|
Name |
Accession |
Description |
Interval |
E-value |
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
16-315 |
2.32e-170 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 475.19 E-value: 2.32e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTTTDVENYPGFRNGITGPELMDEMREQALRFGADLRMEDVES 95
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 96 VSLHGPLKSVVTADGQTHRARAVILAMGAAARYLQVPGEQELLGRGVSSCATCDGFFFRDQDIAVIGGGDSAMEEATFLT 175
Cdd:TIGR01292 81 VDKSDRPFKVYTGDGKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 176 RFARSVTLVHRRDEFRASKIMLDRARNNDKIRFLTNHTVVAVDGDTTVTGLRVRDTNTGAETTLPVTGVFVAIGHEPRSG 255
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDNKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNTE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 256 LVREAIDVDPDGYVLVQGRtTSTSLPGVFAAGDLVDRTYRQAVTAAGSGCAAAIDAERWL 315
Cdd:TIGR01292 241 LLKGLLELDENGYIVTDEG-MRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
16-318 |
2.73e-164 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 459.97 E-value: 2.73e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTTTDVENYPGFRNGITGPELMDEMREQALRFGADLRMEDVES 95
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEEVTS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 96 VSLHGPLKSVVTADGQTHRARAVILAMGAAARYLQVPGEQELLGRGVSSCATCDGFFFRDQDIAVIGGGDSAMEEATFLT 175
Cdd:COG0492 82 VDKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 176 RFARSVTLVHRRDEFRASKIMLDRARNNDKIRFLTNHTVVAVDGDTTVTGLRVRDTNTGAETTLPVTGVFVAIGHEPRSG 255
Cdd:COG0492 162 KFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTE 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
2A87_A 256 LVREA-IDVDPDGYVLVqGRTTSTSLPGVFAAGDLVDRTYRQAVTAAGSGCAAAIDAERWLAEH 318
Cdd:COG0492 242 LLKGLgLELDEDGYIVV-DEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
17-315 |
3.72e-92 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 277.71 E-value: 3.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTTTDVENYPGFRNGITGPELMDEMREQALRFGADLRMEDVESV 96
Cdd:PRK10262 9 LLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDHINKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 97 SLHG-PLKsvVTADGQTHRARAVILAMGAAARYLQVPGEQELLGRGVSSCATCDGFFFRDQDIAVIGGGDSAMEEATFLT 175
Cdd:PRK10262 89 DLQNrPFR--LTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 176 RFARSVTLVHRRDEFRASKIMLDRARN---NDKIRFLTNHTVVAVDGDTT-VTGLRVRDT-NTGAETTLPVTGVFVAIGH 250
Cdd:PRK10262 167 NIASEVHLIHRRDGFRAEKILIKRLMDkveNGNIILHTNRTLEEVTGDQMgVTGVRLRDTqNSDNIESLDVAGLFVAIGH 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2A87_A 251 EPRSGLVREAIDVDpDGYVLVQ----GRTTSTSLPGVFAAGDLVDRTYRQAVTAAGSGCAAAIDAERWL 315
Cdd:PRK10262 247 SPNTAIFEGQLELE-NGYIKVQsgihGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
16-317 |
6.97e-91 |
|
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase homologs is found adjacent to alkylhydroperoxide reductase C subunit predominantly in cases where there is only one C subunit in the genome and that genome is lacking the F subunit partner (also a thioredcxin reductase homolog) that is usually found (TIGR03140).
Pssm-ID: 132187 [Multi-domain] Cd Length: 555 Bit Score: 282.05 E-value: 6.97e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTTTDVENYPGFRNgITGPELMDEMREQALRFGADLRMEDVES 95
Cdd:TIGR03143 6 DLIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILN-TTGPELMQEMRQQAQDFGVKFLQAEVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 96 VSLHGPLKSVVTADGqTHRARAVILAMGAAARYLQVPGEQELLGRGVSSCATCDGFFFRDQDIAVIGGGDSAMEEATFLT 175
Cdd:TIGR03143 85 VDFDGDIKTIKTARG-DYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 176 RFARSVTLVHRRDEFRASKIMLDRARNNDKIRFLTNHTVVAVDGDTTVTGLRVRDTNTGAETTLPVT------GVFVAIG 249
Cdd:TIGR03143 164 RYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEATGDDGLRYAKFVNNVTGEITEYKAPkdagtfGVFVFVG 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2A87_A 250 HEPRSGLVREAIDVDPDGYVlVQGRTTSTSLPGVFAAGDLVDRTYRQAVTAAGSGCAAAIDAERWLAE 317
Cdd:TIGR03143 244 YAPSSELFKGVVELDKRGYI-PTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYVKE 310
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
16-311 |
1.33e-68 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 223.11 E-value: 1.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAP-LVFEgtSFGGALMTTTDVENYPGFRNgITGPELMDEMREQALRFGADLrMEDVE 94
Cdd:PRK15317 213 DVLVVGGGPAGAAAAIYAARKGIRTgIVAE--RFGGQVLDTMGIENFISVPE-TEGPKLAAALEEHVKEYDVDI-MNLQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 95 SVSLH--GPLKSVVTADGQTHRARAVILAMGAAARYLQVPGEQELLGRGVSSCATCDGFFFRDQDIAVIGGGDSAMEEAT 172
Cdd:PRK15317 289 ASKLEpaAGLIEVELANGAVLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAI 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 173 FLTRFARSVTLVHRRDEFRASKIMLDRARNNDKIRFLTNHTVVAVDGDTT-VTGLRVRDTNTGAETTLPVTGVFVAIGHE 251
Cdd:PRK15317 369 DLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDkVTGLTYKDRTTGEEHHLELEGVFVQIGLV 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 252 PRSGLVREAIDVDPDGYVLVQGRtTSTSLPGVFAAGDLVDRTYRQAVTAAGSGCAAAIDA 311
Cdd:PRK15317 449 PNTEWLKGTVELNRRGEIIVDAR-GATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSA 507
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
16-304 |
2.60e-50 |
|
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: 169.42 E-value: 2.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVF--EGTSFGGALMTTTDVENYPGFRNGI-TGPELMDEMREQALRFGADLRME- 91
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIedEGTCPYGGCVLSKALLGAAEAPEIAsLWADLYKRKEEVVKKLNNGIEVLl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 92 DVESVSL-HGP----LKSVVTADGQTHRARAVILAMGAAARYLQVPGEQELLGRGVSSCATCDGFFF--RDQDIAVIGGG 164
Cdd:pfam07992 82 GTEVVSIdPGAkkvvLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLklLPKRVVVVGGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 165 DSAMEEATFLTRFARSVTLVHRRDEF------RASKIMLDRARNNdKIRFLTNHTVVAVDGDTtvTGLRVRDTNtgaETT 238
Cdd:pfam07992 162 YIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKN-GVEVRLGTSVKEIIGDG--DGVEVILKD---GTE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2A87_A 239 LPVTGVFVAIGHEPRSGLVREA-IDVDPDGYVLV--QGRttsTSLPGVFAAGDLVDRTYRQAVTAAGSG 304
Cdd:pfam07992 236 IDADLVVVAIGRRPNTELLEAAgLELDERGGIVVdeYLR---TSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
17-311 |
2.44e-30 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 119.47 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTttdvenY--PGFRngiTGPELMDEMREQALRFGADLRMeDVE 94
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLR------YgiPEFR---LPKDVLDREIELIEALGVEFRT-NVE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 95 svslhgpLKSVVTADGQTHRARAVILAMGA-AARYLQVPGEqELLG--------RGVSSCATCDGFFFRDQDIAVIGGGD 165
Cdd:COG0493 194 -------VGKDITLDELLEEFDAVFLATGAgKPRDLGIPGE-DLKGvhsamdflTAVNLGEAPDTILAVGKRVVVIGGGN 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 166 SAMEEATFLTRF-ARSVTLVHRRD--EFRASKIMLDRARNnDKIRFLTNHTVVAVDGDTT--VTGLRVRDT--------- 231
Cdd:COG0493 266 TAMDCARTALRLgAESVTIVYRRTreEMPASKEEVEEALE-EGVEFLFLVAPVEIIGDENgrVTGLECVRMelgepdesg 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 232 ------NTGAETTLPVTGVFVAIGHEPRSGLVREA--IDVDPDGYVLVQGRTTSTSLPGVFAAGDLVdRTYRQAVTAAGS 303
Cdd:COG0493 345 rrrpvpIEGSEFTLPADLVILAIGQTPDPSGLEEElgLELDKRGTIVVDEETYQTSLPGVFAGGDAV-RGPSLVVWAIAE 423
|
330
....*....|
2A87_A 304 G--CAAAIDA 311
Cdd:COG0493 424 GrkAARAIDR 433
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
17-320 |
1.24e-26 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 109.11 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTttdvenY--PGFRngiTGPELMDEMREQALRFGADLRMeDVE 94
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGLLR------YgiPEFR---LPKDIVDREVERLLKLGVEIRT-NTE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 95 svslhgpLKSVVTADGQTHRARAVILAMGA-AARYLQVPGEQ--------ELLGRgvSSCATCDGFFFRDQDIAVIGGGD 165
Cdd:PRK11749 213 -------VGRDITLDELRAGYDAVFIGTGAgLPRFLGIPGENlggvysavDFLTR--VNQAVADYDLPVGKRVVVIGGGN 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 166 SAMEEATFLTRF-ARSVTLVHRRD--EFRASKIMLDRARNnDKIRFLTNHTVVAVDGD-TTVTGLRVRDTN--------- 232
Cdd:PRK11749 284 TAMDAARTAKRLgAESVTIVYRRGreEMPASEEEVEHAKE-EGVEFEWLAAPVEILGDeGRVTGVEFVRMElgepdasgr 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 233 -----TGAETTLPVTGVFVAIGHEPRSGLVR--EAIDVDPDGYVLVQGRTTSTSLPGVFAAGDLV--DRTYRQAVtAAGS 303
Cdd:PRK11749 363 rrvpiEGSEFTLPADLVIKAIGQTPNPLILSttPGLELNRWGTIIADDETGRTSLPGVFAGGDIVtgAATVVWAV-GDGK 441
|
330
....*....|....*..
2A87_A 304 GCAAAIDaeRWLAEHAA 320
Cdd:PRK11749 442 DAAEAIH--EYLEGAAS 456
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
16-301 |
1.47e-26 |
|
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: 109.02 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGG-----------ALMTTTDV----ENYPGFrnGITG-------PEL 73
Cdd:COG1249 5 DLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGtclnvgcipskALLHAAEVaheaRHAAEF--GISAgapsvdwAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 74 MDEMREQALRFGAD----LRMEDVESVSLHGPLKS---VVTADGQTHRARAVILAMGAAARYLQVPGEQEllGRGVSSca 146
Cdd:COG1249 83 MARKDKVVDRLRGGveelLKKNGVDVIRGRARFVDphtVEVTGGETLTADHIVIATGSRPRVPPIPGLDE--VRVLTS-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 147 tcDGFFFRDQ---DIAVIGGGDSAMEEATFLTRFARSVTLVHRRDEF------RASKIMLDRARnNDKIRFLTNHTVVAV 217
Cdd:COG1249 159 --DEALELEElpkSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpgedpEISEALEKALE-KEGIDILTGAKVTSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 218 DGDTtvTGLRVRDTNTGAETTLPVTGVFVAIGHEPRS---GLvrEA--IDVDPDGYVLV--QGRttsTSLPGVFAAGDLV 290
Cdd:COG1249 236 EKTG--DGVTVTLEDGGGEEAVEADKVLVATGRRPNTdglGL--EAagVELDERGGIKVdeYLR---TSVPGIYAIGDVT 308
|
330
....*....|....*..
2A87_A 291 DRT------YRQAVTAA 301
Cdd:COG1249 309 GGPqlahvaSAEGRVAA 325
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
16-301 |
6.14e-23 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 98.71 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGG-----------ALMTTTDV----ENYPGF-----RNGITGPELMD 75
Cdd:PRK06292 5 DVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGtclnvgcipskALIAAAEAfheaKHAEEFgihadGPKIDFKKVMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 76 EMREQALRF--GADLRMEDVESVSL---HGPLKS--VVTADGQTHRARAVILAMGaaARYLQVPGEQELLGRG-VSScat 147
Cdd:PRK06292 85 RVRRERDRFvgGVVEGLEKKPKIDKikgTARFVDpnTVEVNGERIEAKNIVIATG--SRVPPIPGVWLILGDRlLTS--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 148 cDGFFFRD---QDIAVIGGGDSAMEEATFLTRFARSVTLVHRRDEF----------RASKIMldrarnNDKIRFLTNHTV 214
Cdd:PRK06292 160 -DDAFELDklpKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQAQKIL------SKEFKIKLGAKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 215 VAVDGDttVTGLRVRDTNTGAETTLPVTGVFVAIGHEPRS---GLVREAIDVDPDGYVLVqGRTTSTSLPGVFAAGDLVD 291
Cdd:PRK06292 233 TSVEKS--GDEKVEELEKGGKTETIEADYVLVATGRRPNTdglGLENTGIELDERGRPVV-DEHTQTSVPGIYAAGDVNG 309
|
330
....*....|....*.
2A87_A 292 RT------YRQAVTAA 301
Cdd:PRK06292 310 KPpllheaADEGRIAA 325
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
78-288 |
1.36e-20 |
|
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: 90.64 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 78 REQALRFGADLRMED-VESVSLHGplKSVVTADGQTHRARAVILAMGAAARYLQVPGEQEllgRGVSSCATCDG------ 150
Cdd:COG0446 43 PESFERKGIDVRTGTeVTAIDPEA--KTVTLRDGETLSYDKLVLATGARPRPPPIPGLDL---PGVFTLRTLDDadalre 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 151 --FFFRDQDIAVIGGGDSAMEEATFLTRFARSVTLVHRRD--------EFraSKIMLDRARNNDkIRFLTNHTVVAVDGD 220
Cdd:COG0446 118 alKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPrllgvldpEM--AALLEEELREHG-VELRLGETVVAIDGD 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2A87_A 221 ttvTGLRVRDTNtgaETTLPVTGVFVAIGHEPRSGLVREA-IDVDPDGYVLV--QGRttsTSLPGVFAAGD 288
Cdd:COG0446 195 ---DKVAVTLTD---GEEIPADLVVVAPGVRPNTELAKDAgLALGERGWIKVdeTLQ---TSDPDVYAAGD 256
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
17-311 |
3.12e-19 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 87.91 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEGTS-FGGALMtttdvenY--PGFRngiTGPELMDEMREQalrfgadlrMEDv 93
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERADrIGGLLR-------YgiPDFK---LEKEVIDRRIEL---------MEA- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 94 ESVSLH-----GplkSVVTADGQTHRARAVILAMGA-AARYLQVPGE----------------QELLGRGVSSCATCDGf 151
Cdd:PRK12810 206 EGIEFRtnvevG---KDITAEELLAEYDAVFLGTGAyKPRDLGIPGRdldgvhfamdfliqntRRVLGDETEPFISAKG- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 152 ffrdQDIAVIGGGDSAME-EATFLTRFARSVTlvhRRDEfrASKIMLDRARNN------------------DKIRFLTNh 212
Cdd:PRK12810 282 ----KHVVVIGGGDTGMDcVGTAIRQGAKSVT---QRDI--MPMPPSRRNKNNpwpywpmklevsnaheegVEREFNVQ- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 213 TVVAVDGDTTVTGLRVRDTNTGAETTLPVTG---------VFVAIGHE-PRSGLVRE-AIDVDPDGYVLVQGRTTSTSLP 281
Cdd:PRK12810 352 TKEFEGENGKVTGVKVVRTELGEGDFEPVEGsefvlpadlVLLAMGFTgPEAGLLAQfGVELDERGRVAAPDNAYQTSNP 431
|
330 340 350
....*....|....*....|....*....|....*...
2A87_A 282 GVFAAGD------LVdrtyrqaVTAA--GSGCAAAIDA 311
Cdd:PRK12810 432 KVFAAGDmrrgqsLV-------VWAIaeGRQAARAIDA 462
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
158-231 |
1.55e-17 |
|
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: 76.09 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 158 IAVIGGGDSAMEEATFLTRFARSVTLVHRRDEFR------ASKIMLDRARNNdKIRFLTNHTVVAVDGDTTVTGLRVRDT 231
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGVVVVLTDG 80
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
15-288 |
3.52e-17 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 81.73 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 15 RDVIVIGSGPAGYTAAlyaarAQLAPLVFEG--TSFGGalmtttdvENYPGF-RNGITgPELMDEMREQALRF------- 84
Cdd:COG1251 2 MRIVIIGAGMAGVRAA-----EELRKLDPDGeiTVIGA--------EPHPPYnRPPLS-KVLAGETDEEDLLLrpadfye 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 85 --GADLRMED-VESVSLHGplKSVVTADGQTHRARAVILAMGAAARYLQVPGeqeLLGRGVsscatcdgFFFRDQD---- 157
Cdd:COG1251 68 enGIDLRLGTrVTAIDRAA--RTVTLADGETLPYDKLVLATGSRPRVPPIPG---ADLPGV--------FTLRTLDdada 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 158 ----------IAVIGGGDSAMEEATFLTRFARSVTLVHRRDEF-------RASKIMLDRARNNDkIRFLTNHTVVAVDGD 220
Cdd:COG1251 135 lraalapgkrVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlprqldeEAGALLQRLLEALG-VEVRLGTGVTEIEGD 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2A87_A 221 TTVTGLRVRDtntgaETTLPVTGVFVAIGHEPRSGLVREA-IDVDpDGyVLV--QGRttsTSLPGVFAAGD 288
Cdd:COG1251 214 DRVTGVRLAD-----GEELPADLVVVAIGVRPNTELARAAgLAVD-RG-IVVddYLR---TSDPDIYAAGD 274
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
17-315 |
3.99e-17 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 81.99 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAAlyaarAQLAPLVFEGTSF------GGALmtttdVENYPGFR---NGITGPELmDEMREQALRFGAD 87
Cdd:PRK12831 143 VAVIGSGPAGLTCA-----GDLAKMGYDVTIFealhepGGVL-----VYGIPEFRlpkETVVKKEI-ENIKKLGVKIETN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 88 LrmedvesvslhgPLKSVVTADG--QTHRARAVILAMGAAA-RYLQVPGEQ--------ELLGRGVSSCATCDGF---FF 153
Cdd:PRK12831 212 V------------VVGKTVTIDEllEEEGFDAVFIGSGAGLpKFMGIPGENlngvfsanEFLTRVNLMKAYKPEYdtpIK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 154 RDQDIAVIGGGDSAMEEATFLTRFARSVTLVHRR--DEFRASKIMLDRARNND-KIRFLTNHTVVAVDGDTTVTGLRV-- 228
Cdd:PRK12831 280 VGKKVAVVGGGNVAMDAARTALRLGAEVHIVYRRseEELPARVEEVHHAKEEGvIFDLLTNPVEILGDENGWVKGMKCik 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 229 -----RDTN--------TGAETTLPVTGVFVAIGHEPRSGLVREA--IDVDPDGYVLVQGRTTSTSLPGVFAAGDLVdrt 293
Cdd:PRK12831 360 melgePDASgrrrpveiEGSEFVLEVDTVIMSLGTSPNPLISSTTkgLKINKRGCIVADEETGLTSKEGVFAGGDAV--- 436
|
330 340
....*....|....*....|....*
2A87_A 294 yRQAVT---AAGSGCAAAIDAERWL 315
Cdd:PRK12831 437 -TGAATvilAMGAGKKAAKAIDEYL 460
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
24-287 |
1.19e-15 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 76.11 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 24 PAGYTAALYAARAQLAPLV-------------------FEGTSFGGALMTTTDV-----ENYPGF---RNGITGPELMDE 76
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDYLilekgnignsfyrypthmtFFSPSFTSNGFGIPDLnaispGTSPAFtfnREHPSGNEYAEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 77 MREQALRFGADLRM-EDVESVSLHGPLKsVVTADGQTHRARAVILAMGaaarYLQVPGEQELLGRGVSSCATCDGFFFRD 155
Cdd:pfam13738 81 LRRVADHFELPINLfEEVTSVKKEDDGF-VVTTSKGTYQARYVIIATG----EFDFPNKLGVPELPKHYSYVKDFHPYAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 156 QDIAVIGGGDSAMEEATFLTRFARSVTLVHRRDEFRAS------------KIMLDRARNNDKIRFLTNHTVVAVdgdtTV 223
Cdd:pfam13738 156 QKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRdsdpsyslspdtLNRLEELVKNGKIKAHFNAEVKEI----TE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
2A87_A 224 TGLRVRDTNTGAETTLPVTGVFVAIGHEPRSGLVREA-IDVDPDGYVLVQGRTTSTSLPGVFAAG 287
Cdd:pfam13738 232 VDVSYKVHTEDGRKVTSNDDPILATGYHPDLSFLKKGlFELDEDGRPVLTEETESTNVPGLFLAG 296
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
17-323 |
7.44e-15 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 75.15 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTttdvENYPGFRNgitgPE-LMDEMREQALRFGADLRMEDVes 95
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMR----YGIPRFRL----PEsVIDADIAPLRAMGAEFRFNTV-- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 96 vslhgpLKSVVTADGQTHRARAVILAMGAA-ARYLQVPGEQEllgRGVSSCATcdgfFFRD----------QDIAVIGGG 164
Cdd:PRK12814 266 ------FGRDITLEELQKEFDAVLLAVGAQkASKMGIPGEEL---PGVISGID----FLRNvalgtalhpgKKVVVIGGG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 165 DSAMEEA-TFLTRFARSVTLVHRR--DEFRASKIMLDRARNND-KIRFLTNHTVV-AVDGDTTVTGLRVR----DTN--- 232
Cdd:PRK12814 333 NTAIDAArTALRLGAESVTILYRRtrEEMPANRAEIEEALAEGvSLRELAAPVSIeRSEGGLELTAIKMQqgepDESgrr 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 233 -----TGAETTLPVTGVFVAIGHEPRSGLVREA-IDVDPDGYVLVQGRTTSTSLPGVFAAGDLVDRTyRQAVTAAGSGCA 306
Cdd:PRK12814 413 rpvpvEGSEFTLQADTVISAIGQQVDPPIAEAAgIGTSRNGTVKVDPETLQTSVAGVFAGGDCVTGA-DIAINAVEQGKR 491
|
330
....*....|....*..
2A87_A 307 AAIDAERWLAEHAATGE 323
Cdd:PRK12814 492 AAHAIDLFLNGKPVTAP 508
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
16-288 |
1.70e-14 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 74.08 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALM------TTTDVE-----------NYPGFRngITGP------E 72
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVntgcvpTKTLIAsaraahlarraAEYGVS--VGGPvsvdfkA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 73 LMDEMREQALRFGADL--RMEDVESVSL---HGPLKS--VVTADGQTHRARAVILAMGAAARYLQVPGEQEllgrgvSSC 145
Cdd:PRK06370 85 VMARKRRIRARSRHGSeqWLRGLEGVDVfrgHARFESpnTVRVGGETLRAKRIFINTGARAAIPPIPGLDE------VGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 146 ATCDGFF---FRDQDIAVIGGGDSAMEEATFLTRFARSVTLVHR------RDEFRASKImLDRARNNDKIRFLTNHTVVA 216
Cdd:PRK06370 159 LTNETIFsldELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERgprllpREDEDVAAA-VREILEREGIDVRLNAECIR 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2A87_A 217 VDGDTtvTGLRVRDTNTGAETTLPVTGVFVAIGHEPRS---GLVREAIDVDPDGYVLVQGRtTSTSLPGVFAAGD 288
Cdd:PRK06370 238 VERDG--DGIAVGLDCNGGAPEITGSHILVAVGRVPNTddlGLEAAGVETDARGYIKVDDQ-LRTTNPGIYAAGD 309
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
16-310 |
6.44e-13 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 69.02 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGG-----------ALmtttdvenypgfrngITGPELMDEMREQAlRF 84
Cdd:PRK06416 6 DVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGtclnrgcipskAL---------------LHAAERADEARHSE-DF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 85 G-----ADLRMEDV----ESVS------LHGPLKS-------------------VVTADG-QTHRARAVILAMGAAARYL 129
Cdd:PRK06416 70 GikaenVGIDFKKVqewkNGVVnrltggVEGLLKKnkvdiirgeaklvdpntvrVMTEDGeQTYTAKNIILATGSRPREL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 130 qvPGeQELLGRGVsscATCDGFFFRD---QDIAVIGGGDSAMEEATFLTRFARSVTLVHRRDE----FRA--SKImLDRA 200
Cdd:PRK06416 150 --PG-IEIDGRVI---WTSDEALNLDevpKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRilpgEDKeiSKL-AERA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 201 RNNDKIRFLTNHTVVAVD-GDTTVTglrVRDTNTGAETTLPVTGVFVAIGHEPRS-GLVREAIDVDPD-GYVLV--QGRT 275
Cdd:PRK06416 223 LKKRGIKIKTGAKAKKVEqTDDGVT---VTLEDGGKEETLEADYVLVAVGRRPNTeNLGLEELGVKTDrGFIEVdeQLRT 299
|
330 340 350 360
....*....|....*....|....*....|....*....|...
2A87_A 276 tstSLPGVFAAGDLVD------RTYRQAVTAAG--SGCAAAID 310
Cdd:PRK06416 300 ---NVPNIYAIGDIVGgpmlahKASAEGIIAAEaiAGNPHPID 339
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
16-275 |
7.35e-13 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 68.74 E-value: 7.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFE-GTSFGGA--------LmtTTDVEN----YPGFRNG------ITGPELMDE 76
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEkADDVGGTwrdnrypgL--RLDTPShlysLPFFPNWsddpdfPTGDEILAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 77 MREQALRFGADLRME---DVESVSLH--GPLKSVVTADGQTHRARAVILAMGA--AARYLQVPGEQELLGRGVSSCATCD 149
Cdd:COG2072 86 LEAYADKFGLRRPIRfgtEVTSARWDeaDGRWTVTTDDGETLTARFVVVATGPlsRPKIPDIPGLEDFAGEQLHSADWRN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 150 GFFFRDQDIAVIGGGDSAMEEATFLTRFARSVTLVHR----------------RDEFRASKIMLDRARNNDKIRFLTNHT 213
Cdd:COG2072 166 PVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRtppwvlprpnydpergRPANYLGLEAPPALNRRDARAWLRRLL 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
2A87_A 214 VVAVDGDTtvTGLRVRDTNTGAETTLPVTGVFVAIGHePRSGLVREAID-VDPDGYVLVQGRT 275
Cdd:COG2072 246 RAQVKDPE--LGLLTPDYPPGCKRPLLSTDYYEALRR-GNVELVTGGIErITEDGVVFADGTE 305
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
15-318 |
2.76e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 66.94 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 15 RDVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMtttdVENYPGFR---NGITgpELMDEMREQALRFgaDLRME 91
Cdd:PRK12770 19 KKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLM----LFGIPEFRipiERVR--EGVKELEEAGVVF--HTRTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 92 DVESVSLHGPL-----KSVVTADGQTHRARAVILAMGA-AARYLQVPGEQellGRGVSSCATcdgFFFR----------- 154
Cdd:PRK12770 91 VCCGEPLHEEEgdefvERIVSLEELVKKYDAVLIATGTwKSRKLGIPGED---LPGVYSALE---YLFRiraaklgylpw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 155 -------DQDIAVIGGGDSAM---EEATFLTrfARSVTLVHRR--DEFRASKIMLDRARNNDkIRFLTNHTVVAVDGDTT 222
Cdd:PRK12770 165 ekvppveGKKVVVVGAGLTAVdaaLEAVLLG--AEKVYLAYRRtiNEAPAGKYEIERLIARG-VEFLELVTPVRIIGEGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 223 VTGLRVRDT---------------NTGAETTLPVTGVFVAIGHEPRSGLVREA--IDVDPDGYVLVQGRTTsTSLPGVFA 285
Cdd:PRK12770 242 VEGVELAKMrlgepdesgrprpvpIPGSEFVLEADTVVFAIGEIPTPPFAKEClgIELNRKGEIVVDEKHM-TSREGVFA 320
|
330 340 350
....*....|....*....|....*....|...
2A87_A 286 AGDLVDRTyRQAVTAAGSGCAAAIDAERWLAEH 318
Cdd:PRK12770 321 AGDVVTGP-SKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
17-311 |
3.62e-12 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 67.07 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEgtsfggALMTTTDVENY--PGFR--NGITGPELmDEMREQALRFGADLRMEd 92
Cdd:PRK12778 434 VAVIGSGPAGLSFAGDLAKRGYDVTVFE------ALHEIGGVLKYgiPEFRlpKKIVDVEI-ENLKKLGVKFETDVIVG- 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 93 vesvslhgplKSVVTADGQTHRARAVILAMGAA-ARYLQVPGEQ--------ELLGRGVSSCATCDGF---FFRDQDIAV 160
Cdd:PRK12778 506 ----------KTITIEELEEEGFKGIFIASGAGlPNFMNIPGENsngvmssnEYLTRVNLMDAASPDSdtpIKFGKKVAV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 161 IGGGDSAMEEATFLTRF-ARSVTLVHRR--DEFRASKIMLDRARNnDKIRFLTNHTVVAVDGDTT--VTGLRVR------ 229
Cdd:PRK12778 576 VGGGNTAMDSARTAKRLgAERVTIVYRRseEEMPARLEEVKHAKE-EGIEFLTLHNPIEYLADEKgwVKQVVLQkmelge 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 230 -DTN--------TGAETTLPVTGVFVAIGHEPRSGLVR--EAIDVDPDGYVLVQgRTTSTSLPGVFAAGDLVdrtyRQAV 298
Cdd:PRK12778 655 pDASgrrrpvaiPGSTFTVDVDLVIVSVGVSPNPLVPSsiPGLELNRKGTIVVD-EEMQSSIPGIYAGGDIV----RGGA 729
|
330
....*....|....*...
2A87_A 299 T---AAGSG--CAAAIDA 311
Cdd:PRK12778 730 TvilAMGDGkrAAAAIDE 747
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
17-316 |
6.00e-12 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 66.44 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMtttdvenypgfRNGITG---P--ELMDEMReQALRFGADLRM- 90
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMM-----------RYGIPAyrlPreVLDAEIQ-RILDLGVEVRLg 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 91 ----EDVESVSLhgplksvvtaDGQTHrarAVILAMGA-AARYLQVPGEQ--------ELLgRGVSScatcDGFFFRDQD 157
Cdd:PRK12771 208 vrvgEDITLEQL----------EGEFD---AVFVAIGAqLGKRLPIPGEDaagvldavDFL-RAVGE----GEPPFLGKR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 158 IAVIGGGDSAMEEATFLTRF-ARSVTLVHRR--DEFRASKIMLDRA-RNNDKIRFLTnhTVVAVDGDT-TVTGLRV---- 228
Cdd:PRK12771 270 VVVIGGGNTAMDAARTARRLgAEEVTIVYRRtrEDMPAHDEEIEEAlREGVEINWLR--TPVEIEGDEnGATGLRVitve 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 229 ------RDTN---TGAETTLPVTGVFVAIGHEPRSGLVREAIDVDPDGYVLVQGRTTS-TSLPGVFAAGDLV--DRTYRQ 296
Cdd:PRK12771 348 kmeldeDGRPspvTGEEETLEADLVVLAIGQDIDSAGLESVPGVEVGRGVVQVDPNFMmTGRPGVFAGGDMVpgPRTVTT 427
|
330 340
....*....|....*....|
2A87_A 297 AVtAAGSGCAAAIDAerWLA 316
Cdd:PRK12771 428 AI-GHGKKAARNIDA--FLG 444
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
78-290 |
9.43e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 62.46 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 78 REQALRFGADLRMEDVESVSLHGplKSVVTADGQTHRARAVILAMGAAARYLQVPGEQEllgRGVSSCATCDGFFFRDQ- 156
Cdd:COG1252 63 RELLRRAGVRFIQGEVTGIDPEA--RTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAE---HALPLKTLEDALALRERl 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 157 -------------DIAVIGGGDSAMEEATFLTRFAR-------------SVTLVHRRDEF------RASKIMLDRARNND 204
Cdd:COG1252 138 laaferaerrrllTIVVVGGGPTGVELAGELAELLRkllrypgidpdkvRITLVEAGPRIlpglgeKLSEAAEKELEKRG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 205 kIRFLTNHTVVAVDGDttvtGLRVRDtntgaETTLPVTGVFVAIGHEPrSGLVREA-IDVDPDGYVLVQGRTTSTSLPGV 283
Cdd:COG1252 218 -VEVHTGTRVTEVDAD----GVTLED-----GEEIPADTVIWAAGVKA-PPLLADLgLPTDRRGRVLVDPTLQVPGHPNV 286
|
....*..
2A87_A 284 FAAGDLV 290
Cdd:COG1252 287 FAIGDCA 293
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
17-308 |
1.74e-10 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 62.16 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEG-TSFGGALmtttdvenypgfRNGItgPELmdemreqalRFGADLRMEDVES 95
Cdd:PRK12779 309 IAVVGSGPSGLINAYLLAVEGFPVTVFEAfHDLGGVL------------RYGI--PEF---------RLPNQLIDDVVEK 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 96 VSLHGPL--------KSVVTADGQTHRARAVILAMGAA-ARYLQVPGEQ--------ELLGRgVSSCATCDGFF------ 152
Cdd:PRK12779 366 IKLLGGRfvknfvvgKTATLEDLKAAGFWKIFVGTGAGlPTFMNVPGEHllgvmsanEFLTR-VNLMRGLDDDYetplpe 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 153 FRDQDIAVIGGGDSAMEEATFLTRFARSVTLVHRR--DEFRA----------SKIMLDRAR------NNDKIRFLTnHTV 214
Cdd:PRK12779 445 VKGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRRtkSEMPArveelhhaleEGINLAVLRaprefiGDDHTHFVT-HAL 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 215 VAVD--GDTTVTGlRVRDTNTGAETTLPVTGVFVAIGHEPRSgLVREA---IDVDPDGYVLVQGRTTSTSLPGVFAAGDl 289
Cdd:PRK12779 524 LDVNelGEPDKSG-RRSPKPTGEIERVPVDLVIMALGNTANP-IMKDAepgLKTNKWGTIEVEKGSQRTSIKGVYSGGD- 600
|
330
....*....|....*....
2A87_A 290 VDRTYRQAVTAAGSGCAAA 308
Cdd:PRK12779 601 AARGGSTAIRAAGDGQAAA 619
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
103-307 |
1.09e-09 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 59.46 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 103 KSVVTADGQTHRARAVILAMGAAARYLQVPG--EQELLG-RGVSSCATCDGFFFRDQDIAVIGGGDSAMEEATFLTRFAR 179
Cdd:TIGR02374 85 KQVITDAGRTLSYDKLILATGSYPFILPIPGadKKGVYVfRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGM 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 180 SVTLVHRRDEFRASKI------MLDRARNNDKIRFLTNHTVVAVDGDTTVTGLRVRDTntgaeTTLPVTGVFVAIGHEPR 253
Cdd:TIGR02374 165 DVSVIHHAPGLMAKQLdqtagrLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDG-----SSLEADLIVMAAGIRPN 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2A87_A 254 SGLVREA-IDVdpDGYVLVQgRTTSTSLPGVFAAGD----------LVDRTYRQAVTAA----GSGCAA 307
Cdd:TIGR02374 240 DELAVSAgIKV--NRGIIVN-DSMQTSDPDIYAVGEcaehngrvygLVAPLYEQAKVLAdhicGVECEE 305
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
17-315 |
3.35e-09 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 58.03 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEgtsfggALMTTTDVENY--PGFRngiTGPELMDEMREQALRFGADLRMEDVE 94
Cdd:PRK12775 433 VAICGSGPAGLAAAADLVKYGVDVTVYE------ALHVVGGVLQYgiPSFR---LPRDIIDREVQRLVDIGVKIETNKVI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 95 SVSLHGPlkSVVTADGQThrarAVILAMGAAA-RYLQVPGE--------QELLGRgvSSCATCDGFFFRD------QDIA 159
Cdd:PRK12775 504 GKTFTVP--QLMNDKGFD----AVFLGVGAGApTFLGIPGEfagqvysaNEFLTR--VNLMGGDKFPFLDtpislgKSVV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 160 VIGGGDSAMEEATFLTRF-ARSVTLVHRRDEFRA-SKIMLDRARNNDKIRFLTNHTVVAV--DGDTTVTGLRVRDTNTGA 235
Cdd:PRK12775 576 VIGAGNTAMDCLRVAKRLgAPTVRCVYRRSEAEApARIEEIRHAKEEGIDFFFLHSPVEIyvDAEGSVRGMKVEEMELGE 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 236 E--------------TTLPVTGVFVAIGHEPRS---------GLVREAIDVDPDGYVlvqGRTTSTSLPGVFAAGDLVDR 292
Cdd:PRK12775 656 PdekgrrkpmptgefKDLECDTVIYALGTKANPiitqstpglALNKWGNIAADDGKL---ESTQSTNLPGVFAGGDIVTG 732
|
330 340
....*....|....*....|...
2A87_A 293 TyRQAVTAAGSGCAAAIDAERWL 315
Cdd:PRK12775 733 G-ATVILAMGAGRRAARSIATYL 754
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
17-289 |
4.68e-09 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 57.24 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQlaplvfegtsFGGALMTTTDVENYPGFRNGITGPELMDEMREQALRFGADLRMEDV--- 93
Cdd:PRK09754 6 IIIVGGGQAAAMAAASLRQQG----------FTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNvhl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 94 ---ESVSLHGPLK-SVVTADGQTHRARAVILAMGAAAR---YLQVPGEQELLGRGVSSCATCDGFFFRDQDIAVIGGGDS 166
Cdd:PRK09754 76 hsgVTIKTLGRDTrELVLTNGESWHWDQLFIATGAAARplpLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 167 AMEEATFLTRFARSVTLVHRRDEF--RASKIMLDR---ARNNDK-IRFLTNHTVV-AVDGDTTVTGLrvrdtNTGaeTTL 239
Cdd:PRK09754 156 GLELAASATQRRCKVTVIELAATVmgRNAPPPVQRyllQRHQQAgVRILLNNAIEhVVDGEKVELTL-----QSG--ETL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
2A87_A 240 PVTGVFVAIGHEPRSGLVREAiDVDPDGYVLVQGRtTSTSLPGVFAAGDL 289
Cdd:PRK09754 229 QADVVIYGIGISANDQLAREA-NLDTANGIVIDEA-CRTCDPAIFAGGDV 276
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
154-316 |
7.25e-08 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 53.98 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 154 RDQDIAVIGGGDSAME-EATFLTRFARSVTLVHRRDE--FRASKIMLDRARnNDKIRFLTNHTVVAV--DGDTTVTGLRV 228
Cdd:PRK12769 467 AGLNVVVLGGGDTAMDcVRTALRHGASNVTCAYRRDEanMPGSKKEVKNAR-EEGANFEFNVQPVALelNEQGHVCGIRF 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 229 RDTN---------------TGAETTLPVTGVFVAIGHEPRSGLVREAIDVDPDGyvlvQGRTTS---------TSLPGVF 284
Cdd:PRK12769 546 LRTRlgepdaqgrrrpvpiPGSEFVMPADAVIMAFGFNPHGMPWLESHGVTVDK----WGRIIAdvesqyryqTSNPKIF 621
|
170 180 190
....*....|....*....|....*....|..
2A87_A 285 AAGDLVdRTYRQAVTAAGSGCAAAIDAERWLA 316
Cdd:PRK12769 622 AGGDAV-RGADLVVTAMAEGRHAAQGIIDWLG 652
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
17-310 |
1.11e-07 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 53.11 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTTtdveNYPGFRNGITgpeLMDEMREQALRFGADLRM------ 90
Cdd:PRK12809 313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTF----GIPPFKLDKT---VLSQRREIFTAMGIDFHLnceigr 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 91 --------EDVESVSLHGPLKSVVTADGQTHRARAVILAMG-AAARYLQVPGEQELLGRGVSScatcdgffFRDQDIAVI 161
Cdd:PRK12809 386 ditfsdltSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPfLTAHTRQLMGLPESEEYPLTD--------VEGKRVVVL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 162 GGGDSAME-EATFLTRFARSVTLVHRRDEFR--ASKIMLDRARNND-KIRFLTNHTVVAVDGDTTVTGLRVRDTN----- 232
Cdd:PRK12809 458 GGGDTTMDcLRTSIRLNAASVTCAYRRDEVSmpGSRKEVVNAREEGvEFQFNVQPQYIACDEDGRLTAVGLIRTAmgepg 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 233 ----------TGAETTLPVTGVFVAIGHEPRSGLVREAIDVDPDGYVLVQ----GR-TTSTSLPGVFAAGDLVDRTyRQA 297
Cdd:PRK12809 538 pdgrrrprpvAGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIQtgdvGYlPTQTHLKKVFAGGDAVHGA-DLV 616
|
330
....*....|...
2A87_A 298 VTAAGSGCAAAID 310
Cdd:PRK12809 617 VTAMAAGRQAARD 629
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
16-292 |
1.30e-07 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 53.05 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGP----AGYTAA-LYAARAQLAPL-VFEGTSFGGALM-TTTDVENYPGfRNGITGPELMDEMREQAlRFGADL 88
Cdd:TIGR01423 5 DLVVIGAGSggleAGWNAAtLYKKRVAVVDVqTHHGPPFYAALGgTCVNVGCVPK-KLMVTGAQYMDTLRESA-GFGWEF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 89 RME-----------------------------DVESVSLH---GPL--KSVV----TAD-----GQTHRARAVILAMGAA 125
Cdd:TIGR01423 83 DRSsvkanwkaliaaknkavldinksyegmfaDTEGLTFFlgwGALedKNVVlvreSADpksavKERLQAEHILLATGSW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 126 ARYLQVPGeqellgrgVSSCATCDGFFFRDQD---IAVIGGGDSAMEEATFLTRF---ARSVTLVHRRD------EFRAS 193
Cdd:TIGR01423 163 PQMLGIPG--------IEHCISSNEAFYLDEPprrVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRNNmilrgfDSTLR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 194 KIMLDRARNNDkIRFLTNHTVVAV----DGDTTVTglrvrdTNTGAetTLPVTGVFVAIGHEPRSG---LVREAIDVDPD 266
Cdd:TIGR01423 235 KELTKQLRANG-INIMTNENPAKVtlnaDGSKHVT------FESGK--TLDVDVVMMAIGRVPRTQtlqLDKVGVELTKK 305
|
330 340
....*....|....*....|....*.
2A87_A 267 GYVLVQgRTTSTSLPGVFAAGDLVDR 292
Cdd:TIGR01423 306 GAIQVD-EFSRTNVPNIYAIGDVTDR 330
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
16-317 |
7.61e-07 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 50.62 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFE-------GTSFG-GAlmTTTDVENYPG---FRNGITGPELMD--------- 75
Cdd:TIGR01438 4 DLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplGTRWGiGG--TCVNVGCIPKklmHQAALLGQALKDsrnygwkve 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 76 --------------EMREQALRFG--ADLRMEDVESVSLHGPL--KSVVTA-----DGQTHRARAVILAMGAAARYLQVP 132
Cdd:TIGR01438 82 etvkhdwkrlveavQNHIGSLNWGyrVALREKKVKYENAYAEFvdKHRIKAtnkkgKEKIYSAERFLIATGERPRYPGIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 133 GEQELlgrgvssCATCDGFFFRDQD---IAVIGGGDSAMEEATFLTRFARSVTLVHRR------DEFRASKIMLDRARNN 203
Cdd:TIGR01438 162 GAKEL-------CITSDDLFSLPYCpgkTLVVGASYVALECAGFLAGIGLDVTVMVRSillrgfDQDCANKVGEHMEEHG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 204 DKIRfltNHTVVAvdgDTTVTGLRVRDTNTGAETTLP--VTGVFVAIGHEPRS-GLVREAIDVDPD---GYVLVQgRTTS 277
Cdd:TIGR01438 235 VKFK---RQFVPI---KVEQIEAKVLVEFTDSTNGIEeeYDTVLLAIGRDACTrKLNLENVGVKINkktGKIPAD-EEEQ 307
|
330 340 350 360
....*....|....*....|....*....|....*....|
2A87_A 278 TSLPGVFAAGDLVDRtyRQAVTaagsgcAAAIDAERWLAE 317
Cdd:TIGR01438 308 TNVPYIYAVGDILED--KPELT------PVAIQAGRLLAQ 339
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
2-298 |
1.25e-06 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 50.00 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 2 TAPPVHDRAH-HPVRDVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGalmTTTDVENYPG------------FRN-- 66
Cdd:PTZ00058 35 SSAPTHLKKKpRMVYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGG---TCVNVGCVPKkimfnaasihdiLENsr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 67 --GITGPELMD-----EMREQALR-----FGADLRMEDVESVSLHGPLKSVVTA-------------------------- 108
Cdd:PTZ00058 112 hyGFDTQFSFNlpllvERRDKYIRrlndiYRQNLKKDNVEYFEGKGSLLSENQVlikkvsqvdgeadesdddevtivsag 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 109 -----DGQTHRARAVILAMGAAARYLQVpgeqellgRGVSSCATCDGFFF--RDQDIAVIGGGDSAMEEATFLTRFARSV 181
Cdd:PTZ00058 192 vsqldDGQVIEGKNILIAVGNKPIFPDV--------KGKEFTISSDDFFKikEAKRIGIAGSGYIAVELINVVNRLGAES 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 182 TLVHRR-------DEFRASKIMLDRARNNDKIrfLTNHTVVAVDGDTTvTGLRVRDTNTGAETTLPVtgVFVAIGHEPRS 254
Cdd:PTZ00058 264 YIFARGnrllrkfDETIINELENDMKKNNINI--ITHANVEEIEKVKE-KNLTIYLSDGRKYEHFDY--VIYCVGRSPNT 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
2A87_A 255 -GLVREAI-DVDPDGYVLVQgRTTSTSLPGVFAAGDLVDRTYRQAV 298
Cdd:PTZ00058 339 eDLNLKALnIKTPKGYIKVD-DNQRTSVKHIYAVGDCCMVKKNQEI 383
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
15-75 |
7.24e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 47.58 E-value: 7.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2A87_A 15 RDVIVIGSGPAGYTAALYAARAQLAPLVFEGTS-FGGalMTTTdvENYPGFRNGITG-------PELMD 75
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPvVGG--ISRT--VTYKGNRFDIGGhrffsksPEVMD 69
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
16-120 |
1.28e-05 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 46.45 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMT----TTDVENYPGFRNGITG--PELMDEMREqalRFGADLR 89
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTsglvGPDMGFYLNKEQVVGGiaREFRQRLRA---RGGLPGP 77
|
90 100 110
....*....|....*....|....*....|.
2A87_A 90 MEDVESVSLHGPLKSVVTADGQTHRARAVIL 120
Cdd:pfam12831 78 YGLRGGWVPFDPEVAKAVLDEMLAEAGVTVL 108
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
118-312 |
1.69e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 46.31 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 118 VILAMGAAARYLQVPGEQELLGRGVSSCATCDGFFFRDQ--DIAVIGGGDSAMEEATFLTRFARSVTLVHRRDEFraSKI 195
Cdd:PRK13512 109 LILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQvdKALVVGAGYISLEVLENLYERGLHPTLIHRSDKI--NKL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 196 MlDRARNN--------DKIRFLTNHTVVAVDGDT-TVTGLRVRDTNtgaettLPVTGVfvaiGHEPRSGLVREA-IDVDP 265
Cdd:PRK13512 187 M-DADMNQpildeldkREIPYRLNEEIDAINGNEvTFKSGKVEHYD------MIIEGV----GTHPNSKFIESSnIKLDD 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
2A87_A 266 DGYVLVQgRTTSTSLPGVFAAGDLVDRTYR------QAVTAAGSGCAAAIDAE 312
Cdd:PRK13512 256 KGFIPVN-DKFETNVPNIYAIGDIITSHYRhvdlpaSVPLAWGAHRAASIVAE 307
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
17-288 |
1.75e-05 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 46.19 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQ--LAPLVFEGT---SFGGALMtttdvenyPGFRNGI-TGPELMDE-MREQALRFGADLR 89
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNkeLEITVYEKTdivSFGACGL--------PYFVGGFfDDPNTMIArTPEEFIKSGIDVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 90 MEDvESVSLHGPLKSVVTADGQTHRA-----RAVILAMGAAArylQVPGEQELLGRGVSSCATC-DGFFFRD-------Q 156
Cdd:PRK09564 75 TEH-EVVKVDAKNKTITVKNLKTGSIfndtyDKLMIATGARP---IIPPIKNINLENVYTLKSMeDGLALKEllkdeeiK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 157 DIAVIGGGDSAMEEATFLTRFARSVTLVHRRD---------EFraSKIMLDRARNNDkIRFLTNHTVVAVDGDTTVTGLR 227
Cdd:PRK09564 151 NIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDrilpdsfdkEI--TDVMEEELRENG-VELHLNEFVKSLIGEDKVEGVV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
2A87_A 228 vrdTNTGA-ETTLpvtgVFVAIGHEPRSGLVREA-IDVDPDGYVLVQgRTTSTSLPGVFAAGD 288
Cdd:PRK09564 228 ---TDKGEyEADV----VIVATGVKPNTEFLEDTgLKTLKNGAIIVD-EYGETSIENIYAAGD 282
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
16-136 |
2.12e-05 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 45.62 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARA------------QLA-----P---------LVFEGTSFGGALMTTTDvENYPGFR--NG 67
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMgakvllithntdTIAelscnPsiggiakghLVREIDALGGLMGKAAD-KTGIQFRmlNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 68 ITGPELmdemreQALRFGAD-------------------LRMEDVESVSL-HGPLKSVVTADGQTHRARAVILAMGAAAR 127
Cdd:pfam01134 80 SKGPAV------RALRAQVDrdlyskemtetlenhpnltLIQGEVTDLIPeNGKVKGVVTEDGEEYKAKAVVLATGTFLN 153
|
....*....
2A87_A 128 YLQVPGEQE 136
Cdd:pfam01134 154 GKIHIGLKC 162
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
107-289 |
2.70e-05 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 45.72 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 107 TADGQTHRARAVILAMGAAARYLQVPGEQELlgrgvsSCATCDGFFFRDQ---DIAVIGGGDSAMEEATFLTRFARSVTL 183
Cdd:PRK07846 121 TGDGEEITADQVVIAAGSRPVIPPVIADSGV------RYHTSDTIMRLPElpeSLVIVGGGFIAAEFAHVFSALGVRVTV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 184 VHR-----RDEFRA-SKIMLDRARNNDKIRflTNHTVVAVDGDTTVTGLRVRDtntgaETTLPVTGVFVAIGHEPRSGLV 257
Cdd:PRK07846 195 VNRsgrllRHLDDDiSERFTELASKRWDVR--LGRNVVGVSQDGSGVTLRLDD-----GSTVEADVLLVATGRVPNGDLL 267
|
170 180 190
....*....|....*....|....*....|....*..
2A87_A 258 REA---IDVDPDGYVLVQ--GRTTStslPGVFAAGDL 289
Cdd:PRK07846 268 DAAaagVDVDEDGRVVVDeyQRTSA---EGVFALGDV 301
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
17-288 |
3.53e-05 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 45.24 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 17 VIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTT---------------TDVENYPGFRNGITGPE--------- 72
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTdcvpsktliataevrTELRRAAELGIRFIDDGearvdlpav 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 73 ---LMDEMREQALRFGADLRMEDVESVSLHGPLK---------SVVTADG--QTHRARAVILAMGAAARYLqvPGeqell 138
Cdd:PRK07845 84 narVKALAAAQSADIRARLEREGVRVIAGRGRLIdpglgphrvKVTTADGgeETLDADVVLIATGASPRIL--PT----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 139 grgvsscATCDG---FFFRD--------QDIAVIGGGDSAMEEATFLTRFARSVTLVHRRDefrasKIM----LDRARnn 203
Cdd:PRK07845 157 -------AEPDGeriLTWRQlydldelpEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRD-----RVLpgedADAAE-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 204 dkirflTNHTVVAVDGDTTVTGLR---VRDTNTGAETTLP----VTG--VFVAIGHEPRS---GLVREAIDVDPDGYVLV 271
Cdd:PRK07845 223 ------VLEEVFARRGMTVLKRSRaesVERTGDGVVVTLTdgrtVEGshALMAVGSVPNTaglGLEEAGVELTPSGHITV 296
|
330
....*....|....*..
2A87_A 272 QgRTTSTSLPGVFAAGD 288
Cdd:PRK07845 297 D-RVSRTSVPGIYAAGD 312
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
15-65 |
4.24e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 45.23 E-value: 4.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
2A87_A 15 RDVIVIGSGPAGYTAALYAARAQLAPLVFE-GTSFGGALMTttdvENYPGFR 65
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEkNDTPGGRART----FERPGFR 51
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
16-290 |
5.94e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 44.53 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFE-------GTSFGGalmTTTDVENYPGfRNGITGPELMDEMREQALRFG--- 85
Cdd:PRK06327 6 DVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGG---TCLNVGCIPS-KALLASSEEFENAGHHFADHGihv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 86 ADLRMeDVES------------------------VSL---HGPLKS---------VVTADGQTHRARAVILAMGAAARYL 129
Cdd:PRK06327 82 DGVKI-DVAKmiarkdkvvkkmtggieglfkknkITVlkgRGSFVGktdagyeikVTGEDETVITAKHVIIATGSEPRHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 130 -QVPGEQELLGRGVSSCAtcdgFFFRDQDIAVIGGGDSAMEEATFLTRFARSVTLVHRRDEFRA------SKIMLDrARN 202
Cdd:PRK06327 161 pGVPFDNKIILDNTGALN----FTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAaadeqvAKEAAK-AFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 203 NDKIRFLTNHTVvavdGDTTVTGLRVRDTNT---GAETTLPVTGVFVAIGHEPRS-GLVREAI--DVDPDGYVLVQGrTT 276
Cdd:PRK06327 236 KQGLDIHLGVKI----GEIKTGGKGVSVAYTdadGEAQTLEVDKLIVSIGRVPNTdGLGLEAVglKLDERGFIPVDD-HC 310
|
330
....*....|....
2A87_A 277 STSLPGVFAAGDLV 290
Cdd:PRK06327 311 RTNVPNVYAIGDVV 324
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
16-84 |
9.21e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 43.96 E-value: 9.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSF-GGALMTTTDVENYPGFRNGIT-GPelmDEMREQALRF 84
Cdd:PRK12843 18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYvGGTTATSAGTTWIPGTRHGLAvGP---DDSLEAARTY 85
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
16-50 |
9.82e-05 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 43.46 E-value: 9.82e-05
10 20 30
....*....|....*....|....*....|....*
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGG 50
Cdd:TIGR02032 2 DVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
19-62 |
2.92e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 42.18 E-value: 2.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
2A87_A 19 VIGSGPAGYTAALYAARAQLAPLVFEGTSFGGALMTTTDVENYP 62
Cdd:PRK07233 4 IVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLP 47
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
15-92 |
3.06e-04 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 42.13 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 15 RDVIVIGSGPAGYTAALYAARAQLAPLVFEGTS-FGGALMTttdvENYPGFRngI-TGPELMDEMREQALRFGADLRMED 92
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDrVGGLIRT----VEVDGFR--IdRGPHSFLTRDPEVLELLRELGLGD 75
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
16-289 |
3.75e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 42.04 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYT-AALYAARAQLAPLVFEGTS-FGGalmTTTDVENYP------GFRNGITGPELMDEMREQALRF-GA 86
Cdd:PRK07251 5 DLIVIGFGKAGKTlAAKLASAGKKVALVEESKAmYGG---TCINIGCIPtktllvAAEKNLSFEQVMATKNTVTSRLrGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 87 DLRMEDVESVSLHGPLKSVVT---------ADGQTHRARAVILAMGAAARYLQVPGEQELLG----RGVSSCATcdgfff 153
Cdd:PRK07251 82 NYAMLAGSGVDLYDAEAHFVSnkvievqagDEKIELTAETIVINTGAVSNVLPIPGLADSKHvydsTGIQSLET------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 154 RDQDIAVIGGGDSAMEEATFLTRFARSVTLVHRRDEF--RASKIMLDRARN---NDKIRFLTNHTVVAVDGDttvtGLRV 228
Cdd:PRK07251 156 LPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTIlpREEPSVAALAKQymeEDGITFLLNAHTTEVKND----GDQV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
2A87_A 229 RDTNTGAetTLPVTGVFVAIGHEPRS---GLVREAIDVDPDGYVLVQgRTTSTSLPGVFAAGDL 289
Cdd:PRK07251 232 LVVTEDE--TYRFDALLYATGRKPNTeplGLENTDIELTERGAIKVD-DYCQTSVPGVFAVGDV 292
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
16-51 |
1.04e-03 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 40.59 E-value: 1.04e-03
10 20 30
....*....|....*....|....*....|....*.
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFEGTSFGGA 51
Cdd:COG1053 5 DVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
101-288 |
1.08e-03 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 40.29 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 101 PLKSVVTADGQTHRARAVILAMGAAARYLQVPG-EQELLGRGVSSCATCDGFFFRDQDIAVIGGGDSAMEEATFLTRFAR 179
Cdd:PRK04965 86 AEAQVVKSQGNQWQYDKLVLATGASAFVPPIPGrELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 180 SVTLVHRRD--------EFRASKimLDRARNNDKIRFLTNHTVVAVdgDTTVTGLRVRDTNtgaETTLPVTGVFVAIGHE 251
Cdd:PRK04965 166 AVTLVDNAAsllaslmpPEVSSR--LQHRLTEMGVHLLLKSQLQGL--EKTDSGIRATLDS---GRSIEVDAVIAAAGLR 238
|
170 180 190
....*....|....*....|....*....|....*...
2A87_A 252 PRSGLVREA-IDVdpdGYVLVQGRTTSTSLPGVFAAGD 288
Cdd:PRK04965 239 PNTALARRAgLAV---NRGIVVDSYLQTSAPDIYALGD 273
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
156-310 |
1.12e-03 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 40.52 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 156 QDIAVIGGGDSAMEEATFLTRFARSVTLVHRRDEF-RASKIM---LDRARNNDKIRFLtNHT----VVAVDGDTTVTglr 227
Cdd:PRK13748 271 ERLAVIGSSVVALELAQAFARLGSKVTILARSTLFfREDPAIgeaVTAAFRAEGIEVL-EHTqasqVAHVDGEFVLT--- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 228 vrdTNTGaetTLPVTGVFVAIGHEPRS---GLVREAIDVDPDGYVLVqGRTTSTSLPGVFAAGDLVDRTyrQAV-TAAGS 303
Cdd:PRK13748 347 ---TGHG---ELRADKLLVATGRAPNTrslALDAAGVTVNAQGAIVI-DQGMRTSVPHIYAAGDCTDQP--QFVyVAAAA 417
|
....*..
2A87_A 304 GCAAAID 310
Cdd:PRK13748 418 GTRAAIN 424
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
18-143 |
1.41e-03 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 40.27 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 18 IVIGSGPAGYTAALYAARAQLAPLVFEGT---------SFGG------ALMTTTDVENYPGfrngitGPELMDEmreqAL 82
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNkkigkklliSGGGrcnltnSCPTPEFVAYYPR------NGKFLRS----AL 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2A87_A 83 -RFGAdlrmEDVES-VSLHGpLKSVVTADGQ----THRARAVILAMgaaarylqvpgEQELLGRGVS 143
Cdd:TIGR00275 71 sRFSN----KDLIDfFESLG-LELKVEEDGRvfpcSDSAADVLDAL-----------LNELKELGVE 121
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
4-51 |
1.46e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 40.47 E-value: 1.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
2A87_A 4 PPVHDRAHHPV-RDVIVIGSGPAGYTAALYAARAQLAPLVFEGTS-FGGA 51
Cdd:PRK06134 1 TPSAAAYPPDLeCDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPvFGGT 50
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
23-127 |
1.60e-03 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 39.57 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 23 GPAGYTAALYAARAQLAPLVFEGTSF------GGALMT-TTDVENYPGFRNGITGP------------------------ 71
Cdd:COG0644 2 GPAGSAAARRLARAGLSVLLLEKGSFpgdkicGGGLLPrALEELEPLGLDEPLERPvrgarfyspggksvelppgrgggy 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
2A87_A 72 -----ELMDEMREQALRFGADLRME-DVESVSLHGPLKSVVTADGQTHRARAVILAMGAAAR 127
Cdd:COG0644 82 vvdraRFDRWLAEQAEEAGAEVRTGtRVTDVLRDDGRVVVRTGDGEEIRADYVVDADGARSL 143
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
106-292 |
1.79e-03 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 39.86 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 106 VTADGQTHRARAVILAMGAAARYLQVPGEQELlgrgVSSCATCDgFFFRDQDIAVIGGGDSAMEEATFLTRFARSVTLVH 185
Cdd:PLN02546 208 VDVDGKLYTARNILIAVGGRPFIPDIPGIEHA----IDSDAALD-LPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 186 RR-------DE----FRASKIMLdRArnndkIRFLTNHTVVAV----DGDTTVtglrvrdtNTGAETTLPVTGVFVAIGH 250
Cdd:PLN02546 283 RQkkvlrgfDEevrdFVAEQMSL-RG-----IEFHTEESPQAIiksaDGSLSL--------KTNKGTVEGFSHVMFATGR 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
2A87_A 251 EPRS---GLVREAIDVDPDGYVLVQgRTTSTSLPGVFAAGDLVDR 292
Cdd:PLN02546 349 KPNTknlGLEEVGVKMDKNGAIEVD-EYSRTSVPSIWAVGDVTDR 392
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
199-287 |
2.06e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 39.84 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 199 RARNnDKIRFL--TNHTVVAVDGDTTVtgLRVRDTNTGAETTLPVTGVFVAIGHEPRSGLVREA----IDVDPDGYVL-- 270
Cdd:COG1148 359 RARE-DGVRFIrgRVAEIEEDEGGKLV--VTVEDTLLGEPVEIEADLVVLATGMVPSEDNEELAkllkLPLDQDGFFLea 435
|
90
....*....|....*...
2A87_A 271 -VQGRTTSTSLPGVFAAG 287
Cdd:COG1148 436 hPKLRPVETATDGIFLAG 453
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
15-49 |
2.53e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 39.49 E-value: 2.53e-03
10 20 30
....*....|....*....|....*....|....*.
2A87_A 15 RDVIVIGSGPAGYTAALYAARAQLAPLVFE-GTSFG 49
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEkGKKLG 36
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
16-51 |
3.03e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 39.40 E-value: 3.03e-03
10 20 30
....*....|....*....|....*....|....*..
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFE-GTSFGGA 51
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEkSAHFGGS 49
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
16-52 |
3.06e-03 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 39.19 E-value: 3.06e-03
10 20 30
....*....|....*....|....*....|....*...
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFE-GTSFGGAL 52
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEkGQPFGGAT 38
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
16-50 |
3.39e-03 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 39.25 E-value: 3.39e-03
10 20 30
....*....|....*....|....*....|....*.
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFE-GTSFGG 50
Cdd:PRK07843 9 DVVVVGSGAAGMVAALTAAHRGLSTVVVEkAPHYGG 44
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
105-292 |
3.73e-03 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 39.03 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 105 VVTADG--QTHRARAVILAMGAAARYLQVPGeQELlgrgvsSCATCDGFFFRD--QDIAVIGGGDSAMEEATFLTRFARS 180
Cdd:PLN02507 156 VTQLDGtkLRYTAKHILIATGSRAQRPNIPG-KEL------AITSDEALSLEElpKRAVVLGGGYIAVEFASIWRGMGAT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 181 VTLVHRR--------DEFRASKimldrARNND----KIRFLTNHTVVAVDGDttvtGLRVRdTNTGAETTLPVtgVFVAI 248
Cdd:PLN02507 229 VDLFFRKelplrgfdDEMRAVV-----ARNLEgrgiNLHPRTNLTQLTKTEG----GIKVI-TDHGEEFVADV--VLFAT 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
2A87_A 249 GHEP---RSGLVREAIDVDPDGYVLVQgRTTSTSLPGVFAAGDLVDR 292
Cdd:PLN02507 297 GRAPntkRLNLEAVGVELDKAGAVKVD-EYSRTNIPSIWAIGDVTNR 342
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
12-125 |
8.94e-03 |
|
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: 37.48 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 12 HPVRDVIVIGSGPAGYTAALYAARAQLAPLVFEGTSfggALMTTTDVEnypgfrngiTGPELMDEMREQalrfGADLRME 91
Cdd:COG0446 122 FKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAP---RLLGVLDPE---------MAALLEEELREH----GVELRLG 185
|
90 100 110
....*....|....*....|....*....|....*
2A87_A 92 D-VESVSLHGPLKsVVTADGQTHRARAVILAMGAA 125
Cdd:COG0446 186 EtVVAIDGDDKVA-VTLTDGEEIPADLVVVAPGVR 219
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
16-290 |
9.60e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 37.44 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 16 DVIVIGSGPAGYTAALYAARAQLAPLVFE-GTSFGG-----------ALMTTtdVENYPGFR-NG----------ITGPE 72
Cdd:PRK05249 7 DLVVIGSGPAGEGAAMQAAKLGKRVAVIErYRNVGGgcthtgtipskALREA--VLRLIGFNqNPlyssyrvklrITFAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 73 LMD----------EMREQAL-RFGADL-----RMEDVESVslhgplkSVVTADGQTHRARA--VILAMGA-AARYLQVPG 133
Cdd:PRK05249 85 LLAradhvinkqvEVRRGQYeRNRVDLiqgraRFVDPHTV-------EVECPDGEVETLTAdkIVIATGSrPYRPPDVDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 134 EQEllgRGVSScatcDGFFFRDQD---IAVIGGGDSAMEEATFLTRFARSVTLVHRRD---EFRASKI---MLDRARNND 204
Cdd:PRK05249 158 DHP---RIYDS----DSILSLDHLprsLIIYGAGVIGCEYASIFAALGVKVTLINTRDrllSFLDDEIsdaLSYHLRDSG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A87_A 205 -KIRFLTNHTVVAVDGDTTVTGLRvrdtntgAETTLPVTGVFVAIGhepRSGLVR----EAIDVDPD--GYVLVQGrTTS 277
Cdd:PRK05249 231 vTIRHNEEVEKVEGGDDGVIVHLK-------SGKKIKADCLLYANG---RTGNTDglnlENAGLEADsrGQLKVNE-NYQ 299
|
330
....*....|...
2A87_A 278 TSLPGVFAAGDLV 290
Cdd:PRK05249 300 TAVPHIYAVGDVI 312
|
|
| |
