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Conserved domains on  [gi|226524740|ref|NP_417210|]
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carbamoyl dehydratase HypE [Escherichia coli str. K-12 substr. MG1655]

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 2.23e-179

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: 498.70  E-value: 2.23e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740   15 MQQLINSLFMEAFANPWLAEQEDQARLDLAqlvaeGDRLAFSTDSYVIDPLFFPGGNIGKLAICGTANDVAVSGAIPRYL 94
Cdd:TIGR02124   1 MQQLIQELFLKAFGNEILAAMEDAAVLELS-----GGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740   95 SCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTKVVQRGAVDKLFINTAGMGAIPANIHWGAQTLTAGDVLLVSG 174
Cdd:TIGR02124  76 SCGFILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPISAHNLQPGDKIIVSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  175 TLGDHGATILNLREQLGLDGELVSDCAVLTPLIQTLRDI-PGVKALRDATRGGVNAVVHEFAAACGCGIELSEAALPVKP 253
Cdd:TIGR02124 156 TIGDHGAAILAVREGLGFETNLESDCAPLNGLVETLLNAgPAVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  254 AVRGVCELLGLDALNFANEGKLVIAVERNAAEQVLAALHSHPLGKDAALIGEVVERKG--VRLAGLYGVKRTLDLPHAEP 331
Cdd:TIGR02124 236 EVKGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERKEgrVVLKTAYGGKRILDMPSGEL 315


                  ....*
gi 226524740  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 2.23e-179

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: 498.70  E-value: 2.23e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740   15 MQQLINSLFMEAFANPWLAEQEDQARLDLAqlvaeGDRLAFSTDSYVIDPLFFPGGNIGKLAICGTANDVAVSGAIPRYL 94
Cdd:TIGR02124   1 MQQLIQELFLKAFGNEILAAMEDAAVLELS-----GGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740   95 SCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTKVVQRGAVDKLFINTAGMGAIPANIHWGAQTLTAGDVLLVSG 174
Cdd:TIGR02124  76 SCGFILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPISAHNLQPGDKIIVSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  175 TLGDHGATILNLREQLGLDGELVSDCAVLTPLIQTLRDI-PGVKALRDATRGGVNAVVHEFAAACGCGIELSEAALPVKP 253
Cdd:TIGR02124 156 TIGDHGAAILAVREGLGFETNLESDCAPLNGLVETLLNAgPAVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  254 AVRGVCELLGLDALNFANEGKLVIAVERNAAEQVLAALHSHPLGKDAALIGEVVERKG--VRLAGLYGVKRTLDLPHAEP 331
Cdd:TIGR02124 236 EVKGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERKEgrVVLKTAYGGKRILDMPSGEL 315


                  ....*
gi 226524740  332 LPRIC 336
Cdd:TIGR02124 316 LPRIC 320
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
 10-306 1.33e-167

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: 468.08  E-value: 1.33e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  10 SGGQAMQQLINSLFMEAFANPWLAEQEDQARLDlaqlvAEGDRLAFSTDSYVIDPLFFPGGNIGKLAICGTANDVAVSGA 89
Cdd:cd02197    1 SGGKLMQELIEELFLKAFDNPILEVLEDAAALL-----VGGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDLAMMGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  90 IPRYLSCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTKVVQRGAVDKLFINTAGMGAIPANIHWGAQTLTAGDV 169
Cdd:cd02197   76 KPLYLSLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIPRGVIISPSNIRPGDK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 170 LLVSGTLGDHGATILNLREQLGLDGELVSDCAVLTPLIQTLRD-IPGVKALRDATRGGVNAVVHEFAAACGCGIELSEAA 248
Cdd:cd02197  156 IIVSGTIGDHGAAILAAREGLGFETDIESDCAPLNGLVEALLEaGPGIHAMRDPTRGGLAAVLNEIARASGVGIEIEEEA 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226524740 249 LPVKPAVRGVCELLGLDALNFANEGKLVIAVERNAAEQVLAALHSHPLGKDAALIGEV 306
Cdd:cd02197  236 IPVREEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRSHPLGKEAAIIGEV 293
HypE COG0309
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ...
 6-336 9.16e-166

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


Pssm-ID: 440078 [Multi-domain]  Cd Length: 328  Bit Score: 464.55  E-value: 9.16e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740   6 LAHGSGGQAMQQLINSLFMEAFANPWLAEQEDQARLDLAqlvaeGDRLAFSTDSYVIDPLFFPGGNIGKLAICGTANDVA 85
Cdd:COG0309    1 LAHGSGGKLMRELIEELFLPALGNEVLVGGEDAAVLDLG-----GGRLAFTTDSFVVSPIFFPGGDIGKLAVHGTVNDLA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  86 VSGAIPRYLSCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTKVVQRGAVDKLFINTAGMGAIPANIHWGAQTLT 165
Cdd:COG0309   76 VSGAKPLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGIGVVPKGRLISPSGAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 166 AGDVLLVSGTLGDHGATILNLREQLGLDGELVSDCAVLTPLIQTLRD--IPGVKALRDATRGGVNAVVHEFAAACGCGIE 243
Cdd:COG0309  156 PGDKIIVTGGIGDHGTAILAAREGLELEGELLSDAAPLNDLVSVLLEaaPGGVHAMRDPTRGGLAGALNEIAEASGVGIE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 244 LSEAALPVKPAVRGVCELLGLDALNFANEGKLVIAVERNAAEQVLAALHSHplGKDAALIGEVVE--RKGVRLAGLYGVK 321
Cdd:COG0309  236 IDEDAIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVLEALRAH--GIDAAIIGEVTEgpPGRVVLKTAIGGE 313

                        330
                 ....*....|....*
gi 226524740 322 RTLDLPHAEPLPRIC 336
Cdd:COG0309  314 RILDPPEGDPLPRIC 328
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
 166-314 5.80e-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: 95.88  E-value: 5.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  166 AGDVLLVSGTLGDHGATILNLREQL---GLDGELVSDCAVLTPLIQTLRDIP----GVKALRDATRGGVNAVVHEFAAAC 238
Cdd:pfam02769   2 PGDVLILLGSSGLHGAGLSLSRKGLedsGLAAVQLGDPLLEPTLIYVKLLLAalggLVKAMHDITGGGLAGALAEMAPAS 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226524740  239 GCGIELSEAALPVkpavrgVCEL-LGLDALNFANEGKLVIAVERNAAEQVLAALHSHPLgkDAALIGEVVERKGVRL 314
Cdd:pfam02769  82 GVGAEIDLDKVPI------FEELmLPLEMLLSENQGRGLVVVAPEEAEAVLAILEKEGL--EAAVIGEVTAGGRLTV 150
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
 18-316 1.19e-15

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 76.41  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  18 LINSLFMEAFANPWLAEQEDQARLDlaqlVAEGDRLAFSTDSYVIDPLFFPGG----NIGKLAIcgTAN--DVAVSGAIP 91
Cdd:PRK05731   8 LIARLFARRPSSRELGIGDDAALLG----PPPGQRLVVSTDMLVEGVHFRPDWsspeDLGYKAL--AVNlsDLAAMGARP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  92 RYLSCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTKvvqRGavDKLFIN-TAgMGAIPANihwgaQTLT----- 165
Cdd:PRK05731  82 AAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT---RG--PDLSISvTA-IGDVPGG-----RALRrsgak 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 166 AGDVLLVSGTLGDhGATILNLreqlgLDGELVSDCAVLTPLIQT-LRDIPGVK---ALRDATRG------GVNAVVHEFA 235
Cdd:PRK05731 151 PGDLVAVTGTLGD-SAAGLAL-----LLNGLRVPDADAAALISRhLRPQPRVGlgqALAGLASAaidisdGLAADLGHIA 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 236 AACGCGIELSEAALPVKPAVRGVceLLGLDALNFANEG----KLVIAVERNAAEQVLAALHSHplGKDAALIGEVVERKG 311
Cdd:PRK05731 225 EASGVGADIDLDALPISPALREA--AEGEDALRWALSGgedyELLFTFPPENRGALLAAAGHL--GVGVTIIGRVTEGEG 300


                 ....*
gi 226524740 312 VRLAG 316
Cdd:PRK05731 301 VVVDG 305
 
Name Accession Description Interval E-value
hypE TIGR02124
hydrogenase expression/formation protein HypE; This family contains HypE (or HupE), a protein ...
 15-336 2.23e-179

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: 498.70  E-value: 2.23e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740   15 MQQLINSLFMEAFANPWLAEQEDQARLDLAqlvaeGDRLAFSTDSYVIDPLFFPGGNIGKLAICGTANDVAVSGAIPRYL 94
Cdd:TIGR02124   1 MQQLIQELFLKAFGNEILAAMEDAAVLELS-----GGRLAFSTDSFVVDPLFFPGGDIGKLAVCGTVNDVAVSGAKPLYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740   95 SCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTKVVQRGAVDKLFINTAGMGAIPANIHWGAQTLTAGDVLLVSG 174
Cdd:TIGR02124  76 SCGFILEEGFPIEDLERIVKSMAEAARKAGVKIVTGDTKVVEKGKADGIFINTTGIGVIPSGIPISAHNLQPGDKIIVSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  175 TLGDHGATILNLREQLGLDGELVSDCAVLTPLIQTLRDI-PGVKALRDATRGGVNAVVHEFAAACGCGIELSEAALPVKP 253
Cdd:TIGR02124 156 TIGDHGAAILAVREGLGFETNLESDCAPLNGLVETLLNAgPAVHAMRDATRGGLAAVLNEWAQASGVGIVIEEEKIPVKE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  254 AVRGVCELLGLDALNFANEGKLVIAVERNAAEQVLAALHSHPLGKDAALIGEVVERKG--VRLAGLYGVKRTLDLPHAEP 331
Cdd:TIGR02124 236 EVKGACELLGLDPLYLANEGKLVLAVPPEAAEKVLEILKSHPYGKDAAIIGEVVERKEgrVVLKTAYGGKRILDMPSGEL 315


                  ....*
gi 226524740  332 LPRIC 336
Cdd:TIGR02124 316 LPRIC 320
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
 10-306 1.33e-167

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: 468.08  E-value: 1.33e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  10 SGGQAMQQLINSLFMEAFANPWLAEQEDQARLDlaqlvAEGDRLAFSTDSYVIDPLFFPGGNIGKLAICGTANDVAVSGA 89
Cdd:cd02197    1 SGGKLMQELIEELFLKAFDNPILEVLEDAAALL-----VGGGRLAFTTDSFVVSPLFFPGGDIGKLAVCGTVNDLAMMGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  90 IPRYLSCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTKVVQRGAVDKLFINTAGMGAIPANIHWGAQTLTAGDV 169
Cdd:cd02197   76 KPLYLSLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGKADGIFINTTGIGVIPRGVIISPSNIRPGDK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 170 LLVSGTLGDHGATILNLREQLGLDGELVSDCAVLTPLIQTLRD-IPGVKALRDATRGGVNAVVHEFAAACGCGIELSEAA 248
Cdd:cd02197  156 IIVSGTIGDHGAAILAAREGLGFETDIESDCAPLNGLVEALLEaGPGIHAMRDPTRGGLAAVLNEIARASGVGIEIEEEA 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226524740 249 LPVKPAVRGVCELLGLDALNFANEGKLVIAVERNAAEQVLAALHSHPLGKDAALIGEV 306
Cdd:cd02197  236 IPVREEVRGACEMLGLDPLYLANEGKFVAIVPPEDAEEVLEALRSHPLGKEAAIIGEV 293
HypE COG0309
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ...
 6-336 9.16e-166

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


Pssm-ID: 440078 [Multi-domain]  Cd Length: 328  Bit Score: 464.55  E-value: 9.16e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740   6 LAHGSGGQAMQQLINSLFMEAFANPWLAEQEDQARLDLAqlvaeGDRLAFSTDSYVIDPLFFPGGNIGKLAICGTANDVA 85
Cdd:COG0309    1 LAHGSGGKLMRELIEELFLPALGNEVLVGGEDAAVLDLG-----GGRLAFTTDSFVVSPIFFPGGDIGKLAVHGTVNDLA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  86 VSGAIPRYLSCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTKVVQRGAVDKLFINTAGMGAIPANIHWGAQTLT 165
Cdd:COG0309   76 VSGAKPLYLSVSLILEEGFPLEDLERIVESMAEAAREAGVSIVTGDTKVVERGGVDGPFINTTGIGVVPKGRLISPSGAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 166 AGDVLLVSGTLGDHGATILNLREQLGLDGELVSDCAVLTPLIQTLRD--IPGVKALRDATRGGVNAVVHEFAAACGCGIE 243
Cdd:COG0309  156 PGDKIIVTGGIGDHGTAILAAREGLELEGELLSDAAPLNDLVSVLLEaaPGGVHAMRDPTRGGLAGALNEIAEASGVGIE 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 244 LSEAALPVKPAVRGVCELLGLDALNFANEGKLVIAVERNAAEQVLAALHSHplGKDAALIGEVVE--RKGVRLAGLYGVK 321
Cdd:COG0309  236 IDEDAIPVRPEVRGICELLGLDPLYLANEGKLVAVVPPEDAEAVLEALRAH--GIDAAIIGEVTEgpPGRVVLKTAIGGE 313

                        330
                 ....*....|....*
gi 226524740 322 RTLDLPHAEPLPRIC 336
Cdd:COG0309  314 RILDPPEGDPLPRIC 328
PurM-like1 cd06061
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ...
 42-306 1.51e-37

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: 135.80  E-value: 1.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  42 DLAQLVAEGDRLAFSTDsyvidPLFFPGGNIGKLAICGTANDVAVSGAIPRYLSCGFILEEGLPMETLKAVVTSMAETAR 121
Cdd:cd06061   34 DAAVVDFGGKVLVVSTD-----PITGAGKDAGWLAVHIAANDIATSGARPRWLLVTLLLPPGTDEEELKAIMREINEAAK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 122 AAGIAIVTGDTKVVqrGAVDKLFINTAGMGAIPANIHWGAQTLTAGDVLLVSGTLGDHGATIL--NLREQL--GLDGELV 197
Cdd:cd06061  109 ELGVSIVGGHTEVT--PGVTRPIISVTAIGKGEKDKLVTPSGAKPGDDIVMTKGAGIEGTAILanDFEEELkkRLSEEEL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 198 SDCAVLTPLIQTLRDI-----PGVKALRDATRGGVNAVVHEFAAACGCGIELSEAALPVKPAVRGVCELLGLDALNFANE 272
Cdd:cd06061  187 REAAKLFYKISVVKEAliaaeAGVTAMHDATEGGILGALWEVAEASGVGLRIEKDKIPIRQETKEICEALGIDPLRLISS 266

                        250       260       270
                 ....*....|....*....|....*....|....
gi 226524740 273 GKLVIAVERNAAEQVLAALHSHplGKDAALIGEV 306
Cdd:cd06061  267 GTLLITVPPEKGDELVDALEEA--GIPASVIGKI 298
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
 53-305 5.68e-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: 132.13  E-value: 5.68e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  53 LAFSTDSYViDPLFFPGGNIGKLAICGTANDVAVSGAIPRYLSCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDT 132
Cdd:cd00396    2 LAMSTDGIN-PPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAEACNQLGVPIVGGHT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 133 KVVQRGAVDKLFINTAGMGAIPANIHWGAQTLTAGDVLLVSGTLgdhgatilnlreqlgldgelvsdcavltpLIQTLRD 212
Cdd:cd00396   81 SVSPGTMGHKLSLAVFAIGVVEKDRVIDSSGARPGDVLILTGVD-----------------------------AVLELVA 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 213 IPGVKALRDATRGGVNAVVHEFAAACGCGIELSEAALPVKPAVRGVCELLGLDALNFANEGKLVIAVERNAAEQVLAALH 292
Cdd:cd00396  132 AGDVHAMHDITDGGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWLCVEHIEEALLFNSSGGLLIAVPAEEADAVLLLLN 211

                        250
                 ....*....|...
gi 226524740 293 SHplGKDAALIGE 305
Cdd:cd00396  212 GN--GIDAAVIGR 222
ThiL COG0611
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 42-325 2.35e-24

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: 100.99  E-value: 2.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  42 DLAQLVAEGDRLAFSTDSYVIDPLFFPGG----NIGKLAICGTANDVAVSGAIPRYLSCGFILEEGLPMETLKAVVTSMA 117
Cdd:COG0611   28 DAAVLDPPGGRLVVTTDMLVEGVHFPLDWmspeDLGWKAVAVNLSDLAAMGARPLAALLSLALPPDTDVEWLEEFARGLA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 118 ETARAAGIAIVTGDTKvvqRGavDKLFINTAGMGAIPANIHW---GAQtltAGDVLLVSGTLGDHGATILNLREQLGLDG 194
Cdd:COG0611  108 EAADRYGVDLVGGDTT---RS--PELTISVTAIGEVPGGRPLlrsGAR---PGDLVYVTGTLGDAAAGLALLLRGLRVPL 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 195 ELVSDC--AVLTP-----LIQTLRDIPGVKA--------LRDAtrggvnavvHEFAAACGCGIELSEAALPVKPAVRGVC 259
Cdd:COG0611  180 EAREYLleRHLRPeprlaLGRALAEAGLATAmidisdglAADL---------GHIAEASGVGAEIDLDALPLSPALREAA 250

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 260 elLGLDALNFA-NEG---KLVIAVERNAAEQVLAALhshpLGKDAALIGEVVERKGVRLAGLYGVKRTLD 325
Cdd:COG0611  251 --LGLDPLELAlTGGedyELLFTVPPEALEALEAAA----LGVPLTVIGRVTEGEGVTLDDADGRPIPLE 314
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
 166-314 5.80e-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: 95.88  E-value: 5.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  166 AGDVLLVSGTLGDHGATILNLREQL---GLDGELVSDCAVLTPLIQTLRDIP----GVKALRDATRGGVNAVVHEFAAAC 238
Cdd:pfam02769   2 PGDVLILLGSSGLHGAGLSLSRKGLedsGLAAVQLGDPLLEPTLIYVKLLLAalggLVKAMHDITGGGLAGALAEMAPAS 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226524740  239 GCGIELSEAALPVkpavrgVCEL-LGLDALNFANEGKLVIAVERNAAEQVLAALHSHPLgkDAALIGEVVERKGVRL 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 ...
 42-307 2.44e-21

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: 92.23  E-value: 2.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  42 DLAQLVAEGDRLAFSTDSYVID---PLFFPGGNIGKLAICGTANDVAVSGAIPRYLSCGFILEEGLPMETLKAVVTSMAE 118
Cdd:cd02194   26 DAAVLKPPGGRLVVTTDTLVEGvhfPPDTTPEDIGWKALAVNLSDLAAMGARPLGFLLSLGLPPDTDEEWLEEFYRGLAE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 119 TARAAGIAIVTGDTKvvqRGavDKLFINTAGMGAIPANIHW---GAQtltAGDVLLVSGTLGDHGATILNLREQLGLDGE 195
Cdd:cd02194  106 AADRYGVPLVGGDTT---SG--SELVISVTALGEVEKGKPLrrsGAK---PGDLLYVTGTLGDAAAGLALLLGGLKLPEE 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 196 LVSdcavltPLIQTLRD-IPGVKALRDATRGGVNAV----------VHEFAAACGCGIELSEAALPVKPAVRgvCELLGL 264
Cdd:cd02194  178 LYE------ELIERHLRpEPRLELGRALAEGLATAMidisdglladLGHIAEASGVGAVIDLDKLPLSPALR--AAELGE 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 226524740 265 DALNFANEG----KLVIAVERNAAEQVLAAlhshpLGKDAALIGEVV 307
Cdd:cd02194  250 DALELALSGgedyELLFTVPPENAEAAAAK-----LGVPVTVIGRVT 291
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
 53-153 5.56e-20

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


Pssm-ID: 459859 [Multi-domain]  Cd Length: 104  Bit Score: 83.26  E-value: 5.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740   53 LAFSTDS----YVIDPLFFPGgnigKLAICGTANDVAVSGAIPRYLSCGFILEEGL-PMETLKAVVTSMAETARAAGIAI 127
Cdd:pfam00586   5 VAVTTDGhgtpSLVDPYHFPG----AKAVAGNLSDIAAMGARPLAFLDSLALPGGPeVEWVLEEIVEGIAEACREAGVPL 80

                          90       100
                  ....*....|....*....|....*.
gi 226524740  128 VTGDTKVVQRGavDKLFINTAGMGAI 153
Cdd:pfam00586  81 VGGDTSFDPEG--GKPTISVTAVGIV 104
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
 18-316 1.19e-15

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 76.41  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  18 LINSLFMEAFANPWLAEQEDQARLDlaqlVAEGDRLAFSTDSYVIDPLFFPGG----NIGKLAIcgTAN--DVAVSGAIP 91
Cdd:PRK05731   8 LIARLFARRPSSRELGIGDDAALLG----PPPGQRLVVSTDMLVEGVHFRPDWsspeDLGYKAL--AVNlsDLAAMGARP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  92 RYLSCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTKvvqRGavDKLFIN-TAgMGAIPANihwgaQTLT----- 165
Cdd:PRK05731  82 AAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTT---RG--PDLSISvTA-IGDVPGG-----RALRrsgak 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 166 AGDVLLVSGTLGDhGATILNLreqlgLDGELVSDCAVLTPLIQT-LRDIPGVK---ALRDATRG------GVNAVVHEFA 235
Cdd:PRK05731 151 PGDLVAVTGTLGD-SAAGLAL-----LLNGLRVPDADAAALISRhLRPQPRVGlgqALAGLASAaidisdGLAADLGHIA 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 236 AACGCGIELSEAALPVKPAVRGVceLLGLDALNFANEG----KLVIAVERNAAEQVLAALHSHplGKDAALIGEVVERKG 311
Cdd:PRK05731 225 EASGVGADIDLDALPISPALREA--AEGEDALRWALSGgedyELLFTFPPENRGALLAAAGHL--GVGVTIIGRVTEGEG 300


                 ....*
gi 226524740 312 VRLAG 316
Cdd:PRK05731 301 VVVDG 305
SelD cd02195
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ...
 99-306 1.73e-04

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: 42.51  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  99 ILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTkVVQRGavdkLFINTAGMGAIPANIHWGAQTLTAGDVLLVSGTLGd 178
Cdd:cd02195  102 RKLPALQEEVLREILAGGKDKLREAGAVLVGGHT-IEGPE----PKYGLSVTGLVHPNKILRNSGAKPGDVLILTKPLG- 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 179 hGATILNLREQLGLDGELVSDC-AVLTPLIQTLRDI---PGVKALRDATRGGVNAVVHEFAAACGCGIELSEAALPVkpa 254
Cdd:cd02195  176 -TGILFAAEMAGLARGEDIDAAlESMARLNRAAAELlrkYGAHACTDVTGFGLLGHLLEMARASGVSAEIDLDKLPL--- 251

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226524740 255 vrgvcellgldalnFANEGKLVIAVERNAAEQVLAALHShpLGKDAALIGEV 306
Cdd:cd02195  252 --------------LQTSGGLLAAVPPEDAAALLALLKA--GGPPAAIIGEV 287
SelD COG0709
Selenophosphate synthase [Amino acid transport and metabolism];
273-314 6.27e-04

Selenophosphate synthase [Amino acid transport and metabolism];


Pssm-ID: 440473 [Multi-domain]  Cd Length: 346  Bit Score: 41.21  E-value: 6.27e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 226524740 273 GKLVIAVERNAAEQVLAALHSHplGKDAALIGEVVERKGVRL 314
Cdd:COG0709  304 GGLLIAVPPEAAEELLAALRAA--GYAAAIIGEVTAGEGGAI 343
PLN03206 PLN03206
phosphoribosylformylglycinamidine synthase; Provisional
 189-306 4.29e-03

phosphoribosylformylglycinamidine synthase; Provisional


Pssm-ID: 178745 [Multi-domain]  Cd Length: 1307  Bit Score: 38.98  E-value: 4.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740  189 QLGLDGELVSDCAVLTPL---IQTLRDIPGVKALRDATRGGVNAVVHEFAAACGCGIELsEAALPVKPAvrgvcellgLD 265
Cdd:PLN03206  852 QIGDDCPDLDDVAYLKKAfeaTQDLIAKRLISAGHDISDGGLVVTLLEMAFAGNCGINV-DLPSSGHSA---------FE 921

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 226524740  266 ALnFANEGKLVIAVERNAAEQVLAALHSHplGKDAALIGEV 306
Cdd:PLN03206  922 TL-FAEELGLVLEVSRKNLDAVMEKLAAA--GVTAEVIGQV 959
PRK00943 PRK00943
selenide, water dikinase SelD;
210-315 6.20e-03

selenide, water dikinase SelD;


Pssm-ID: 234870 [Multi-domain]  Cd Length: 347  Bit Score: 37.91  E-value: 6.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226524740 210 LRDIPGVKALRDATRGGVNAVVHEFAAACGCGIELSEAALPVKPAVRGVCEL---LGLDALNFANEGK------------ 274
Cdd:PRK00943 216 FAKLPGVHAMTDVTGFGLLGHLLEMCQGAGLTARVDYAAVPLLPGVEEYIAQgcvPGGTGRNFASYGHligelpdeqral 295

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226524740 275 ---------LVIAVERNAAEQVLAALHSHplGKDAALIGEVVERKGVRLA 315
Cdd:PRK00943 296 lcdpqtsggLLVAVAPEAEAEVLAIAAEH--GIELAAIGELVEARGGRAR 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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