|
Name |
Accession |
Description |
Interval |
E-value |
| Nterm_to_SelD |
TIGR03169 |
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family ... |
11-368 |
0e+00 |
|
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown.
Pssm-ID: 274465 Cd Length: 364 Bit Score: 553.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 11 DLVLVGGGHTHALLLRMWGMKPLPGVRLTLINPGPTAPYSGMLPGFVAGHYTRDALDIDLVKLARFAGARLILGAAEEID 90
Cdd:TIGR03169 1 DLVLIGGGHSHALVLRMWGMKPLPGVRLTLINPGPTTPYSGMLPGHVAGHYTRDELHIDLVRLARFAGARLILDRAIGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 91 PISKRITVPGRPAIAYDVASIDIGITSAMPELVGFDDFAIPAKPLGRFATRWDAFRNGSD---PARIACIGGGVAGVELI 167
Cdd:TIGR03169 81 LAAKQVICAGRPPIAYDVLSIDIGSTPALPDVPGFAEHAIPAKPLGQFAQRWQRFLERAKpqqPPRIAVIGGGAAGVELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 168 LAMAHALRQQQRLAQATLIDSGSVL-SVLTSQSQTRLRKALDANGVRILQQTRIDHLSAGRIHLEGGRVIDSDFTVGAAG 246
Cdd:TIGR03169 161 LAMAHRLRQLGRNAEVTLIDRGNVLlPGHNARVRRRLERALQERGVTLHLGATVAEVTADAVRLEDGQTLPADFTFWATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 247 ARAYGWLETSGLQQHE-GALVISETLQT-SDPDVFACGDCAHMAYAPRPKAGVYAVRQAPVLYHNLKAVLGGGSLKSYQP 324
Cdd:TIGR03169 241 ARPPGWLAESGLALDEdGFIRVGPTLQSlSHPDIFAAGDCAHLVHAPRPKAGVFAVRQAPVLAENLRAALTGGPLRPYRP 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499858144 325 QKDYLKLISMGDKSALADRDGRSFAGGLLWRWKDHIDRKFMGKF 368
Cdd:TIGR03169 321 QSDYLKLISTGDKSAVASRGGLAFSGAWLWRWKDRIDRKFMDKF 364
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
387-719 |
9.33e-111 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 338.97 E-value: 9.33e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 387 MEAV-LGSKPMCGGCGSKVGRHALHAGLGAFSGAQRADVTPL--PGDDAAQLMTGSAT-QVISTDHLRAFTEDPVVMTAI 462
Cdd:COG0709 2 MEEIrLTQLSHGGGCGAKIGPGVLAQILAGLPPPSDPNLLVGleTSDDAAVYRLGDDQaLVQTTDFFTPIVDDPYDFGRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 463 AAQHALNDIWAMGAHPQAATVTLILPRqsADLQERLLAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCETP- 541
Cdd:COG0709 82 AAANALSDVYAMGGRPLTALAIVGFPI--DKLPEEVLAEILAGGADKCREAGAPLAGGHSIDDPEPKYGLAVTGLVHPDk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 542 PLTLAGAQAGDHLILTKPIGSGTLMAAEMSGTAPGACVAEALDLMCQSQRDAATVLRPV-AHAMTDVTGFGLLGHLQGLC 620
Cdd:COG0709 160 VLRNAGARPGDVLILTKPLGTGILTTAIKAGLADGEDIAAAIASMTTLNKAAAELARLYgVHACTDVTGFGLLGHLLEMA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 621 AASDLGAEVDFDAIPLMAGAAALAEAGVRSTIFEDNAALLPGIGTAGA------RALLFDPQTSGGLLASVDPARASDAL 694
Cdd:COG0709 240 RGSGVSAEIDLDAVPLLPGALELAEQGIVPGGTYRNRASYGAKVEFAEgldeaqRDLLFDPQTSGGLLIAVPPEAAEELL 319
|
330 340
....*....|....*....|....*
gi 499858144 695 RELKNHGYHAAKIGEIRDADQGIVI 719
Cdd:COG0709 320 AALRAAGYAAAIIGEVTAGEGGAIE 344
|
|
| selD |
TIGR00476 |
selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino ... |
391-690 |
4.18e-108 |
|
selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelD, known as selenophosphate synthetase, selenium donor protein, and selenide,water dikinase. SelD provides reduced selenium for the selenium transferase SelA. This protein itself contains selenocysteine in many species; any sequence scoring well but not aligning to the beginning of the model is likely to have a selenocysteine residue incorrectly interpreted as a stop codon upstream of the given sequence. The SelD protein also provides selenophosphate for the enzyme tRNA 2-selenouridine synthase, which catalyzes a tRNA base modification. It also contributes to selenium incorporation by selenium-dependent molybdenum hydroxylases (SDMH), in genomes with the marker TIGR03309. All genomes with SelD should make selenocysteine, selenouridine, SDMH, or some combination.
Pssm-ID: 273100 [Multi-domain] Cd Length: 301 Bit Score: 330.61 E-value: 4.18e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 391 LGSKPMCGGCGSKVGRHALHAGLGAFSGA--QRADVTPLPGDDAAQL-MTGSATQVISTDHLRAFTEDPVVMTAIAAQHA 467
Cdd:TIGR00476 2 LTEYSHGGGCGCKIGPGVLDKILASLPAApdPNLLVGNDTGDDAAVYkLNDGLALVSTTDFFTPIVDDPYDFGRIAATNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 468 LNDIWAMGAHPQAATVTLILPRQSadLQERLLAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCETPPLTL-A 546
Cdd:TIGR00476 82 LSDIYAMGGTPLTALAILGWPRNK--LPPEVLREILAGGADVCAEAGAPLAGGHSIDDPEPKYGLAVTGLVHPDKLKRnD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 547 GAQAGDHLILTKPIGSGTLMAAEMSGTAPGACVAEALDLMCQ--SQRDAATVLRPVaHAMTDVTGFGLLGHLQGLCAASD 624
Cdd:TIGR00476 160 GAQPGDVLILTKPLGVGVLTAALKKGGLAEEAYAAAIASMTTlnKQAAELAALAGV-HAMTDVTGFGLLGHLLEMCRGSG 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499858144 625 LGAEVDFDAIPLMagaaalAEAGVRSTIFEDNAALLPGIGTAGA---RALLFDPQTSGGLLASVDPARA 690
Cdd:TIGR00476 239 VSAEIDFDAVPLL------AEQGCVPGGTGRNFASYGEKVPEPAgeqRDLLCDPQTSGGLLIAVAPEAA 301
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
391-710 |
1.00e-100 |
|
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: 310.99 E-value: 1.00e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 391 LGSKPMCGGCGSKVGRHALHAGLGAFSGAQR--ADVTPLPGDDAAQL-MTGSATQVISTDHLRAFTEDPVVMTAIAAQHA 467
Cdd:cd02195 1 LTSFMKCAGCGAKVGPGVLSQLLAGLPLPTDpnLLVGLGTGDDAAVYrLPGGLALVQTTDFFPPIVDDPYLFGRIAAANA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 468 LNDIWAMGAHPQAATVTLILPRQSADLQERLLAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCETPPLTL-A 546
Cdd:cd02195 81 LSDIYAMGAKPLSALAIVTLPRKLPALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEPKYGLSVTGLVHPNKILRnS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 547 GAQAGDHLILTKPIGSGTLMAAEMSGTAPGACVAEALDLMCQSQRDAATVLR-PVAHAMTDVTGFGLLGHLQGLCAASDL 625
Cdd:cd02195 161 GAKPGDVLILTKPLGTGILFAAEMAGLARGEDIDAALESMARLNRAAAELLRkYGAHACTDVTGFGLLGHLLEMARASGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 626 GAEVDFDAIPLMagaaalaeagvrstifednaallpgigtagarallfdpQTSGGLLASVDPARASDALRELKNHGYHAA 705
Cdd:cd02195 241 SAEIDLDKLPLL--------------------------------------QTSGGLLAAVPPEDAAALLALLKAGGPPAA 282
|
....*
gi 499858144 706 KIGEI 710
Cdd:cd02195 283 IIGEV 287
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
9-368 |
2.09e-93 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 295.50 E-value: 2.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 9 TRDLVLVGGGHTHALLLRMWGMKPLPGVRLTLINPGPTAPYSGMLPGFVAGHYTRDALDIDLVKLARFAGARLILGAAEE 88
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 89 IDPISKRITVPGRPAIAYDVASIDIGITSAMPELVGFDDFAIPAKPLGRFATRWDAFRN------GSDPARIACIGGGVA 162
Cdd:COG1252 81 IDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAaferaeRRRLLTIVVVGGGPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 163 GVELILAMAHALRQQQRL-------AQATLIDSGS-VLSVLTSQSQTRLRKALDANGVRILQQTRIDHLSAGRIHLEGGR 234
Cdd:COG1252 161 GVELAGELAELLRKLLRYpgidpdkVRITLVEAGPrILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 235 VIDSDFTVGAAGARAYGWLETSGLQQ-HEGALVISETLQT-SDPDVFACGDCAHMAYA---PRPKAGVYAVRQAPVLYHN 309
Cdd:COG1252 241 EIPADTVIWAAGVKAPPLLADLGLPTdRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDPdgkPVPKTAQAAVQQAKVLAKN 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 499858144 310 LKAVLGGGSLKSYQPQkDYLKLISMGDKSALADRDGRSFAGGLLWRWKDHIDRKFMGKF 368
Cdd:COG1252 321 IAALLRGKPLKPFRYR-DKGCLASLGRGAAVADVGGLKLSGFLAWLLKRAIHLYFLPGF 378
|
|
| PRK00943 |
PRK00943 |
selenide, water dikinase SelD; |
398-716 |
2.02e-44 |
|
selenide, water dikinase SelD;
Pssm-ID: 234870 [Multi-domain] Cd Length: 347 Bit Score: 163.10 E-value: 2.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 398 GGCGSKVGRHALHAGLgAFSGAQRADVTPLPG----DDAAQLMTGSATQVIST-DHLRAFTEDPVVMTAIAAQHALNDIW 472
Cdd:PRK00943 15 AGCGCKISPKVLETIL-ASEQAKFVDPNLLVGnetrDDAAVYDLNDGTGIISTtDFFMPIVDDPFDFGRIAATNAISDIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 473 AMGAHPQAATVTL-----ILPRQSAdlqerllAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCETPPL-TLA 546
Cdd:PRK00943 94 AMGGKPIMAIAILgwpinKLPPEVA-------REVLEGGRAACRQAGIPLAGGHSIDAPEPIFGLAVTGVVPPERVkRNA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 547 GAQAGDHLILTKPIGSGTLMAAEMSGTAPGACVAEALDLMCQSQRDAATVLR-PVAHAMTDVTGFGLLGHLQGLCAASDL 625
Cdd:PRK00943 167 TAQAGDKLFLTKPLGIGILTTAEKKSKLKPEHYGLAIEAMCQLNRPGADFAKlPGVHAMTDVTGFGLLGHLLEMCQGAGL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 626 GAEVDFDAIPLMAGAAALAEAGV------RStiFEDNAALLPGIgTAGARALLFDPQTSGGLLASVDPARASDALRELKN 699
Cdd:PRK00943 247 TARVDYAAVPLLPGVEEYIAQGCvpggtgRN--FASYGHLIGEL-PDEQRALLCDPQTSGGLLVAVAPEAEAEVLAIAAE 323
|
330
....*....|....*..
gi 499858144 700 HGYHAAKIGEIRDADQG 716
Cdd:PRK00943 324 HGIELAAIGELVEARGG 340
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
11-303 |
1.60e-20 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 92.77 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 11 DLVLVGGGH---THALLLRMWGMKplpgvrLTLINPGPTAPYSGMLP----------GFVAGHYTRDALDIDLVKLARFA 77
Cdd:pfam07992 2 DVVVIGGGPaglAAALTLAQLGGK------VTLIEDEGTCPYGGCVLskallgaaeaPEIASLWADLYKRKEEVVKKLNN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 78 GARLILGA-AEEIDPISKRITVPGRPA-----IAYDVASIDIGITSAMPELVGFDDFAIPakpLGRFATRWDAFRNGSDP 151
Cdd:pfam07992 76 GIEVLLGTeVVSIDPGAKKVVLEELVDgdgetITYDRLVIATGARPRLPPIPGVELNVGF---LVRTLDSAEALRLKLLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 152 ARIACIGGGVAGVELilamAHALRQQQrlAQATLIDSGS-VLSVLTSQSQTRLRKALDANGVRILQQT---RIDHLSAG- 226
Cdd:pfam07992 153 KRVVVVGGGYIGVEL----AAALAKLG--KEVTLIEALDrLLRAFDEEISAALEKALEKNGVEVRLGTsvkEIIGDGDGv 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499858144 227 RIHLEGGRVIDSDFTVGAAGARAY-GWLETSGLQQHE-GALVISETLQTSDPDVFACGDCAHmayaPRPKAGVYAVRQA 303
Cdd:pfam07992 227 EVILKDGTEIDADLVVVAIGRRPNtELLEAAGLELDErGGIVVDEYLRTSVPGIYAAGDCRV----GGPELAQNAVAQG 301
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
430-538 |
2.32e-15 |
|
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: 72.09 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 430 DDAAQlmtgsatqVISTD-HLRAFTEDPVVMTA-IAAQHALNDIWAMGAHPQAATVTLILPRqsADLQERLLAEIMHSAH 507
Cdd:pfam00586 1 DDAAV--------AVTTDgHGTPSLVDPYHFPGaKAVAGNLSDIAAMGARPLAFLDSLALPG--GPEVEWVLEEIVEGIA 70
|
90 100 110
....*....|....*....|....*....|....
gi 499858144 508 QEMTAAGAAIVGGHTSLGEE---LTIGFTLTGLC 538
Cdd:pfam00586 71 EACREAGVPLVGGDTSFDPEggkPTISVTAVGIV 104
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
149-285 |
8.26e-13 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 70.72 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 149 SDPARIACIGGGVAGVELILAMAHALRQqqrlaqATLIDSGSVL--SVLTSQSQTRLRKALDANGVRIL---QQTRIDHL 223
Cdd:PRK04965 139 RDAQRVLVVGGGLIGTELAMDLCRAGKA------VTLVDNAASLlaSLMPPEVSSRLQHRLTEMGVHLLlksQLQGLEKT 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499858144 224 SAG-RIHLEGGRVIDSDFTVGAAGARAYGWLET-SGLQQHEGALVISeTLQTSDPDVFACGDCA 285
Cdd:PRK04965 213 DSGiRATLDSGRSIEVDAVIAAAGLRPNTALARrAGLAVNRGIVVDS-YLQTSAPDIYALGDCA 275
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Nterm_to_SelD |
TIGR03169 |
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family ... |
11-368 |
0e+00 |
|
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown.
Pssm-ID: 274465 Cd Length: 364 Bit Score: 553.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 11 DLVLVGGGHTHALLLRMWGMKPLPGVRLTLINPGPTAPYSGMLPGFVAGHYTRDALDIDLVKLARFAGARLILGAAEEID 90
Cdd:TIGR03169 1 DLVLIGGGHSHALVLRMWGMKPLPGVRLTLINPGPTTPYSGMLPGHVAGHYTRDELHIDLVRLARFAGARLILDRAIGLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 91 PISKRITVPGRPAIAYDVASIDIGITSAMPELVGFDDFAIPAKPLGRFATRWDAFRNGSD---PARIACIGGGVAGVELI 167
Cdd:TIGR03169 81 LAAKQVICAGRPPIAYDVLSIDIGSTPALPDVPGFAEHAIPAKPLGQFAQRWQRFLERAKpqqPPRIAVIGGGAAGVELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 168 LAMAHALRQQQRLAQATLIDSGSVL-SVLTSQSQTRLRKALDANGVRILQQTRIDHLSAGRIHLEGGRVIDSDFTVGAAG 246
Cdd:TIGR03169 161 LAMAHRLRQLGRNAEVTLIDRGNVLlPGHNARVRRRLERALQERGVTLHLGATVAEVTADAVRLEDGQTLPADFTFWATG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 247 ARAYGWLETSGLQQHE-GALVISETLQT-SDPDVFACGDCAHMAYAPRPKAGVYAVRQAPVLYHNLKAVLGGGSLKSYQP 324
Cdd:TIGR03169 241 ARPPGWLAESGLALDEdGFIRVGPTLQSlSHPDIFAAGDCAHLVHAPRPKAGVFAVRQAPVLAENLRAALTGGPLRPYRP 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499858144 325 QKDYLKLISMGDKSALADRDGRSFAGGLLWRWKDHIDRKFMGKF 368
Cdd:TIGR03169 321 QSDYLKLISTGDKSAVASRGGLAFSGAWLWRWKDRIDRKFMDKF 364
|
|
| SelD |
COG0709 |
Selenophosphate synthase [Amino acid transport and metabolism]; |
387-719 |
9.33e-111 |
|
Selenophosphate synthase [Amino acid transport and metabolism];
Pssm-ID: 440473 [Multi-domain] Cd Length: 346 Bit Score: 338.97 E-value: 9.33e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 387 MEAV-LGSKPMCGGCGSKVGRHALHAGLGAFSGAQRADVTPL--PGDDAAQLMTGSAT-QVISTDHLRAFTEDPVVMTAI 462
Cdd:COG0709 2 MEEIrLTQLSHGGGCGAKIGPGVLAQILAGLPPPSDPNLLVGleTSDDAAVYRLGDDQaLVQTTDFFTPIVDDPYDFGRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 463 AAQHALNDIWAMGAHPQAATVTLILPRqsADLQERLLAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCETP- 541
Cdd:COG0709 82 AAANALSDVYAMGGRPLTALAIVGFPI--DKLPEEVLAEILAGGADKCREAGAPLAGGHSIDDPEPKYGLAVTGLVHPDk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 542 PLTLAGAQAGDHLILTKPIGSGTLMAAEMSGTAPGACVAEALDLMCQSQRDAATVLRPV-AHAMTDVTGFGLLGHLQGLC 620
Cdd:COG0709 160 VLRNAGARPGDVLILTKPLGTGILTTAIKAGLADGEDIAAAIASMTTLNKAAAELARLYgVHACTDVTGFGLLGHLLEMA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 621 AASDLGAEVDFDAIPLMAGAAALAEAGVRSTIFEDNAALLPGIGTAGA------RALLFDPQTSGGLLASVDPARASDAL 694
Cdd:COG0709 240 RGSGVSAEIDLDAVPLLPGALELAEQGIVPGGTYRNRASYGAKVEFAEgldeaqRDLLFDPQTSGGLLIAVPPEAAEELL 319
|
330 340
....*....|....*....|....*
gi 499858144 695 RELKNHGYHAAKIGEIRDADQGIVI 719
Cdd:COG0709 320 AALRAAGYAAAIIGEVTAGEGGAIE 344
|
|
| selD |
TIGR00476 |
selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino ... |
391-690 |
4.18e-108 |
|
selenium donor protein; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelD, known as selenophosphate synthetase, selenium donor protein, and selenide,water dikinase. SelD provides reduced selenium for the selenium transferase SelA. This protein itself contains selenocysteine in many species; any sequence scoring well but not aligning to the beginning of the model is likely to have a selenocysteine residue incorrectly interpreted as a stop codon upstream of the given sequence. The SelD protein also provides selenophosphate for the enzyme tRNA 2-selenouridine synthase, which catalyzes a tRNA base modification. It also contributes to selenium incorporation by selenium-dependent molybdenum hydroxylases (SDMH), in genomes with the marker TIGR03309. All genomes with SelD should make selenocysteine, selenouridine, SDMH, or some combination.
Pssm-ID: 273100 [Multi-domain] Cd Length: 301 Bit Score: 330.61 E-value: 4.18e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 391 LGSKPMCGGCGSKVGRHALHAGLGAFSGA--QRADVTPLPGDDAAQL-MTGSATQVISTDHLRAFTEDPVVMTAIAAQHA 467
Cdd:TIGR00476 2 LTEYSHGGGCGCKIGPGVLDKILASLPAApdPNLLVGNDTGDDAAVYkLNDGLALVSTTDFFTPIVDDPYDFGRIAATNA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 468 LNDIWAMGAHPQAATVTLILPRQSadLQERLLAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCETPPLTL-A 546
Cdd:TIGR00476 82 LSDIYAMGGTPLTALAILGWPRNK--LPPEVLREILAGGADVCAEAGAPLAGGHSIDDPEPKYGLAVTGLVHPDKLKRnD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 547 GAQAGDHLILTKPIGSGTLMAAEMSGTAPGACVAEALDLMCQ--SQRDAATVLRPVaHAMTDVTGFGLLGHLQGLCAASD 624
Cdd:TIGR00476 160 GAQPGDVLILTKPLGVGVLTAALKKGGLAEEAYAAAIASMTTlnKQAAELAALAGV-HAMTDVTGFGLLGHLLEMCRGSG 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499858144 625 LGAEVDFDAIPLMagaaalAEAGVRSTIFEDNAALLPGIGTAGA---RALLFDPQTSGGLLASVDPARA 690
Cdd:TIGR00476 239 VSAEIDFDAVPLL------AEQGCVPGGTGRNFASYGEKVPEPAgeqRDLLCDPQTSGGLLIAVAPEAA 301
|
|
| SelD |
cd02195 |
Selenophosphate synthetase (SelD) catalyzes the conversion of selenium to selenophosphate ... |
391-710 |
1.00e-100 |
|
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: 310.99 E-value: 1.00e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 391 LGSKPMCGGCGSKVGRHALHAGLGAFSGAQR--ADVTPLPGDDAAQL-MTGSATQVISTDHLRAFTEDPVVMTAIAAQHA 467
Cdd:cd02195 1 LTSFMKCAGCGAKVGPGVLSQLLAGLPLPTDpnLLVGLGTGDDAAVYrLPGGLALVQTTDFFPPIVDDPYLFGRIAAANA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 468 LNDIWAMGAHPQAATVTLILPRQSADLQERLLAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCETPPLTL-A 546
Cdd:cd02195 81 LSDIYAMGAKPLSALAIVTLPRKLPALQEEVLREILAGGKDKLREAGAVLVGGHTIEGPEPKYGLSVTGLVHPNKILRnS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 547 GAQAGDHLILTKPIGSGTLMAAEMSGTAPGACVAEALDLMCQSQRDAATVLR-PVAHAMTDVTGFGLLGHLQGLCAASDL 625
Cdd:cd02195 161 GAKPGDVLILTKPLGTGILFAAEMAGLARGEDIDAALESMARLNRAAAELLRkYGAHACTDVTGFGLLGHLLEMARASGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 626 GAEVDFDAIPLMagaaalaeagvrstifednaallpgigtagarallfdpQTSGGLLASVDPARASDALRELKNHGYHAA 705
Cdd:cd02195 241 SAEIDLDKLPLL--------------------------------------QTSGGLLAAVPPEDAAALLALLKAGGPPAA 282
|
....*
gi 499858144 706 KIGEI 710
Cdd:cd02195 283 IIGEV 287
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
9-368 |
2.09e-93 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 295.50 E-value: 2.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 9 TRDLVLVGGGHTHALLLRMWGMKPLPGVRLTLINPGPTAPYSGMLPGFVAGHYTRDALDIDLVKLARFAGARLILGAAEE 88
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 89 IDPISKRITVPGRPAIAYDVASIDIGITSAMPELVGFDDFAIPAKPLGRFATRWDAFRN------GSDPARIACIGGGVA 162
Cdd:COG1252 81 IDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAaferaeRRRLLTIVVVGGGPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 163 GVELILAMAHALRQQQRL-------AQATLIDSGS-VLSVLTSQSQTRLRKALDANGVRILQQTRIDHLSAGRIHLEGGR 234
Cdd:COG1252 161 GVELAGELAELLRKLLRYpgidpdkVRITLVEAGPrILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 235 VIDSDFTVGAAGARAYGWLETSGLQQ-HEGALVISETLQT-SDPDVFACGDCAHMAYA---PRPKAGVYAVRQAPVLYHN 309
Cdd:COG1252 241 EIPADTVIWAAGVKAPPLLADLGLPTdRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDPdgkPVPKTAQAAVQQAKVLAKN 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 499858144 310 LKAVLGGGSLKSYQPQkDYLKLISMGDKSALADRDGRSFAGGLLWRWKDHIDRKFMGKF 368
Cdd:COG1252 321 IAALLRGKPLKPFRYR-DKGCLASLGRGAAVADVGGLKLSGFLAWLLKRAIHLYFLPGF 378
|
|
| PRK00943 |
PRK00943 |
selenide, water dikinase SelD; |
398-716 |
2.02e-44 |
|
selenide, water dikinase SelD;
Pssm-ID: 234870 [Multi-domain] Cd Length: 347 Bit Score: 163.10 E-value: 2.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 398 GGCGSKVGRHALHAGLgAFSGAQRADVTPLPG----DDAAQLMTGSATQVIST-DHLRAFTEDPVVMTAIAAQHALNDIW 472
Cdd:PRK00943 15 AGCGCKISPKVLETIL-ASEQAKFVDPNLLVGnetrDDAAVYDLNDGTGIISTtDFFMPIVDDPFDFGRIAATNAISDIY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 473 AMGAHPQAATVTL-----ILPRQSAdlqerllAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCETPPL-TLA 546
Cdd:PRK00943 94 AMGGKPIMAIAILgwpinKLPPEVA-------REVLEGGRAACRQAGIPLAGGHSIDAPEPIFGLAVTGVVPPERVkRNA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 547 GAQAGDHLILTKPIGSGTLMAAEMSGTAPGACVAEALDLMCQSQRDAATVLR-PVAHAMTDVTGFGLLGHLQGLCAASDL 625
Cdd:PRK00943 167 TAQAGDKLFLTKPLGIGILTTAEKKSKLKPEHYGLAIEAMCQLNRPGADFAKlPGVHAMTDVTGFGLLGHLLEMCQGAGL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 626 GAEVDFDAIPLMAGAAALAEAGV------RStiFEDNAALLPGIgTAGARALLFDPQTSGGLLASVDPARASDALRELKN 699
Cdd:PRK00943 247 TARVDYAAVPLLPGVEEYIAQGCvpggtgRN--FASYGHLIGEL-PDEQRALLCDPQTSGGLLVAVAPEAEAEVLAIAAE 323
|
330
....*....|....*..
gi 499858144 700 HGYHAAKIGEIRDADQG 716
Cdd:PRK00943 324 HGIELAAIGELVEARGG 340
|
|
| PRK14105 |
PRK14105 |
selenide, water dikinase SelD; |
429-720 |
1.47e-32 |
|
selenide, water dikinase SelD;
Pssm-ID: 237611 [Multi-domain] Cd Length: 345 Bit Score: 129.12 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 429 GDDAAQLMTGSATQVISTDHLRAFTEDPVVMTAIAAQHALNDIWAMGAHP-QAATVTLILPRQsadLQERLLAEIMHSAH 507
Cdd:PRK14105 47 GDDAAVIIKNGLAIVKTVDVFTPIVDDPYIQGKIAACNSTSDVYAMGLSEiIGVLVILGIPPE---LPIEVAKEMLQGFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 508 QEMTAAGAAIVGGHTSLGEELTIGFTLTGLC-ETPPLTLAGAQAGDHLILTKPIGSGTLMAA-----------EMSGTAP 575
Cdd:PRK14105 124 DFCRENDTTIIGGHTILNPWPLIGGAVTGVGkEEDILTKAGAKEGDVLILTKPLGTQSAMALsrvpeefedliDITKEEK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 576 GACVAEALDLMCQSQRDAATVLR--------PVAHAMTDVTGFGLLGHLQGLCAASDLgaEVDFDAIPLMAGAAALaeag 647
Cdd:PRK14105 204 EYIINKAIELMTTSNRYALLALReaeeevgeKIANAMTDVTGFGILGHSQEMAEQSNV--EIEISTLPVIKGTPEL---- 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499858144 648 vrSTIFedNAALLPGIGTagarallfdpQTSGGLLASVDPARASDALRELKNHGYHAAKIGEIRDADQGIVIR 720
Cdd:PRK14105 278 --SSLF--GHALLDGYGA----------ETAGGLLISVKPEYKDKLIDKLEKNNVYAFEVGKVVKNGVGKAKL 336
|
|
| HypE |
COG0309 |
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, ... |
427-719 |
2.11e-32 |
|
Carbamoyl dehydratase HypE (hydrogenase maturation factor) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440078 [Multi-domain] Cd Length: 328 Bit Score: 128.27 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 427 LPGDDAAQLMTGSATQVISTDhlrAFTEDPVVMTA-----IAAQHALNDIWAMGAHPQAATVTLILPrqsADLQERLLAE 501
Cdd:COG0309 28 VGGEDAAVLDLGGGRLAFTTD---SFVVSPIFFPGgdigkLAVHGTVNDLAVSGAKPLYLSVSLILE---EGFPLEDLER 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 502 IMHSAHQEMTAAGAAIVGGHT-----SLGEELTIGFTLTGLCETP-PLTLAGAQAGDHLILTKPIG-SGT-LMAAEmsgt 573
Cdd:COG0309 102 IVESMAEAAREAGVSIVTGDTkvverGGVDGPFINTTGIGVVPKGrLISPSGARPGDKIIVTGGIGdHGTaILAAR---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 574 apgacvaEALDLMCQSQRDAATVLRPVA----------HAMTDVTGFGLLGHLQGLCAASDLGAEVDFDAIPlmagaaal 643
Cdd:COG0309 178 -------EGLELEGELLSDAAPLNDLVSvlleaapggvHAMRDPTRGGLAGALNEIAEASGVGIEIDEDAIP-------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 644 aeagVRStifednaallpgiGTAGARALL-FDPQT---SGGLLASVDPARASDALRELKNHGYHAAKIGEIRDADQGIVI 719
Cdd:COG0309 243 ----VRP-------------EVRGICELLgLDPLYlanEGKLVAVVPPEDAEAVLEALRAHGIDAAIIGEVTEGPPGRVV 305
|
|
| ThiL |
COG0611 |
Thiamine monophosphate kinase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
413-720 |
4.12e-28 |
|
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: 115.63 E-value: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 413 LGAFSGAQRADVTPLPGDDAAQLMTGSATQVISTD------HLRAFTEDP--VVMTAIAAqhALNDIWAMGAHPQAATVT 484
Cdd:COG0611 10 LFKRLALRGPDVLLGIGDDAAVLDPPGGRLVVTTDmlvegvHFPLDWMSPedLGWKAVAV--NLSDLAAMGARPLAALLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 485 LILPRqsaDLQERLLAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCET-PPLTLAGAQAGDHLILTKPIGSG 563
Cdd:COG0611 88 LALPP---DTDVEWLEEFARGLAEAADRYGVDLVGGDTTRSPELTISVTAIGEVPGgRPLLRSGARPGDLVYVTGTLGDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 564 T--LMAAEMSGTAPGACVAEALDLMC--QSQRDAATVLR--PVAHAMTDVTGfGLLGHLQGLCAASDLGAEVDFDAIPLm 637
Cdd:COG0611 165 AagLALLLRGLRVPLEAREYLLERHLrpEPRLALGRALAeaGLATAMIDISD-GLAADLGHIAEASGVGAEIDLDALPL- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 638 agaaalaEAGVRSTIFEDNAALLpgigtagarALlfdpqtSGG----LLASVDPARASDALRELKNHGYHaaKIGEIRdA 713
Cdd:COG0611 243 -------SPALREAALGLDPLEL---------AL------TGGedyeLLFTVPPEALEALEAAALGVPLT--VIGRVT-E 297
|
....*..
gi 499858144 714 DQGIVIR 720
Cdd:COG0611 298 GEGVTLD 304
|
|
| PurM-like1 |
cd06061 |
AIR synthase (PurM) related protein, subgroup 1 of unknown function. The family of PurM ... |
403-710 |
3.11e-27 |
|
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: 112.30 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 403 KVGRHALHAGLGAFSGAQRADVTPLP--GDDAAQLMTGSATQVISTDHLRAFTEDPVVmtaIAAQHALNDIWAMGAHPQA 480
Cdd:cd06061 4 KLPPEFLKRLILKNLGADRDEVLVGPggGEDAAVVDFGGKVLVVSTDPITGAGKDAGW---LAVHIAANDIATSGARPRW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 481 ATVTLILPRQSAdlqERLLAEIMHSAHQEMTAAGAAIVGGHTSLGEELT---IGFTLTGlcETPP---LTLAGAQAGDHL 554
Cdd:cd06061 81 LLVTLLLPPGTD---EEELKAIMREINEAAKELGVSIVGGHTEVTPGVTrpiISVTAIG--KGEKdklVTPSGAKPGDDI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 555 ILTKPIG-SGTLMAA-----EMSGTAPGACVAEA--LDLMCQSQRDAATVLRPVAHAMTDVTGFGLLGHLQGLCAASDLG 626
Cdd:cd06061 156 VMTKGAGiEGTAILAndfeeELKKRLSEEELREAakLFYKISVVKEALIAAEAGVTAMHDATEGGILGALWEVAEASGVG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 627 AEVDFDAIPLMagaaalaeagvRSTIfednaallpgigtAGARALLFDPQT---SGGLLASVDPARASDALRELKNHGYH 703
Cdd:cd06061 236 LRIEKDKIPIR-----------QETK-------------EICEALGIDPLRlisSGTLLITVPPEKGDELVDALEEAGIP 291
|
....*..
gi 499858144 704 AAKIGEI 710
Cdd:cd06061 292 ASVIGKI 298
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
34-310 |
1.24e-24 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 105.28 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 34 PGVRLTLINPGPTAPYSG-MLPGFVAG-HYTRDALDIDLVKLARFAGARLILGA-AEEIDPISKRITV-PGRpAIAYD-- 107
Cdd:COG0446 4 PDAEITVIEKGPHHSYQPcGLPYYVGGgIKDPEDLLVRTPESFERKGIDVRTGTeVTAIDPEAKTVTLrDGE-TLSYDkl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 108 -VASidiGITSAMPELVGFDDFAIPakPLGRF--ATRWDAFRNGSDPARIACIGGGVAGVElilaMAHALRQQQRlaQAT 184
Cdd:COG0446 83 vLAT---GARPRPPPIPGLDLPGVF--TLRTLddADALREALKEFKGKRAVVIGGGPIGLE----LAEALRKRGL--KVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 185 LIDSGS-VLSVLTSQSQTRLRKALDANGVRILQQTRIDHLSAG---RIHLEGGRVIDSDFTVGAAGARA-YGWLETSGLQ 259
Cdd:COG0446 152 LVERAPrLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDdkvAVTLTDGEEIPADLVVVAPGVRPnTELAKDAGLA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 499858144 260 QHE-GALVISETLQTSDPDVFACGDCAHMAYAPRPKA-----GVYAVRQAPVLYHNL 310
Cdd:COG0446 232 LGErGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTvyiplASAANKQGRVAAENI 288
|
|
| ThiL |
cd02194 |
ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage ... |
419-711 |
4.41e-24 |
|
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: 103.02 E-value: 4.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 419 AQRADVTPLPGDDAAQLMTGSATQVISTDhlrAFTED---PVVMT-------AIAAqhALNDIWAMGAHPQAATVTLILP 488
Cdd:cd02194 14 GAGPGVLLGIGDDAAVLKPPGGRLVVTTD---TLVEGvhfPPDTTpedigwkALAV--NLSDLAAMGARPLGFLLSLGLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 489 RqsaDLQERLLAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCE-TPPLTLAGAQAGDHLILTKPIGSGT--L 565
Cdd:cd02194 89 P---DTDEEWLEEFYRGLAEAADRYGVPLVGGDTTSGSELVISVTALGEVEkGKPLRRSGAKPGDLLYVTGTLGDAAagL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 566 MAAEMSGTAPGACVAEALD--LMCQSQRDAATVLR-PVAHAMTDVTGfGLLGHLQGLCAASDLGAEVDFDAIPLmagaaa 642
Cdd:cd02194 166 ALLLGGLKLPEELYEELIErhLRPEPRLELGRALAeGLATAMIDISD-GLLADLGHIAEASGVGAVIDLDKLPL------ 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499858144 643 laEAGVRSTIFEDNaallpgigtagARALLFdpqtSGG----LLASVDParaSDALRELKNHGYHAAKIGEIR 711
Cdd:cd02194 239 --SPALRAAELGED-----------ALELAL----SGGedyeLLFTVPP---ENAEAAAAKLGVPVTVIGRVT 291
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
9-336 |
4.57e-24 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 105.22 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 9 TRDLVLVGGGHT-HALL--LRMWGmkplPGVRLTLINPGPTAPYSG-MLPGFVAGHYTRDALDIDLVKLARFAGARLILG 84
Cdd:COG1251 1 KMRIVIIGAGMAgVRAAeeLRKLD----PDGEITVIGAEPHPPYNRpPLSKVLAGETDEEDLLLRPADFYEENGIDLRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 85 A-AEEIDPISKRITVPGRPAIAYDVASIDIGITSAMPELVGFDdfaipaKPlGRFATR----WDAFRNGSDPA-RIACIG 158
Cdd:COG1251 77 TrVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGAD------LP-GVFTLRtlddADALRAALAPGkRVVVIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 159 GGVAGVELilamAHALRQQQrlAQATLIDSGSVL--SVLTSQSQTRLRKALDANGVRILQQTRIDHL----SAGRIHLEG 232
Cdd:COG1251 150 GGLIGLEA----AAALRKRG--LEVTVVERAPRLlpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIegddRVTGVRLAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 233 GRVIDSDFTVGAAGAR-AYGWLETSGLQqHEGALVISETLQTSDPDVFACGDCA---HMAYAPRPKAGVY-AVRQAPVLY 307
Cdd:COG1251 224 GEELPADLVVVAIGVRpNTELARAAGLA-VDRGIVVDDYLRTSDPDIYAAGDCAehpGPVYGRRVLELVApAYEQARVAA 302
|
330 340 350
....*....|....*....|....*....|....*.
gi 499858144 308 HNLkavLGGGslKSYQPQKDY-------LKLISMGD 336
Cdd:COG1251 303 ANL---AGGP--AAYEGSVPStklkvfgVDVASAGD 333
|
|
| PRK05731 |
PRK05731 |
thiamine monophosphate kinase; Provisional |
428-712 |
2.10e-22 |
|
thiamine monophosphate kinase; Provisional
Pssm-ID: 235583 [Multi-domain] Cd Length: 318 Bit Score: 98.75 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 428 PGDDAAqLMTGSATQ--VISTDhlrAFTED----PVVMT-------AIAAqhALNDIWAMGAHPQAATVTLILPRqsaDL 494
Cdd:PRK05731 24 IGDDAA-LLGPPPGQrlVVSTD---MLVEGvhfrPDWSSpedlgykALAV--NLSDLAAMGARPAAFLLALALPK---DL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 495 QERLLAEIMHSAHQEMTAAGAAIVGGHTSLGEELTIGFTLTGLCE-TPPLTLAGAQAGDHLILTKPIGSGtlmAAE---- 569
Cdd:PRK05731 95 DEAWLEALADGLFELADRYGAELIGGDTTRGPDLSISVTAIGDVPgGRALRRSGAKPGDLVAVTGTLGDS---AAGlall 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 570 MSGTAPGACVAEALD---LMCQSQRDAATVLRPVAHAMTDVTGfGLLGHLQGLCAASDLGAEVDFDAIPLMagaaalaea 646
Cdd:PRK05731 172 LNGLRVPDADAAALIsrhLRPQPRVGLGQALAGLASAAIDISD-GLAADLGHIAEASGVGADIDLDALPIS--------- 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499858144 647 gvrstifednAALLPGIGTAGAR--ALlfdpqtSGG----LLASVDPARASDALRELKNHGYHAAKIGEIRD 712
Cdd:PRK05731 242 ----------PALREAAEGEDALrwAL------SGGedyeLLFTFPPENRGALLAAAGHLGVGVTIIGRVTE 297
|
|
| PurM-like |
cd00396 |
AIR (aminoimidazole ribonucleotide) synthase related protein. This family includes Hydrogen ... |
461-709 |
1.05e-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: 91.30 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 461 AIAAQHALNDIWAMGAHPQAATVTLILPRqsaDLQERLLAEIMHSAHQEMTAAGAAIVGGHTS-----LGEELTIGFTLT 535
Cdd:cd00396 22 RLAVGGAVNDIAAMGARPIALLASLSLSN---GLEVDILEDVVDGVAEACNQLGVPIVGGHTSvspgtMGHKLSLAVFAI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 536 GLCETPPLTLA-GAQAGDHLILTKpigsgtLMAAEmsgtapgACVAEALdlmcqsqrdaatvlrpvAHAMTDVTGFGLLG 614
Cdd:cd00396 99 GVVEKDRVIDSsGARPGDVLILTG------VDAVL-------ELVAAGD-----------------VHAMHDITDGGLLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 615 HLQGLCAASDLGAEVDFDAIPLMagaaalaeAGVRSTIFEDnaallpgigtagaRALLFDPQTSGGLLASVDPARASDAL 694
Cdd:cd00396 149 TLPELAQASGVGAEIDLEAIPLD--------EVVRWLCVEH-------------IEEALLFNSSGGLLIAVPAEEADAVL 207
|
250
....*....|....*
gi 499858144 695 RELKNHGYHAAKIGE 709
Cdd:cd00396 208 LLLNGNGIDAAVIGR 222
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
11-303 |
1.60e-20 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 92.77 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 11 DLVLVGGGH---THALLLRMWGMKplpgvrLTLINPGPTAPYSGMLP----------GFVAGHYTRDALDIDLVKLARFA 77
Cdd:pfam07992 2 DVVVIGGGPaglAAALTLAQLGGK------VTLIEDEGTCPYGGCVLskallgaaeaPEIASLWADLYKRKEEVVKKLNN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 78 GARLILGA-AEEIDPISKRITVPGRPA-----IAYDVASIDIGITSAMPELVGFDDFAIPakpLGRFATRWDAFRNGSDP 151
Cdd:pfam07992 76 GIEVLLGTeVVSIDPGAKKVVLEELVDgdgetITYDRLVIATGARPRLPPIPGVELNVGF---LVRTLDSAEALRLKLLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 152 ARIACIGGGVAGVELilamAHALRQQQrlAQATLIDSGS-VLSVLTSQSQTRLRKALDANGVRILQQT---RIDHLSAG- 226
Cdd:pfam07992 153 KRVVVVGGGYIGVEL----AAALAKLG--KEVTLIEALDrLLRAFDEEISAALEKALEKNGVEVRLGTsvkEIIGDGDGv 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499858144 227 RIHLEGGRVIDSDFTVGAAGARAY-GWLETSGLQQHE-GALVISETLQTSDPDVFACGDCAHmayaPRPKAGVYAVRQA 303
Cdd:pfam07992 227 EVILKDGTEIDADLVVVAIGRRPNtELLEAAGLELDErGGIVVDEYLRTSVPGIYAAGDCRV----GGPELAQNAVAQG 301
|
|
| AIRS |
pfam00586 |
AIR synthase related protein, N-terminal domain; This family includes Hydrogen expression ... |
430-538 |
2.32e-15 |
|
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: 72.09 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 430 DDAAQlmtgsatqVISTD-HLRAFTEDPVVMTA-IAAQHALNDIWAMGAHPQAATVTLILPRqsADLQERLLAEIMHSAH 507
Cdd:pfam00586 1 DDAAV--------AVTTDgHGTPSLVDPYHFPGaKAVAGNLSDIAAMGARPLAFLDSLALPG--GPEVEWVLEEIVEGIA 70
|
90 100 110
....*....|....*....|....*....|....
gi 499858144 508 QEMTAAGAAIVGGHTSLGEE---LTIGFTLTGLC 538
Cdd:pfam00586 71 EACREAGVPLVGGDTSFDPEggkPTISVTAVGIV 104
|
|
| AIRS_C |
pfam02769 |
AIR synthase related protein, C-terminal domain; This family includes Hydrogen expression ... |
549-719 |
3.77e-15 |
|
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: 73.15 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 549 QAGDHLILTKPIG--SGTLMAAEMSGTAPG-ACVAEALDLMCQSQRDAATVL---RPVAHAMTDVTGFGLLGHLQGLCAA 622
Cdd:pfam02769 1 KPGDVLILLGSSGlhGAGLSLSRKGLEDSGlAAVQLGDPLLEPTLIYVKLLLaalGGLVKAMHDITGGGLAGALAEMAPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 623 SDLGAEVDFDAIPlmagaaalaeagvrstIFEdnaallpgigtagARALLFDP---QTSGGLLASVDPARASDALRELKN 699
Cdd:pfam02769 81 SGVGAEIDLDKVP----------------IFE-------------ELMLPLEMllsENQGRGLVVVAPEEAEAVLAILEK 131
|
170 180
....*....|....*....|
gi 499858144 700 HGYHAAKIGEIRDADQGIVI 719
Cdd:pfam02769 132 EGLEAAVIGEVTAGGRLTVI 151
|
|
| HypE |
cd02197 |
HypE (Hydrogenase expression/formation protein). HypE is involved in Ni-Fe hydrogenase ... |
429-710 |
6.41e-15 |
|
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: 75.95 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 429 GDDAAQLMTGSATQVISTDhlrAFTEDPVV-----MTAIAAQHALNDIWAMGAHPQAATVTLILprqsadlQERL----L 499
Cdd:cd02197 26 LEDAAALLVGGGRLAFTTD---SFVVSPLFfpggdIGKLAVCGTVNDLAMMGAKPLYLSLGFIL-------EEGFpledL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 500 AEIMHSAHQEMTAAGAAIVGGHTSLGEE-----LTIgfTLTGLCETPP---LTLAGAQAGDHLILTKPIG--SGTLMAAE 569
Cdd:cd02197 96 ERIVKSMAEAAREAGVKIVTGDTKVVPKgkadgIFI--NTTGIGVIPRgviISPSNIRPGDKIIVSGTIGdhGAAILAAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 570 msgtapgacvaEALDLMCQSQRDAATVLRPVA---------HAMTDVTGFGLLGHLQGLCAASDLGAEVDFDAIPlmaga 640
Cdd:cd02197 174 -----------EGLGFETDIESDCAPLNGLVEalleagpgiHAMRDPTRGGLAAVLNEIARASGVGIEIEEEAIP----- 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499858144 641 aalaeagVRStifednaallpgiGTAGARALL-FDPQT---SGGLLASVDPARASDALRELKNHGY--HAAKIGEI 710
Cdd:cd02197 238 -------VRE-------------EVRGACEMLgLDPLYlanEGKFVAIVPPEDAEEVLEALRSHPLgkEAAIIGEV 293
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
69-303 |
8.44e-14 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 74.35 E-value: 8.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 69 DLVKLARFAGARLILGAAEEIDPisKRITVPGRPAIAYDVASIDIGITSAMPELVGFDDfaipakplGRFATRWDAFRNG 148
Cdd:COG1249 96 GVEELLKKNGVDVIRGRARFVDP--HTVEVTGGETLTADHIVIATGSRPRVPPIPGLDE--------VRVLTSDEALELE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 149 SDPARIACIGGGVAGVElilaMAHALRqqqRL-AQATLIDSGS-VLSVLTSQSQTRLRKALDANGVRILQQTRIDHLSAG 226
Cdd:COG1249 166 ELPKSLVVIGGGYIGLE----FAQIFA---RLgSEVTLVERGDrLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 227 ----RIHLEGGR---VIDSDFTVGAAGARAY----GwLETSGLQQHE-GALVISETLQTSDPDVFACGDC------AHMA 288
Cdd:COG1249 239 gdgvTVTLEDGGgeeAVEADKVLVATGRRPNtdglG-LEAAGVELDErGGIKVDEYLRTSVPGIYAIGDVtggpqlAHVA 317
|
250
....*....|....*
gi 499858144 289 YAprpkAGVYAVRQA 303
Cdd:COG1249 318 SA----EGRVAAENI 328
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
149-285 |
8.26e-13 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 70.72 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 149 SDPARIACIGGGVAGVELILAMAHALRQqqrlaqATLIDSGSVL--SVLTSQSQTRLRKALDANGVRIL---QQTRIDHL 223
Cdd:PRK04965 139 RDAQRVLVVGGGLIGTELAMDLCRAGKA------VTLVDNAASLlaSLMPPEVSSRLQHRLTEMGVHLLlksQLQGLEKT 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499858144 224 SAG-RIHLEGGRVIDSDFTVGAAGARAYGWLET-SGLQQHEGALVISeTLQTSDPDVFACGDCA 285
Cdd:PRK04965 213 DSGiRATLDSGRSIEVDAVIAAAGLRPNTALARrAGLAVNRGIVVDS-YLQTSAPDIYALGDCA 275
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
12-285 |
4.49e-09 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 59.84 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 12 LVLVGGGHT-----HALLLRMWGMkplpgVRLTLINPGPTAPYSGM-LPGFVAGHYTRDALDIDLVKLARFAGARLILGA 85
Cdd:TIGR02374 1 LVLVGNGMAghrciEEVLKLNRHM-----FEITIFGEEPHPNYNRIlLSSVLQGEADLDDITLNSKDWYEKHGITLYTGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 86 -AEEIDPISKRITVPGRPAIAYDVASIDIGITSAMPELVGFDdfaIPAKPLGRFATRWDAFRNGSDPA-RIACIGGGVAG 163
Cdd:TIGR02374 76 tVIQIDTDQKQVITDAGRTLSYDKLILATGSYPFILPIPGAD---KKGVYVFRTIEDLDAIMAMAQRFkKAAVIGGGLLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 164 VELILAM------AHALRQQQRLAQATLIDSGSVLsvltsqsqtrLRKALDANGVRILQQTR----IDHLSAGRIHLEGG 233
Cdd:TIGR02374 153 LEAAVGLqnlgmdVSVIHHAPGLMAKQLDQTAGRL----------LQRELEQKGLTFLLEKDtveiVGATKADRIRFKDG 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499858144 234 RVIDSDFTVGAAGARAYGWLETSGLQQHEGALVISETLQTSDPDVFACGDCA 285
Cdd:TIGR02374 223 SSLEADLIVMAAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECA 274
|
|
| PurM-like3 |
cd02192 |
AIR synthase (PurM) related protein, subgroup 3 of unknown function. The family of PurM ... |
468-635 |
1.22e-08 |
|
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: 56.84 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 468 LNDIWAMGAHPQAatVTLILPRQSADLQERLLAEIMHSAHqemtAAGAAIVGGHTSLGEELT-IGFTLTGLCETPPLTLA 546
Cdd:cd02192 76 VSDIAAMGGRPLA--MVDALWSPSAEAAAQVLEGMRDAAE----KFGVPIVGGHTHPDSPYNaLSVAILGRARKDLLISF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 547 GAQAGDHLILT-----KPIGSGTLM--AAEMsgtAPGACVAEALDLMcqsqrdAATVLRPVAHAMTDVTGFGLLGHLQGL 619
Cdd:cd02192 150 GAKPGDRLILAidldgRVHPSPPPNwdATTM---KSPALLRRQIALL------PELAERGLVHAAKDISNPGIIGTLGML 220
|
170
....*....|....*.
gi 499858144 620 CAASDLGAEVDFDAIP 635
Cdd:cd02192 221 LEASGVGAEIDLDAIP 236
|
|
| COG2144 |
COG2144 |
Selenophosphate synthetase-related protein [General function prediction only]; |
415-712 |
1.74e-08 |
|
Selenophosphate synthetase-related protein [General function prediction only];
Pssm-ID: 441747 [Multi-domain] Cd Length: 323 Bit Score: 56.71 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 415 AFSGAQRADVTPLPGDDAAQLMTGSATQVISTDH-LRAFTE-DP------VVMTAIaaqhalNDIWAMGAHPQAatVTLI 486
Cdd:COG2144 29 ALGLASSGGTAAAFGDDAAAIPDGDGYLLLAAEGiWPKFVEaDPwfagycSVLVNV------SDIAAMGGRPLA--VVDA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 487 LPRQSADLQERLLaeimhsahQEMTAAGAA----IVGGHTSLG-EELTIGFTLTGLCETpPLTLAGAQAGDHLIltkpig 561
Cdd:COG2144 101 LWSSDEEAAAPVL--------AGMRAASRKfgvpIVGGHTHPDtPYNALAVAILGRAKK-LLTSFTARPGDRLI------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 562 sgtlMAAEMSG-------------TAPGACVAEALDLMcqsQRDAATVLrpvAHAMTDVTGFGLLGHLQGLCAASDLGAE 628
Cdd:COG2144 166 ----AAIDLDGryhppfpywdattGKPPERLRAQLELL---PELAEAGL---VTAAKDISNPGIIGTLGMLLECSGVGAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 629 VDFDAIPLmagaaalaeagvrstifEDNAALLpgigtagaRALLFDPqtSGGLLASVDPARASDALRELKNHGYHAAKIG 708
Cdd:COG2144 236 IDLDAIPR-----------------PEGVDLE--------RWLKAFP--SFGFLLTVPPENVDEVLARFAARGITAAVIG 288
|
....
gi 499858144 709 EIRD 712
Cdd:COG2144 289 EVTD 292
|
|
| PurM-like2 |
cd02691 |
AIR synthase (PurM) related protein, archaeal subgroup 2 of unknown function. The family of ... |
398-614 |
3.20e-08 |
|
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: 56.24 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 398 GGCGSK-VGRHALHAGLGAFSGAQRADVTPLPGDDAAQLMTGSATQVISTD--HLRaFTEDPVVMTAIAAQHALNDIWAM 474
Cdd:cd02691 4 FGVGSRgEGDFYVHEKLAELIGKTGEVSIVAQDDDAGVDAADVEYIVVAIDgiHSR-LSDFPFLAGFHATRAALRDVMVM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 475 GAHPQAATVTLILPRQSaDLQERLLAEIMHSAHQEMTaaGAAIVGGHT-------SLGEELTIGFTLTGLCETPPLTLAG 547
Cdd:cd02691 83 GARPVALLSDIHLADDG-DVGKLFDFTAGVTAVSEAT--GVPLVAGSTlriggdmVLGDRLVGGVGAVGRSKSDPSRRKN 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499858144 548 AQAGDHLILTKPIGSGTLMAAEMSGTAPGAcVAEALDL----MCQSQRDAAtvLRPVAHAMTDVTGFGLLG 614
Cdd:cd02691 160 AEPGDLILMTEGAGGGTITTTAIYHGMPDV-VEETLNVdfikACEALRDSG--LVSKVHSMTDVTNGGIRG 227
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
157-357 |
7.38e-08 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 55.54 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 157 IGGGVAGVELILAMAHALRQQQR--------LAQATLIDSGS-VLSVLTSQSQTRLRKALDANGVRILQQTRIDHLSAGR 227
Cdd:PTZ00318 179 VGGGPTGVEFAAELADFFRDDVRnlnpelveECKVTVLEAGSeVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 228 IHLEGGRVIDSDFTVGAAGARAYGWLETSGLQQ-HEGALVISETLQTSD-PDVFACGDCAHMAYAPRPKAGVYAVRQAPV 305
Cdd:PTZ00318 259 VVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKtSRGRISVDDHLRVKPiPNVFALGDCAANEERPLPTLAQVASQQGVY 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499858144 306 LYHNLKavlggGSLKSYQPQKDYL-----KLISMGDKSALADRDGRSFAGGL-LWRWK 357
Cdd:PTZ00318 339 LAKEFN-----NELKGKPMSKPFVyrslgSLAYLGNYSAIVQLGAFDLSGFKaLLFWR 391
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
153-285 |
1.86e-06 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 50.69 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 153 RIACIGGGVAGVELilamahALRQQQRLAQATLIDSGSvlSVLTSQSQTRLRKAL----DANGVRILQQTRIDHLSAGR- 227
Cdd:PRK09754 146 SVVIVGAGTIGLEL------AASATQRRCKVTVIELAA--TVMGRNAPPPVQRYLlqrhQQAGVRILLNNAIEHVVDGEk 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499858144 228 --IHLEGGRVIDSDFTVGAAGARAYGWLET-SGLQQHeGALVISETLQTSDPDVFACGDCA 285
Cdd:PRK09754 218 veLTLQSGETLQADVVIYGIGISANDQLAReANLDTA-NGIVIDEACRTCDPAIFAGGDVA 277
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
104-287 |
3.95e-05 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 47.07 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 104 IAYDVASIDIGITSAMPELVGFDDfaipaKPlgrFATRWDAFRNGSDPARIACIGGGVAGVELILAMAHALRQQQRLAQA 183
Cdd:PRK13748 231 VAFDRCLIATGASPAVPPIPGLKE-----TP---YWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARS 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 184 TLI--DSGSVLSVLTSqsqtrlrkALDANGVRILQQTRIDHLSagriHLEGGRVIDSDF-----------TVGAAGARAY 250
Cdd:PRK13748 303 TLFfrEDPAIGEAVTA--------AFRAEGIEVLEHTQASQVA----HVDGEFVLTTGHgelradkllvaTGRAPNTRSL 370
|
170 180 190
....*....|....*....|....*....|....*...
gi 499858144 251 GwLETSGLQ-QHEGALVISETLQTSDPDVFACGDCAHM 287
Cdd:PRK13748 371 A-LDAAGVTvNAQGAIVIDQGMRTSVPHIYAAGDCTDQ 407
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
151-310 |
5.51e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 46.32 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 151 PARIACIGGGVAGVELilamAHALRqqqRL-AQATLID-SGSVL----SVLTSQSQTRLRKALDAN-GVRILQQTRI-DH 222
Cdd:PRK06292 169 PKSLAVIGGGVIGLEL----GQALS---RLgVKVTVFErGDRILpledPEVSKQAQKILSKEFKIKlGAKVTSVEKSgDE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 223 LSAGRIHLEGGRVIDSDFTVGAAGARAY----GwLETSGLQQHE-GALVISETLQTSDPDVFACGDcahmAYAPRPKAGV 297
Cdd:PRK06292 242 KVEELEKGGKTETIEADYVLVATGRRPNtdglG-LENTGIELDErGRPVVDEHTQTSVPGIYAAGD----VNGKPPLLHE 316
|
170
....*....|...
gi 499858144 298 yAVRQAPVLYHNL 310
Cdd:PRK06292 317 -AADEGRIAAENA 328
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
153-285 |
2.07e-04 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 44.72 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 153 RIACIGGGVAGVElilaMAHALRQqqrLAQAT-LIDSGSVLSV--LTSQSQTRLRKALDANGVR---------ILQQtri 220
Cdd:PRK14989 147 RGAVVGGGLLGLE----AAGALKN---LGVEThVIEFAPMLMAeqLDQMGGEQLRRKIESMGVRvhtskntleIVQE--- 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499858144 221 DHLSAGRIHLEGGRVIDSDFTVGAAGARAYGWLET-SGLQQHE-GALVISETLQTSDPDVFACGDCA 285
Cdd:PRK14989 217 GVEARKTMRFADGSELEVDFIVFSTGIRPQDKLATqCGLAVAPrGGIVINDSCQTSDPDIYAIGECA 283
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
77-284 |
4.75e-04 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 43.22 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 77 AGARLILGAAEEIDPIS-----KRITVP-------GRPAIAyDVASIDIGITSampelvgfDDFaipakplgrFAtrWDA 144
Cdd:PRK06116 106 NGVDLIEGFARFVDAHTvevngERYTADhiliatgGRPSIP-DIPGAEYGITS--------DGF---------FA--LEE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 145 FrngsdPARIACIGGGVAGVEL--ILamaHALRqqqrlAQATLIDSG-SVLSVLTSQSQTRLRKALDANGVRILQQT--- 218
Cdd:PRK06116 166 L-----PKRVAVVGAGYIAVEFagVL---NGLG-----SETHLFVRGdAPLRGFDPDIRETLVEEMEKKGIRLHTNAvpk 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499858144 219 RIDHLSAGR--IHLEGGRVIDSDFTVGAAGARAY----GwLETSGLQQHE-GALVISETLQTSDPDVFACGDC 284
Cdd:PRK06116 233 AVEKNADGSltLTLEDGETLTVDCLIWAIGREPNtdglG-LENAGVKLNEkGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
153-285 |
5.73e-04 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 43.11 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 153 RIACIGGGVAGVELILAmAHALRQQQRLAQAtlidSGSVLSVLTSQSQTR-LRKALDANGVRIlqqtridHLSAGRIHLE 231
Cdd:PRK09564 151 NIVIIGAGFIGLEAVEA-AKHLGKNVRIIQL----EDRILPDSFDKEITDvMEEELRENGVEL-------HLNEFVKSLI 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499858144 232 G-GRV---------IDSDFTVGAAGAR-AYGWLETSGLQQHE-GALVISETLQTSDPDVFACGDCA 285
Cdd:PRK09564 219 GeDKVegvvtdkgeYEADVVIVATGVKpNTEFLEDTGLKTLKnGAIIVDEYGETSIENIYAAGDCA 284
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
150-283 |
6.46e-04 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 42.84 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 150 DPARIACIGGGVAGVEL--ILAmahALRqqqrlAQATLIDS-GSVLSVLTSQSQTRLRKALDANGVRILQQTRIDHLSAG 226
Cdd:PRK05249 174 LPRSLIIYGAGVIGCEYasIFA---ALG-----VKVTLINTrDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGG 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499858144 227 R----IHLEGGRVIDSD---FTVGAAGARAYGWLETSGLQ-QHEGALVISETLQTSDPDVFACGD 283
Cdd:PRK05249 246 DdgviVHLKSGKKIKADcllYANGRTGNTDGLNLENAGLEaDSRGQLKVNENYQTAVPHIYAVGD 310
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
151-313 |
1.66e-03 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 41.67 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 151 PARIACIGGGVAGVELILAMAhALRqqqrlAQATLIDSG-SVLSVLTSQSQTRLRKALDANGVRILQQTRIDHLSAG--- 226
Cdd:PRK06416 172 PKSLVVIGGGYIGVEFASAYA-SLG-----AEVTIVEALpRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQTddg 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 227 -RIHLEGG---RVIDSDF---TVGAAGARAYGWLETSGLQQHEGALVISETLQTSDPDVFACGDC------AHMAYAprp 293
Cdd:PRK06416 246 vTVTLEDGgkeETLEADYvlvAVGRRPNTENLGLEELGVKTDRGFIEVDEQLRTNVPNIYAIGDIvggpmlAHKASA--- 322
|
170 180
....*....|....*....|....*
gi 499858144 294 kAGVYAV-----RQAPVLYHNLKAV 313
Cdd:PRK06416 323 -EGIIAAeaiagNPHPIDYRGIPAV 346
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
153-220 |
3.09e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 37.18 E-value: 3.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 153 RIACIGGGVAGVElilaMAHALRqqqRLA-QATLID-SGSVLSVLTSQSQTRLRKALDANGVRILQQTRI 220
Cdd:pfam00070 1 RVVVVGGGYIGLE----LAGALA---RLGsKVTVVErRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
73-290 |
3.47e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 40.57 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 73 LARFAGARLILGAAEEIDPisKRITVPGRPAIAYDVAsIDIGITSAMPELVGFDDfaIPakplgrFATRWDAFRNGSDPA 152
Cdd:PRK06370 104 LRGLEGVDVFRGHARFESP--NTVRVGGETLRAKRIF-INTGARAAIPPIPGLDE--VG------YLTNETIFSLDELPE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499858144 153 RIACIGGGVAGVElilaMAHALRqqqRL-AQATLIDSGS-VLSVLTSQSQTRLRKALDANGVRILQQTRIDHLSA----G 226
Cdd:PRK06370 173 HLVIIGGGYIGLE----FAQMFR---RFgSEVTVIERGPrLLPREDEDVAAAVREILEREGIDVRLNAECIRVERdgdgI 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499858144 227 RIHLE---GGRVIDSDFTVGAAGAR----AYGwLETSGLQQHE-GALVISETLQTSDPDVFACGDC------AHMAYA 290
Cdd:PRK06370 246 AVGLDcngGAPEITGSHILVAVGRVpntdDLG-LEAAGVETDArGYIKVDDQLRTTNPGIYAAGDCngrgafTHTAYN 322
|
|
| |
