|
Name |
Accession |
Description |
Interval |
E-value |
| hypE |
TIGR02124 |
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ... |
15-336 |
3.38e-175 |
|
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: 488.30 E-value: 3.38e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 15 MQQLIDHLFMQAFANPWLAEQEDQARLPLAeltaaGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVAVSGAVPRWL 94
Cdd:TIGR02124 1 MQQLIQELFLKAFGNEILAAMEDAAVLELS-----GGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 95 SCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLVSG 174
Cdd:TIGR02124 76 SCGFILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPISAHNLQPGDKIIVSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 175 TLGDHGATILNLREQLGLEGELASDCALLSPLIQQLR-AVPGVKALRDATRGGVNAVVHEFAASAGCGIELQERALPLKP 253
Cdd:TIGR02124 156 TIGDHGAAILAVREGLGFETNLESDCAPLNGLVETLLnAGPAVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 254 AVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEAVRAHPLGQDAAIIGEVVAQ--RGVRLAGIYGVKRTLDLPHSEP 331
Cdd:TIGR02124 236 EVKGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERkeGRVVLKTAYGGKRILDMPSGEL 315
|
....*
gi 1069456130 332 LPRIC 336
Cdd:TIGR02124 316 LPRIC 320
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
10-306 |
5.08e-168 |
|
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: 468.85 E-value: 5.08e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 10 SGGQAMQQLIDHLFMQAFANPWLAEQEDQARLPlaeltAAGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVAVSGA 89
Cdd:cd02197 1 SGGKLMQELIEELFLKAFDNPILEVLEDAAALL-----VGGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDLAMMGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 90 VPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDV 169
Cdd:cd02197 76 KPLYLSLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIPRGVIISPSNIRPGDK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 170 LLVSGTLGDHGATILNLREQLGLEGELASDCALLSPLIQQLR-AVPGVKALRDATRGGVNAVVHEFAASAGCGIELQERA 248
Cdd:cd02197 156 IIVSGTIGDHGAAILAAREGLGFETDIESDCAPLNGLVEALLeAGPGIHAMRDPTRGGLAAVLNEIARASGVGIEIEEEA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1069456130 249 LPLKPAVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEAVRAHPLGQDAAIIGEV 306
Cdd:cd02197 236 IPVREEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRSHPLGKEAAIIGEV 293
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
6-336 |
2.83e-165 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 463.39 E-value: 2.83e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 6 LAHGSGGQAMQQLIDHLFMQAFANPWLAEQEDQARLPLAeltaaGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVA 85
Cdd:COG0309 1 LAHGSGGKLMRELIEELFLPALGNEVLVGGEDAAVLDLG-----GGRLAFTTDSFVVSPIFFPGGDIGKLAVHGTVNDLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 86 VSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLA 165
Cdd:COG0309 76 VSGAKPLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGIGVVPKGRLISPSGAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELASDCALLSPLIQQLRAV--PGVKALRDATRGGVNAVVHEFAASAGCGIE 243
Cdd:COG0309 156 PGDKIIVTGGIGDHGTAILAAREGLELEGELLSDAAPLNDLVSVLLEAapGGVHAMRDPTRGGLAGALNEIAEASGVGIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 244 LQERALPLKPAVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEAVRAHplGQDAAIIGEVVAQRG--VRLAGIYGVK 321
Cdd:COG0309 236 IDEDAIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVLEALRAH--GIDAAIIGEVTEGPPgrVVLKTAIGGE 313
|
330
....*....|....*
gi 1069456130 322 RTLDLPHSEPLPRIC 336
Cdd:COG0309 314 RILDPPEGDPLPRIC 328
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
166-314 |
1.08e-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: 97.80 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELA---SDCALLSPLIQQLRAVP----GVKALRDATRGGVNAVVHEFAASA 238
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDSGLAAvqlGDPLLEPTLIYVKLLLAalggLVKAMHDITGGGLAGALAEMAPAS 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069456130 239 GCGIELQERALPLkpavrgVCEL-LGLDALNFANEGKLVIGVAREAAQHVLEAVRAHPLgqDAAIIGEVVAQRGVRL 314
Cdd:pfam02769 82 GVGAEIDLDKVPI------FEELmLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGL--EAAVIGEVTAGGRLTV 150
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
18-316 |
3.55e-19 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 86.42 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 18 LIDHLFMQAFANPWLAEQEDQARLPLAEltaaGDRLAFSTDSYVIDPLFFPGG----DIGKLAVcgTAN--DVAVSGAVP 91
Cdd:PRK05731 8 LIARLFARRPSSRELGIGDDAALLGPPP----GQRLVVSTDMLVEGVHFRPDWsspeDLGYKAL--AVNlsDLAAMGARP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 92 RWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKvvprgAADKLFINTAGLGAIPA------DihwGAQqla 165
Cdd:PRK05731 82 AAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT-----RGPDLSISVTAIGDVPGgralrrS---GAK--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELASDC--ALLSPliqQLRaVPGVKALRDATRG------GVNAVVHEFAAS 237
Cdd:PRK05731 151 PGDLVAVTGTLGDSAAGLALLLNGLRVPDADAAALisRHLRP---QPR-VGLGQALAGLASAaidisdGLAADLGHIAEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 238 AGCGIELQERALPLKPAVRGVceLLGLDALNFANEG----KLVIGVAREAAQHVLEAvrAHPLGQDAAIIGEVVAQRGVR 313
Cdd:PRK05731 227 SGVGADIDLDALPISPALREA--AEGEDALRWALSGgedyELLFTFPPENRGALLAA--AGHLGVGVTIIGRVTEGEGVV 302
|
...
gi 1069456130 314 LAG 316
Cdd:PRK05731 303 VDG 305
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| hypE |
TIGR02124 |
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ... |
15-336 |
3.38e-175 |
|
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: 488.30 E-value: 3.38e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 15 MQQLIDHLFMQAFANPWLAEQEDQARLPLAeltaaGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVAVSGAVPRWL 94
Cdd:TIGR02124 1 MQQLIQELFLKAFGNEILAAMEDAAVLELS-----GGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 95 SCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLVSG 174
Cdd:TIGR02124 76 SCGFILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPISAHNLQPGDKIIVSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 175 TLGDHGATILNLREQLGLEGELASDCALLSPLIQQLR-AVPGVKALRDATRGGVNAVVHEFAASAGCGIELQERALPLKP 253
Cdd:TIGR02124 156 TIGDHGAAILAVREGLGFETNLESDCAPLNGLVETLLnAGPAVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 254 AVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEAVRAHPLGQDAAIIGEVVAQ--RGVRLAGIYGVKRTLDLPHSEP 331
Cdd:TIGR02124 236 EVKGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERkeGRVVLKTAYGGKRILDMPSGEL 315
|
....*
gi 1069456130 332 LPRIC 336
Cdd:TIGR02124 316 LPRIC 320
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
10-306 |
5.08e-168 |
|
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: 468.85 E-value: 5.08e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 10 SGGQAMQQLIDHLFMQAFANPWLAEQEDQARLPlaeltAAGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVAVSGA 89
Cdd:cd02197 1 SGGKLMQELIEELFLKAFDNPILEVLEDAAALL-----VGGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDLAMMGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 90 VPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDV 169
Cdd:cd02197 76 KPLYLSLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIPRGVIISPSNIRPGDK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 170 LLVSGTLGDHGATILNLREQLGLEGELASDCALLSPLIQQLR-AVPGVKALRDATRGGVNAVVHEFAASAGCGIELQERA 248
Cdd:cd02197 156 IIVSGTIGDHGAAILAAREGLGFETDIESDCAPLNGLVEALLeAGPGIHAMRDPTRGGLAAVLNEIARASGVGIEIEEEA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1069456130 249 LPLKPAVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEAVRAHPLGQDAAIIGEV 306
Cdd:cd02197 236 IPVREEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRSHPLGKEAAIIGEV 293
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
6-336 |
2.83e-165 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 463.39 E-value: 2.83e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 6 LAHGSGGQAMQQLIDHLFMQAFANPWLAEQEDQARLPLAeltaaGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVA 85
Cdd:COG0309 1 LAHGSGGKLMRELIEELFLPALGNEVLVGGEDAAVLDLG-----GGRLAFTTDSFVVSPIFFPGGDIGKLAVHGTVNDLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 86 VSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLA 165
Cdd:COG0309 76 VSGAKPLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGIGVVPKGRLISPSGAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELASDCALLSPLIQQLRAV--PGVKALRDATRGGVNAVVHEFAASAGCGIE 243
Cdd:COG0309 156 PGDKIIVTGGIGDHGTAILAAREGLELEGELLSDAAPLNDLVSVLLEAapGGVHAMRDPTRGGLAGALNEIAEASGVGIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 244 LQERALPLKPAVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEAVRAHplGQDAAIIGEVVAQRG--VRLAGIYGVK 321
Cdd:COG0309 236 IDEDAIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVLEALRAH--GIDAAIIGEVTEGPPgrVVLKTAIGGE 313
|
330
....*....|....*
gi 1069456130 322 RTLDLPHSEPLPRIC 336
Cdd:COG0309 314 RILDPPEGDPLPRIC 328
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
53-305 |
3.86e-40 |
|
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: 140.61 E-value: 3.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 53 LAFSTDSYViDPLFFPGGDIGKLAVCGTANDVAVSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDT 132
Cdd:cd00396 2 LAMSTDGIN-PPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAEACNQLGVPIVGGHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 133 KVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLVSGTLgdhgatilnlreqlglegelasdcallspLIQQLRA 212
Cdd:cd00396 81 SVSPGTMGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTGVD-----------------------------AVLELVA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 213 VPGVKALRDATRGGVNAVVHEFAASAGCGIELQERALPLKPAVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEAVR 292
Cdd:cd00396 132 AGDVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWLCVEHIEEALLFNSSGGLLIAVPAEEADAVLLLLN 211
|
250
....*....|...
gi 1069456130 293 AHplGQDAAIIGE 305
Cdd:cd00396 212 GN--GIDAAVIGR 222
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
44-306 |
6.04e-38 |
|
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: 136.96 E-value: 6.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 44 AELTAAGDRLAFSTDsyvidPLFFPGGDIGKLAVCGTANDVAVSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAA 123
Cdd:cd06061 36 AVVDFGGKVLVVSTD-----PITGAGKDAGWLAVHIAANDIATSGARPRWLLVTLLLPPGTDEEELKAIMREINEAAKEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 124 GIQIVTGDTKVVPrgAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLVSGTLGDHGATIL--NLREQL---GLEGELAS 198
Cdd:cd06061 111 GVSIVGGHTEVTP--GVTRPIISVTAIGKGEKDKLVTPSGAKPGDDIVMTKGAGIEGTAILanDFEEELkkrLSEEELRE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 199 DCAL---LSPLIQQLRAVP-GVKALRDATRGGVNAVVHEFAASAGCGIELQERALPLKPAVRGVCELLGLDALNFANEGK 274
Cdd:cd06061 189 AAKLfykISVVKEALIAAEaGVTAMHDATEGGILGALWEVAEASGVGLRIEKDKIPIRQETKEICEALGIDPLRLISSGT 268
|
250 260 270
....*....|....*....|....*....|..
gi 1069456130 275 LVIGVAREAAQHVLEAVRAHplGQDAAIIGEV 306
Cdd:cd06061 269 LLITVPPEKGDELVDALEEA--GIPASVIGKI 298
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
16-325 |
4.17e-28 |
|
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: 111.39 E-value: 4.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 16 QQLIDHLFmqafanPWLAEQEDQARLPL----AELTAAGDRLAFSTDSYVIDPLFFPGG----DIGKLAVCGTANDVAVS 87
Cdd:COG0611 4 FGLIERLF------KRLALRGPDVLLGIgddaAVLDPPGGRLVVTTDMLVEGVHFPLDWmspeDLGWKAVAVNLSDLAAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 88 GAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTkvvprGAADKLFINTAGLGAIPADIHW---GAQql 164
Cdd:COG0611 78 GARPLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDT-----TRSPELTISVTAIGEVPGGRPLlrsGAR-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 165 aPGDVLLVSGTLGDHGAtilnlreqlGL---EGELASDCALLSPLIQ-QLRAVPGVKALRD-ATRGGVNAV--------- 230
Cdd:COG0611 151 -PGDLVYVTGTLGDAAA---------GLallLRGLRVPLEAREYLLErHLRPEPRLALGRAlAEAGLATAMidisdglaa 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 231 -VHEFAASAGCGIELQERALPLKPAVRGVCelLGLDALNFA-NEG---KLVIGVAREAAqhvlEAVRAHPLGQDAAIIGE 305
Cdd:COG0611 221 dLGHIAEASGVGAEIDLDALPLSPALREAA--LGLDPLELAlTGGedyELLFTVPPEAL----EALEAAALGVPLTVIGR 294
|
330 340
....*....|....*....|
gi 1069456130 306 VVAQRGVRLAGIYGVKRTLD 325
Cdd:COG0611 295 VTEGEGVTLDDADGRPIPLE 314
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
166-314 |
1.08e-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: 97.80 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELA---SDCALLSPLIQQLRAVP----GVKALRDATRGGVNAVVHEFAASA 238
Cdd:pfam02769 2 PGDVLILLGSSGLHGAGLSLSRKGLEDSGLAAvqlGDPLLEPTLIYVKLLLAalggLVKAMHDITGGGLAGALAEMAPAS 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069456130 239 GCGIELQERALPLkpavrgVCEL-LGLDALNFANEGKLVIGVAREAAQHVLEAVRAHPLgqDAAIIGEVVAQRGVRL 314
Cdd:pfam02769 82 GVGAEIDLDKVPI------FEELmLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGL--EAAVIGEVTAGGRLTV 150
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
44-307 |
2.62e-24 |
|
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: 100.32 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 44 AELTAAGDRLAFSTDSYVID---PLFFPGGDIGKLAVCGTANDVAVSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATA 120
Cdd:cd02194 28 AVLKPPGGRLVVTTDTLVEGvhfPPDTTPEDIGWKALAVNLSDLAAMGARPLGFLLSLGLPPDTDEEWLEEFYRGLAEAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 121 RAAGIQIVTGDTKvvprgAADKLFINTAGLGAIPADIHW---GAQqlaPGDVLLVSGTLGDHGAtILNLreqlgLEGELA 197
Cdd:cd02194 108 DRYGVPLVGGDTT-----SGSELVISVTALGEVEKGKPLrrsGAK---PGDLLYVTGTLGDAAA-GLAL-----LLGGLK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 198 SDCALLSPLIQ-QLRAVPGVKALRDATRGGVNAV----------VHEFAASAGCGIELQERALPLKPAVRgvCELLGLDA 266
Cdd:cd02194 174 LPEELYEELIErHLRPEPRLELGRALAEGLATAMidisdglladLGHIAEASGVGAVIDLDKLPLSPALR--AAELGEDA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1069456130 267 LNFANEG----KLVIGVAREAAQhvleaVRAHPLGQDAAIIGEVV 307
Cdd:cd02194 252 LELALSGgedyELLFTVPPENAE-----AAAAKLGVPVTVIGRVT 291
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
53-153 |
4.91e-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: 83.65 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 53 LAFSTDS----YVIDPLFFPGgdigKLAVCGTANDVAVSGAVPRWLSCGFILEEGLA-MATLEKVAHSMAATARAAGIQI 127
Cdd:pfam00586 5 VAVTTDGhgtpSLVDPYHFPG----AKAVAGNLSDIAAMGARPLAFLDSLALPGGPEvEWVLEEIVEGIAEACREAGVPL 80
|
90 100
....*....|....*....|....*.
gi 1069456130 128 VTGDTKVVPRGaaDKLFINTAGLGAI 153
Cdd:pfam00586 81 VGGDTSFDPEG--GKPTISVTAVGIV 104
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
18-312 |
2.89e-19 |
|
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: 86.62 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 18 LIDHLFMQAFANPWLAEQ--EDQARLPLAEltaaGDRLAFSTDSYVIDPLFFPG---GDIGKLAVCGTANDVAVSGAVPR 92
Cdd:TIGR01379 5 LIDRILRRLVQDPDVALGigDDAALVSAPE----GRDLVLTTDTLVEGVHFPPDttpEDLGWKAVAVNLSDLAAMGATPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 93 WLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKvvprgAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLV 172
Cdd:TIGR01379 81 WFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTV-----SSPELVVTVTAIGEAPKGRALLRSGAKPGDLVFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 173 SGTLGDhGATILNLREQlGLEGELASDCALLspLIQQLRAVPGVKaLRDATRGGVNAV----------VHEFAASAGCGI 242
Cdd:TIGR01379 156 TGTLGD-SAAGLALLLK-GKKEPDEEDDEAL--LQRHLRPEPRVE-EGLALAGYANAAidvsdglaadLGHIAEASGVGI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069456130 243 ELQERALPLKPAVRGVCEllGLDALNFANEG----KLVIGVAREAAQHVLEAvrahpLGQDAAIIGEVVAQRGV 312
Cdd:TIGR01379 231 VIDLDRLPLSSELAAWAE--GKNPLEWALSGgedyELVFTVPPERREALLDA-----AKGPLTRIGRVTEGEGV 297
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
18-316 |
3.55e-19 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 86.42 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 18 LIDHLFMQAFANPWLAEQEDQARLPLAEltaaGDRLAFSTDSYVIDPLFFPGG----DIGKLAVcgTAN--DVAVSGAVP 91
Cdd:PRK05731 8 LIARLFARRPSSRELGIGDDAALLGPPP----GQRLVVSTDMLVEGVHFRPDWsspeDLGYKAL--AVNlsDLAAMGARP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 92 RWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKvvprgAADKLFINTAGLGAIPA------DihwGAQqla 165
Cdd:PRK05731 82 AAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT-----RGPDLSISVTAIGDVPGgralrrS---GAK--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELASDC--ALLSPliqQLRaVPGVKALRDATRG------GVNAVVHEFAAS 237
Cdd:PRK05731 151 PGDLVAVTGTLGDSAAGLALLLNGLRVPDADAAALisRHLRP---QPR-VGLGQALAGLASAaidisdGLAADLGHIAEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 238 AGCGIELQERALPLKPAVRGVceLLGLDALNFANEG----KLVIGVAREAAQHVLEAvrAHPLGQDAAIIGEVVAQRGVR 313
Cdd:PRK05731 227 SGVGADIDLDALPISPALREA--AEGEDALRWALSGgedyELLFTFPPENRGALLAA--AGHLGVGVTIIGRVTEGEGVV 302
|
...
gi 1069456130 314 LAG 316
Cdd:PRK05731 303 VDG 305
|
|
| PurM-like2 |
cd02691 |
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ... |
83-325 |
2.01e-05 |
|
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: 45.84 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 83 DVAVSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKvvpRGAADKLFIN--TAGLGAIPADIH-W 159
Cdd:cd02691 78 DVMVMGARPVALLSDIHLADDGDVGKLFDFTAGVTAVSEATGVPLVAGSTL---RIGGDMVLGDrlVGGVGAVGRSKSdP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 160 GAQQLA-PGDVLLVsgTLGDHGATILN----------LREQLGLEGELASDCALLSPLIQQlravpgVKALRDATRGGVN 228
Cdd:cd02691 155 SRRKNAePGDLILM--TEGAGGGTITTtaiyhgmpdvVEETLNVDFIKACEALRDSGLVSK------VHSMTDVTNGGIR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 229 AVVHEFAASAGCGIELQE---RALpLKPAVRGVCELLGLDALNFANEGKLVIgVAREAAQHVLEAVRAHplGQDAAIIGE 305
Cdd:cd02691 227 GDALEISKTAGVSLVFDEekvRSL-INPKVLKMLEELGIDPLGVSLDSLMII-APEEDAVDIIRTLREA--GVRADEVGR 302
|
250 260
....*....|....*....|
gi 1069456130 306 VVAQRGVRLAgIYGVKRTLD 325
Cdd:cd02691 303 VEEGRGVPLV-VTGEGRELK 321
|
|
| PLN03206 |
PLN03206 |
phosphoribosylformylglycinamidine synthase; Provisional |
207-315 |
3.31e-04 |
|
phosphoribosylformylglycinamidine synthase; Provisional
Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 42.45 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069456130 207 IQQLRAVPGVKALRDATRGGVNAVVHEFAASAGCGIELqerALPLkpavrgvCELLGLDALnFANEGKLVIGVAREAAQH 286
Cdd:PLN03206 873 TQDLIAKRLISAGHDISDGGLVVTLLEMAFAGNCGINV---DLPS-------SGHSAFETL-FAEELGLVLEVSRKNLDA 941
|
90 100
....*....|....*....|....*....
gi 1069456130 287 VLEAVRAHplGQDAAIIGEVVAQRGVRLA 315
Cdd:PLN03206 942 VMEKLAAA--GVTAEVIGQVTASPLIEVK 968
|
|
| |
