|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
1-322 |
9.05e-174 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 484.34 E-value: 9.05e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 1 MSCGEFSLIARYFDRVRSSRLdveTGIGDDCALLTVPEKQTLAISTDTLVSGIHFLPD-IDPRDLGYKALAVNVSDLAAM 79
Cdd:PRK05731 1 MAMGEFDLIARLFARRPSSRE---LGIGDDAALLGPPPGQRLVVSTDMLVEGVHFRPDwSSPEDLGYKALAVNLSDLAAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 80 GADPAWLTLALTLP-EVNETWLEAFSDSLFEQLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPAGRALKRSGARPGDWVFI 157
Cdd:PRK05731 78 GARPAAFLLALALPkDLDEAWLEALADGLFELADRYGAELIGGDTTRGPdLSISVTAIGDVPGGRALRRSGAKPGDLVAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 158 TGTPGDSAAGLAILQKRLHVEDtSDAGYLVKRHLRPTPRVLHGQALRGLASAAIDLSDGLISDLGHILKASDCGARIELN 237
Cdd:PRK05731 158 TGTLGDSAAGLALLLNGLRVPD-ADAAALISRHLRPQPRVGLGQALAGLASAAIDISDGLAADLGHIAEASGVGADIDLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 238 DLPYSDALSRHVDPEQALRWALSGGEDYELCFTVSELNRGALEVAVSHLGVPVTCIGQLTtasEGMVFLRDGAPVTLDWK 317
Cdd:PRK05731 237 ALPISPALREAAEGEDALRWALSGGEDYELLFTFPPENRGALLAAAGHLGVGVTIIGRVT---EGEGVVVDGEPVTLDLK 313
|
....*
gi 1755430050 318 GYDHF 322
Cdd:PRK05731 314 GYDHF 318
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
3-322 |
8.36e-154 |
|
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: 433.80 E-value: 8.36e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 3 CGEFSLIARYFDRVRSSRLDVETGIGDDCALLTVPEKQtLAISTDTLVSGIHFLPD-IDPRDLGYKALAVNVSDLAAMGA 81
Cdd:COG0611 1 MGEFGLIERLFKRLALRGPDVLLGIGDDAAVLDPPGGR-LVVTTDMLVEGVHFPLDwMSPEDLGWKAVAVNLSDLAAMGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 82 DPAWLTLALTLPE-VNETWLEAFSDSLFEQLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPAGRALKRSGARPGDWVFITG 159
Cdd:COG0611 80 RPLAALLSLALPPdTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPeLTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 160 TPGDSAAGLAILQKRLHVEDtSDAGYLVKRHLRPTPRVLHGQALR--GLASAAIDLSDGLISDLGHILKASDCGARIELN 237
Cdd:COG0611 160 TLGDAAAGLALLLRGLRVPL-EAREYLLERHLRPEPRLALGRALAeaGLATAMIDISDGLAADLGHIAEASGVGAEIDLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 238 DLPYSDALSRHVDPEQALRWALSGGEDYELCFTVSELNRGALEVAVshLGVPVTCIGQLTTASEGMVFLRDGAPVTLDWK 317
Cdd:COG0611 239 ALPLSPALREAALGLDPLELALTGGEDYELLFTVPPEALEALEAAA--LGVPLTVIGRVTEGEGVTLDDADGRPIPLEAR 316
|
....*
gi 1755430050 318 GYDHF 322
Cdd:COG0611 317 GWDHF 321
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
4-322 |
1.46e-144 |
|
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: 410.18 E-value: 1.46e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 4 GEFSLIARYFDRvRSSRLDVETGIGDDCALLTVPEKQTLAISTDTLVSGIHFLPDIDPRDLGYKALAVNVSDLAAMGADP 83
Cdd:TIGR01379 1 GEFELIDRILRR-LVQDPDVALGIGDDAALVSAPEGRDLVLTTDTLVEGVHFPPDTTPEDLGWKAVAVNLSDLAAMGATP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 84 AWLTLALTLPE-VNETWLEAFSDSLFEQLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPAGRALKRSGARPGDWVFITGTP 161
Cdd:TIGR01379 80 KWFLLSLGLPSdLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPeLVVTVTAIGEAPKGRALLRSGAKPGDLVFVTGTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 162 GDSAAGLAILQKRLHVEDTSDAGYLVKRHLRPTPRVLHGQALRGLASAAIDLSDGLISDLGHILKASDCGARIELNDLPY 241
Cdd:TIGR01379 160 GDSAAGLALLLKGKKEPDEEDDEALLQRHLRPEPRVEEGLALAGYANAAIDVSDGLAADLGHIAEASGVGIVIDLDRLPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 242 SDALSRHVDPEQALRWALSGGEDYELCFTVSELNRGALEVAvshLGVPVTCIGQLtTASEGMVFLRDGAPVT-LDWKGYD 320
Cdd:TIGR01379 240 SSELAAWAEGKNPLEWALSGGEDYELVFTVPPERREALLDA---AKGPLTRIGRV-TEGEGVVLLADGKTVElLDRLGWQ 315
|
..
gi 1755430050 321 HF 322
Cdd:TIGR01379 316 HF 317
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
4-297 |
1.67e-132 |
|
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: 378.43 E-value: 1.67e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 4 GEFSLIARYFDRVRSSRlDVETGIGDDCALLTvPEKQTLAISTDTLVSGIHFLPDIDPRDLGYKALAVNVSDLAAMGADP 83
Cdd:cd02194 1 GEFELIDRLFKRLGAGP-GVLLGIGDDAAVLK-PPGGRLVVTTDTLVEGVHFPPDTTPEDIGWKALAVNLSDLAAMGARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 84 AWLTLALTLPE-VNETWLEAFSDSLFEQLNYYDMQLIGGDTTRG-PLSMTLGIHGFVPAGRALKRSGARPGDWVFITGTP 161
Cdd:cd02194 79 LGFLLSLGLPPdTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGsELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 162 GDSAAGLAILQKRLHVEDtSDAGYLVKRHLRPTPRVLHGQALR-GLASAAIDLSDGLISDLGHILKASDCGARIELNDLP 240
Cdd:cd02194 159 GDAAAGLALLLGGLKLPE-ELYEELIERHLRPEPRLELGRALAeGLATAMIDISDGLLADLGHIAEASGVGAVIDLDKLP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755430050 241 YSDALSRHVDPEQALRWALSGGEDYELCFTVSElnrGALEVAVSHLGVPVTCIGQLT 297
Cdd:cd02194 238 LSPALRAAELGEDALELALSGGEDYELLFTVPP---ENAEAAAAKLGVPVTVIGRVT 291
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
29-138 |
5.57e-19 |
|
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: 80.57 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 29 DDCALLTvpekQTLAISTDTLVSGIHFLpdidprdlGYKALAVNVSDLAAMGADPAWLTLALTLPEVNET--WLEAFSDS 106
Cdd:pfam00586 1 DDAAVAV----TTDGHGTPSLVDPYHFP--------GAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVewVLEEIVEG 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 1755430050 107 LFEQLNYYDMQLIGGDTTRGP----LSMTLGIHGFV 138
Cdd:pfam00586 69 IAEACREAGVPLVGGDTSFDPeggkPTISVTAVGIV 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
1-322 |
9.05e-174 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 484.34 E-value: 9.05e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 1 MSCGEFSLIARYFDRVRSSRLdveTGIGDDCALLTVPEKQTLAISTDTLVSGIHFLPD-IDPRDLGYKALAVNVSDLAAM 79
Cdd:PRK05731 1 MAMGEFDLIARLFARRPSSRE---LGIGDDAALLGPPPGQRLVVSTDMLVEGVHFRPDwSSPEDLGYKALAVNLSDLAAM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 80 GADPAWLTLALTLP-EVNETWLEAFSDSLFEQLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPAGRALKRSGARPGDWVFI 157
Cdd:PRK05731 78 GARPAAFLLALALPkDLDEAWLEALADGLFELADRYGAELIGGDTTRGPdLSISVTAIGDVPGGRALRRSGAKPGDLVAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 158 TGTPGDSAAGLAILQKRLHVEDtSDAGYLVKRHLRPTPRVLHGQALRGLASAAIDLSDGLISDLGHILKASDCGARIELN 237
Cdd:PRK05731 158 TGTLGDSAAGLALLLNGLRVPD-ADAAALISRHLRPQPRVGLGQALAGLASAAIDISDGLAADLGHIAEASGVGADIDLD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 238 DLPYSDALSRHVDPEQALRWALSGGEDYELCFTVSELNRGALEVAVSHLGVPVTCIGQLTtasEGMVFLRDGAPVTLDWK 317
Cdd:PRK05731 237 ALPISPALREAAEGEDALRWALSGGEDYELLFTFPPENRGALLAAAGHLGVGVTIIGRVT---EGEGVVVDGEPVTLDLK 313
|
....*
gi 1755430050 318 GYDHF 322
Cdd:PRK05731 314 GYDHF 318
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
3-322 |
8.36e-154 |
|
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: 433.80 E-value: 8.36e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 3 CGEFSLIARYFDRVRSSRLDVETGIGDDCALLTVPEKQtLAISTDTLVSGIHFLPD-IDPRDLGYKALAVNVSDLAAMGA 81
Cdd:COG0611 1 MGEFGLIERLFKRLALRGPDVLLGIGDDAAVLDPPGGR-LVVTTDMLVEGVHFPLDwMSPEDLGWKAVAVNLSDLAAMGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 82 DPAWLTLALTLPE-VNETWLEAFSDSLFEQLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPAGRALKRSGARPGDWVFITG 159
Cdd:COG0611 80 RPLAALLSLALPPdTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPeLTISVTAIGEVPGGRPLLRSGARPGDLVYVTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 160 TPGDSAAGLAILQKRLHVEDtSDAGYLVKRHLRPTPRVLHGQALR--GLASAAIDLSDGLISDLGHILKASDCGARIELN 237
Cdd:COG0611 160 TLGDAAAGLALLLRGLRVPL-EAREYLLERHLRPEPRLALGRALAeaGLATAMIDISDGLAADLGHIAEASGVGAEIDLD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 238 DLPYSDALSRHVDPEQALRWALSGGEDYELCFTVSELNRGALEVAVshLGVPVTCIGQLTTASEGMVFLRDGAPVTLDWK 317
Cdd:COG0611 239 ALPLSPALREAALGLDPLELALTGGEDYELLFTVPPEALEALEAAA--LGVPLTVIGRVTEGEGVTLDDADGRPIPLEAR 316
|
....*
gi 1755430050 318 GYDHF 322
Cdd:COG0611 317 GWDHF 321
|
|
| thiL |
TIGR01379 |
thiamine-phosphate kinase; This model describes thiamine-monophosphate kinase, an enzyme that ... |
4-322 |
1.46e-144 |
|
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: 410.18 E-value: 1.46e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 4 GEFSLIARYFDRvRSSRLDVETGIGDDCALLTVPEKQTLAISTDTLVSGIHFLPDIDPRDLGYKALAVNVSDLAAMGADP 83
Cdd:TIGR01379 1 GEFELIDRILRR-LVQDPDVALGIGDDAALVSAPEGRDLVLTTDTLVEGVHFPPDTTPEDLGWKAVAVNLSDLAAMGATP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 84 AWLTLALTLPE-VNETWLEAFSDSLFEQLNYYDMQLIGGDTTRGP-LSMTLGIHGFVPAGRALKRSGARPGDWVFITGTP 161
Cdd:TIGR01379 80 KWFLLSLGLPSdLDEAWLEAFYDGLFEAAKQYGVPLVGGDTVSSPeLVVTVTAIGEAPKGRALLRSGAKPGDLVFVTGTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 162 GDSAAGLAILQKRLHVEDTSDAGYLVKRHLRPTPRVLHGQALRGLASAAIDLSDGLISDLGHILKASDCGARIELNDLPY 241
Cdd:TIGR01379 160 GDSAAGLALLLKGKKEPDEEDDEALLQRHLRPEPRVEEGLALAGYANAAIDVSDGLAADLGHIAEASGVGIVIDLDRLPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 242 SDALSRHVDPEQALRWALSGGEDYELCFTVSELNRGALEVAvshLGVPVTCIGQLtTASEGMVFLRDGAPVT-LDWKGYD 320
Cdd:TIGR01379 240 SSELAAWAEGKNPLEWALSGGEDYELVFTVPPERREALLDA---AKGPLTRIGRV-TEGEGVVLLADGKTVElLDRLGWQ 315
|
..
gi 1755430050 321 HF 322
Cdd:TIGR01379 316 HF 317
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
4-297 |
1.67e-132 |
|
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: 378.43 E-value: 1.67e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 4 GEFSLIARYFDRVRSSRlDVETGIGDDCALLTvPEKQTLAISTDTLVSGIHFLPDIDPRDLGYKALAVNVSDLAAMGADP 83
Cdd:cd02194 1 GEFELIDRLFKRLGAGP-GVLLGIGDDAAVLK-PPGGRLVVTTDTLVEGVHFPPDTTPEDIGWKALAVNLSDLAAMGARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 84 AWLTLALTLPE-VNETWLEAFSDSLFEQLNYYDMQLIGGDTTRG-PLSMTLGIHGFVPAGRALKRSGARPGDWVFITGTP 161
Cdd:cd02194 79 LGFLLSLGLPPdTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGsELVISVTALGEVEKGKPLRRSGAKPGDLLYVTGTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 162 GDSAAGLAILQKRLHVEDtSDAGYLVKRHLRPTPRVLHGQALR-GLASAAIDLSDGLISDLGHILKASDCGARIELNDLP 240
Cdd:cd02194 159 GDAAAGLALLLGGLKLPE-ELYEELIERHLRPEPRLELGRALAeGLATAMIDISDGLLADLGHIAEASGVGAVIDLDKLP 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1755430050 241 YSDALSRHVDPEQALRWALSGGEDYELCFTVSElnrGALEVAVSHLGVPVTCIGQLT 297
Cdd:cd02194 238 LSPALRAAELGEDALELALSGGEDYELLFTVPP---ENAEAAAAKLGVPVTVIGRVT 291
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
28-307 |
1.55e-23 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 98.61 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 28 GDDCALLTVPEKqTLAISTDTLVSGIHFLPDidpRDLGYKALAVNVSDLAAMGADPAWLTLALTLPE-VNETWLEAFSDS 106
Cdd:COG0309 30 GEDAAVLDLGGG-RLAFTTDSFVVSPIFFPG---GDIGKLAVHGTVNDLAVSGAKPLYLSVSLILEEgFPLEDLERIVES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 107 LFEQLNYYDMQLIGGDTTR-------GPLSMTLGIhGFVPAGRALKRSGARPGDWVFITGTPGDSaaGLAILQKR----L 175
Cdd:COG0309 106 MAEAAREAGVSIVTGDTKVverggvdGPFINTTGI-GVVPKGRLISPSGARPGDKIIVTGGIGDH--GTAILAARegleL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 176 HVEDTSDA---GYLVKRHLRPTPRVLHgqALR-----GLASAAIDLSDglisdlghilkASDCGARIELNDLPYSD---A 244
Cdd:COG0309 183 EGELLSDAaplNDLVSVLLEAAPGGVH--AMRdptrgGLAGALNEIAE-----------ASGVGIEIDEDAIPVRPevrG 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755430050 245 LSRH--VDPeqalrWAL-SGGedyELCFTVSELNRGALEVAVSHLGVPVTCIGQLTTASEGMVFLR 307
Cdd:COG0309 250 ICELlgLDP-----LYLaNEG---KLVAVVPPEDAEAVLEALRAHGIDAAIIGEVTEGPPGRVVLK 307
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
42-295 |
1.82e-21 |
|
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: 90.92 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 42 LAISTDtlvsGIHFLPDIDPRDLGYKALAVNVSDLAAMGADPAWLTLALTLPEVNE-TWLEAFSDSLFEQLNYYDMQLIG 120
Cdd:cd00396 2 LAMSTD----GINPPLAINPWAGGRLAVGGAVNDIAAMGARPIALLASLSLSNGLEvDILEDVVDGVAEACNQLGVPIVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 121 GDTTRGP------LSMTLGIHGFVPAGRALKRSGARPGDWVFITGTpgDSAAGLailqkrlhvedtsdagylvkrhlrpt 194
Cdd:cd00396 78 GHTSVSPgtmghkLSLAVFAIGVVEKDRVIDSSGARPGDVLILTGV--DAVLEL-------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 195 prvlhgQALRGLaSAAIDLSD-GLISDLGHILKASDCGARIELNDLPysdalSRHVDPE---QALRWALSGGEDYELCFT 270
Cdd:cd00396 130 ------VAAGDV-HAMHDITDgGLLGTLPELAQASGVGAEIDLEAIP-----LDEVVRWlcvEHIEEALLFNSSGGLLIA 197
|
250 260
....*....|....*....|....*
gi 1755430050 271 VSELNRGALEVAVSHLGVPVTCIGQ 295
Cdd:cd00396 198 VPAEEADAVLLLLNGNGIDAAVIGR 222
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
26-294 |
4.02e-20 |
|
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: 88.81 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 26 GIGDDCALLTVPEKqTLAISTDtLVSGihflpdiDPRDLGYKALAVNVSDLAAMGADPAWLTLALTLPEVN-ETWLEAFS 104
Cdd:cd06061 30 GGGEDAAVVDFGGK-VLVVSTD-PITG-------AGKDAGWLAVHIAANDIATSGARPRWLLVTLLLPPGTdEEELKAIM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 105 DSLFEQLNYYDMQLIGGDTTRGP------LSMTLgiHGFVPAGRALKRSGARPGDWVFITGTPGDSAAGLAILQKRLHVE 178
Cdd:cd06061 101 REINEAAKELGVSIVGGHTEVTPgvtrpiISVTA--IGKGEKDKLVTPSGAKPGDDIVMTKGAGIEGTAILANDFEEELK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 179 DTSDAGYLVK-RHLRPTPRVLH--GQALRGLASAAIDLSD-GLISDLGHILKASDCGARIELNDLPYSDALSR-----HV 249
Cdd:cd06061 179 KRLSEEELREaAKLFYKISVVKeaLIAAEAGVTAMHDATEgGILGALWEVAEASGVGLRIEKDKIPIRQETKEicealGI 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1755430050 250 DPeqalrWAL-SGGedyELCFTVSELNRGALEVAVSHLGVPVTCIG 294
Cdd:cd06061 259 DP-----LRLiSSG---TLLITVPPEKGDELVDALEEAGIPASVIG 296
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
20-241 |
6.42e-20 |
|
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: 87.96 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 20 RLDVETGIGDDCALLTVPEKQTLAISTDtlvsgiHFLPDI-DPRDLGyKALAVNV-SDLAAMGADP----AWLTLALTLP 93
Cdd:cd02195 33 NLLVGLGTGDDAAVYRLPGGLALVQTTD------FFPPIVdDPYLFG-RIAAANAlSDIYAMGAKPlsalAIVTLPRKLP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 94 EVNETWL----EAFSDSLFEQlnyyDMQLIGGDTTRGP-LSMTLGIHGFVPAGRALKRSGARPGDWVFITGTPGDSAAGL 168
Cdd:cd02195 106 ALQEEVLreilAGGKDKLREA----GAVLVGGHTIEGPePKYGLSVTGLVHPNKILRNSGAKPGDVLILTKPLGTGILFA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755430050 169 AILQKRLHVEDTSDAGYLVKRHLRPTPRVLHGQAlrglASAAIDLSD-GLisdLGH---ILKASDCGARIELNDLPY 241
Cdd:cd02195 182 AEMAGLARGEDIDAALESMARLNRAAAELLRKYG----AHACTDVTGfGL---LGHlleMARASGVSAEIDLDKLPL 251
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
29-138 |
5.57e-19 |
|
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: 80.57 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 29 DDCALLTvpekQTLAISTDTLVSGIHFLpdidprdlGYKALAVNVSDLAAMGADPAWLTLALTLPEVNET--WLEAFSDS 106
Cdd:pfam00586 1 DDAAVAV----TTDGHGTPSLVDPYHFP--------GAKAVAGNLSDIAAMGARPLAFLDSLALPGGPEVewVLEEIVEG 68
|
90 100 110
....*....|....*....|....*....|....*.
gi 1755430050 107 LFEQLNYYDMQLIGGDTTRGP----LSMTLGIHGFV 138
Cdd:pfam00586 69 IAEACREAGVPLVGGDTSFDPeggkPTISVTAVGIV 104
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
7-244 |
1.17e-14 |
|
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: 72.87 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 7 SLIARYFDrvrssrlDVETGIGDDCALLTVPEKqTLAISTDTLVsgihflpdIDPR-----DLGykALAVN--VSDLAAM 79
Cdd:cd02197 12 ELFLKAFD-------NPILEVLEDAAALLVGGG-RLAFTTDSFV--------VSPLffpggDIG--KLAVCgtVNDLAMM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 80 GADPAWLTLALTLPE---VNEtwLEAFSDSLFEQLNYYDMQLIGGDTT---RGPLS----MTLGIhGFVPAGRALKRSGA 149
Cdd:cd02197 74 GAKPLYLSLGFILEEgfpLED--LERIVKSMAEAAREAGVKIVTGDTKvvpKGKADgifiNTTGI-GVIPRGVIISPSNI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 150 RPGDWVFITGTPGDSaaGLAILQKR----LHVEDTSDAGYLVK--RHLRPTPRVLHgqALR-----GLASAaidlsdgli 218
Cdd:cd02197 151 RPGDKIIVSGTIGDH--GAAILAAReglgFETDIESDCAPLNGlvEALLEAGPGIH--AMRdptrgGLAAV--------- 217
|
250 260
....*....|....*....|....*.
gi 1755430050 219 sdLGHILKASDCGARIELNDLPYSDA 244
Cdd:cd02197 218 --LNEIARASGVGIEIEEEAIPVREE 241
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
9-241 |
3.68e-12 |
|
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: 65.70 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 9 IARYFDRVRSSRLDVETGIGDDCALLTVPEKQTLAIStdtlvSGIH-FLPDIDPRDLGYKALAVNVSDLAAMGADPawlt 87
Cdd:cd02192 16 VVAILPDAPFDSLGVAADLGDDAAAIPDGDGYLLLAA-----DGIWpSLVEADPWWAGYCSVLVNVSDIAAMGGRP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 88 LALtlpeVNETWLE--AFSDSLFEQLNY----YDMQLIGG----DTTRGPLSMT-LGIhgfvPAGRALKRSGARPGDWVF 156
Cdd:cd02192 87 LAM----VDALWSPsaEAAAQVLEGMRDaaekFGVPIVGGhthpDSPYNALSVAiLGR----ARKDLLISFGAKPGDRLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 157 ITgtpgdsaaglAILQKRLHVED-------TSDAGYLVKRHLrptpRVLHGQALRGLASAAIDLSD-GLISDLGHILKAS 228
Cdd:cd02192 159 LA----------IDLDGRVHPSPppnwdatTMKSPALLRRQI----ALLPELAERGLVHAAKDISNpGIIGTLGMLLEAS 224
|
250
....*....|...
gi 1755430050 229 DCGARIELNDLPY 241
Cdd:cd02192 225 GVGAEIDLDAIPR 237
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
9-256 |
1.03e-09 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 58.64 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 9 IARYFDRVRSsrLDVETGIGDDCALLTVPEK-QTLAIStdtlvsGIhfLPDI---DPRDLGYKALAVNVSDLAAMGADPa 84
Cdd:COG2144 26 VVRALGLASS--GGTAAAFGDDAAAIPDGDGyLLLAAE------GI--WPKFveaDPWFAGYCSVLVNVSDIAAMGGRP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 85 wltLALtlpeVNETWleAFSDSLFEQL--------NYYDMQLIGG----DTTRGPLSMT-LGIhgfvpAGRALKRSGARP 151
Cdd:COG2144 95 ---LAV----VDALW--SSDEEAAAPVlagmraasRKFGVPIVGGhthpDTPYNALAVAiLGR-----AKKLLTSFTARP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 152 GDWVFitgtpgdsaagLAI-LQKRLH--------VEDTSDAgyLVKRHLRPTPRVlhgqALRGLASAAIDLSD-GLISDL 221
Cdd:COG2144 161 GDRLI-----------AAIdLDGRYHppfpywdaTTGKPPE--RLRAQLELLPEL----AEAGLVTAAKDISNpGIIGTL 223
|
250 260 270
....*....|....*....|....*....|....*
gi 1755430050 222 GHILKASDCGARIELNDLPYSDalsrHVDPEQALR 256
Cdd:COG2144 224 GMLLECSGVGATIDLDAIPRPE----GVDLERWLK 254
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
150-297 |
1.21e-09 |
|
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: 56.20 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 150 RPGDWVFITGTPGDSAAGLAiLQKRLHVEDTSDAGYLVKRHLRPTP--RVLHGQALRGLASAAIDLSD-GLISDLGHILK 226
Cdd:pfam02769 1 KPGDVLILLGSSGLHGAGLS-LSRKGLEDSGLAAVQLGDPLLEPTLiyVKLLLAALGGLVKAMHDITGgGLAGALAEMAP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755430050 227 ASDCGARIELNDLPYSDALSRHVDPeqalrwALSGGEDYELCFTVSELNRGALEVAVSHlGVPVTCIGQLT 297
Cdd:pfam02769 80 ASGVGAEIDLDKVPIFEELMLPLEM------LLSENQGRGLVVVAPEEAEAVLAILEKE-GLEAAVIGEVT 143
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
20-307 |
3.69e-09 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 57.01 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 20 RLDVETGIGDDCALLTVPEKQTLAISTDtlvsgiHFLPDI-DPRDLGYKAlAVN-VSDLAAMGADPaWLTLA-LTLP--- 93
Cdd:COG0709 39 NLLVGLETSDDAAVYRLGDDQALVQTTD------FFTPIVdDPYDFGRIA-AANaLSDVYAMGGRP-LTALAiVGFPidk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 94 -------EVnetwLEAFSDSLFEqlnyYDMQLIGGDTTRGP-----LSMTlgihGFVPAGRALKRSGARPGDWVFIT--- 158
Cdd:COG0709 111 lpeevlaEI----LAGGADKCRE----AGAPLAGGHSIDDPepkygLAVT----GLVHPDKVLRNAGARPGDVLILTkpl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 159 GTpgdsaaGL---AILQKRLHVEDTSDAGYLVKRHLRPTPRVLHGQAlrglASAAIDLSD-GLisdLGH---ILKASDCG 231
Cdd:COG0709 179 GT------GIlttAIKAGLADGEDIAAAIASMTTLNKAAAELARLYG----VHACTDVTGfGL---LGHlleMARGSGVS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 232 ARIELNDLPY--------------------SDALSRHVDPEQAL---RWAL------SGGedyeLCFTVSELNRGALEVA 282
Cdd:COG0709 246 AEIDLDAVPLlpgalelaeqgivpggtyrnRASYGAKVEFAEGLdeaQRDLlfdpqtSGG----LLIAVPPEAAEELLAA 321
|
330 340
....*....|....*....|....*
gi 1755430050 283 VSHLGVPVTCIGQLTTASEGMVFLR 307
Cdd:COG0709 322 LRAAGYAAAIIGEVTAGEGGAIEVR 346
|
|
| PurL1 |
COG0046 |
Phosphoribosylformylglycinamidine (FGAM) synthase, synthetase domain [Nucleotide transport and ... |
29-312 |
6.32e-08 |
|
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: 53.90 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 29 DDCALLTVPEKQT-LAISTDtlVSGIHFLpdIDPRDLGYKALAVNVSDLAAMGADPawltLALTL---------PEVnet 98
Cdd:COG0046 443 ADAAVVRVDGTYKgLAMSTG--ENPRYAL--LDPYAGARMAVAEAARNLAAVGAEP----LAITDclnwgnpekPEE--- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 99 wLEAFSDS---LFEQLNYYDMQLIGG------DTTRG----PLSMTLGIHGFVPAGRALKRSGAR-PGDWVFITGTPGDS 164
Cdd:COG0046 512 -MAQLVEAvkgLADACRALGIPVPSGnvslynETKDGkvaiPPTPVIGAVGLVDDVRKTVTPDLKkEGDLLYLIGETKNE 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 165 AAGLAILQKRLHVEDTS---DAGYLVKRHlrptpRVLHGQALRGLASAAIDLSDG-LISDLGHILKASDCGARIELNDLP 240
Cdd:COG0046 591 LGGSEYAQVLGQLGGEPpdvDLEAEKALF-----EAVQELIREGLILAAHDVSDGgLAVALAEMAFAGGLGADIDLDALG 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 241 --------YSDALSRHVdpeqalrwalsggedyelcFTVSELNRGALEVAVSHLGVPVTCIGQlTTASEGMVFLRDGAPV 312
Cdd:COG0046 666 dlrpdaalFSESQGRAV-------------------VQVAPEDAEAVEALLAEAGLPAHVIGT-VTGDDRLVIRRGGETL 725
|
|
| PurL_repeat2 |
cd02204 |
PurL subunit of the formylglycinamide ribonucleotide amidotransferase (FGAR-AT), second repeat. ... |
30-295 |
1.72e-06 |
|
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: 48.69 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 30 DCALLTVPE--KQTLAISTDtlvsgihFLP---DIDPRDLGYKALAVNVSDLAAMGADPawltLALTL------PEVNET 98
Cdd:cd02204 1 DAAVLRIPGetDKGLAMSTG-------ENPrysLLDPYAGAALAVAEAVRNLVAVGADP----LAITDclnfgnPEKPEG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 99 WLEAFSDS---LFEQLNYYDMQLIGG-D----TTRG---PLSMTLGIHGFVPAGRALKRSGAR-PGDWVFITGTP----G 162
Cdd:cd02204 70 EMGQLVEAvlgLGDACRALGTPVIGGkDslynETEGvaiPPTLVIGAVGVVDDVRKIVTLDFKkEGDLLYLIGETkdelG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 163 DSAAGLAILQKRLHVEDTSDAGYLVKRHlrptpRVLHGQALRGLASAAIDLSD-GLISDLGHILKASDCGARIELNDLP- 240
Cdd:cd02204 150 GSEYALAYHGLGGGAPPLVDLEREKALF-----DAVQELIKEGLVLSAHDVSDgGLAVALAEMAFAGGLGAEVDLSKDDa 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 241 -----YSDALSRHVdpeqalrwalsggedyelcFTVSELNRGALEVAvsHLGVPVTCIGQ 295
Cdd:cd02204 225 edellFSESLGRVL-------------------VEVKPENEEVFEAE--EAGVPATVIGT 263
|
|
| PRK14105 |
PRK14105 |
selenide, water dikinase SelD; |
22-240 |
4.90e-05 |
|
selenide, water dikinase SelD;
Pssm-ID: 237611 [Multi-domain] Cd Length: 345 Bit Score: 44.38 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 22 DVETGIGDDCAlltVPEKQTLAISTDTLVsgihFLPDI-DPRDLGYKALAVNVSDLAAMGADPAWLTLAL-----TLP-E 94
Cdd:PRK14105 41 HTKVGLGDDAA---VIIKNGLAIVKTVDV----FTPIVdDPYIQGKIAACNSTSDVYAMGLSEIIGVLVIlgippELPiE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 95 VNETWLEAFSDSLFEQlnyyDMQLIGGDTTRGPLSMTLG-IHGFVPAGRALKRSGARPGDWVFITGTPGDSAAgLAILQK 173
Cdd:PRK14105 114 VAKEMLQGFQDFCREN----DTTIIGGHTILNPWPLIGGaVTGVGKEEDILTKAGAKEGDVLILTKPLGTQSA-MALSRV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 174 RLHVED-----TSDAGYLVKR--HLRPTPRVLHGQALRGLASAAIDLSDGLISD------LGHILK-ASDCGARIELNDL 239
Cdd:PRK14105 189 PEEFEDliditKEEKEYIINKaiELMTTSNRYALLALREAEEEVGEKIANAMTDvtgfgiLGHSQEmAEQSNVEIEISTL 268
|
.
gi 1755430050 240 P 240
Cdd:PRK14105 269 P 269
|
|
| PRK01213 |
PRK01213 |
phosphoribosylformylglycinamidine synthase subunit PurL; |
28-315 |
5.36e-04 |
|
phosphoribosylformylglycinamidine synthase subunit PurL;
Pssm-ID: 234921 [Multi-domain] Cd Length: 724 Bit Score: 41.63 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 28 GDDCALLTVPEKQT-LAISTDtlVSGIH-FLpdiDPRDLGYKALAVNVSDLAAMGADPawltLALT--L-------PEVn 96
Cdd:PRK01213 427 GGDAAVLRIRGGGKgLALTTD--CNPRYvYL---DPYEGAKLAVAEAARNLAAVGATP----LAITdcLnfgnpekPEV- 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 97 eTWleAFSDSLF------EQLNyydMQLIGG------DTTRGPL--SMTLGIHGFVPAGRALKRSG-ARPGDWVFITGTP 161
Cdd:PRK01213 497 -MW--QFVEAVRgladacRALG---TPVVGGnvslynETGGTAIypTPVIGMVGLIDDVSKRTTSGfKKEGDLIYLLGET 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 162 GDSAAGlAILQKRLHVEDTSDAgylvkrhlrptPRV------LHGQALR-----GLASAAIDLSD-GLISDLGHILKASD 229
Cdd:PRK01213 571 KDELGG-SEYLKVIHGHVGGRP-----------PKVdleaekRLQELVReaireGLVTSAHDVSEgGLAVALAEMAIAGG 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 230 CGARIELNDLPYSDAL--SrhvdpEQALRWALSggedyelcftVSELNRGALEVAVSHLGVPVTCIGqltTASEGMVFLR 307
Cdd:PRK01213 639 LGAEVDLSDGLRPDALlfS-----ESQGRYVVS----------VPPENEEAFEALAEAAGVPATRIG---VVGGDALKVK 700
|
....*...
gi 1755430050 308 DGAPVTLD 315
Cdd:PRK01213 701 GNDTESLE 708
|
|
| FGAM_synth_II |
TIGR01736 |
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a ... |
28-240 |
9.89e-03 |
|
phosphoribosylformylglycinamidine synthase II; Phosphoribosylformylglycinamidine synthase is a single, long polypeptide in most Proteobacteria and eukarotes. Three proteins are required in Bacillus subtilis and many other species. This is the longest of the three and is designated PurL, phosphoribosylformylglycinamidine synthase II, or FGAM synthase II. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273781 [Multi-domain] Cd Length: 715 Bit Score: 37.67 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 28 GDDCALLTVPE--KQTLAISTDtlVSGIHFLpdIDPRDLGYKALAVNVSDLAAMGADPAWLTLALTL-----PEVNETWL 100
Cdd:TIGR01736 417 GEDAAVLRIKEtgKLGLALTAD--CNPRYVY--LDPYAGAAGAVAEAYRNLAAVGAEPLAAVDCLNFgnperPEVYWQFV 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 101 EAFsDSLFEQLNYYDMQLIGG------DTTRGPL--SMTLGIHGFVP-AGRALKRSGARPGDWVFITGTPGDSAAGlAIL 171
Cdd:TIGR01736 493 EAV-KGLGDACRALGTPVVGGnvslynETNGVPIapTPTIGMVGLVEdVEKLLTSNFKKEGDAIYLIGETKDELGG-SEY 570
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755430050 172 QKRLHVEDTSDAGYLVKRHLRPTPRVLHGQALRGLASAAIDLSD-GLISDLGHILKASDCGARIELNDLP 240
Cdd:TIGR01736 571 LRVIHGIVSGQVPAVDLEEEKELADAVREAIRAGLVSAAHDVSRgGLAVALAEMAAASGIGAEVDIDEIA 640
|
|
| |
