e-29 |
|
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: 113.80 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 18 EIIEKFFVNLFKIKRVGEGIGlDDledsATIPLSDGGHLAFTIDSYTVNPIFFPG---GNIGKLAATGTINDLAVMGAKP 94
Cdd:cd02194 4 ELIDRLFKRLGAGPGVLLGIG-DD----AAVLKPPGGRLVVTTDTLVEGVHFPPDttpEDIGWKALAVNLSDLAAMGARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 95 LAAMDSMVIEEGFSIEDLEKILSSMKGVLEKYNIALIGGDFkvmpkDQVDKIVLTMAGIGLIPKGRLIKDSYVKPGDKIV 174
Cdd:cd02194 79 LGFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDT-----TSGSELVISVTALGEVEKGKPLRRSGAKPGDLLY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 175 VTGPIGEHGAAIMIAQAGL----EAEAPNIKSDCAPI--IDAMEAAfTIGGIHAAKDpTRGGLAMALNDWAKKAKVSIII 248
Cdd:cd02194 154 VTGTLGDAAAGLALLLGGLklpeELYEELIERHLRPEprLELGRAL-AEGLATAMID-ISDGLLADLGHIAEASGVGAVI 231
|
250 260
....*....|....*....|....*.
gi 1491196573 249 WEEKVPLREEVRiySEMLGIDPFTLA 274
Cdd:cd02194 232 DLDKLPLSPALR--AAELGEDALELA 255
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
168-319 |
1.57e-24 |
|
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: 97.42 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 168 KPGDKIVVTGPIGEHGAAIMIAQAGLEAEAPN--IKSDCA---PIIDAM-EAAFTIGGIHAAKDPTRGGLAMALNDWAKK 241
Cdd:pfam02769 1 KPGDVLILLGSSGLHGAGLSLSRKGLEDSGLAavQLGDPLlepTLIYVKlLLAALGGLVKAMHDITGGGLAGALAEMAPA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196573 242 AKVSIIIWEEKVPLREEVriyseMLGIDPFTLASEGIALIAVKQDKAEELVNKLKNMGYkKAEIIGEVRKEREGYVLV 319
Cdd:pfam02769 81 SGVGAEIDLDKVPIFEEL-----MLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGL-EAAVIGEVTAGGRLTVIV 152
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
18-314 |
3.45e-23 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 97.98 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 18 EIIEKFFVnlFKIKRVGEGIGldDleDSATIPLSDGGHLAFTIDSYTVNPIFFPGG----NIGKLAATGTINDLAVMGAK 93
Cdd:PRK05731 7 DLIARLFA--RRPSSRELGIG--D--DAALLGPPPGQRLVVSTDMLVEGVHFRPDWsspeDLGYKALAVNLSDLAAMGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 94 PLAAMDSMVIEEGFSIEDLEKILSSMKGVLEKYNIALIGGDFKvmpkdQVDKIVLTMAGIGLIPKGRLIKDSYVKPGDKI 173
Cdd:PRK05731 81 PAAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT-----RGPDLSISVTAIGDVPGGRALRRSGAKPGDLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 174 VVTGPIGEHGAAIMIAQAGLEAEAPniksDCAPIIDAME------AAFTI--GGIHAAKDpTRGGLAMALNDWAKKAKVS 245
Cdd:PRK05731 156 AVTGTLGDSAAGLALLLNGLRVPDA----DAAALISRHLrpqprvGLGQAlaGLASAAID-ISDGLAADLGHIAEASGVG 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196573 246 IIIWEEKVPLREEVRIYseMLGIDP--FTLAS-EGIALIA-VKQDKAEELVNKLKNMGyKKAEIIGEVRKERE 314
Cdd:PRK05731 231 ADIDLDALPISPALREA--AEGEDAlrWALSGgEDYELLFtFPPENRGALLAAAGHLG-VGVTIIGRVTEGEG 300
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
37-309 |
3.43e-20 |
|
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: 88.73 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 37 IGLDDLEDSATIPLSDGGHLAFTIDsytvnpiFFPGgnI-------GKLAATGTINDLAVMGAKPLAAMDSM---VIEEG 106
Cdd:cd02195 36 VGLGTGDDAAVYRLPGGLALVQTTD-------FFPP--IvddpylfGRIAAANALSDIYAMGAKPLSALAIVtlpRKLPA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 107 FSIEDLEKILSSMKGVLEKYNIALIGG----DfkvmpkdqvDKIVLTMAGIGLIPKGRLIKDSYVKPGDKIVVTGPIGEh 182
Cdd:cd02195 107 LQEEVLREILAGGKDKLREAGAVLVGGhtieG---------PEPKYGLSVTGLVHPNKILRNSGAKPGDVLILTKPLGT- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 183 G---AAIMIAQAGLEAEAPNIKSDCAPIIDAMEAAfTIGGIHAAKDPTRGGLAMALNDWAKKAKVSIIIWEEKVPLreev 259
Cdd:cd02195 177 GilfAAEMAGLARGEDIDAALESMARLNRAAAELL-RKYGAHACTDVTGFGLLGHLLEMARASGVSAEIDLDKLPL---- 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1491196573 260 riysemlgidpftLASEGIALIAVKQDKAEELVNKLKNmGYKKAEIIGEV 309
Cdd:cd02195 252 -------------LQTSGGLLAAVPPEDAAALLALLKA-GGPPAAIIGEV 287
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
37-320 |
7.12e-20 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 88.98 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 37 IGLDDLEDSATIPLSDGGHLAFTIDsytvnpiFFPGgnI-------GKLAATGTINDLAVMGAKPLAAMdSMVieeGFSI 109
Cdd:COG0709 42 VGLETSDDAAVYRLGDDQALVQTTD-------FFTP--IvddpydfGRIAAANALSDVYAMGGRPLTAL-AIV---GFPI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 110 EDL-EKILSS-MKGVLEK---YNIALIGG---DfkvmpkDQVDKIVLtmAGIGLIPKGRLIKDSYVKPGDKIVVTGPIGE 181
Cdd:COG0709 109 DKLpEEVLAEiLAGGADKcreAGAPLAGGhsiD------DPEPKYGL--AVTGLVHPDKVLRNAGARPGDVLILTKPLGT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 182 hG---AAIMIAQAGLEAEAPNIKSDCAPIIDAMEAAfTIGGIHAAKDPTRGGLA-----MalndwAKKAKVSIIIWEEKV 253
Cdd:COG0709 181 -GiltTAIKAGLADGEDIAAAIASMTTLNKAAAELA-RLYGVHACTDVTGFGLLghlleM-----ARGSGVSAEIDLDAV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 254 PLREEVRIYSEMlGIDP------------FTLASEGIA----------------LIAVKQDKAEELVNKLKNMGYkKAEI 305
Cdd:COG0709 254 PLLPGALELAEQ-GIVPggtyrnrasygaKVEFAEGLDeaqrdllfdpqtsgglLIAVPPEAAEELLAALRAAGY-AAAI 331
|
330
....*....|....*
gi 1491196573 306 IGEVRKEREGYVLVE 320
Cdd:COG0709 332 IGEVTAGEGGAIEVR 346
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
56-156 |
8.45e-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: 82.88 E-value: 8.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 56 LAFTIDS----YTVNPIFFPGgnigKLAATGTINDLAVMGAKPLAAMDSMVIEEGFSIED-LEKILSSMKGVLEKYNIAL 130
Cdd:pfam00586 5 VAVTTDGhgtpSLVDPYHFPG----AKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvLEEIVEGIAEACREAGVPL 80
|
90 100
....*....|....*....|....*.
gi 1491196573 131 IGGDFKVMPKDqvDKIVLTMAGIGLI 156
Cdd:pfam00586 81 VGGDTSFDPEG--GKPTISVTAVGIV 104
|
|
| PurM-like2 |
cd02691 |
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ... |
10-331 |
1.16e-13 |
|
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: 70.88 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 10 GAGGRETGEiiekFFVN--LFKI-KRVGEGIGLDDLeDSATIPLSDGGHLAFTIDSYTVNPIFFPGgNIGKLAATGTIND 86
Cdd:cd02691 5 GVGSRGEGD----FYVHekLAELiGKTGEVSIVAQD-DDAGVDAADVEYIVVAIDGIHSRLSDFPF-LAGFHATRAALRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 87 LAVMGAKPLAAM-DSMVIEEGfsieDLEKILSSMKGVL---EKYNIALIGGDFKVMPKDQV--DKIVLTMAGIGlIPKGR 160
Cdd:cd02691 79 VMVMGARPVALLsDIHLADDG----DVGKLFDFTAGVTavsEATGVPLVAGSTLRIGGDMVlgDRLVGGVGAVG-RSKSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 161 LIKDSYVKPGDKIVVTgpIGEHGA-----AIMIAQAGLEAEAPNIK--SDCAPIIDAMEaaftIGGIHAAKDPTRGGLAM 233
Cdd:cd02691 154 PSRRKNAEPGDLILMT--EGAGGGtitttAIYHGMPDVVEETLNVDfiKACEALRDSGL----VSKVHSMTDVTNGGIRG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 234 ALNDWAKKAKVSIIIWEEKV--PLREEVRIYSEMLGIDPFTLASEGIaLIAVKQDKAEELVNKLKNMGYkKAEIIGEVrK 311
Cdd:cd02691 228 DALEISKTAGVSLVFDEEKVrsLINPKVLKMLEELGIDPLGVSLDSL-MIIAPEEDAVDIIRTLREAGV-RADEVGRV-E 304
|
330 340
....*....|....*....|
gi 1491196573 312 EREGYVLVETISGglRILEP 331
Cdd:cd02691 305 EGRGVPLVVTGEG--RELKP 322
|
|
| PurL_repeat1 |
cd02203 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first repeat. ... |
55-313 |
1.19e-12 |
|
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), first 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: 100034 [Multi-domain] Cd Length: 313 Bit Score: 67.50 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 55 HLAFTIDSY----TVNPifFPGgnigklAATGT---INDLAVMGAKPLAAMDSMvieeGFS-----IEDLEKILSS---M 119
Cdd:cd02203 27 AVVFKVETHnhpsAIEP--FGG------AATGVggiIRDILSMGARPIALLDGL----RFGdldipGYEPKGKLSPrriL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 120 KGVLEKYN-------IALIGGDFKVMPKDQVDKIVLTMaGIGLIPKGRLIKDSYVKPGDKIVV----TGPIGEHGAA--- 185
Cdd:cd02203 95 DGVVAGISdygncigIPTVGGEVRFDPSYYGNPLVNVG-CVGIVPKDHIVKSKAPGPGDLVVLvggrTGRDGIGGATfss 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 186 IMIAQAGLEAEAPNIKSDCAP----IIDAMEAAFTIGGIHAAKDPTRGGLAMALNDWAKKAKVSIIIWEEKVPLREEvri 261
Cdd:cd02203 174 KELSENSSELDRPAVQVGDPFmekkLQEAILEARETGLIVGIQDLGAGGLSSAVSEMAAKGGLGAEIDLDKVPLREP--- 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196573 262 ysemlGIDPFTLAsegIA------LIAVKQDKAEELVNKLKNMGYkKAEIIGEVRKER 313
Cdd:cd02203 251 -----GMSPWEIW---ISesqermLLVVPPEDLEEFLAICKKEDL-EAAVIGEVTDDG 299
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
43-258 |
1.28e-11 |
|
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: 65.46 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 43 EDSATIPLSDGGHLAFTIDSY----TVNPifFPGgnigklAATGT---INDLAVMGAKPLAAMDSmvieegFSIEDLEKI 115
Cdd:COG0046 81 DNAGVVDIGDGLAVVFKVESHnhpsAIEP--YQG------AATGVggiIRDIFGMGARPIAGLDS------LRFGNLDQP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 116 LSSMKGVLEK-------YN----IALIGGDFKVMPkDQVDK-IVLTMaGIGLIPKGRLIKDSYVKPGDKIVV----TGPI 179
Cdd:COG0046 147 PASPRYILIGvvagiadYGncfgVPTVGGEVRFDE-SYEGNpLVNAG-GVGIIRADHIFKAKAPGVGNKVVYvggpTGRD 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 180 GEHGAAimIAQAGLEAEAPnikSDCA------PI-----IDAMEAAFTIGGIHAAKDPTRGGLAMALNDWAKKAKVSIII 248
Cdd:COG0046 225 GIGGAT--FASEELGEDSE---LDRPavqvgdPFmekrlIEAILELGDTGLIVGIQDMGAGGLSSASSEMAAKGGLGAEI 299
|
250
....*....|
gi 1491196573 249 WEEKVPLREE 258
Cdd:COG0046 300 DLDKVPLREP 309
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
22-320 |
2.88e-11 |
|
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: 64.63 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 22 KFFVNLFKIK--RVGEGIGlddlEDSATIPLSDGGHLAFTIDSYT----VNPIffpGGnigklAATGT---INDLAVMGA 92
Cdd:TIGR01736 39 KKLLKQFPTKgpNVIQGPG----EDAGVVDIGDGYAVVFKMESHNhpsaIEPY---NG-----AATGVggiLRDILSMGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 93 KPLAAMDSMVieegFSIEDLEKILSSMKGVLE-------KYNIALIGGDFKVMPKDQVDKIVLTMAgIGLIPKGRLIKDS 165
Cdd:TIGR01736 107 RPIALLDSLR----FGPLDDPKNRYLFEGVVAgisdygnRIGVPTVGGEVEFDESYNGNPLVNVMC-VGLVRKDDIVTGK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 166 YVKPGDKIVV----TGPIGEHGAAIMIAQAGLEAEAPNIKS----DC---APIIDAMEAAFTIGGIHAAKDPTRGGLAMA 234
Cdd:TIGR01736 182 AKGPGNKLVLvggkTGRDGIGGATFASEELSEEAEEEDRPAvqvgDPfteKLLIEATLEAVDTGLVKGIKDLGAAGLTSA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 235 LNDWAKKAKVSIIIWEEKVPLREEvriysEMLGIDPFTLASEGIALIAVKQDKAEELVNKLKNMGYkKAEIIGEVRKER- 313
Cdd:TIGR01736 262 SSEMAAKGGLGAEIYLDKVPLREP-----GMTPYEIMLSESQERMLLVVAPEDVEEVLEIFEKYEL-PASVIGEVTDEGr 335
|
330
....*....|..
gi 1491196573 314 -----EGYVLVE 320
Cdd:TIGR01736 336 irlyyKGEVVAD 347
|
|
| PRK00943 |
PRK00943 |
selenide, water dikinase SelD; |
76-322 |
1.01e-09 |
|
selenide, water dikinase SelD;
Pssm-ID: 234870 [Multi-domain] Cd Length: 347 Bit Score: 59.09 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 76 GKLAATGTINDLAVMGAKPLAAMdSMVieeGFSIEDL-----EKILSSMKGVLEKYNIALIGGDfkvmPKDQVDKIvLTM 150
Cdd:PRK00943 81 GRIAATNAISDIYAMGGKPIMAI-AIL---GWPINKLppevaREVLEGGRAACRQAGIPLAGGH----SIDAPEPI-FGL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 151 AGIGLIPKGRLIKDSYVKPGDKIVVTGPIgehGAAIMIA---QAGLEAEapniksDCAPIIDAMEAAFTIG-------GI 220
Cdd:PRK00943 152 AVTGVVPPERVKRNATAQAGDKLFLTKPL---GIGILTTaekKSKLKPE------HYGLAIEAMCQLNRPGadfaklpGV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 221 HAAKDPTRGGLAMALNDWAKKAKVSIIIWEEKVPLREEVRIYSEM---------------------------LGIDPFTl 273
Cdd:PRK00943 223 HAMTDVTGFGLLGHLLEMCQGAGLTARVDYAAVPLLPGVEEYIAQgcvpggtgrnfasyghligelpdeqraLLCDPQT- 301
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1491196573 274 aSEGIaLIAVKQDKAEELVNKLKNMGYkKAEIIGEVRKEREGYVLVETI 322
Cdd:PRK00943 302 -SGGL-LVAVAPEAEAEVLAIAAEHGI-ELAAIGELVEARGGRARVEVR 347
|
|
| PurM |
cd02196 |
PurM (Aminoimidazole Ribonucleotide [AIR] synthetase), one of eleven enzymes required for ... |
84-174 |
1.90e-07 |
|
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: 51.71 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 84 INDLAVMGAKPLAAMDSMVIEEGfsieDLEKILSSMKGVLE---KYNIALIGGDFKVMPkDQVDKIVLTMAG--IGLIPK 158
Cdd:cd02196 54 VNDILCQGAEPLFFLDYIATGKL----DPEVAAEIVKGIAEgcrQAGCALLGGETAEMP-GVYAEGEYDLAGfaVGVVEK 128
|
90
....*....|....*.
gi 1491196573 159 GRLIKDSYVKPGDKIV 174
Cdd:cd02196 129 DKIIDGSKIKPGDVLI 144
|
|
| PRK14090 |
PRK14090 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
44-312 |
2.10e-06 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 184499 [Multi-domain] Cd Length: 601 Bit Score: 49.47 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 44 DSATIPLSDGGHLAFTIDSYTvNPIFFPGGNIGKLAATGTINDLAVMGAKPLAAMDSMVIEegfsiEDLEKILSSMKGVL 123
Cdd:PRK14090 51 NAGVVNLDDYYSIAFKIESHN-HPSAIEPYNGAATGVGGIIRDVLAMGARPTAIFDSLHMS-----RIIDGIIEGIADYG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 124 EKYNIALIGGDFKVMPKDQVDKIVLTMAgIGLIPKGRLIKDSYVKPGDKIVV----TGPIGEHGAAimIAQAGLEAEAPN 199
Cdd:PRK14090 125 NSIGVPTVGGELRISSLYAHNPLVNVLA-AGVVRNDMLVDSKASRPGQVIVIfggaTGRDGIHGAS--FASEDLTGEKAT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 200 IKS-------DCAPIIDAMEAAFTIGGIHAAKDPTRGGLAMALNDWAKKAKVSIIIWEEKVPLREEVRIYSEMLgidpFT 272
Cdd:PRK14090 202 KLSiqvgdpfAEKMLIEAFLEMVEEGLVEGAQDLGAGGVLSATSELVAKGGLGAIVHLDRVPLREPDMEPWEIL----IS 277
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1491196573 273 LASEGIALIAVKQdKAEELVNKLKNMGYKKAeIIGEVRKE 312
Cdd:PRK14090 278 ESQERMAVVTSPE-KASRILEIAKKHLLFGD-IVAEVIDD 315
|
|
| PRK14105 |
PRK14105 |
selenide, water dikinase SelD; |
42-330 |
4.59e-06 |
|
selenide, water dikinase SelD;
Pssm-ID: 237611 [Multi-domain] Cd Length: 345 Bit Score: 47.85 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 42 LEDSATIPLSDGGHLAFTIDSYTvnPIFFPGGNIGKLAATGTINDLAVMGAKP-LAAMDSMVIEEGFSIEDLEKILSSMK 120
Cdd:PRK14105 46 LGDDAAVIIKNGLAIVKTVDVFT--PIVDDPYIQGKIAACNSTSDVYAMGLSEiIGVLVILGIPPELPIEVAKEMLQGFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 121 GVLEKYNIALIGGDFKVMPkdqVDKIVLTMAGIGliPKGRLIKDSYVKPGDKIVVTGPIGEHGAAIMI-------AQAGL 193
Cdd:PRK14105 124 DFCRENDTTIIGGHTILNP---WPLIGGAVTGVG--KEEDILTKAGAKEGDVLILTKPLGTQSAMALSrvpeefeDLIDI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 194 EAEAPNIKSDCApiIDAM------------EAAFTIG--GIHAAKDPTRGGLAMALNDWAKKAKVSIIIweEKVPLREEV 259
Cdd:PRK14105 199 TKEEKEYIINKA--IELMttsnryallalrEAEEEVGekIANAMTDVTGFGILGHSQEMAEQSNVEIEI--STLPVIKGT 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196573 260 RIYSEMLG---IDPFTLASEGIALIAVKQDKAEELVNKLKNMGYKKAEiIGEVRKEREGyvlVETISGGLRILE 330
Cdd:PRK14105 275 PELSSLFGhalLDGYGAETAGGLLISVKPEYKDKLIDKLEKNNVYAFE-VGKVVKNGVG---KAKLSENVKILE 344
|
|
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
149-309 |
5.04e-06 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 48.18 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 149 TMAGIGLIP-KGRLIKDSYVKPGDKIVVTGPIGEH--GAAIMIAQAGLEA---EAPNIKSDCApIIDAMEAAFTIGGIHA 222
Cdd:PRK01213 539 VIGMVGLIDdVSKRTTSGFKKEGDLIYLLGETKDElgGSEYLKVIHGHVGgrpPKVDLEAEKR-LQELVREAIREGLVTS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 223 AKDPTRGGLAMALNDWAKK----AKVSIiiweeKVPLREEVRIYSEmlgidpftlaSEGIALIAVKQDKAEELVNKLKNM 298
Cdd:PRK01213 618 AHDVSEGGLAVALAEMAIAgglgAEVDL-----SDGLRPDALLFSE----------SQGRYVVSVPPENEEAFEALAEAA 682
|
170
....*....|.
gi 1491196573 299 GYkKAEIIGEV 309
Cdd:PRK01213 683 GV-PATRIGVV 692
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
87-309 |
5.68e-06 |
|
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: 47.14 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 87 LAVMGAKPLAAMDSMvieEGFSIEDLEKILSSMKGVLE-------KYNIALIGG------DFK---VMPkdqvdkiVLTM 150
Cdd:cd02204 45 LVAVGADPLAITDCL---NFGNPEKPEGEMGQLVEAVLglgdacrALGTPVIGGkdslynETEgvaIPP-------TLVI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 151 AGIGLIPKGRLIKDSYVK-PGDKIVVTGPIGEHgaaimIAQAGLEAEAPNIKSDCAPIIDAMEAAFTIGGIH-------- 221
Cdd:cd02204 115 GAVGVVDDVRKIVTLDFKkEGDLLYLIGETKDE-----LGGSEYALAYHGLGGGAPPLVDLEREKALFDAVQelikeglv 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 222 -AAKDPTRGGLAMALNDWAKKAKVSIIIwEEKVPLREEVRIYSEMLgidpftlaseGIALIAVKQDKAEELVNKLKNMGY 300
Cdd:cd02204 190 lSAHDVSDGGLAVALAEMAFAGGLGAEV-DLSKDDAEDELLFSESL----------GRVLVEVKPENEEVFEAEEAGVPA 258
|
....*....
gi 1491196573 301 KKaeiIGEV 309
Cdd:cd02204 259 TV---IGTV 264
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
43-313 |
6.73e-06 |
|
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: 47.68 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 43 EDSATIPL--SDGGHLAFTIDSytvNPIF-----FPGGnigKLAATGTINDLAVMGAKPLAAMDSMVI-----EEGFSie 110
Cdd:TIGR01736 418 EDAAVLRIkeTGKLGLALTADC---NPRYvyldpYAGA---AGAVAEAYRNLAAVGAEPLAAVDCLNFgnperPEVYW-- 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 111 DLEKILSSMKGVLEKYNIALIGGdfKVMPKDQVDKIVL----TMAGIGLIPK-GRLIKDSYVKPGDKIVVTGPIGEH--G 183
Cdd:TIGR01736 490 QFVEAVKGLGDACRALGTPVVGG--NVSLYNETNGVPIaptpTIGMVGLVEDvEKLLTSNFKKEGDAIYLIGETKDElgG 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 184 AAIMIAQAGLEA-EAPNIKSDCAP-IIDAMEAAFTIGGIHAAKDPTRGGLAMALNDWAKKAKVSIIIWEEKVP-LREEVR 260
Cdd:TIGR01736 568 SEYLRVIHGIVSgQVPAVDLEEEKeLADAVREAIRAGLVSAAHDVSRGGLAVALAEMAAASGIGAEVDIDEIAsARPDEL 647
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1491196573 261 IYSEmlgidpftlaSEGIALIAVKQDKAEELVNKLKNmgykKAEIIGEVRKER 313
Cdd:TIGR01736 648 LFSE----------SNGRAIVAVPEEKAEEAVKSKGV----PAKVIGKTGGDR 686
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
84-259 |
1.12e-05 |
|
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: 46.44 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 84 INDLAVMGAKPLAAMDSMVIEegfSIEDLEKILSSMKGVLEKYNIALIGGdfKVMPKDQVDKIVLTMAGIGlipKGRLIK 163
Cdd:cd02192 76 VSDIAAMGGRPLAMVDALWSP---SAEAAAQVLEGMRDAAEKFGVPIVGG--HTHPDSPYNALSVAILGRA---RKDLLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 164 DSYVKPGDKIVVT-----GPIGEHG----AAIMIAQAGLEAEapniksdcapiIDAMEAAFTIGGIHAAKDPTRGGLAMA 234
Cdd:cd02192 148 SFGAKPGDRLILAidldgRVHPSPPpnwdATTMKSPALLRRQ-----------IALLPELAERGLVHAAKDISNPGIIGT 216
|
170 180
....*....|....*....|....*
gi 1491196573 235 LNDWAKKAKVSIIIWEEKVPLREEV 259
Cdd:cd02192 217 LGMLLEASGVGAEIDLDAIPRPEGV 241
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
44-314 |
1.12e-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: 40.80 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 44 DSATIPLSDGGH-LAFTIDsytVNPIF----FPGGniGKLAATGTINDLAVMGAKPLAAMDS---MVIEEgfSIED--LE 113
Cdd:COG0046 444 DAAVVRVDGTYKgLAMSTG---ENPRYalldPYAG--ARMAVAEAARNLAAVGAEPLAITDClnwGNPEK--PEEMaqLV 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 114 KILSSMKGVLEKYNIALIGGdfKV-MPKDQVDKIV-----LTMAGIGLIPKGRLIKDSYVK-PGDKIVVtgpIGEHGA-- 184
Cdd:COG0046 517 EAVKGLADACRALGIPVPSG--NVsLYNETKDGKVaipptPVIGAVGLVDDVRKTVTPDLKkEGDLLYL---IGETKNel 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 185 -----AIMIAQAGLEAEAPNIKSDCApIIDAMEAAFTIGGIHAAKDPTRGGLAMALNDWAKKAKVSIIIW-EEKVPLREE 258
Cdd:COG0046 592 ggseyAQVLGQLGGEPPDVDLEAEKA-LFEAVQELIREGLILAAHDVSDGGLAVALAEMAFAGGLGADIDlDALGDLRPD 670
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196573 259 VRIYSEmlgidpftlaSEGIALIAVKQDKAEELVNKLKNMGYkKAEIIGEVRKERE 314
Cdd:COG0046 671 AALFSE----------SQGRAVVQVAPEDAEAVEALLAEAGL-PAHVIGTVTGDDR 715
|
|
| PurL |
cd02193 |
Formylglycinamide ribonucleotide amidotransferase (FGAR-AT) catalyzes the ATP-dependent ... |
72-257 |
5.20e-03 |
|
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: 38.05 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 72 GGNIGKLAATGtindlavMGAKPLAAMDSMVIEEGFSIEDlEKILSSMKGVLE---KYNIALIGGDFKVMPK-------- 140
Cdd:cd02193 27 GGAIRDIAATG-------IDAKPIALSANWMASAGHPGED-AILYDAVKGVAElcnQLGLPIPVGKDRMSMKtrwqegne 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 141 --DQVDKIVLTMAGIGLIPKGRLIKDSYVKPGDKIVV----TGPIGEHGAAI-MIAQAGLEAEAPNIKSD----CAPIID 209
Cdd:cd02193 99 qrEMTHPPSLVISAFGRVRDDRHTLPQLSTEGNALLLigggKGHNGLGGTALaSVALSYRQLGDKSAQVRdpaqEKGFYE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1491196573 210 AMEAAFTIGGIHAAKDPTRGGLAMALNDWAKKAKVSIIIWEEKVPLRE 257
Cdd:cd02193 179 AMQALVAAGKLLAWHDRGAGGLLVALAELVFAGHCGVQVDLAALGDDE 226
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
43-175 |
7.88e-03 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 37.84 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196573 43 EDSATIPLSDGgHLAFTIDsytvnpiffpgGNIGKLAAT-----G------TINDLAVMGAKPLAAMDSMVIEegfSIED 111
Cdd:COG2144 44 DDAAAIPDGDG-YLLLAAE-----------GIWPKFVEAdpwfaGycsvlvNVSDIAAMGGRPLAVVDALWSS---DEEA 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196573 112 LEKILSSMKGVLEKYNIALIGG----DfkvMPKDQVDkivltMAGIGLIPKgrLIKDSYVKPGDKIVV 175
Cdd:COG2144 109 AAPVLAGMRAASRKFGVPIVGGhthpD---TPYNALA-----VAILGRAKK--LLTSFTARPGDRLIA 166
|
|
| |
