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Conserved domains on  [gi|2468518132|ref|WP_276814333|]
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thiamine-monophosphate kinase, partial [Desulfurococcus amylolyticus]

Protein Classification

thiamine-phosphate kinase( domain architecture ID 11427471)

thiamine-phosphate kinase catalyzes the formation of thiamine pyrophosphate (TPP) from thiamine monophosphate in an ATP- and Mg2+-dependent manner

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ThiL COG0611
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
11-274 9.73e-63

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: 200.37  E-value: 9.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  11 LPWRTWSDIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDTNESLDPWIAVS 90
Cdd:COG0611    54 LDWMSPEDLGWKAVAVNLSDLAAMGARPLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPELTISVT 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  91 VMGFTTCKHPPSRRGARPGDIVIATGSYG--SMGFVAL--HGVVEASGISWVVDNTKRVYLKLEVAnVIMSTYRFIHASM 166
Cdd:COG0611   134 AIGEVPGGRPLLRSGARPGDLVYVTGTLGdaAAGLALLlrGLRVPLEAREYLLERHLRPEPRLALG-RALAEAGLATAMI 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 167 DVSDGLGYTLEQLSELSGYGILLE--NLPVHPAgLREYCKNsiECMWRHVLVGGEEYGAVLIVAGEYLDKVAEELdyYEI 244
Cdd:COG0611   213 DISDGLAADLGHIAEASGVGAEIDldALPLSPA-LREAALG--LDPLELALTGGEDYELLFTVPPEALEALEAAA--LGV 287
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2468518132 245 PYSIIGRVGNmSPGIYI---NGARITVER--WDQF 274
Cdd:COG0611   288 PLTVIGRVTE-GEGVTLddaDGRPIPLEArgWDHF 321
 
Name Accession Description Interval E-value
ThiL COG0611
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
11-274 9.73e-63

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: 200.37  E-value: 9.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  11 LPWRTWSDIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDTNESLDPWIAVS 90
Cdd:COG0611    54 LDWMSPEDLGWKAVAVNLSDLAAMGARPLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPELTISVT 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  91 VMGFTTCKHPPSRRGARPGDIVIATGSYG--SMGFVAL--HGVVEASGISWVVDNTKRVYLKLEVAnVIMSTYRFIHASM 166
Cdd:COG0611   134 AIGEVPGGRPLLRSGARPGDLVYVTGTLGdaAAGLALLlrGLRVPLEAREYLLERHLRPEPRLALG-RALAEAGLATAMI 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 167 DVSDGLGYTLEQLSELSGYGILLE--NLPVHPAgLREYCKNsiECMWRHVLVGGEEYGAVLIVAGEYLDKVAEELdyYEI 244
Cdd:COG0611   213 DISDGLAADLGHIAEASGVGAEIDldALPLSPA-LREAALG--LDPLELALTGGEDYELLFTVPPEALEALEAAA--LGV 287
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2468518132 245 PYSIIGRVGNmSPGIYI---NGARITVER--WDQF 274
Cdd:COG0611   288 PLTVIGRVTE-GEGVTLddaDGRPIPLEArgWDHF 321
ThiL cd02194
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
10-252 3.03e-55

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: 180.06  E-value: 3.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  10 MLPWRTWSDIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDTNESLDPWIAV 89
Cdd:cd02194    50 FPPDTTPEDIGWKALAVNLSDLAAMGARPLGFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELVISV 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  90 SVMGFTTCKHPPSRRGARPGDIVIATGSYG--SMGFVAL--HGVVEASGISWVVDNTKRVYLKLEVAnvIMSTYRFIHAS 165
Cdd:cd02194   130 TALGEVEKGKPLRRSGAKPGDLLYVTGTLGdaAAGLALLlgGLKLPEELYEELIERHLRPEPRLELG--RALAEGLATAM 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 166 MDVSDGLGYTLEQLSELSGYGILLEN--LPVHPAGLREYCKNSIecmWRHVLVGGEEYGAVLIVAGEYLDKVAEELDyye 243
Cdd:cd02194   208 IDISDGLLADLGHIAEASGVGAVIDLdkLPLSPALRAAELGEDA---LELALSGGEDYELLFTVPPENAEAAAAKLG--- 281

                  ....*....
gi 2468518132 244 IPYSIIGRV 252
Cdd:cd02194   282 VPVTVIGRV 290
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
14-274 1.64e-40

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 142.66  E-value: 1.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  14 RTWS---DIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDTNESLDPWIAVS 90
Cdd:PRK05731   54 PDWSspeDLGYKALAVNLSDLAAMGARPAAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTTRGPDLSISVT 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  91 VMGFTTCKHPPSRRGARPGDIVIATG----SYGSMGFVALHGVVEASGISWVVDNTKRVYLKLEVAnVIMStyRFIHASM 166
Cdd:PRK05731  134 AIGDVPGGRALRRSGAKPGDLVAVTGtlgdSAAGLALLLNGLRVPDADAAALISRHLRPQPRVGLG-QALA--GLASAAI 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 167 DVSDGLGYTLEQLSELSGYGILLE--NLPVHPAgLREYckNSIECMWRHVLVGGEEYGAVLIVAGEYLDKVAEELDYYEI 244
Cdd:PRK05731  211 DISDGLAADLGHIAEASGVGADIDldALPISPA-LREA--AEGEDALRWALSGGEDYELLFTFPPENRGALLAAAGHLGV 287
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2468518132 245 PYSIIGRVGNmSPGIYINGARITVER--WDQF 274
Cdd:PRK05731  288 GVTIIGRVTE-GEGVVVDGEPVTLDLkgYDHF 318
thiL TIGR01379
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ...
18-277 8.67e-33

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: 122.44  E-value: 8.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  18 DIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDTNESLDPWIAVSVMGFTTC 97
Cdd:TIGR01379  59 DLGWKAVAVNLSDLAAMGATPKWFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPELVVTVTAIGEAPK 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  98 KHPPSRRGARPGDIVIATGSYGSMGFVALHGVVEASGISWVVDN---------TKRVYLKLEVAnvimstyRFIHASMDV 168
Cdd:TIGR01379 139 GRALLRSGAKPGDLVFVTGTLGDSAAGLALLLKGKKEPDEEDDEallqrhlrpEPRVEEGLALA-------GYANAAIDV 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 169 SDGLGYTLEQLSELSGYGILLEN--LPVHPAgLREYCKNsiECMWRHVLVGGEEYGAVLIVAGEYLDKVAEELdyyEIPY 246
Cdd:TIGR01379 212 SDGLAADLGHIAEASGVGIVIDLdrLPLSSE-LAAWAEG--KNPLEWALSGGEDYELVFTVPPERREALLDAA---KGPL 285
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2468518132 247 SIIGRVGNMSPGIYINGARitVERWDQFRGW 277
Cdd:TIGR01379 286 TRIGRVTEGEGVVLLADGK--TVELLDRLGW 314
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
19-93 5.02e-13

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: 64.00  E-value: 5.02e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468518132  19 IGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILD-LEELVKGLREASNYYDVRITGGDT---NESLDPWIAVSVMG 93
Cdd:pfam00586  24 PGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvLEEIVEGIAEACREAGVPLVGGDTsfdPEGGKPTISVTAVG 102
 
Name Accession Description Interval E-value
ThiL COG0611
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
11-274 9.73e-63

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: 200.37  E-value: 9.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  11 LPWRTWSDIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDTNESLDPWIAVS 90
Cdd:COG0611    54 LDWMSPEDLGWKAVAVNLSDLAAMGARPLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPELTISVT 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  91 VMGFTTCKHPPSRRGARPGDIVIATGSYG--SMGFVAL--HGVVEASGISWVVDNTKRVYLKLEVAnVIMSTYRFIHASM 166
Cdd:COG0611   134 AIGEVPGGRPLLRSGARPGDLVYVTGTLGdaAAGLALLlrGLRVPLEAREYLLERHLRPEPRLALG-RALAEAGLATAMI 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 167 DVSDGLGYTLEQLSELSGYGILLE--NLPVHPAgLREYCKNsiECMWRHVLVGGEEYGAVLIVAGEYLDKVAEELdyYEI 244
Cdd:COG0611   213 DISDGLAADLGHIAEASGVGAEIDldALPLSPA-LREAALG--LDPLELALTGGEDYELLFTVPPEALEALEAAA--LGV 287
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2468518132 245 PYSIIGRVGNmSPGIYI---NGARITVER--WDQF 274
Cdd:COG0611   288 PLTVIGRVTE-GEGVTLddaDGRPIPLEArgWDHF 321
ThiL cd02194
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ...
10-252 3.03e-55

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: 180.06  E-value: 3.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  10 MLPWRTWSDIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDTNESLDPWIAV 89
Cdd:cd02194    50 FPPDTTPEDIGWKALAVNLSDLAAMGARPLGFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELVISV 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  90 SVMGFTTCKHPPSRRGARPGDIVIATGSYG--SMGFVAL--HGVVEASGISWVVDNTKRVYLKLEVAnvIMSTYRFIHAS 165
Cdd:cd02194   130 TALGEVEKGKPLRRSGAKPGDLLYVTGTLGdaAAGLALLlgGLKLPEELYEELIERHLRPEPRLELG--RALAEGLATAM 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 166 MDVSDGLGYTLEQLSELSGYGILLEN--LPVHPAGLREYCKNSIecmWRHVLVGGEEYGAVLIVAGEYLDKVAEELDyye 243
Cdd:cd02194   208 IDISDGLLADLGHIAEASGVGAVIDLdkLPLSPALRAAELGEDA---LELALSGGEDYELLFTVPPENAEAAAAKLG--- 281

                  ....*....
gi 2468518132 244 IPYSIIGRV 252
Cdd:cd02194   282 VPVTVIGRV 290
PRK05731 PRK05731
thiamine monophosphate kinase; Provisional
14-274 1.64e-40

thiamine monophosphate kinase; Provisional


Pssm-ID: 235583 [Multi-domain]  Cd Length: 318  Bit Score: 142.66  E-value: 1.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  14 RTWS---DIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDTNESLDPWIAVS 90
Cdd:PRK05731   54 PDWSspeDLGYKALAVNLSDLAAMGARPAAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTTRGPDLSISVT 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  91 VMGFTTCKHPPSRRGARPGDIVIATG----SYGSMGFVALHGVVEASGISWVVDNTKRVYLKLEVAnVIMStyRFIHASM 166
Cdd:PRK05731  134 AIGDVPGGRALRRSGAKPGDLVAVTGtlgdSAAGLALLLNGLRVPDADAAALISRHLRPQPRVGLG-QALA--GLASAAI 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 167 DVSDGLGYTLEQLSELSGYGILLE--NLPVHPAgLREYckNSIECMWRHVLVGGEEYGAVLIVAGEYLDKVAEELDYYEI 244
Cdd:PRK05731  211 DISDGLAADLGHIAEASGVGADIDldALPISPA-LREA--AEGEDALRWALSGGEDYELLFTFPPENRGALLAAAGHLGV 287
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2468518132 245 PYSIIGRVGNmSPGIYINGARITVER--WDQF 274
Cdd:PRK05731  288 GVTIIGRVTE-GEGVVVDGEPVTLDLkgYDHF 318
thiL TIGR01379
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ...
18-277 8.67e-33

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: 122.44  E-value: 8.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  18 DIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDTNESLDPWIAVSVMGFTTC 97
Cdd:TIGR01379  59 DLGWKAVAVNLSDLAAMGATPKWFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPELVVTVTAIGEAPK 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  98 KHPPSRRGARPGDIVIATGSYGSMGFVALHGVVEASGISWVVDN---------TKRVYLKLEVAnvimstyRFIHASMDV 168
Cdd:TIGR01379 139 GRALLRSGAKPGDLVFVTGTLGDSAAGLALLLKGKKEPDEEDDEallqrhlrpEPRVEEGLALA-------GYANAAIDV 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 169 SDGLGYTLEQLSELSGYGILLEN--LPVHPAgLREYCKNsiECMWRHVLVGGEEYGAVLIVAGEYLDKVAEELdyyEIPY 246
Cdd:TIGR01379 212 SDGLAADLGHIAEASGVGIVIDLdrLPLSSE-LAAWAEG--KNPLEWALSGGEDYELVFTVPPERREALLDAA---KGPL 285
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2468518132 247 SIIGRVGNMSPGIYINGARitVERWDQFRGW 277
Cdd:TIGR01379 286 TRIGRVTEGEGVVLLADGK--TVELLDRLGW 314
PurM-like cd00396
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ...
18-251 2.61e-19

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: 83.98  E-value: 2.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  18 DIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDTNES-----LDPWIAVSVM 92
Cdd:cd00396    19 AGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAEACNQLGVPIVGGHTSVSpgtmgHKLSLAVFAI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  93 GFTTCKHPPSRRGARPGDIVIATGsygsmgfvalhgvveasgiswvVDNTKRvylklevanviMSTYRFIHASMDVSD-G 171
Cdd:cd00396    99 GVVEKDRVIDSSGARPGDVLILTG----------------------VDAVLE-----------LVAAGDVHAMHDITDgG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 172 LGYTLEQLSELSGYG--ILLENLPVHPaGLREYCKNSIECMWRhvlvGGEEYGAVLIVAGEYLDKVAEELDYYEIPYSII 249
Cdd:cd00396   146 LLGTLPELAQASGVGaeIDLEAIPLDE-VVRWLCVEHIEEALL----FNSSGGLLIAVPAEEADAVLLLLNGNGIDAAVI 220

                  ..
gi 2468518132 250 GR 251
Cdd:cd00396   221 GR 222
PurM-like1 cd06061
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ...
15-252 3.69e-16

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: 76.87  E-value: 3.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  15 TWSDIGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDT--NESLDPWIAVS-V 91
Cdd:cd06061    55 AGKDAGWLAVHIAANDIATSGARPRWLLVTLLLPPGTDEEELKAIMREINEAAKELGVSIVGGHTevTPGVTRPIISVtA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  92 MGFTTCKHPPSRRGARPGDIVIATGSYGsMGFVAL-----HGVVEASGISWVVDNTKRVYLKLEVAN-VIMSTYRFIHAS 165
Cdd:cd06061   135 IGKGEKDKLVTPSGAKPGDDIVMTKGAG-IEGTAIlandfEEELKKRLSEEELREAAKLFYKISVVKeALIAAEAGVTAM 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 166 MDVSDG--LGYTLEqLSELSGYG--ILLENLPVhPAGLREYCK-------NSIECmwrhvlvggeeyGAVLI-VAGEYLD 233
Cdd:cd06061   214 HDATEGgiLGALWE-VAEASGVGlrIEKDKIPI-RQETKEICEalgidplRLISS------------GTLLItVPPEKGD 279
                         250
                  ....*....|....*....
gi 2468518132 234 KVAEELDYYEIPYSIIGRV 252
Cdd:cd06061   280 ELVDALEEAGIPASVIGKI 298
AIRS pfam00586
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ...
19-93 5.02e-13

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: 64.00  E-value: 5.02e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468518132  19 IGWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILD-LEELVKGLREASNYYDVRITGGDT---NESLDPWIAVSVMG 93
Cdd:pfam00586  24 PGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvLEEIVEGIAEACREAGVPLVGGDTsfdPEGGKPTISVTAVG 102
HypE cd02197
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ...
18-252 2.10e-10

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: 60.16  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  18 DIGWMALTGALSDVVVKGGVP---SVAMI---GLGLSsetdilDLEELVKGLREASNYYDVRITGGDTN----ESLDP-W 86
Cdd:cd02197    57 DIGKLAVCGTVNDLAMMGAKPlylSLGFIleeGFPLE------DLERIVKSMAEAAREAGVKIVTGDTKvvpkGKADGiF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  87 IAVSVMGFTTCKHPPSRRGARPGDIVIATGSYG-----------SMGFV--------ALHGVVEAsgiswvvdntkrvyl 147
Cdd:cd02197   131 INTTGIGVIPRGVIISPSNIRPGDKIIVSGTIGdhgaailaareGLGFEtdiesdcaPLNGLVEA--------------- 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 148 klevanvIMSTYRFIHASMDVS-DGLGYTLEQLSELSGYGILL--ENLPVHPAgLREYCKnsiecmwrhvLVGGE----- 219
Cdd:cd02197   196 -------LLEAGPGIHAMRDPTrGGLAAVLNEIARASGVGIEIeeEAIPVREE-VRGACE----------MLGLDplyla 257
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2468518132 220 -EYGAVLIVAGEYLDKVAEELDyyEIPY----SIIGRV 252
Cdd:cd02197   258 nEGKFVAIVPPEDAEEVLEALR--SHPLgkeaAIIGEV 293
SelD cd02195
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ...
27-252 3.55e-08

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: 53.29  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  27 ALSDVVVKGGVPSVAMIGLGLSSETDILD---LEELVKGLREASNYYDVRITGGDTNESLDPWIAVSVMGFTTCKHPPSR 103
Cdd:cd02195    80 ALSDIYAMGAKPLSALAIVTLPRKLPALQeevLREILAGGKDKLREAGAVLVGGHTIEGPEPKYGLSVTGLVHPNKILRN 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 104 RGARPGDIVIATGSYGSMGFVALHGVVEASGisWVVDNTKRVYLKLE-VANVIMSTYrFIHASMDVSdG---LGYTLEqL 179
Cdd:cd02195   160 SGAKPGDVLILTKPLGTGILFAAEMAGLARG--EDIDAALESMARLNrAAAELLRKY-GAHACTDVT-GfglLGHLLE-M 234
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468518132 180 SELSGYGILL--ENLPVHpaglreycknsiecmwrhvlvggEEYGAVLI-VAGEYLDKVAEELDYYEIPYSIIGRV 252
Cdd:cd02195   235 ARASGVSAEIdlDKLPLL-----------------------QTSGGLLAaVPPEDAAALLALLKAGGPPAAIIGEV 287
AIRS_C pfam02769
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ...
107-252 1.26e-06

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: 47.34  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 107 RPGDIVIATGSYG--SMGFVALHGVVEASGISWV-VDNTKRVYLKLEVANVIMSTYRFIHASMDVSD-GLGYTLEQLSEL 182
Cdd:pfam02769   1 KPGDVLILLGSSGlhGAGLSLSRKGLEDSGLAAVqLGDPLLEPTLIYVKLLLAALGGLVKAMHDITGgGLAGALAEMAPA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468518132 183 SGYG--ILLENLPV-HPAGLREYcknsiecMWRhvlvGGEEYGAVLIVAGEYLDKVAEELDYYEIPYSIIGRV 252
Cdd:pfam02769  81 SGVGaeIDLDKVPIfEELMLPLE-------MLL----SENQGRGLVVVAPEEAEAVLAILEKEGLEAAVIGEV 142
PurM-like2 cd02691
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ...
20-275 5.51e-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: 43.92  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  20 GWMALTGALSDVVVKGGVPSVAMIGLGLSSETDILDLEELVKGLREASNYYDVRITGGDT---------NESLDPwiAVS 90
Cdd:cd02691    68 GFHATRAALRDVMVMGARPVALLSDIHLADDGDVGKLFDFTAGVTAVSEATGVPLVAGSTlriggdmvlGDRLVG--GVG 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  91 VMGFTtcKHPPSRRG-ARPGDIVIAT-GSYGsmGFVA----LHGVVEasgiswVVDNTKRVYLKLEVANVIMS-TYRFIH 163
Cdd:cd02691   146 AVGRS--KSDPSRRKnAEPGDLILMTeGAGG--GTITttaiYHGMPD------VVEETLNVDFIKACEALRDSgLVSKVH 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132 164 ASMDVSDG--LGYTLEqLSELSGYGILL-----ENLpVHPAGLREYCKNSIECMwrhvlvgGEEYGAVLIVA-GEYLDKV 235
Cdd:cd02691   216 SMTDVTNGgiRGDALE-ISKTAGVSLVFdeekvRSL-INPKVLKMLEELGIDPL-------GVSLDSLMIIApEEDAVDI 286
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2468518132 236 AEELDYYEIPYSIIGRVGNmSPGIYINGARITVERWDQFR 275
Cdd:cd02691   287 IRTLREAGVRADEVGRVEE-GRGVPLVVTGEGRELKPAFR 325
SelD COG0709
Selenophosphate synthase [Amino acid transport and metabolism];
27-115 7.16e-04

Selenophosphate synthase [Amino acid transport and metabolism];


Pssm-ID: 440473 [Multi-domain]  Cd Length: 346  Bit Score: 40.44  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518132  27 ALSDVVVKGGVPSVAMIGLGLSSET-DILDLEELVKGLREASNYYDVRITGGDTNESLDPWIAVSVMGFTTCKHPPSRRG 105
Cdd:COG0709    86 ALSDVYAMGGRPLTALAIVGFPIDKlPEEVLAEILAGGADKCREAGAPLAGGHSIDDPEPKYGLAVTGLVHPDKVLRNAG 165
                          90
                  ....*....|
gi 2468518132 106 ARPGDIVIAT 115
Cdd:COG0709   166 ARPGDVLILT 175
 
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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