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Conserved domains on  [gi|1354929802|gb|PQX81902|]
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hydrogenase expression/formation protein HypE [Cronobacter sakazakii]

Protein Classification

hydrogenase expression/formation protein HypE( domain architecture ID 11493751)

HypE catalyzes the ATP-dependent dehydration of its own carbamoylated C-terminal cysteine to yield HypE-thiocyanate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hypE TIGR02124
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ...
15-336 1.58e-176

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: 491.77  E-value: 1.58e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  15 MQQLIDRLFMQAFANPWLAEQEDQARLPLAeltaaGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVAVSGAVPRWL 94
Cdd:TIGR02124   1 MQQLIQELFLKAFGNEILAAMEDAAVLELS-----GGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  95 SCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLVSG 174
Cdd:TIGR02124  76 SCGFILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPISAHNLQPGDKIIVSG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 175 TLGDHGATILNLREQLGLEGELASDCALLSPLIQQLR-AVPGVKALRDATRGGVNAVVHEFAASAGCGIELQERALPLKP 253
Cdd:TIGR02124 156 TIGDHGAAILAVREGLGFETNLESDCAPLNGLVETLLnAGPAVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 254 AVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEALRAHPLGQDAAIIGEVVAQKG--VRLAGIYGVKRTLDLPHSEP 331
Cdd:TIGR02124 236 EVKGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERKEgrVVLKTAYGGKRILDMPSGEL 315

                  ....*
gi 1354929802 332 LPRIC 336
Cdd:TIGR02124 316 LPRIC 320
 
Name Accession Description Interval E-value
hypE TIGR02124
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ...
15-336 1.58e-176

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: 491.77  E-value: 1.58e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  15 MQQLIDRLFMQAFANPWLAEQEDQARLPLAeltaaGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVAVSGAVPRWL 94
Cdd:TIGR02124   1 MQQLIQELFLKAFGNEILAAMEDAAVLELS-----GGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  95 SCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLVSG 174
Cdd:TIGR02124  76 SCGFILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPISAHNLQPGDKIIVSG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 175 TLGDHGATILNLREQLGLEGELASDCALLSPLIQQLR-AVPGVKALRDATRGGVNAVVHEFAASAGCGIELQERALPLKP 253
Cdd:TIGR02124 156 TIGDHGAAILAVREGLGFETNLESDCAPLNGLVETLLnAGPAVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 254 AVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEALRAHPLGQDAAIIGEVVAQKG--VRLAGIYGVKRTLDLPHSEP 331
Cdd:TIGR02124 236 EVKGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERKEgrVVLKTAYGGKRILDMPSGEL 315

                  ....*
gi 1354929802 332 LPRIC 336
Cdd:TIGR02124 316 LPRIC 320
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
10-306 4.28e-169

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: 471.93  E-value: 4.28e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  10 SGGQAMQQLIDRLFMQAFANPWLAEQEDQARLPlaeltAAGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVAVSGA 89
Cdd:cd02197     1 SGGKLMQELIEELFLKAFDNPILEVLEDAAALL-----VGGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDLAMMGA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  90 VPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDV 169
Cdd:cd02197    76 KPLYLSLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIPRGVIISPSNIRPGDK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 170 LLVSGTLGDHGATILNLREQLGLEGELASDCALLSPLIQQLR-AVPGVKALRDATRGGVNAVVHEFAASAGCGIELQERA 248
Cdd:cd02197   156 IIVSGTIGDHGAAILAAREGLGFETDIESDCAPLNGLVEALLeAGPGIHAMRDPTRGGLAAVLNEIARASGVGIEIEEEA 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1354929802 249 LPLKPAVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEALRAHPLGQDAAIIGEV 306
Cdd:cd02197   236 IPVREEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRSHPLGKEAAIIGEV 293
HypE COG0309
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ...
6-336 4.52e-167

Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440078 [Multi-domain]  Cd Length: 328  Bit Score: 468.01  E-value: 4.52e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802   6 LAHGSGGQAMQQLIDRLFMQAFANPWLAEQEDQARLPLAeltaaGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVA 85
Cdd:COG0309     1 LAHGSGGKLMRELIEELFLPALGNEVLVGGEDAAVLDLG-----GGRLAFTTDSFVVSPIFFPGGDIGKLAVHGTVNDLA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  86 VSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLA 165
Cdd:COG0309    76 VSGAKPLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGIGVVPKGRLISPSGAR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELASDCALLSPLIQQLRAV--PGVKALRDATRGGVNAVVHEFAASAGCGIE 243
Cdd:COG0309   156 PGDKIIVTGGIGDHGTAILAAREGLELEGELLSDAAPLNDLVSVLLEAapGGVHAMRDPTRGGLAGALNEIAEASGVGIE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 244 LQERALPLKPAVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEALRAHplGQDAAIIGEVVAQKG--VRLAGIYGVK 321
Cdd:COG0309   236 IDEDAIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVLEALRAH--GIDAAIIGEVTEGPPgrVVLKTAIGGE 313
                         330
                  ....*....|....*
gi 1354929802 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 2.12e-25

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: 99.73  E-value: 2.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELA---SDCALLSPLIQQLRAVP----GVKALRDATRGGVNAVVHEFAASA 238
Cdd:pfam02769   2 PGDVLILLGSSGLHGAGLSLSRKGLEDSGLAAvqlGDPLLEPTLIYVKLLLAalggLVKAMHDITGGGLAGALAEMAPAS 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1354929802 239 GCGIELQERALPLkpavrgVCEL-LGLDALNFANEGKLVIGVAREAAQHVLEALRAHPLgqDAAIIGEVVAQKGVRL 314
Cdd:pfam02769  82 GVGAEIDLDKVPI------FEELmLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGL--EAAVIGEVTAGGRLTV 150
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
18-316 5.95e-20

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 88.74  E-value: 5.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  18 LIDRLFMQAFANPWLAEQEDQARLPLAEltaaGDRLAFSTDSYVIDPLFFPGG----DIGKLAVcgTAN--DVAVSGAVP 91
Cdd:PRK05731    8 LIARLFARRPSSRELGIGDDAALLGPPP----GQRLVVSTDMLVEGVHFRPDWsspeDLGYKAL--AVNlsDLAAMGARP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  92 RWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKvvprgAADKLFINTAGLGAIPA------DihwGAQqla 165
Cdd:PRK05731   82 AAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT-----RGPDLSISVTAIGDVPGgralrrS---GAK--- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELASDC--ALLSPliqQLRaVPGVKALRDATRG------GVNAVVHEFAAS 237
Cdd:PRK05731  151 PGDLVAVTGTLGDSAAGLALLLNGLRVPDADAAALisRHLRP---QPR-VGLGQALAGLASAaidisdGLAADLGHIAEA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 238 AGCGIELQERALPLKPAVRGVceLLGLDALNFANEG----KLVIGVAREAAQHVLEAlrAHPLGQDAAIIGEVVAQKGVR 313
Cdd:PRK05731  227 SGVGADIDLDALPISPALREA--AEGEDALRWALSGgedyELLFTFPPENRGALLAA--AGHLGVGVTIIGRVTEGEGVV 302

                  ...
gi 1354929802 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 1.58e-176

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: 491.77  E-value: 1.58e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  15 MQQLIDRLFMQAFANPWLAEQEDQARLPLAeltaaGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVAVSGAVPRWL 94
Cdd:TIGR02124   1 MQQLIQELFLKAFGNEILAAMEDAAVLELS-----GGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  95 SCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLVSG 174
Cdd:TIGR02124  76 SCGFILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPISAHNLQPGDKIIVSG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 175 TLGDHGATILNLREQLGLEGELASDCALLSPLIQQLR-AVPGVKALRDATRGGVNAVVHEFAASAGCGIELQERALPLKP 253
Cdd:TIGR02124 156 TIGDHGAAILAVREGLGFETNLESDCAPLNGLVETLLnAGPAVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 254 AVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEALRAHPLGQDAAIIGEVVAQKG--VRLAGIYGVKRTLDLPHSEP 331
Cdd:TIGR02124 236 EVKGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERKEgrVVLKTAYGGKRILDMPSGEL 315

                  ....*
gi 1354929802 332 LPRIC 336
Cdd:TIGR02124 316 LPRIC 320
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
10-306 4.28e-169

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: 471.93  E-value: 4.28e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  10 SGGQAMQQLIDRLFMQAFANPWLAEQEDQARLPlaeltAAGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVAVSGA 89
Cdd:cd02197     1 SGGKLMQELIEELFLKAFDNPILEVLEDAAALL-----VGGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDLAMMGA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  90 VPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDV 169
Cdd:cd02197    76 KPLYLSLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIPRGVIISPSNIRPGDK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 170 LLVSGTLGDHGATILNLREQLGLEGELASDCALLSPLIQQLR-AVPGVKALRDATRGGVNAVVHEFAASAGCGIELQERA 248
Cdd:cd02197   156 IIVSGTIGDHGAAILAAREGLGFETDIESDCAPLNGLVEALLeAGPGIHAMRDPTRGGLAAVLNEIARASGVGIEIEEEA 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1354929802 249 LPLKPAVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEALRAHPLGQDAAIIGEV 306
Cdd:cd02197   236 IPVREEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRSHPLGKEAAIIGEV 293
HypE COG0309
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ...
6-336 4.52e-167

Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440078 [Multi-domain]  Cd Length: 328  Bit Score: 468.01  E-value: 4.52e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802   6 LAHGSGGQAMQQLIDRLFMQAFANPWLAEQEDQARLPLAeltaaGDRLAFSTDSYVIDPLFFPGGDIGKLAVCGTANDVA 85
Cdd:COG0309     1 LAHGSGGKLMRELIEELFLPALGNEVLVGGEDAAVLDLG-----GGRLAFTTDSFVVSPIFFPGGDIGKLAVHGTVNDLA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  86 VSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKVVPRGAADKLFINTAGLGAIPADIHWGAQQLA 165
Cdd:COG0309    76 VSGAKPLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGIGVVPKGRLISPSGAR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELASDCALLSPLIQQLRAV--PGVKALRDATRGGVNAVVHEFAASAGCGIE 243
Cdd:COG0309   156 PGDKIIVTGGIGDHGTAILAAREGLELEGELLSDAAPLNDLVSVLLEAapGGVHAMRDPTRGGLAGALNEIAEASGVGIE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 244 LQERALPLKPAVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEALRAHplGQDAAIIGEVVAQKG--VRLAGIYGVK 321
Cdd:COG0309   236 IDEDAIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVLEALRAH--GIDAAIIGEVTEGPPgrVVLKTAIGGE 313
                         330
                  ....*....|....*
gi 1354929802 322 RTLDLPHSEPLPRIC 336
Cdd:COG0309   314 RILDPPEGDPLPRIC 328
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
53-305 6.90e-41

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: 142.54  E-value: 6.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  53 LAFSTDSYViDPLFFPGGDIGKLAVCGTANDVAVSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDT 132
Cdd:cd00396     2 LAMSTDGIN-PPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAEACNQLGVPIVGGHT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 133 KVVPRGAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLVSGTLgdhgatilnlreqlglegelasdcallspLIQQLRA 212
Cdd:cd00396    81 SVSPGTMGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTGVD-----------------------------AVLELVA 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 213 VPGVKALRDATRGGVNAVVHEFAASAGCGIELQERALPLKPAVRGVCELLGLDALNFANEGKLVIGVAREAAQHVLEALR 292
Cdd:cd00396   132 AGDVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWLCVEHIEEALLFNSSGGLLIAVPAEEADAVLLLLN 211
                         250
                  ....*....|...
gi 1354929802 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 3.53e-39

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: 140.42  E-value: 3.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  44 AELTAAGDRLAFSTDsyvidPLFFPGGDIGKLAVCGTANDVAVSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAA 123
Cdd:cd06061    36 AVVDFGGKVLVVSTD-----PITGAGKDAGWLAVHIAANDIATSGARPRWLLVTLLLPPGTDEEELKAIMREINEAAKEL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 124 GIQIVTGDTKVVPrgAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLVSGTLGDHGATIL--NLREQL---GLEGELAS 198
Cdd:cd06061   111 GVSIVGGHTEVTP--GVTRPIISVTAIGKGEKDKLVTPSGAKPGDDIVMTKGAGIEGTAILanDFEEELkkrLSEEELRE 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 199 DCAL---LSPLIQQLRAVP-GVKALRDATRGGVNAVVHEFAASAGCGIELQERALPLKPAVRGVCELLGLDALNFANEGK 274
Cdd:cd06061   189 AAKLfykISVVKEALIAAEaGVTAMHDATEGGILGALWEVAEASGVGLRIEKDKIPIRQETKEICEALGIDPLRLISSGT 268
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1354929802 275 LVIGVAREAAQHVLEALRAHplGQDAAIIGEV 306
Cdd:cd06061   269 LLITVPPEKGDELVDALEEA--GIPASVIGKI 298
ThiL COG0611
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
16-325 8.65e-29

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: 112.93  E-value: 8.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  16 QQLIDRLFmqafanPWLAEQEDQARLPL----AELTAAGDRLAFSTDSYVIDPLFFPGG----DIGKLAVCGTANDVAVS 87
Cdd:COG0611     4 FGLIERLF------KRLALRGPDVLLGIgddaAVLDPPGGRLVVTTDMLVEGVHFPLDWmspeDLGWKAVAVNLSDLAAM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  88 GAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTkvvprGAADKLFINTAGLGAIPADIHW---GAQql 164
Cdd:COG0611    78 GARPLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDT-----TRSPELTISVTAIGEVPGGRPLlrsGAR-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 165 aPGDVLLVSGTLGDHGAtilnlreqlGL---EGELASDCALLSPLIQ-QLRAVPGVKALRD-ATRGGVNAV--------- 230
Cdd:COG0611   151 -PGDLVYVTGTLGDAAA---------GLallLRGLRVPLEAREYLLErHLRPEPRLALGRAlAEAGLATAMidisdglaa 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 231 -VHEFAASAGCGIELQERALPLKPAVRGVCelLGLDALNFA-NEG---KLVIGVAREAAqhvlEALRAHPLGQDAAIIGE 305
Cdd:COG0611   221 dLGHIAEASGVGAEIDLDALPLSPALREAA--LGLDPLELAlTGGedyELLFTVPPEAL----EALEAAALGVPLTVIGR 294
                         330       340
                  ....*....|....*....|
gi 1354929802 306 VVAQKGVRLAGIYGVKRTLD 325
Cdd:COG0611   295 VTEGEGVTLDDADGRPIPLE 314
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
166-314 2.12e-25

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: 99.73  E-value: 2.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELA---SDCALLSPLIQQLRAVP----GVKALRDATRGGVNAVVHEFAASA 238
Cdd:pfam02769   2 PGDVLILLGSSGLHGAGLSLSRKGLEDSGLAAvqlGDPLLEPTLIYVKLLLAalggLVKAMHDITGGGLAGALAEMAPAS 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1354929802 239 GCGIELQERALPLkpavrgVCEL-LGLDALNFANEGKLVIGVAREAAQHVLEALRAHPLgqDAAIIGEVVAQKGVRL 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 ...
18-307 9.50e-25

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: 101.48  E-value: 9.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  18 LIDRLFmqafanPWLAEQEDQARLPL---AELTAAGDRLAFSTDSYVID---PLFFPGGDIGKLAVCGTANDVAVSGAVP 91
Cdd:cd02194     5 LIDRLF------KRLGAGPGVLLGIGddaAVLKPPGGRLVVTTDTLVEGvhfPPDTTPEDIGWKALAVNLSDLAAMGARP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  92 RWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKvvprgAADKLFINTAGLGAIPADIHW---GAQqlaPGD 168
Cdd:cd02194    79 LGFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTT-----SGSELVISVTALGEVEKGKPLrrsGAK---PGD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 169 VLLVSGTLGDHGAtILNLreqlgLEGELASDCALLSPLIQ-QLRAVPGVKALRDATRGGVNAV----------VHEFAAS 237
Cdd:cd02194   151 LLYVTGTLGDAAA-GLAL-----LLGGLKLPEELYEELIErHLRPEPRLELGRALAEGLATAMidisdglladLGHIAEA 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1354929802 238 AGCGIELQERALPLKPAVRgvCELLGLDALNFANEG----KLVIGVAREAAQhvleaLRAHPLGQDAAIIGEVV 307
Cdd:cd02194   225 SGVGAVIDLDKLPLSPALR--AAELGEDALELALSGgedyELLFTVPPENAE-----AAAAKLGVPVTVIGRVT 291
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
53-153 3.88e-20

AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression/formation protein HypE, AIR synthases EC:6.3.3.1, FGAM synthase EC:6.3.5.3 and selenide, water dikinase EC:2.7.9.3. The N-terminal domain of AIR synthase forms the dimer interface of the protein, and is suggested as a putative ATP binding domain.


Pssm-ID: 459859 [Multi-domain]  Cd Length: 104  Bit Score: 84.03  E-value: 3.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  53 LAFSTDS----YVIDPLFFPGgdigKLAVCGTANDVAVSGAVPRWLSCGFILEEGLA-MATLEKVAHSMAATARAAGIQI 127
Cdd:pfam00586   5 VAVTTDGhgtpSLVDPYHFPG----AKAVAGNLSDIAAMGARPLAFLDSLALPGGPEvEWVLEEIVEGIAEACREAGVPL 80
                          90       100
                  ....*....|....*....|....*.
gi 1354929802 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 4.35e-20

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: 88.93  E-value: 4.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  18 LIDRLFMQAFANPWLAEQ--EDQARLPLAEltaaGDRLAFSTDSYVIDPLFFPG---GDIGKLAVCGTANDVAVSGAVPR 92
Cdd:TIGR01379   5 LIDRILRRLVQDPDVALGigDDAALVSAPE----GRDLVLTTDTLVEGVHFPPDttpEDLGWKAVAVNLSDLAAMGATPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  93 WLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKvvprgAADKLFINTAGLGAIPADIHWGAQQLAPGDVLLV 172
Cdd:TIGR01379  81 WFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTV-----SSPELVVTVTAIGEAPKGRALLRSGAKPGDLVFV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 173 SGTLGDhGATILNLREQlGLEGELASDCALLspLIQQLRAVPGVKaLRDATRGGVNAV----------VHEFAASAGCGI 242
Cdd:TIGR01379 156 TGTLGD-SAAGLALLLK-GKKEPDEEDDEAL--LQRHLRPEPRVE-EGLALAGYANAAidvsdglaadLGHIAEASGVGI 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1354929802 243 ELQERALPLKPAVRGVCEllGLDALNFANEG----KLVIGVAREAAQHVLEAlrahpLGQDAAIIGEVVAQKGV 312
Cdd:TIGR01379 231 VIDLDRLPLSSELAAWAE--GKNPLEWALSGgedyELVFTVPPERREALLDA-----AKGPLTRIGRVTEGEGV 297
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
18-316 5.95e-20

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 88.74  E-value: 5.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  18 LIDRLFMQAFANPWLAEQEDQARLPLAEltaaGDRLAFSTDSYVIDPLFFPGG----DIGKLAVcgTAN--DVAVSGAVP 91
Cdd:PRK05731    8 LIARLFARRPSSRELGIGDDAALLGPPP----GQRLVVSTDMLVEGVHFRPDWsspeDLGYKAL--AVNlsDLAAMGARP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  92 RWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKvvprgAADKLFINTAGLGAIPA------DihwGAQqla 165
Cdd:PRK05731   82 AAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT-----RGPDLSISVTAIGDVPGgralrrS---GAK--- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 166 PGDVLLVSGTLGDHGATILNLREQLGLEGELASDC--ALLSPliqQLRaVPGVKALRDATRG------GVNAVVHEFAAS 237
Cdd:PRK05731  151 PGDLVAVTGTLGDSAAGLALLLNGLRVPDADAAALisRHLRP---QPR-VGLGQALAGLASAaidisdGLAADLGHIAEA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 238 AGCGIELQERALPLKPAVRGVceLLGLDALNFANEG----KLVIGVAREAAQHVLEAlrAHPLGQDAAIIGEVVAQKGVR 313
Cdd:PRK05731  227 SGVGADIDLDALPISPALREA--AEGEDALRWALSGgedyELLFTFPPENRGALLAA--AGHLGVGVTIIGRVTEGEGVV 302

                  ...
gi 1354929802 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 4.75e-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: 44.69  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  83 DVAVSGAVPRWLSCGFILEEGLAMATLEKVAHSMAATARAAGIQIVTGDTKvvpRGAADKLFIN--TAGLGAIPADIH-W 159
Cdd:cd02691    78 DVMVMGARPVALLSDIHLADDGDVGKLFDFTAGVTAVSEATGVPLVAGSTL---RIGGDMVLGDrlVGGVGAVGRSKSdP 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 160 GAQQLA-PGDVLLVsgTLGDHGATILN----------LREQLGLEGELASDCALLSPLIQQlravpgVKALRDATRGGVN 228
Cdd:cd02691   155 SRRKNAePGDLILM--TEGAGGGTITTtaiyhgmpdvVEETLNVDFIKACEALRDSGLVSK------VHSMTDVTNGGIR 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802 229 AVVHEFAASAGCGIELQE---RALpLKPAVRGVCELLGLDALNFANEGKLVIgVAREAAQHVLEALRAHplGQDAAIIGE 305
Cdd:cd02691   227 GDALEISKTAGVSLVFDEekvRSL-INPKVLKMLEELGIDPLGVSLDSLMII-APEEDAVDIIRTLREA--GVRADEVGR 302
                         250       260
                  ....*....|....*....|
gi 1354929802 306 VVAQKGVRLAgIYGVKRTLD 325
Cdd:cd02691   303 VEEGRGVPLV-VTGEGRELK 321
PLN03206 PLN03206
phosphoribosylformylglycinamidine synthase; Provisional
207-315 8.70e-05

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 178745 [Multi-domain]  Cd Length: 1307  Bit Score: 44.37  E-value: 8.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1354929802  207 IQQLRAVPGVKALRDATRGGVNAVVHEFAASAGCGIELqerALPLkpavrgvCELLGLDALnFANEGKLVIGVAREAAQH 286
Cdd:PLN03206   873 TQDLIAKRLISAGHDISDGGLVVTLLEMAFAGNCGINV---DLPS-------SGHSAFETL-FAEELGLVLEVSRKNLDA 941
                           90       100
                   ....*....|....*....|....*....
gi 1354929802  287 VLEALRAHplGQDAAIIGEVVAQKGVRLA 315
Cdd:PLN03206   942 VMEKLAAA--GVTAEVIGQVTASPLIEVK 968
SelD COG0709
Selenophosphate synthase [Amino acid transport and metabolism];
273-314 1.49e-03

Selenophosphate synthase [Amino acid transport and metabolism];


Pssm-ID: 440473 [Multi-domain]  Cd Length: 346  Bit Score: 40.06  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1354929802 273 GKLVIGVAREAAQHVLEALRAHplGQDAAIIGEVVAQKGVRL 314
Cdd:COG0709   304 GGLLIAVPPEAAEELLAALRAA--GYAAAIIGEVTAGEGGAI 343
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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