|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
1-322 |
5.66e-173 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 482.02 E-value: 5.66e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 1 MACGEFSLIARYFDRVRSSRLdveLGIGDDCALLNIPEKQTLAISTDTLVAGNHFLPD-IDPADLAYKALAVNLSDLAAM 79
Cdd:PRK05731 1 MAMGEFDLIARLFARRPSSRE---LGIGDDAALLGPPPGQRLVVSTDMLVEGVHFRPDwSSPEDLGYKALAVNLSDLAAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 80 GADPAWLTLALTLP-DVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPMGRALTRSGAKPGDWIYV 157
Cdd:PRK05731 78 GARPAAFLLALALPkDLDEAWLEALADGLFELADRYGAELIGGDTTRGPdLSISVTAIGDVPGGRALRRSGAKPGDLVAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 158 TGTPGDSAAGLAILQNRLQVADAkDADYLIKRHLRPSPRILQGQALRDLANSAIDLSDGLISDLGHIVKASDCGARIDLA 237
Cdd:PRK05731 158 TGTLGDSAAGLALLLNGLRVPDA-DAAALISRHLRPQPRVGLGQALAGLASAAIDISDGLAADLGHIAEASGVGADIDLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 238 LLPFSDALSRHVEPEQALRWALSGGEDYELCFTVPELNRGALDVALGHLGVPFTCIGQMTAdieGLCFIRDGEPVTFDWK 317
Cdd:PRK05731 237 ALPISPALREAAEGEDALRWALSGGEDYELLFTFPPENRGALLAAAGHLGVGVTIIGRVTE---GEGVVVDGEPVTLDLK 313
|
....*
gi 446664761 318 GYDHF 322
Cdd:PRK05731 314 GYDHF 318
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
3-322 |
8.74e-153 |
|
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: 431.11 E-value: 8.74e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 3 CGEFSLIARYFDRVRSSRLDVELGIGDDCALLNIPEKQtLAISTDTLVAGNHFLPD-IDPADLAYKALAVNLSDLAAMGA 81
Cdd:COG0611 1 MGEFGLIERLFKRLALRGPDVLLGIGDDAAVLDPPGGR-LVVTTDMLVEGVHFPLDwMSPEDLGWKAVAVNLSDLAAMGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 82 DPAWLTLALTLP-DVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPMGRALTRSGAKPGDWIYVTG 159
Cdd:COG0611 80 RPLAALLSLALPpDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPeLTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 160 TPGDSAAGLAILQNRLQVADAkDADYLIKRHLRPSPRILQGQALR--DLANSAIDLSDGLISDLGHIVKASDCGARIDLA 237
Cdd:COG0611 160 TLGDAAAGLALLLRGLRVPLE-AREYLLERHLRPEPRLALGRALAeaGLATAMIDISDGLAADLGHIAEASGVGAEIDLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 238 LLPFSDALSRHVEPEQALRWALSGGEDYELCFTVPELNRGALDVALghLGVPFTCIGQMTADIEGLCFIRDGEPVTFDWK 317
Cdd:COG0611 239 ALPLSPALREAALGLDPLELALTGGEDYELLFTVPPEALEALEAAA--LGVPLTVIGRVTEGEGVTLDDADGRPIPLEAR 316
|
....*
gi 446664761 318 GYDHF 322
Cdd:COG0611 317 GWDHF 321
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
4-322 |
4.09e-149 |
|
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: 421.74 E-value: 4.09e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 4 GEFSLIARYFDRvRSSRLDVELGIGDDCALLNIPEKQTLAISTDTLVAGNHFLPDIDPADLAYKALAVNLSDLAAMGADP 83
Cdd:TIGR01379 1 GEFELIDRILRR-LVQDPDVALGIGDDAALVSAPEGRDLVLTTDTLVEGVHFPPDTTPEDLGWKAVAVNLSDLAAMGATP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 84 AWLTLALTLP-DVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPMGRALTRSGAKPGDWIYVTGTP 161
Cdd:TIGR01379 80 KWFLLSLGLPsDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPeLVVTVTAIGEAPKGRALLRSGAKPGDLVFVTGTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 162 GDSAAGLAILQNRLQVADAKDADYLIKRHLRPSPRILQGQALRDLANSAIDLSDGLISDLGHIVKASDCGARIDLALLPF 241
Cdd:TIGR01379 160 GDSAAGLALLLKGKKEPDEEDDEALLQRHLRPEPRVEEGLALAGYANAAIDVSDGLAADLGHIAEASGVGIVIDLDRLPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 242 SDALSRHVEPEQALRWALSGGEDYELCFTVPELNRGALDVALGHlgvPFTCIGQMTADIEGLCFIRDGEPVTFDWKGYDH 321
Cdd:TIGR01379 240 SSELAAWAEGKNPLEWALSGGEDYELVFTVPPERREALLDAAKG---PLTRIGRVTEGEGVVLLADGKTVELLDRLGWQH 316
|
.
gi 446664761 322 F 322
Cdd:TIGR01379 317 F 317
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
4-297 |
5.00e-133 |
|
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: 379.98 E-value: 5.00e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 4 GEFSLIARYFDRVRSSRlDVELGIGDDCALLNIPEKQtLAISTDTLVAGNHFLPDIDPADLAYKALAVNLSDLAAMGADP 83
Cdd:cd02194 1 GEFELIDRLFKRLGAGP-GVLLGIGDDAAVLKPPGGR-LVVTTDTLVEGVHFPPDTTPEDIGWKALAVNLSDLAAMGARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 84 AWLTLALTLP-DVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRG-PLSMTLGIHGFVPMGRALTRSGAKPGDWIYVTGTP 161
Cdd:cd02194 79 LGFLLSLGLPpDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGsELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 162 GDSAAGLAILQNRLQVaDAKDADYLIKRHLRPSPRILQGQALRD-LANSAIDLSDGLISDLGHIVKASDCGARIDLALLP 240
Cdd:cd02194 159 GDAAAGLALLLGGLKL-PEELYEELIERHLRPEPRLELGRALAEgLATAMIDISDGLLADLGHIAEASGVGAVIDLDKLP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446664761 241 FSDALSRHVEPEQALRWALSGGEDYELCFTVPELNRGALDValgHLGVPFTCIGQMT 297
Cdd:cd02194 238 LSPALRAAELGEDALELALSGGEDYELLFTVPPENAEAAAA---KLGVPVTVIGRVT 291
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
29-138 |
2.01e-17 |
|
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: 76.33 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 29 DDCALlnipekqtlAISTD-----TLVAGNHFLpdidpadlAYKALAVNLSDLAAMGADPAWLTLALTLP--DVDEAWLE 101
Cdd:pfam00586 1 DDAAV---------AVTTDghgtpSLVDPYHFP--------GAKAVAGNLSDIAAMGARPLAFLDSLALPggPEVEWVLE 63
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446664761 102 SFSDSLFDLLNYYDMQLIGGDTTRGP----LSMTLGIHGFV 138
Cdd:pfam00586 64 EIVEGIAEACREAGVPLVGGDTSFDPeggkPTISVTAVGIV 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
1-322 |
5.66e-173 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 482.02 E-value: 5.66e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 1 MACGEFSLIARYFDRVRSSRLdveLGIGDDCALLNIPEKQTLAISTDTLVAGNHFLPD-IDPADLAYKALAVNLSDLAAM 79
Cdd:PRK05731 1 MAMGEFDLIARLFARRPSSRE---LGIGDDAALLGPPPGQRLVVSTDMLVEGVHFRPDwSSPEDLGYKALAVNLSDLAAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 80 GADPAWLTLALTLP-DVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPMGRALTRSGAKPGDWIYV 157
Cdd:PRK05731 78 GARPAAFLLALALPkDLDEAWLEALADGLFELADRYGAELIGGDTTRGPdLSISVTAIGDVPGGRALRRSGAKPGDLVAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 158 TGTPGDSAAGLAILQNRLQVADAkDADYLIKRHLRPSPRILQGQALRDLANSAIDLSDGLISDLGHIVKASDCGARIDLA 237
Cdd:PRK05731 158 TGTLGDSAAGLALLLNGLRVPDA-DAAALISRHLRPQPRVGLGQALAGLASAAIDISDGLAADLGHIAEASGVGADIDLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 238 LLPFSDALSRHVEPEQALRWALSGGEDYELCFTVPELNRGALDVALGHLGVPFTCIGQMTAdieGLCFIRDGEPVTFDWK 317
Cdd:PRK05731 237 ALPISPALREAAEGEDALRWALSGGEDYELLFTFPPENRGALLAAAGHLGVGVTIIGRVTE---GEGVVVDGEPVTLDLK 313
|
....*
gi 446664761 318 GYDHF 322
Cdd:PRK05731 314 GYDHF 318
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
3-322 |
8.74e-153 |
|
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: 431.11 E-value: 8.74e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 3 CGEFSLIARYFDRVRSSRLDVELGIGDDCALLNIPEKQtLAISTDTLVAGNHFLPD-IDPADLAYKALAVNLSDLAAMGA 81
Cdd:COG0611 1 MGEFGLIERLFKRLALRGPDVLLGIGDDAAVLDPPGGR-LVVTTDMLVEGVHFPLDwMSPEDLGWKAVAVNLSDLAAMGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 82 DPAWLTLALTLP-DVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPMGRALTRSGAKPGDWIYVTG 159
Cdd:COG0611 80 RPLAALLSLALPpDTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPeLTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 160 TPGDSAAGLAILQNRLQVADAkDADYLIKRHLRPSPRILQGQALR--DLANSAIDLSDGLISDLGHIVKASDCGARIDLA 237
Cdd:COG0611 160 TLGDAAAGLALLLRGLRVPLE-AREYLLERHLRPEPRLALGRALAeaGLATAMIDISDGLAADLGHIAEASGVGAEIDLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 238 LLPFSDALSRHVEPEQALRWALSGGEDYELCFTVPELNRGALDVALghLGVPFTCIGQMTADIEGLCFIRDGEPVTFDWK 317
Cdd:COG0611 239 ALPLSPALREAALGLDPLELALTGGEDYELLFTVPPEALEALEAAA--LGVPLTVIGRVTEGEGVTLDDADGRPIPLEAR 316
|
....*
gi 446664761 318 GYDHF 322
Cdd:COG0611 317 GWDHF 321
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
4-322 |
4.09e-149 |
|
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: 421.74 E-value: 4.09e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 4 GEFSLIARYFDRvRSSRLDVELGIGDDCALLNIPEKQTLAISTDTLVAGNHFLPDIDPADLAYKALAVNLSDLAAMGADP 83
Cdd:TIGR01379 1 GEFELIDRILRR-LVQDPDVALGIGDDAALVSAPEGRDLVLTTDTLVEGVHFPPDTTPEDLGWKAVAVNLSDLAAMGATP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 84 AWLTLALTLP-DVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPMGRALTRSGAKPGDWIYVTGTP 161
Cdd:TIGR01379 80 KWFLLSLGLPsDLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPeLVVTVTAIGEAPKGRALLRSGAKPGDLVFVTGTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 162 GDSAAGLAILQNRLQVADAKDADYLIKRHLRPSPRILQGQALRDLANSAIDLSDGLISDLGHIVKASDCGARIDLALLPF 241
Cdd:TIGR01379 160 GDSAAGLALLLKGKKEPDEEDDEALLQRHLRPEPRVEEGLALAGYANAAIDVSDGLAADLGHIAEASGVGIVIDLDRLPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 242 SDALSRHVEPEQALRWALSGGEDYELCFTVPELNRGALDVALGHlgvPFTCIGQMTADIEGLCFIRDGEPVTFDWKGYDH 321
Cdd:TIGR01379 240 SSELAAWAEGKNPLEWALSGGEDYELVFTVPPERREALLDAAKG---PLTRIGRVTEGEGVVLLADGKTVELLDRLGWQH 316
|
.
gi 446664761 322 F 322
Cdd:TIGR01379 317 F 317
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
4-297 |
5.00e-133 |
|
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: 379.98 E-value: 5.00e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 4 GEFSLIARYFDRVRSSRlDVELGIGDDCALLNIPEKQtLAISTDTLVAGNHFLPDIDPADLAYKALAVNLSDLAAMGADP 83
Cdd:cd02194 1 GEFELIDRLFKRLGAGP-GVLLGIGDDAAVLKPPGGR-LVVTTDTLVEGVHFPPDTTPEDIGWKALAVNLSDLAAMGARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 84 AWLTLALTLP-DVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRG-PLSMTLGIHGFVPMGRALTRSGAKPGDWIYVTGTP 161
Cdd:cd02194 79 LGFLLSLGLPpDTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGsELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 162 GDSAAGLAILQNRLQVaDAKDADYLIKRHLRPSPRILQGQALRD-LANSAIDLSDGLISDLGHIVKASDCGARIDLALLP 240
Cdd:cd02194 159 GDAAAGLALLLGGLKL-PEELYEELIERHLRPEPRLELGRALAEgLATAMIDISDGLLADLGHIAEASGVGAVIDLDKLP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446664761 241 FSDALSRHVEPEQALRWALSGGEDYELCFTVPELNRGALDValgHLGVPFTCIGQMT 297
Cdd:cd02194 238 LSPALRAAELGEDALELALSGGEDYELLFTVPPENAEAAAA---KLGVPVTVIGRVT 291
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
7-244 |
2.84e-21 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 92.44 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 7 SLIARYFdrvrSSRLDVE-LGIGDDCALLNIPEKqTLAISTDTLVAGNHFLPDIDPADLAYkalAVNLSDLAAMGADPAW 85
Cdd:COG0309 12 ELIEELF----LPALGNEvLVGGEDAAVLDLGGG-RLAFTTDSFVVSPIFFPGGDIGKLAV---HGTVNDLAVSGAKPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 86 LTLALTLP-DVDEAWLESFSDSLFDLLNYYDMQLIGGDTTR-------GPLSMTLGIhGFVPMGRALTRSGAKPGDWIYV 157
Cdd:COG0309 84 LSVSLILEeGFPLEDLERIVESMAEAAREAGVSIVTGDTKVverggvdGPFINTTGI-GVVPKGRLISPSGARPGDKIIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 158 TGTPGDSaaGLAILQNRLQ-------VADAKDADYLIkrhlrpsprilqgQALRDLANSAID-LSD----GLISDLGHIV 225
Cdd:COG0309 163 TGGIGDH--GTAILAAREGlelegelLSDAAPLNDLV-------------SVLLEAAPGGVHaMRDptrgGLAGALNEIA 227
|
250
....*....|....*....
gi 446664761 226 KASDCGARIDLALLPFSDA 244
Cdd:COG0309 228 EASGVGIEIDEDAIPVRPE 246
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
42-295 |
1.11e-20 |
|
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: 88.61 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 42 LAISTDTLVAGnhflPDIDPADLAYKALAVNLSDLAAMGADPAWLTLALTLP-DVDEAWLESFSDSLFDLLNYYDMQLIG 120
Cdd:cd00396 2 LAMSTDGINPP----LAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSnGLEVDILEDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 121 GDTTRGP------LSMTLGIHGFVPMGRALTRSGAKPGDWIYVTGTpgDSAAGLailqnrlqvadakdadylikrhlrps 194
Cdd:cd00396 78 GHTSVSPgtmghkLSLAVFAIGVVEKDRVIDSSGARPGDVLILTGV--DAVLEL-------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 195 prilqgQALRDLaNSAIDLSD-GLISDLGHIVKASDCGARIDLALLPfSDALSRHVEPEQALrWALSGGEDYELCFTVPE 273
Cdd:cd00396 130 ------VAAGDV-HAMHDITDgGLLGTLPELAQASGVGAEIDLEAIP-LDEVVRWLCVEHIE-EALLFNSSGGLLIAVPA 200
|
250 260
....*....|....*....|..
gi 446664761 274 LNRGALDVALGHLGVPFTCIGQ 295
Cdd:cd00396 201 EEADAVLLLLNGNGIDAAVIGR 222
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
20-241 |
2.44e-19 |
|
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: 86.04 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 20 RLDVELGIGDDCALLNIPEKQTLAISTDtlvagnHFLPDI-DPADLAyKALAVN-LSDLAAMGADP----AWLTLALTLP 93
Cdd:cd02195 33 NLLVGLGTGDDAAVYRLPGGLALVQTTD------FFPPIVdDPYLFG-RIAAANaLSDIYAMGAKPlsalAIVTLPRKLP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 94 DVDEAWLESFSDSLFDLLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPMGRALTRSGAKPGDWIYVT---GTpgdsaaGLA 169
Cdd:cd02195 106 ALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPePKYGLSVTGLVHPNKILRNSGAKPGDVLILTkplGT------GIL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446664761 170 ILQNRLQVADAKDADYLIKrHLRPSPRILQGQALRDLANSAIDLSD-GLisdLGH---IVKASDCGARIDLALLPF 241
Cdd:cd02195 180 FAAEMAGLARGEDIDAALE-SMARLNRAAAELLRKYGAHACTDVTGfGL---LGHlleMARASGVSAEIDLDKLPL 251
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
26-294 |
2.53e-19 |
|
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: 86.50 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 26 GIGDDCALLNIPEKqTLAISTD-TLVAGNhflpdidpaDLAYKALAVNLSDLAAMGADPAWLTLALTLPD-VDEAWLESF 103
Cdd:cd06061 30 GGGEDAAVVDFGGK-VLVVSTDpITGAGK---------DAGWLAVHIAANDIATSGARPRWLLVTLLLPPgTDEEELKAI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 104 SDSLFDLLNYYDMQLIGGDTTRGP------LSMTLgiHGFVPMGRALTRSGAKPGDWIYVTGTPGDSAAGLAILQNRLQV 177
Cdd:cd06061 100 MREINEAAKELGVSIVGGHTEVTPgvtrpiISVTA--IGKGEKDKLVTPSGAKPGDDIVMTKGAGIEGTAILANDFEEEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 178 ADAKDADYLIKRHLRPSPRILQGQAL---RDLANSAIDLSD-GLISDLGHIVKASDCGARIDLALLPFSDALSR-----H 248
Cdd:cd06061 178 KKRLSEEELREAAKLFYKISVVKEALiaaEAGVTAMHDATEgGILGALWEVAEASGVGLRIEKDKIPIRQETKEicealG 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446664761 249 VEPeqalrWAL-SGGedyELCFTVPELNRGALDVALGHLGVPFTCIG 294
Cdd:cd06061 258 IDP-----LRLiSSG---TLLITVPPEKGDELVDALEEAGIPASVIG 296
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
29-138 |
2.01e-17 |
|
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: 76.33 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 29 DDCALlnipekqtlAISTD-----TLVAGNHFLpdidpadlAYKALAVNLSDLAAMGADPAWLTLALTLP--DVDEAWLE 101
Cdd:pfam00586 1 DDAAV---------AVTTDghgtpSLVDPYHFP--------GAKAVAGNLSDIAAMGARPLAFLDSLALPggPEVEWVLE 63
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446664761 102 SFSDSLFDLLNYYDMQLIGGDTTRGP----LSMTLGIHGFV 138
Cdd:pfam00586 64 EIVEGIAEACREAGVPLVGGDTSFDPeggkPTISVTAVGIV 104
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
7-244 |
1.85e-12 |
|
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: 66.70 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 7 SLIARYFDrvrssrlDVELGIGDDCALLNIPEKqTLAISTDTLVAGNHFLP--DIDpadlaykALAVN--LSDLAAMGAD 82
Cdd:cd02197 12 ELFLKAFD-------NPILEVLEDAAALLVGGG-RLAFTTDSFVVSPLFFPggDIG-------KLAVCgtVNDLAMMGAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 83 PAWLTLALTLP---DVDEawLESFSDSLFDLLNYYDMQLIGGDTT---RGPLS----MTLGIhGFVPMGRALTRSGAKPG 152
Cdd:cd02197 77 PLYLSLGFILEegfPLED--LERIVKSMAEAAREAGVKIVTGDTKvvpKGKADgifiNTTGI-GVIPRGVIISPSNIRPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 153 DWIYVTGTPGDSaaGLAILQNRLQVA-------DAKDADYLIKRHLRPSPRIlqgQALRDLANSaidlsdGLISDLGHIV 225
Cdd:cd02197 154 DKIIVSGTIGDH--GAAILAAREGLGfetdiesDCAPLNGLVEALLEAGPGI---HAMRDPTRG------GLAAVLNEIA 222
|
250
....*....|....*....
gi 446664761 226 KASDCGARIDLALLPFSDA 244
Cdd:cd02197 223 RASGVGIEIEEEAIPVREE 241
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
29-312 |
5.03e-11 |
|
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439816 [Multi-domain] Cd Length: 747 Bit Score: 63.53 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 29 DDCALLNIPEKQT-LAISTDtlvaGNHFLPDIDPADLAYKALAVNLSDLAAMGADPawltLALTL---------PDVDEA 98
Cdd:COG0046 443 ADAAVVRVDGTYKgLAMSTG----ENPRYALLDPYAGARMAVAEAARNLAAVGAEP----LAITDclnwgnpekPEEMAQ 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 99 wlesFSDS---LFDLLNYYDMQLIGG------DTTRG----PLSMTLGIHGFVP-MGRALTRSGAKPGDWIYVTGTPGDS 164
Cdd:COG0046 515 ----LVEAvkgLADACRALGIPVPSGnvslynETKDGkvaiPPTPVIGAVGLVDdVRKTVTPDLKKEGDLLYLIGETKNE 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 165 AAGLAILQNRLQVADAK---DADYLIKRHlrpspRILQGQALRDLANSAIDLSDG-LISDLGHIVKASDCGARIDLALLP 240
Cdd:COG0046 591 LGGSEYAQVLGQLGGEPpdvDLEAEKALF-----EAVQELIREGLILAAHDVSDGgLAVALAEMAFAGGLGADIDLDALG 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 241 --------FSDALSRHVepeqalrwalsggedyelcFTVPELNRGALDVALGHLGVPFTCIGQMTADiEGLCFIRDGEPV 312
Cdd:COG0046 666 dlrpdaalFSESQGRAV-------------------VQVAPEDAEAVEALLAEAGLPAHVIGTVTGD-DRLVIRRGGETL 725
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
9-240 |
1.31e-10 |
|
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: 61.07 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 9 IARYFDRVRSSRLDVELGIGDDCALLNIPekqtlaiSTDTLVAGNHFLPDI---DPADLAYKALAVNLSDLAAMGADPAW 85
Cdd:cd02192 16 VVAILPDAPFDSLGVAADLGDDAAAIPDG-------DGYLLLAADGIWPSLveaDPWWAGYCSVLVNVSDIAAMGGRPLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 86 LTLALTLPDVDEAwlESFSDSLFDLLNYYDMQLIGG----DTTRGPLSMT-LGIHGfvpmGRALTRSGAKPGDWIYVT-- 158
Cdd:cd02192 89 MVDALWSPSAEAA--AQVLEGMRDAAEKFGVPIVGGhthpDSPYNALSVAiLGRAR----KDLLISFGAKPGDRLILAid 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 159 --GTPG-------DSAAGlailqnrlqvadaKDADYLiKRHLrpspRILQGQALRDLANSAIDLSD-GLISDLGHIVKAS 228
Cdd:cd02192 163 ldGRVHpspppnwDATTM-------------KSPALL-RRQI----ALLPELAERGLVHAAKDISNpGIIGTLGMLLEAS 224
|
250
....*....|..
gi 446664761 229 DCGARIDLALLP 240
Cdd:cd02192 225 GVGAEIDLDAIP 236
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
150-299 |
7.47e-10 |
|
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: 56.59 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 150 KPGDWIYVTGTPGDSAAGLAiLQNRLQVADAKDADYLIKRHLRPSP--RILQGQALRDLANSAIDLSD-GLISDLGHIVK 226
Cdd:pfam02769 1 KPGDVLILLGSSGLHGAGLS-LSRKGLEDSGLAAVQLGDPLLEPTLiyVKLLLAALGGLVKAMHDITGgGLAGALAEMAP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446664761 227 ASDCGARIDLALLPFSDALSRHVEPeqalrwALSGGEDYELCFTVPELNRGALDVALGHlGVPFTCIGQMTAD 299
Cdd:pfam02769 80 ASGVGAEIDLDKVPIFEELMLPLEM------LLSENQGRGLVVVAPEEAEAVLAILEKE-GLEAAVIGEVTAG 145
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
30-295 |
7.77e-09 |
|
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, phosphate, and glutamate in the fourth step of the purine biosynthetic pathway. In eukaryotes and Gram-negative bacteria, FGAR-AT is encoded by the purL gene as a multidomain protein with a molecular mass of about 140 kDa. In Gram-positive bacteria and archaea FGAR-AT is a complex of three proteins: PurS, PurL, and PurQ. PurL itself contains two tandem N- and C-terminal domains (four domains altogether). The N-terminal domains bind ATP and are related to the ATP-binding domains of HypE, ThiL, SelD and PurM.
Pssm-ID: 100035 [Multi-domain] Cd Length: 264 Bit Score: 55.62 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 30 DCALLNIPE--KQTLAISTDtlvaGNHFLPDIDPADLAYKALAVNLSDLAAMGADPawltLALTL--------PDVDEAW 99
Cdd:cd02204 1 DAAVLRIPGetDKGLAMSTG----ENPRYSLLDPYAGAALAVAEAVRNLVAVGADP----LAITDclnfgnpeKPEGEMG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 100 leSFSDS---LFDLLNYYDMQLIGG------DTTRGPLSMTLGIHGFVPMG---RALTRSGAKPGDWIYVTGTP----GD 163
Cdd:cd02204 73 --QLVEAvlgLGDACRALGTPVIGGkdslynETEGVAIPPTLVIGAVGVVDdvrKIVTLDFKKEGDLLYLIGETkdelGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 164 SAAGLAILQNRLQVADAKDADYLIKRHlrpspRILQGQALRDLANSAIDLSD-GLISDLGHIVKASDCGARIDLALLP-- 240
Cdd:cd02204 151 SEYALAYHGLGGGAPPLVDLEREKALF-----DAVQELIKEGLVLSAHDVSDgGLAVALAEMAFAGGLGAEVDLSKDDae 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446664761 241 ----FSDALSRHVepeqalrwalsggedyelcFTVPELNrgALDVALGHLGVPFTCIGQ 295
Cdd:cd02204 226 dellFSESLGRVL-------------------VEVKPEN--EEVFEAEEAGVPATVIGT 263
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
20-298 |
4.87e-08 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 53.54 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 20 RLDVELGIGDDCALLNIPEKQTLAISTDtlvagnHFLPDI-DPADLAYKAlAVN-LSDLAAMGADP--AWLTLALTLPDV 95
Cdd:COG0709 39 NLLVGLETSDDAAVYRLGDDQALVQTTD------FFTPIVdDPYDFGRIA-AANaLSDVYAMGGRPltALAIVGFPIDKL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 96 DEAWLESFSDSLFDLLNYYDMQLIGGDTTRGP-----LSMTlgihGFVPMGRALTRSGAKPGDWIYVT---GTpgdsaaG 167
Cdd:COG0709 112 PEEVLAEILAGGADKCREAGAPLAGGHSIDDPepkygLAVT----GLVHPDKVLRNAGARPGDVLILTkplGT------G 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 168 L---AILQNRLQVADAKDADYLIKRHLRPSPRILQGQAlrdlANSAIDLSD-GLisdLGH---IVKASDCGARIDLALLP 240
Cdd:COG0709 182 IlttAIKAGLADGEDIAAAIASMTTLNKAAAELARLYG----VHACTDVTGfGL---LGHlleMARGSGVSAEIDLDAVP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 241 F--------------------SDALSRHVEPEQAL---RWAL------SGGedyeLCFTVPELNRGALDVALGHLGVPFT 291
Cdd:COG0709 255 LlpgalelaeqgivpggtyrnRASYGAKVEFAEGLdeaQRDLlfdpqtSGG----LLIAVPPEAAEELLAALRAAGYAAA 330
|
....*..
gi 446664761 292 CIGQMTA 298
Cdd:COG0709 331 IIGEVTA 337
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
9-240 |
6.64e-08 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 53.24 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 9 IARYFDRVRSsrLDVELGIGDDCALLNIPEKqtlaistDTLVAGNHFLPDI---DPADLAYKALAVNLSDLAAMGADPAW 85
Cdd:COG2144 26 VVRALGLASS--GGTAAAFGDDAAAIPDGDG-------YLLLAAEGIWPKFveaDPWFAGYCSVLVNVSDIAAMGGRPLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 86 LTLALTLPDVDEAwlESFSDSLFDLLNYYDMQLIGG----DTTRGPLSMTlgIHGFVPmgRALTRSGAKPGDWIYV---- 157
Cdd:COG2144 97 VVDALWSSDEEAA--APVLAGMRAASRKFGVPIVGGhthpDTPYNALAVA--ILGRAK--KLLTSFTARPGDRLIAaidl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 158 TGTPG------DSAAGlailqnrlqvadaKDADYLiKRHLRPSPRIlqgqALRDLANSAIDLSD-GLISDLGHIVKASDC 230
Cdd:COG2144 171 DGRYHppfpywDATTG-------------KPPERL-RAQLELLPEL----AEAGLVTAAKDISNpGIIGTLGMLLECSGV 232
|
250
....*....|
gi 446664761 231 GARIDLALLP 240
Cdd:COG2144 233 GATIDLDAIP 242
|
|
| PRK14105 |
PRK14105 |
selenide, water dikinase SelD; |
22-247 |
6.79e-07 |
|
selenide, water dikinase SelD;
Pssm-ID: 237611 [Multi-domain] Cd Length: 345 Bit Score: 50.16 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 22 DVELGIGDDCALLnipEKQTLAISTDTLVagnhFLPDIDPADLAYKALAVN-LSDLAAMGADPAWLTLA-------LTLP 93
Cdd:PRK14105 41 HTKVGLGDDAAVI---IKNGLAIVKTVDV----FTPIVDDPYIQGKIAACNsTSDVYAMGLSEIIGVLVilgippeLPIE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 94 DVDEAwLESFSDSLFDLlnyyDMQLIGGDTTRGPLSMTLG-IHGFVPMGRALTRSGAKPGDWIYVTGTPGDSAAgLAILQ 172
Cdd:PRK14105 114 VAKEM-LQGFQDFCREN----DTTIIGGHTILNPWPLIGGaVTGVGKEEDILTKAGAKEGDVLILTKPLGTQSA-MALSR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 173 -----NRLQVADAKDADYLIKR--HLRPSPRILQGQALRDLANSAIDLSDGLISD------LGH---IVKASDCGARID- 235
Cdd:PRK14105 188 vpeefEDLIDITKEEKEYIINKaiELMTTSNRYALLALREAEEEVGEKIANAMTDvtgfgiLGHsqeMAEQSNVEIEISt 267
|
250
....*....|..
gi 446664761 236 LALLPFSDALSR 247
Cdd:PRK14105 268 LPVIKGTPELSS 279
|
|
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
142-300 |
4.39e-04 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 42.01 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 142 RALTRSGAKPGDWIYVTGTPGDSAAG---LAILQNRLQvADAKDADY-LIKRHLRpsprILQGQALRDLANSAIDLSDG- 216
Cdd:PRK01213 551 KRTTSGFKKEGDLIYLLGETKDELGGseyLKVIHGHVG-GRPPKVDLeAEKRLQE----LVREAIREGLVTSAHDVSEGg 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664761 217 LISDLGHIVKASDCGARIDL-------ALLpFSDALSRHVepeqalrwalsggedyelcFTVPELNRGALDVALGHLGVP 289
Cdd:PRK01213 626 LAVALAEMAIAGGLGAEVDLsdglrpdALL-FSESQGRYV-------------------VSVPPENEEAFEALAEAAGVP 685
|
170
....*....|.
gi 446664761 290 FTCIGQMTADI 300
Cdd:PRK01213 686 ATRIGVVGGDA 696
|
|
| |
