|
Name |
Accession |
Description |
Interval |
E-value |
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
15-344 |
2.86e-150 |
|
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: 425.71 E-value: 2.86e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 15 LGEFGLIDHLTKHFDITQESTLKSIGDDAAVLDFKDKKVVVSTDLLIEGVHFDLAYMPLKHLGYKAVVVNVSDICAMNAK 94
Cdd:COG0611 1 MGEFGLIERLFKRLALRGPDVLLGIGDDAAVLDPPGGRLVVTTDMLVEGVHFPLDWMSPEDLGWKAVAVNLSDLAAMGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 95 PTQITVSVAVSNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSqKGLIISITAIGEADENELVYRNGAKKTDLLVVTG 174
Cdd:COG0611 81 PLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRS-PELTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 175 DLGAAYMGLQVLEREKQVFqvnpnnqpdLDPYTYLVERQLKPEARKDVRTLLHALDIkPNAMIDISDGLSSEIMHICKQS 254
Cdd:COG0611 160 TLGDAAAGLALLLRGLRVP---------LEAREYLLERHLRPEPRLALGRALAEAGL-ATAMIDISDGLAADLGHIAEAS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 255 KVGCNLYEDKLPLDPQFISTCeeFNIDSTTVAINGGEDYELLFTIDINDFDKIKG---NPNFSVIGHMTEEnEGIHLVTR 331
Cdd:COG0611 230 GVGAEIDLDALPLSPALREAA--LGLDPLELALTGGEDYELLFTVPPEALEALEAaalGVPLTVIGRVTEG-EGVTLDDA 306
|
330
....*....|...
gi 1053293782 332 ANTKIALKARGWD 344
Cdd:COG0611 307 DGRPIPLEARGWD 319
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
16-320 |
2.25e-113 |
|
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: 331.05 E-value: 2.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 16 GEFGLIDHLTKHFDiTQESTLKSIGDDAAVLDFKDKKVVVSTDLLIEGVHFDLAyMPLKHLGYKAVVVNVSDICAMNAKP 95
Cdd:cd02194 1 GEFELIDRLFKRLG-AGPGVLLGIGDDAAVLKPPGGRLVVTTDTLVEGVHFPPD-TTPEDIGWKALAVNLSDLAAMGARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 96 TQITVSVAVSNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSqKGLIISITAIGEADENELVYRNGAKKTDLLVVTGD 175
Cdd:cd02194 79 LGFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSG-SELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 176 LGAAYMGLQVLEREKqvfqvnpnnQPDLDPYTYLVERQLKPEARkdVRTLLHALDIKPNAMIDISDGLSSEIMHICKQSK 255
Cdd:cd02194 158 LGDAAAGLALLLGGL---------KLPEELYEELIERHLRPEPR--LELGRALAEGLATAMIDISDGLLADLGHIAEASG 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053293782 256 VGCNLYEDKLPLDPQFisTCEEFNIDSTTVAINGGEDYELLFTIDINDFDKI--KGNPNFSVIGHMT 320
Cdd:cd02194 227 VGAVIDLDKLPLSPAL--RAAELGEDALELALSGGEDYELLFTVPPENAEAAaaKLGVPVTVIGRVT 291
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
16-344 |
1.21e-102 |
|
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: 304.64 E-value: 1.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 16 GEFGLIDHLTKHFdITQESTLKSIGDDAAVLDFKD-KKVVVSTDLLIEGVHFdLAYMPLKHLGYKAVVVNVSDICAMNAK 94
Cdd:TIGR01379 1 GEFELIDRILRRL-VQDPDVALGIGDDAALVSAPEgRDLVLTTDTLVEGVHF-PPDTTPEDLGWKAVAVNLSDLAAMGAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 95 PTQITVSVAVSNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSqKGLIISITAIGEADENELVYRNGAKKTDLLVVTG 174
Cdd:TIGR01379 79 PKWFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSS-PELVVTVTAIGEAPKGRALLRSGAKPGDLVFVTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 175 DLGAAYMGLQVLEREKQVfqvnpnnqPDLDPYTYLVERQLKPEARKDVRtllHALDIKPNAMIDISDGLSSEIMHICKQS 254
Cdd:TIGR01379 158 TLGDSAAGLALLLKGKKE--------PDEEDDEALLQRHLRPEPRVEEG---LALAGYANAAIDVSDGLAADLGHIAEAS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 255 KVGCNLYEDKLPLDPQFISTCEefNIDSTTVAINGGEDYELLFTIDINDFDKIKG--NPNFSVIGHMTEEnEGIHLVTRA 332
Cdd:TIGR01379 227 GVGIVIDLDRLPLSSELAAWAE--GKNPLEWALSGGEDYELVFTVPPERREALLDaaKGPLTRIGRVTEG-EGVVLLADG 303
|
330
....*....|..
gi 1053293782 333 NTKIALKARGWD 344
Cdd:TIGR01379 304 KTVELLDRLGWQ 315
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
13-344 |
7.91e-95 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 284.80 E-value: 7.91e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 13 AQLGEFGLIDHLTKHFditQESTLKSIGDDAAVLDFK-DKKVVVSTDLLIEGVHFDLAYMPLKHLGYKAVVVNVSDICAM 91
Cdd:PRK05731 1 MAMGEFDLIARLFARR---PSSRELGIGDDAALLGPPpGQRLVVSTDMLVEGVHFRPDWSSPEDLGYKALAVNLSDLAAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 92 NAKPTQITVSVAVSNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSQKgLIISITAIGEADENELVYRNGAKKTDLLV 171
Cdd:PRK05731 78 GARPAAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTTRGPD-LSISVTAIGDVPGGRALRRSGAKPGDLVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 172 VTGDLGAAYMGLQVLEREKQVFQvnpnnqpdlDPYTYLVERQLKPEARKDvrtLLHALDIKPNAMIDISDGLSSEIMHIC 251
Cdd:PRK05731 157 VTGTLGDSAAGLALLLNGLRVPD---------ADAAALISRHLRPQPRVG---LGQALAGLASAAIDISDGLAADLGHIA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 252 KQSKVGCNLYEDKLPLDPQFistcEEFNIDST--TVAINGGEDYELLFTIDINDFDKI-----KGNPNFSVIGHMTEEne 324
Cdd:PRK05731 225 EASGVGADIDLDALPISPAL----REAAEGEDalRWALSGGEDYELLFTFPPENRGALlaaagHLGVGVTIIGRVTEG-- 298
|
330 340
....*....|....*....|
gi 1053293782 325 giHLVTRANTKIALKARGWD 344
Cdd:PRK05731 299 --EGVVVDGEPVTLDLKGYD 316
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
41-153 |
7.23e-25 |
|
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: 96.75 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 41 DDAAVldfkdkkvVVSTD-----LLIEGVHFdlaymplkhLGYKAVVVNVSDICAMNAKPTQITVSVAVSNRFPLEA-LE 114
Cdd:pfam00586 1 DDAAV--------AVTTDghgtpSLVDPYHF---------PGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvLE 63
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1053293782 115 ELFAGITLAAKEYKVDVIGGDTTSS--QKGLIISITAIGEA 153
Cdd:pfam00586 64 EIVEGIAEACREAGVPLVGGDTSFDpeGGKPTISVTAVGIV 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
15-344 |
2.86e-150 |
|
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: 425.71 E-value: 2.86e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 15 LGEFGLIDHLTKHFDITQESTLKSIGDDAAVLDFKDKKVVVSTDLLIEGVHFDLAYMPLKHLGYKAVVVNVSDICAMNAK 94
Cdd:COG0611 1 MGEFGLIERLFKRLALRGPDVLLGIGDDAAVLDPPGGRLVVTTDMLVEGVHFPLDWMSPEDLGWKAVAVNLSDLAAMGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 95 PTQITVSVAVSNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSqKGLIISITAIGEADENELVYRNGAKKTDLLVVTG 174
Cdd:COG0611 81 PLAALLSLALPPDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRS-PELTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 175 DLGAAYMGLQVLEREKQVFqvnpnnqpdLDPYTYLVERQLKPEARKDVRTLLHALDIkPNAMIDISDGLSSEIMHICKQS 254
Cdd:COG0611 160 TLGDAAAGLALLLRGLRVP---------LEAREYLLERHLRPEPRLALGRALAEAGL-ATAMIDISDGLAADLGHIAEAS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 255 KVGCNLYEDKLPLDPQFISTCeeFNIDSTTVAINGGEDYELLFTIDINDFDKIKG---NPNFSVIGHMTEEnEGIHLVTR 331
Cdd:COG0611 230 GVGAEIDLDALPLSPALREAA--LGLDPLELALTGGEDYELLFTVPPEALEALEAaalGVPLTVIGRVTEG-EGVTLDDA 306
|
330
....*....|...
gi 1053293782 332 ANTKIALKARGWD 344
Cdd:COG0611 307 DGRPIPLEARGWD 319
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
16-320 |
2.25e-113 |
|
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: 331.05 E-value: 2.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 16 GEFGLIDHLTKHFDiTQESTLKSIGDDAAVLDFKDKKVVVSTDLLIEGVHFDLAyMPLKHLGYKAVVVNVSDICAMNAKP 95
Cdd:cd02194 1 GEFELIDRLFKRLG-AGPGVLLGIGDDAAVLKPPGGRLVVTTDTLVEGVHFPPD-TTPEDIGWKALAVNLSDLAAMGARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 96 TQITVSVAVSNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSqKGLIISITAIGEADENELVYRNGAKKTDLLVVTGD 175
Cdd:cd02194 79 LGFLLSLGLPPDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSG-SELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 176 LGAAYMGLQVLEREKqvfqvnpnnQPDLDPYTYLVERQLKPEARkdVRTLLHALDIKPNAMIDISDGLSSEIMHICKQSK 255
Cdd:cd02194 158 LGDAAAGLALLLGGL---------KLPEELYEELIERHLRPEPR--LELGRALAEGLATAMIDISDGLLADLGHIAEASG 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053293782 256 VGCNLYEDKLPLDPQFisTCEEFNIDSTTVAINGGEDYELLFTIDINDFDKI--KGNPNFSVIGHMT 320
Cdd:cd02194 227 VGAVIDLDKLPLSPAL--RAAELGEDALELALSGGEDYELLFTVPPENAEAAaaKLGVPVTVIGRVT 291
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
16-344 |
1.21e-102 |
|
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: 304.64 E-value: 1.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 16 GEFGLIDHLTKHFdITQESTLKSIGDDAAVLDFKD-KKVVVSTDLLIEGVHFdLAYMPLKHLGYKAVVVNVSDICAMNAK 94
Cdd:TIGR01379 1 GEFELIDRILRRL-VQDPDVALGIGDDAALVSAPEgRDLVLTTDTLVEGVHF-PPDTTPEDLGWKAVAVNLSDLAAMGAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 95 PTQITVSVAVSNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSqKGLIISITAIGEADENELVYRNGAKKTDLLVVTG 174
Cdd:TIGR01379 79 PKWFLLSLGLPSDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSS-PELVVTVTAIGEAPKGRALLRSGAKPGDLVFVTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 175 DLGAAYMGLQVLEREKQVfqvnpnnqPDLDPYTYLVERQLKPEARKDVRtllHALDIKPNAMIDISDGLSSEIMHICKQS 254
Cdd:TIGR01379 158 TLGDSAAGLALLLKGKKE--------PDEEDDEALLQRHLRPEPRVEEG---LALAGYANAAIDVSDGLAADLGHIAEAS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 255 KVGCNLYEDKLPLDPQFISTCEefNIDSTTVAINGGEDYELLFTIDINDFDKIKG--NPNFSVIGHMTEEnEGIHLVTRA 332
Cdd:TIGR01379 227 GVGIVIDLDRLPLSSELAAWAE--GKNPLEWALSGGEDYELVFTVPPERREALLDaaKGPLTRIGRVTEG-EGVVLLADG 303
|
330
....*....|..
gi 1053293782 333 NTKIALKARGWD 344
Cdd:TIGR01379 304 KTVELLDRLGWQ 315
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
13-344 |
7.91e-95 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 284.80 E-value: 7.91e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 13 AQLGEFGLIDHLTKHFditQESTLKSIGDDAAVLDFK-DKKVVVSTDLLIEGVHFDLAYMPLKHLGYKAVVVNVSDICAM 91
Cdd:PRK05731 1 MAMGEFDLIARLFARR---PSSRELGIGDDAALLGPPpGQRLVVSTDMLVEGVHFRPDWSSPEDLGYKALAVNLSDLAAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 92 NAKPTQITVSVAVSNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSQKgLIISITAIGEADENELVYRNGAKKTDLLV 171
Cdd:PRK05731 78 GARPAAFLLALALPKDLDEAWLEALADGLFELADRYGAELIGGDTTRGPD-LSISVTAIGDVPGGRALRRSGAKPGDLVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 172 VTGDLGAAYMGLQVLEREKQVFQvnpnnqpdlDPYTYLVERQLKPEARKDvrtLLHALDIKPNAMIDISDGLSSEIMHIC 251
Cdd:PRK05731 157 VTGTLGDSAAGLALLLNGLRVPD---------ADAAALISRHLRPQPRVG---LGQALAGLASAAIDISDGLAADLGHIA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 252 KQSKVGCNLYEDKLPLDPQFistcEEFNIDST--TVAINGGEDYELLFTIDINDFDKI-----KGNPNFSVIGHMTEEne 324
Cdd:PRK05731 225 EASGVGADIDLDALPISPAL----REAAEGEDalRWALSGGEDYELLFTFPPENRGALlaaagHLGVGVTIIGRVTEG-- 298
|
330 340
....*....|....*....|
gi 1053293782 325 giHLVTRANTKIALKARGWD 344
Cdd:PRK05731 299 --EGVVVDGEPVTLDLKGYD 316
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
40-326 |
5.63e-33 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 124.80 E-value: 5.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 40 GDDAAVLDFKDKKVVVSTDLL----IEGvhfdlaymPLKHLGYKAVVVNVSDICAMNAKPTQITVSVAVSNRFPLEALEE 115
Cdd:COG0309 30 GEDAAVLDLGGGRLAFTTDSFvvspIFF--------PGGDIGKLAVHGTVNDLAVSGAKPLYLSVSLILEEGFPLEDLER 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 116 LFAGITLAAKEYKVDVIGGDT----TSSQKGLIISITAIGEADENELVYRNGAKKTDLLVVTGDL---GAAYMglqvLER 188
Cdd:COG0309 102 IVESMAEAAREAGVSIVTGDTkvveRGGVDGPFINTTGIGVVPKGRLISPSGARPGDKIIVTGGIgdhGTAIL----AAR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 189 EKQVFQVNPnnQPDLDPYTYLVErQLKPEARKDVRtllhaldikpnAMIDISD-GLSSEIMHICKQSKVGCNLYEDKLPL 267
Cdd:COG0309 178 EGLELEGEL--LSDAAPLNDLVS-VLLEAAPGGVH-----------AMRDPTRgGLAGALNEIAEASGVGIEIDEDAIPV 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1053293782 268 DPQFISTCEEFNIDSTTVAiNGGedyELLFTIDINDFDKI-----KGNPNFSVIGHMTEENEGI 326
Cdd:COG0309 244 RPEVRGICELLGLDPLYLA-NEG---KLVAVVPPEDAEAVlealrAHGIDAAIIGEVTEGPPGR 303
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
38-281 |
1.46e-30 |
|
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: 117.70 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 38 SIGDDAAVLDFKDKKVVVSTDLLIEGVhfdlaymplKHLGYKAVVVNVSDICAMNAKPTQITVSVAVSNRFPLEALEELF 117
Cdd:cd06061 30 GGGEDAAVVDFGGKVLVVSTDPITGAG---------KDAGWLAVHIAANDIATSGARPRWLLVTLLLPPGTDEEELKAIM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 118 AGITLAAKEYKVDVIGGDT--TSSQKGLIISITAIGEADENELVYRNGAKKTDLLVVTGDLGAAYMGLQVLEREKQVFQV 195
Cdd:cd06061 101 REINEAAKELGVSIVGGHTevTPGVTRPIISVTAIGKGEKDKLVTPSGAKPGDDIVMTKGAGIEGTAILANDFEEELKKR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 196 npnnqpdldpytyLVERQLKPEARKD-----VRTLLHALDIKPNAMIDISD-GLSSEIMHICKQSKVGCNLYEDKLPLDP 269
Cdd:cd06061 181 -------------LSEEELREAAKLFykisvVKEALIAAEAGVTAMHDATEgGILGALWEVAEASGVGLRIEKDKIPIRQ 247
|
250
....*....|..
gi 1053293782 270 QFISTCEEFNID 281
Cdd:cd06061 248 ETKEICEALGID 259
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
41-153 |
7.23e-25 |
|
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: 96.75 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 41 DDAAVldfkdkkvVVSTD-----LLIEGVHFdlaymplkhLGYKAVVVNVSDICAMNAKPTQITVSVAVSNRFPLEA-LE 114
Cdd:pfam00586 1 DDAAV--------AVTTDghgtpSLVDPYHF---------PGAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVEWvLE 63
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1053293782 115 ELFAGITLAAKEYKVDVIGGDTTSS--QKGLIISITAIGEA 153
Cdd:pfam00586 64 EIVEGIAEACREAGVPLVGGDTSFDpeGGKPTISVTAVGIV 104
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
20-286 |
1.96e-19 |
|
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: 87.12 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 20 LIDHL-TKHFDitqeSTLKSIGDDAAVLDFKDKKVVVSTDlliegvhfdlAYM--PLK----HLGYKAVVVNVSDICAMN 92
Cdd:cd02197 9 LIEELfLKAFD----NPILEVLEDAAALLVGGGRLAFTTD----------SFVvsPLFfpggDIGKLAVCGTVNDLAMMG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 93 AKPTQITVSVAVSNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSQKG----LIISITAIGEADENELVYRNGAKKTD 168
Cdd:cd02197 75 AKPLYLSLGFILEEGFPLEDLERIVKSMAEAAREAGVKIVTGDTKVVPKGkadgIFINTTGIGVIPRGVIISPSNIRPGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 169 LLVVTGDL---GAAYMglqvLEREKQVFQVNPnnQPDLDPYTYLVErqlkpearkdvrTLLHAlDIKPNAMIDIS-DGLS 244
Cdd:cd02197 155 KIIVSGTIgdhGAAIL----AAREGLGFETDI--ESDCAPLNGLVE------------ALLEA-GPGIHAMRDPTrGGLA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1053293782 245 SEIMHICKQSKVGCNLYEDKLPLDPQFISTCEEFNIDSTTVA 286
Cdd:cd02197 216 AVLNEIARASGVGIEIEEEAIPVREEVRGACEMLGLDPLYLA 257
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
61-298 |
3.64e-18 |
|
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: 82.06 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 61 IEGVHFDLAYMPlKHLGYKAVVVNVSDICAMNAKPTQITVSVAVSNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSQ 140
Cdd:cd00396 6 TDGINPPLAINP-WAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEVDILEDVVDGVAEACNQLGVPIVGGHTSVSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 141 KG----LIISITAIGEADENELVYRNGAKKTDLLVVTGdlgaaymglqvlerekqvfqvnpnnqpdldpytylverqlkp 216
Cdd:cd00396 85 GTmghkLSLAVFAIGVVEKDRVIDSSGARPGDVLILTG------------------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 217 eaRKDVRTLLHALDIkpNAMIDISD-GLSSEIMHICKQSKVGCNLYEDKLPLDPQFISTCEEFNIDsttvAINGGEDYEL 295
Cdd:cd00396 123 --VDAVLELVAAGDV--HAMHDITDgGLLGTLPELAQASGVGAEIDLEAIPLDEVVRWLCVEHIEE----ALLFNSSGGL 194
|
...
gi 1053293782 296 LFT 298
Cdd:cd00396 195 LIA 197
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
38-319 |
3.46e-16 |
|
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: 77.56 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 38 SIGDDAAVLDFKDKKVVV-STDlliegvHFdlayMPL----KHLGyKAVVVNV-SDICAMNAKPTQITVSVAV---SNRF 108
Cdd:cd02195 39 GTGDDAAVYRLPGGLALVqTTD------FF----PPIvddpYLFG-RIAAANAlSDIYAMGAKPLSALAIVTLprkLPAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 109 PLEALEELFAGITLAAKEYKVDVIGGDTTSSQkGLIISITAIGEADENELVYRNGAKKTDLLVVTGDLG-----AAYMGL 183
Cdd:cd02195 108 QEEVLREILAGGKDKLREAGAVLVGGHTIEGP-EPKYGLSVTGLVHPNKILRNSGAKPGDVLILTKPLGtgilfAAEMAG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 184 QVLERekqvfqvnpnnqpDLDpytylverqlkpEARKDVRTLLH-----ALDIKPNAMIDISD-GLSSEIMHICKQSKVG 257
Cdd:cd02195 187 LARGE-------------DID------------AALESMARLNRaaaelLRKYGAHACTDVTGfGLLGHLLEMARASGVS 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1053293782 258 CNLYEDKLPLdpqfISTCeefnidsttvainGGedyeLLFTIDINDFDKIK-----GNPNFSVIGHM 319
Cdd:cd02195 242 AEIDLDKLPL----LQTS-------------GG----LLAAVPPEDAAALLallkaGGPPAAIIGEV 287
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
21-176 |
2.05e-13 |
|
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM related proteins includes Hydrogen expression/formation protein HypE, AIR synthases, FGAM synthase and Selenophosphate synthetase (SelD). They all contain two conserved domains and seem to dimerize. The N-terminal domain forms the dimer interface and is a putative ATP binding domain.
Pssm-ID: 100028 [Multi-domain] Cd Length: 283 Bit Score: 69.55 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 21 IDHLTKHFDITQESTLK---SIGDDAAVLDfkdkkvVVSTDLL--IEGVHFDL-AYMPlKHLGYKAVVVNVSDICAMNAK 94
Cdd:cd02192 13 IQDVVAILPDAPFDSLGvaaDLGDDAAAIP------DGDGYLLlaADGIWPSLvEADP-WWAGYCSVLVNVSDIAAMGGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 95 PTQITVSVAVSNRfplEALEELFAGITLAAKEYKVDVIGG----DTTSSQkgliISITAIGEADEnELVYRNGAKKTDLL 170
Cdd:cd02192 86 PLAMVDALWSPSA---EAAAQVLEGMRDAAEKFGVPIVGGhthpDSPYNA----LSVAILGRARK-DLLISFGAKPGDRL 157
|
....*.
gi 1053293782 171 VVTGDL 176
Cdd:cd02192 158 ILAIDL 163
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
21-176 |
6.20e-13 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 68.65 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 21 IDHLTKHFDITQE-STLKSIGDDAAVLDFKDKKVVvstdLLIEGVHFDL-AYMPlKHLGYKAVVVNVSDICAMNAKPTQI 98
Cdd:COG2144 23 IADVVRALGLASSgGTAAAFGDDAAAIPDGDGYLL----LAAEGIWPKFvEADP-WFAGYCSVLVNVSDIAAMGGRPLAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 99 TVSVAVSNRfplEALEELFAGITLAAKEYKVDVIGG----DTTSSQkgliISITAIGEADenELVYRNGAKKTDLLVVTG 174
Cdd:COG2144 98 VDALWSSDE---EAAAPVLAGMRAASRKFGVPIVGGhthpDTPYNA----LAVAILGRAK--KLLTSFTARPGDRLIAAI 168
|
..
gi 1053293782 175 DL 176
Cdd:COG2144 169 DL 170
|
|
| PurM-like2 |
cd02691 |
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ... |
31-331 |
1.22e-06 |
|
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: 49.69 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 31 TQESTLKSIGDDAAVLDFKDKKVVVSTDllieGVHFDLAYMPLKhLGYKAVVVNVSDICAMNAKPTQITVSVAVSNRFPL 110
Cdd:cd02691 27 TGEVSIVAQDDDAGVDAADVEYIVVAID----GIHSRLSDFPFL-AGFHATRAALRDVMVMGARPVALLSDIHLADDGDV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 111 EALEELFAGITLAAKEYKVDVIGGDTTSSQKGLII------SITAIGEADENELVYRNgAKKTDLLVVTGDLGAAYMGLQ 184
Cdd:cd02691 102 GKLFDFTAGVTAVSEATGVPLVAGSTLRIGGDMVLgdrlvgGVGAVGRSKSDPSRRKN-AEPGDLILMTEGAGGGTITTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 185 VLErekqvfqvnpNNQPDldpytyLVERQLKPEARKDVRTLLHA-LDIKPNAMIDISD-GLSSEIMHICKQSKVGCNLYE 262
Cdd:cd02691 181 AIY----------HGMPD------VVEETLNVDFIKACEALRDSgLVSKVHSMTDVTNgGIRGDALEISKTAGVSLVFDE 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1053293782 263 DKL--PLDPQFISTCEEFNIDSTTVAINggedyELLFTIDINDFDKIKGNPN-----FSVIGHMTEENEGIHLVTR 331
Cdd:cd02691 245 EKVrsLINPKVLKMLEELGIDPLGVSLD-----SLMIIAPEEDAVDIIRTLReagvrADEVGRVEEGRGVPLVVTG 315
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
40-189 |
1.70e-06 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 49.30 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 40 GDDAAVLDFKDKKVVVST-DlliegvHFdlayMPlkhlgykavVVN-------------VSDICAMNAKPTQITVSVAV- 104
Cdd:COG0709 47 SDDAAVYRLGDDQALVQTtD------FF----TP---------IVDdpydfgriaaanaLSDVYAMGGRPLTALAIVGFp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 105 SNRFPLEALEELFAGITLAAKEYKVDVIGGDTTSSQKgLIISITAIGEADENELVYRNGAKKTDLLVVTGDLG-----AA 179
Cdd:COG0709 108 IDKLPEEVLAEILAGGADKCREAGAPLAGGHSIDDPE-PKYGLAVTGLVHPDKVLRNAGARPGDVLILTKPLGtgiltTA 186
|
170
....*....|
gi 1053293782 180 YMGLQVLERE 189
Cdd:COG0709 187 IKAGLADGED 196
|
|
| PRK14105 |
PRK14105 |
selenide, water dikinase SelD; |
33-256 |
6.91e-04 |
|
selenide, water dikinase SelD;
Pssm-ID: 237611 [Multi-domain] Cd Length: 345 Bit Score: 40.91 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 33 ESTLKSIGDDAAVLdFKDKKVVVSTDLLIEGVHFDlAYMPlkhlGYKAVVVNVSDICAMNAkpTQIT---VSVAVSNRFP 109
Cdd:PRK14105 40 KHTKVGLGDDAAVI-IKNGLAIVKTVDVFTPIVDD-PYIQ----GKIAACNSTSDVYAMGL--SEIIgvlVILGIPPELP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1053293782 110 LEALEELFAGITLAAKEYKVDVIGGDTTSSQKGLI-ISITAIGEadENELVYRNGAKKTDLLVVTGDLG--AAYMGLQVL 186
Cdd:PRK14105 112 IEVAKEMLQGFQDFCRENDTTIIGGHTILNPWPLIgGAVTGVGK--EEDILTKAGAKEGDVLILTKPLGtqSAMALSRVP 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1053293782 187 EREKQVFQVNPNNQpdldpyTYLVERQLKPEARKDVRTLLH-------ALDIKPNAMIDISD-GLSSEIMHICKQSKV 256
Cdd:PRK14105 190 EEFEDLIDITKEEK------EYIINKAIELMTTSNRYALLAlreaeeeVGEKIANAMTDVTGfGILGHSQEMAEQSNV 261
|
|
| |
