|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
5-440 |
3.46e-121 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 363.98 E-value: 3.46e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 5 RIIIIGGLSAGPSAAAKARRTDENAEIILFEKTEHISYATCGIPYTMSGKIKSRDKLMVVSPELLENRfKVDLHLNEPVI 84
Cdd:PRK09564 2 KIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIKS-GIDVKTEHEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 85 DIDPDAHEVrTHKD-------SYKYDKLIVATGGRAFLPPIKGIdNYENWAFAKTIEDFDEITKKGVIKEADHITIVGAG 157
Cdd:PRK09564 81 KVDAKNKTI-TVKNlktgsifNDTYDKLMIATGARPIIPPIKNI-NLENVYTLKSMEDGLALKELLKDEEIKNIVIIGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 158 LIGLETAENLIHAGKKVTVVELSDHVLVN-WDKKFTQMAANELVRNGVDLKLGVSVIEVNAESN-ELVLSNGERFNTDFM 235
Cdd:PRK09564 159 FIGLEAVEAAKHLGKNVRIIQLEDRILPDsFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKvEGVVTDKGEYEADVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 236 LVSISVKPNTEILVEKGAKHLPNGALIVNEYMETSLADIYAAGDCAAIPNLLIQESGWFPMGTHSNKAGRVAGANAAGAQ 315
Cdd:PRK09564 239 IVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGRH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 316 ETFSGGYGTSIMQLFDYTIARTGLGPKELAKRGVPFESSMIIAGTTPGFYPDPKDIFLEIYYAPDTGVLLGAEMIGEKGV 395
Cdd:PRK09564 319 VSFKGTLGSACIKVLDLEAARTGLTEEEAKKLGIDYKTVFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQIIGKKGA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2175630195 396 DKRVDVLSTAIYAKLTIHDLPRLDLAYAPPFSPAKDPVVVMGYVA 440
Cdd:PRK09564 399 VLRIDALAVAIYAKLTTQELGMMDFCYAPPFARTWDALNVAGNVA 443
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
24-338 |
1.53e-104 |
|
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: 317.14 E-value: 1.53e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 24 RTDENAEIILFEKTEHISYATCGIPYTMSGKIKSRDKLMVVSPELLEnRFKVDLHLNEPVIDIDPDAHEVRTHKD-SYKY 102
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFE-RKGIDVRTGTEVTAIDPEAKTVTLRDGeTLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 103 DKLIVATGGRAFLPPIKGIDNyENWAFAKTIEDFDEITKKGVIKEADHITIVGAGLIGLETAENLIHAGKKVTVVELSDH 182
Cdd:COG0446 80 DKLVLATGARPRPPPIPGLDL-PGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 183 VLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNAESN-ELVLSNGERFNTDFMLVSISVKPNTEILVEKGAKHLPNGAL 261
Cdd:COG0446 159 LLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDKvAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGERGWI 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2175630195 262 IVNEYMETSLADIYAAGDCAAIPNLLIQESGWFPMGTHSNKAGRVAGANAAGAQETFSGGyGTSIMQLFDYTIARTG 338
Cdd:COG0446 239 KVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPGL-GTFISKVFDLCIASTG 314
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
4-441 |
1.53e-77 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 251.24 E-value: 1.53e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 4 NRIIIIGGLSAGPSAAAKARRTDENAEIILFEKTEHISYATCGIPYTMSGKIKSRDKLMVVSPELLENRFKVDLHLNEPV 83
Cdd:PRK13512 2 PKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALAYTPEKFYDRKQITVKTYHEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 84 IDIDPDAH--EVRTHKDSYK----YDKLIVATGGRAFLPPIKgidnyENWAFA-KTIEDFDEITKKGVIKEADHITIVGA 156
Cdd:PRK13512 82 IAINDERQtvTVLNRKTNEQfeesYDKLILSPGASANSLGFE-----SDITFTlRNLEDTDAIDQFIKANQVDKALVVGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 157 GLIGLETAENLIHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNAesNELVLSNGERFNTDFML 236
Cdd:PRK13512 157 GYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAING--NEVTFKSGKVEHYDMII 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 237 VSISVKPNTEILVEKGAKHLPNGALIVNEYMETSLADIYAAGDCAAIPNLLIQESGWFPMGTHSNKAGRVAGANAAG-AQ 315
Cdd:PRK13512 235 EGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLAWGAHRAASIVAEQIAGnDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 316 ETFSGGYGTSIMQLFDYTIARTGLGPKELAKrgvpFESSMIIA--GTTPGFYPDPKDIFLEIYYAPDTGVLLGAEMIGEK 393
Cdd:PRK13512 315 IEFKGFLGNNIVKFFDYTFASVGVKPNELKQ----FDYKMVEVtqGAHANYYPGNSPLHLRVYYDTSNRKILRAAAVGKE 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2175630195 394 GVDKRVDVLSTAIYAKLTIHDLPRLDLAYAPPFSPAKDPVVVMGYVAE 441
Cdd:PRK13512 391 GADKRIDVLSMAMMNQLTVDELTEFEVAYAPPYSHPKDLINMIGYKAK 438
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
5-339 |
2.69e-71 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 233.49 E-value: 2.69e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 5 RIIIIGGLSAGPSAAAKARRTDENAEIILFEKTEHISYATCGIPYTMSGKiKSRDKLMVVSPELLEnRFKVDLHLNEPVI 84
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGE-TDEEDLLLRPADFYE-ENGIDLRLGTRVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 85 DIDPDAHEVRTHK-DSYKYDKLIVATGGRAFLPPIKGIDNYENWAFaKTIEDFDEItkKGVIKEADHITIVGAGLIGLET 163
Cdd:COG1251 81 AIDRAARTVTLADgETLPYDKLVLATGSRPRVPPIPGADLPGVFTL-RTLDDADAL--RAALAPGKRVVVIGGGLIGLEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 164 AENLIHAGKKVTVVELSDHVLVNW-DKKFTQMAANELVRNGVDLKLGVSVIEVNAESN--ELVLSNGERFNTDFMLVSIS 240
Cdd:COG1251 158 AAALRKRGLEVTVVERAPRLLPRQlDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRvtGVRLADGEELPADLVVVAIG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 241 VKPNTEILVEKGAKHlpNGALIVNEYMETSLADIYAAGDCAAIPNLLIQESGwFPMGTHSNKAGRVAGANAAGAQETFSG 320
Cdd:COG1251 238 VRPNTELARAAGLAV--DRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRV-LELVAPAYEQARVAAANLAGGPAAYEG 314
|
330
....*....|....*....
gi 2175630195 321 GYGTSIMQLFDYTIARTGL 339
Cdd:COG1251 315 SVPSTKLKVFGVDVASAGD 333
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
5-280 |
9.91e-58 |
|
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: 194.84 E-value: 9.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 5 RIIIIGGLSAGPSAAAKARRtdENAEIILFEKTEHISYATCGIPYTMSGKIKSRD------KLM-VVSPELLENRFKVDL 77
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQ--LGGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEiaslwaDLYkRKEEVVKKLNNGIEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 78 HLNEPVIDIDPDAHEVRTHKD------SYKYDKLIVATGGRAFLPPIKGIDNYeNWAFAKTIEDFDEITKKGVikeADHI 151
Cdd:pfam07992 80 LLGTEVVSIDPGAKKVVLEELvdgdgeTITYDRLVIATGARPRLPPIPGVELN-VGFLVRTLDSAEALRLKLL---PKRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 152 TIVGAGLIGLETAENLIHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNAESN--ELVLSNGER 229
Cdd:pfam07992 156 VVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDgvEVILKDGTE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2175630195 230 FNTDFMLVSISVKPNTEILVEKGAKHLPNGALIVNEYMETSLADIYAAGDC 280
Cdd:pfam07992 236 IDADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDC 286
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
89-417 |
7.50e-42 |
|
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: 156.40 E-value: 7.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 89 DAHEVR-THKDSYKYDKLIVATGGRAFLPPIKGIDNyenwafaKTIEDFDEITKkgvIKEA-DHITIVGAGLIGLETAEN 166
Cdd:COG1249 117 DPHTVEvTGGETLTADHIVIATGSRPRVPPIPGLDE-------VRVLTSDEALE---LEELpKSLVVIGGGYIGLEFAQI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 167 LIHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSV--IEVNAESNELVLSNGER---FNTDFMLVSISV 241
Cdd:COG1249 187 FARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVtsVEKTGDGVTVTLEDGGGeeaVEADKVLVATGR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 242 KPNTEIL-VEK-GAKHLPNGALIVNEYMETSLADIYAAGDCAAIPNLliqesgwfpmgTH-SNKAGRVAGANAAGAQETf 318
Cdd:COG1249 267 RPNTDGLgLEAaGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQL-----------AHvASAEGRVAAENILGKKPR- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 319 sggygtsimqLFDYT-----------IARTGLGPKELAKRGVPFESSM---------IIAGTTPGfypdpkdiFLEIYYA 378
Cdd:COG1249 335 ----------PVDYRaipsvvftdpeIASVGLTEEEAREAGIDVKVGKfpfaangraLALGETEG--------FVKLIAD 396
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2175630195 379 PDTGVLLGAEMIGEkgvdkRVD----VLSTAIYAKLTIHDLPR 417
Cdd:COG1249 397 AETGRILGAHIVGP-----HAGelihEAALAMEMGLTVEDLAD 434
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
6-283 |
1.71e-37 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 142.36 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 6 IIIIGGLSAGPSAAAKARRTDENAEIILFEKTEHISYATCGIPYTMSgKIKSRDKLMVVSPELLENRFKVDLHLNEPVID 85
Cdd:PRK04965 5 IVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVFS-QGQRADDLTRQSAGEFAEQFNLRLFPHTWVTD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 86 IDPDAHEVRTHKDSYKYDKLIVATGGRAFLPPIKGidnYENWAFAKTIEDFDEITKKgvIKEADHITIVGAGLIGLETAE 165
Cdd:PRK04965 84 IDAEAQVVKSQGNQWQYDKLVLATGASAFVPPIPG---RELMLTLNSQQEYRAAETQ--LRDAQRVLVVGGGLIGTELAM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 166 NLIHAGKKVTVVELSDHVLVNWDKKF-TQMAANELVRNGVDLKLG--VSVIEVNAESNELVLSNGERFNTDFMLVSISVK 242
Cdd:PRK04965 159 DLCRAGKAVTLVDNAASLLASLMPPEvSSRLQHRLTEMGVHLLLKsqLQGLEKTDSGIRATLDSGRSIEVDAVIAAAGLR 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2175630195 243 PNTEILVEKGAKhlPNGALIVNEYMETSLADIYAAGDCAAI 283
Cdd:PRK04965 239 PNTALARRAGLA--VNRGIVVDSYLQTSAPDIYALGDCAEI 277
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
6-285 |
1.65e-35 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 141.89 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 6 IIIIGGLSAGPSAAAKAR-RTDENAEIILFEKTEHISYATCGIPYTMSGKiKSRDKLMVVSPELLENRfKVDLHLNEPVI 84
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLkLNRHMFEITIFGEEPHPNYNRILLSSVLQGE-ADLDDITLNSKDWYEKH-GITLYTGETVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 85 DIDPDAHEVRTHKD-SYKYDKLIVATGGRAFLPPIKGIDNYENWAFaKTIEDFDEI------TKKGVIkeadhitiVGAG 157
Cdd:TIGR02374 79 QIDTDQKQVITDAGrTLSYDKLILATGSYPFILPIPGADKKGVYVF-RTIEDLDAImamaqrFKKAAV--------IGGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 158 LIGLETAENLIHAGKKVTVVELSDHVLvnwDKKFTQMAA----NELVRNGVDLKLGVSVIEVNAES--NELVLSNGERFN 231
Cdd:TIGR02374 150 LLGLEAAVGLQNLGMDVSVIHHAPGLM---AKQLDQTAGrllqRELEQKGLTFLLEKDTVEIVGATkaDRIRFKDGSSLE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2175630195 232 TDFMLVSISVKPNTEILVEKGAKhlPNGALIVNEYMETSLADIYAAGDCAAIPN 285
Cdd:TIGR02374 227 ADLIVMAAGIRPNDELAVSAGIK--VNRGIIVNDSMQTSDPDIYAVGECAEHNG 278
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
5-310 |
3.77e-35 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 136.03 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 5 RIIIIGGLSAGPSAAAK-ARRTDENAEIILFEKTEHISYATcGIPYTMSGKIKSRDklmvVSPELLE--NRFKVDLHLNE 81
Cdd:COG1252 3 RIVIVGGGFAGLEAARRlRKKLGGDAEVTLIDPNPYHLFQP-LLPEVAAGTLSPDD----IAIPLREllRRAGVRFIQGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 82 pVIDIDPDAHEVRT-HKDSYKYDKLIVATGGRAFLPPIKGIDNYenwAFA-KTIEDFDEI-------TKKGVIKEADHIT 152
Cdd:COG1252 78 -VTGIDPEARTVTLaDGRTLSYDYLVIATGSVTNFFGIPGLAEH---ALPlKTLEDALALrerllaaFERAERRRLLTIV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 153 IVGAGLIGLETAENLIHAGKK-------------VTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVnaES 219
Cdd:COG1252 154 VVGGGPTGVELAGELAELLRKllrypgidpdkvrITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEV--DA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 220 NELVLSNGERFNTDFMLVSISVKPNtEILVEKGAKHLPNGALIVNEYMET-SLADIYAAGDCAAIPNlliQESGWFPM-G 297
Cdd:COG1252 232 DGVTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAVPD---PDGKPVPKtA 307
|
330
....*....|...
gi 2175630195 298 THSNKAGRVAGAN 310
Cdd:COG1252 308 QAAVQQAKVLAKN 320
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
89-425 |
2.40e-34 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 135.31 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 89 DAHEVRTHKDSYKYDKLIVATGGRafLPPIKGIDNyenwafaktIEDFDEITKKGVIKEAD---HITIVGAGLIGLETAE 165
Cdd:PRK06292 118 DPNTVEVNGERIEAKNIVIATGSR--VPPIPGVWL---------ILGDRLLTSDDAFELDKlpkSLAVIGGGVIGLELGQ 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 166 NLIHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNgVDLKLGVSVIEVNAESNELVLS-----NGERFNTDFMLVSIS 240
Cdd:PRK06292 187 ALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEElekggKTETIEADYVLVATG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 241 VKPNTEIL-VEKGAKHL-PNGALIVNEYMETSLADIYAAGDCAAIPNLLiqesgwfpmgtHS-NKAGRVAGANAAGAQET 317
Cdd:PRK06292 266 RRPNTDGLgLENTGIELdERGRPVVDEHTQTSVPGIYAAGDVNGKPPLL-----------HEaADEGRIAAENAAGDVAG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 318 FsggygtsimqlFDYT-----------IARTGLGPKELAKRGVPFESsmiiagttpGFYP---DPK-------DIFLEIY 376
Cdd:PRK06292 335 G-----------VRYHpipsvvftdpqIASVGLTEEELKAAGIDYVV---------GEVPfeaQGRarvmgknDGFVKVY 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2175630195 377 YAPDTGVLLGAEMIGEkgvdkrvDV------LSTAIYAKLTIHDLprLDLAYAPP 425
Cdd:PRK06292 395 ADKKTGRLLGAHIIGP-------DAehlihlLAWAMQQGLTVEDL--LRMPFYHP 440
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1-417 |
4.27e-31 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 126.09 E-value: 4.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 1 MKRNRIIIIGGLSAGPSAAAKArrTDENAEIILFEKteHISYATC---------------------------GIPYTMS- 52
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARA--AGLGMKVALIER--GLLGGTCvntgcvptktliasaraahlarraaeyGVSVGGPv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 53 ----GKIKSR-DKLMVVSPELLENRFK----VDLHLNEPVIDidpDAHEVRTHKDSYKYDKLIVATGGRAFLPPIKGIDN 123
Cdd:PRK06370 79 svdfKAVMARkRRIRARSRHGSEQWLRglegVDVFRGHARFE---SPNTVRVGGETLRAKRIFINTGARAAIPPIPGLDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 124 ---YENwafaKTIEDFDEITKkgvikeadHITIVGAGLIGLETAENLIHAGKKVTVVELSDHVLVNWDKKFTQMAANELV 200
Cdd:PRK06370 156 vgyLTN----ETIFSLDELPE--------HLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 201 RNGVDLKLGVSVIEVNAESNELVL-----SNGERFNTDFMLVSISVKPNTEIL-VEK-GAKHLPNGALIVNEYMETSLAD 273
Cdd:PRK06370 224 REGIDVRLNAECIRVERDGDGIAVgldcnGGAPEITGSHILVAVGRVPNTDDLgLEAaGVETDARGYIKVDDQLRTTNPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 274 IYAAGDCaaipnlliqESGW-FpmgTH-SNKAGRVAGANAagaqeTFSGGYGTS--IMQLFDYT---IARTGLGPKELAK 346
Cdd:PRK06370 304 IYAAGDC---------NGRGaF---THtAYNDARIVAANL-----LDGGRRKVSdrIVPYATYTdppLARVGMTEAEARK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 347 RGVPFESSM---------IIAGTTPGfypdpkdiFLEIYYAPDTGVLLGAEMIGEKGvDKRVDVLSTAIYAKLTIHDLPR 417
Cdd:PRK06370 367 SGRRVLVGTrpmtrvgraVEKGETQG--------FMKVVVDADTDRILGATILGVHG-DEMIHEILDAMYAGAPYTTLSR 437
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
1-281 |
6.27e-30 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 121.57 E-value: 6.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 1 MKRNRIIIIGGLSAGPSAAAKARRTDENAEIILFEKTEHISYATcgIPYTMSGKIKSRDKLMVVSPE--LLENRfkVDLH 78
Cdd:PRK09754 1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYER--PPLSKSMLLEDSPQLQQVLPAnwWQENN--VHLH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 79 LNEPVIDIDPDAHE-VRTHKDSYKYDKLIVATGGRAFLPPIkgIDNY-ENWAFAKTIEDFDEItkKGVIKEADHITIVGA 156
Cdd:PRK09754 77 SGVTIKTLGRDTRElVLTNGESWHWDQLFIATGAAARPLPL--LDALgERCFTLRHAGDAARL--REVLQPERSVVIVGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 157 GLIGLETAENLIHAGKKVTVVELSDHVLVNWDKKFTQ-MAANELVRNGVDLKLGVSVIEV-NAESNELVLSNGERFNTDF 234
Cdd:PRK09754 153 GTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQrYLLQRHQQAGVRILLNNAIEHVvDGEKVELTLQSGETLQADV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2175630195 235 MLVSISVKPNTEILVEKGAkhLPNGALIVNEYMETSLADIYAAGDCA 281
Cdd:PRK09754 233 VIYGIGISANDQLAREANL--DTANGIVIDEACRTCDPAIFAGGDVA 277
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
446-542 |
2.66e-27 |
|
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440372 [Multi-domain] Cd Length: 106 Bit Score: 105.82 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 446 GNFIEVNVTQAENLIDKQELLtILDVRSPLEIQNnGAIEGSVNIPLDELRNRIEELDPSQPMLVYCAKGLRGYLSSLILA 525
Cdd:COG0607 1 ASVKEISPAELAELLESEDAV-LLDVREPEEFAA-GHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLR 78
|
90
....*....|....*..
gi 2175630195 526 HHGFDTIYNLAGGYTAW 542
Cdd:COG0607 79 RAGYTNVYNLAGGIEAW 95
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
87-415 |
3.95e-26 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 111.36 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 87 DPDAHEVRTHKDSYKYDKLIVATGGRAFLPPIKGIDNYENWafakTIEDFDEITKKgvikeADHITIVGAGLIGLETAEN 166
Cdd:TIGR02053 114 DPKTVKVDLGREVRGAKRFLIATGARPAIPPIPGLKEAGYL----TSEEALALDRI-----PESLAVIGGGAIGVELAQA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 167 LIHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLG--VSVIEVNAE----SNELVLSNGErFNTDFMLVSIS 240
Cdd:TIGR02053 185 FARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSaqVKAVSVRGGgkiiTVEKPGGQGE-VEADELLVATG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 241 VKPNTEIL-VEK-GAKHLPNGALIVNEYMETSLADIYAAGDCAAIPNLLiqesgwfpmgTHSNKAGRVAGANAAgaqetf 318
Cdd:TIGR02053 264 RRPNTDGLgLEKaGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLE----------YVAAKEGVVAAENAL------ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 319 sGGYGTSimqlFDYT-----------IARTGLGPKELAKRGVPFESSMI---------IAGTTPGfypdpkdiFLEIYYA 378
Cdd:TIGR02053 328 -GGANAK----LDLLviprvvftdpaVASVGLTEAEAQKAGIECDCRTLpltnvprarINRDTRG--------FIKLVAE 394
|
330 340 350
....*....|....*....|....*....|....*..
gi 2175630195 379 PDTGVLLGAEMIGEKGVDKrVDVLSTAIYAKLTIHDL 415
Cdd:TIGR02053 395 PGTGKVLGVQVVAPEAAEV-INEAALAIRAGMTVDDL 430
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
466-542 |
4.49e-26 |
|
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.
Pssm-ID: 238782 [Multi-domain] Cd Length: 90 Bit Score: 101.96 E-value: 4.49e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2175630195 466 LTILDVRSPLEIQNnGAIEGSVNIPLDELRNRIEELDPSQPMLVYCAKGLRGYLSSLILAHHGFDtIYNLAGGYTAW 542
Cdd:cd01524 14 VTLIDVRTPQEFEK-GHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFK-VKNLDGGYKTY 88
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
6-281 |
2.79e-25 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 105.97 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 6 IIIIGGLSAGPSAAAKARRtdENAEIILFEKTEH---ISYATC-----GIPYTMSGkiksrdklmvvsPELLEN------ 71
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAAR--AGLKTLVIEGGEPggqLATTKEienypGFPEGISG------------PELAERlreqae 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 72 RFKVDLHLNEpVIDIDPD--AHEVRTHK-DSYKYDKLIVATGGRAFLPPIKGIDNYENwafaktiedfdeitkKGV---- 144
Cdd:COG0492 69 RFGAEILLEE-VTSVDKDdgPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEG---------------RGVsyca 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 145 -----IKEADHITIVGAGLIGLETAENLIHAGKKVTVVELSDHVlvnwdkkftqMAANELVR-----NGVDLKLGVSVIE 214
Cdd:COG0492 133 tcdgfFFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDEL----------RASKILVErlranPKIEVLWNTEVTE 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2175630195 215 VNAES--NELVLSNG-----ERFNTDFMLVSISVKPNTEILVEKGAKHLPNGALIVNEYMETSLADIYAAGDCA 281
Cdd:COG0492 203 IEGDGrvEGVTLKNVktgeeKELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVR 276
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
1-392 |
1.16e-21 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 99.42 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 1 MKRNRIIIIG-GLSAGPSAAAKARRTD-ENAEIILFEKTEHISYATCGIPYTMSGKikSRDKLMVVSPELLEnRFKVDLH 78
Cdd:PRK14989 1 MSKVRLAIIGnGMVGHRFIEDLLDKADaANFDITVFCEEPRIAYDRVHLSSYFSHH--TAEELSLVREGFYE-KHGIKVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 79 LNEPVIDIDPDAHEVRTHKD-SYKYDKLIVATGGRAFLPPIKGIDNYENWAFaKTIEDFDEI------TKKGVIkeadhi 151
Cdd:PRK14989 78 VGERAITINRQEKVIHSSAGrTVFYDKLIMATGSYPWIPPIKGSETQDCFVY-RTIEDLNAIeacarrSKRGAV------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 152 tiVGAGLIGLETAENLIHAGKKVTVVELSDHVLVnwdKKFTQMAANELVRN----GVDLKLGVSVIEVNAESNE----LV 223
Cdd:PRK14989 151 --VGGGLLGLEAAGALKNLGVETHVIEFAPMLMA---EQLDQMGGEQLRRKiesmGVRVHTSKNTLEIVQEGVEarktMR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 224 LSNGERFNTDFMLVSISVKPNTEILVEKGAKHLPNGALIVNEYMETSLADIYAAGDCAAIPNLLiqesgwFPMGTHSNKA 303
Cdd:PRK14989 226 FADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECASWNNRV------FGLVAPGYKM 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 304 GRVAGANAAGAQETFSGGYGTSIMQLFdytiartglgpkelakrGVPFESSMIIAGTTPG-----FYPDPKDIFLEIYYA 378
Cdd:PRK14989 300 AQVAVDHLLGSENAFEGADLSAKLKLL-----------------GVDVGGIGDAHGRTPGarsyvYLDESKEIYKRLIVS 362
|
410
....*....|....
gi 2175630195 379 PDTGVLLGAEMIGE 392
Cdd:PRK14989 363 EDNKTLLGAVLVGD 376
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
89-392 |
8.71e-20 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 92.14 E-value: 8.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 89 DAHEVRTHKDS-----YKYDKLIVATGGRAFLPPIKGIDNyenwafaKTIEDFDEITkkGVIKEADHITIVGAGLIGLET 163
Cdd:PRK05249 120 DPHTVEVECPDgevetLTADKIVIATGSRPYRPPDVDFDH-------PRIYDSDSIL--SLDHLPRSLIIYGAGVIGCEY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 164 AENLIHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSV--IEVNAESNELVLSNGERFNTDFMLVSISV 241
Cdd:PRK05249 191 ASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVekVEGGDDGVIVHLKSGKKIKADCLLYANGR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 242 KPNTEILvekgakHLPN--------GALIVNEYMETSLADIYAAGDCAAIPNLliqesgwfpmGTHSNKAGRVAGANAAG 313
Cdd:PRK05249 271 TGNTDGL------NLENagleadsrGQLKVNENYQTAVPHIYAVGDVIGFPSL----------ASASMDQGRIAAQHAVG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 314 AQE-TFSGGYGTSImqlfdYT---IARTGLGPKELAKRGVPFE---------SSMIIAGTTPGfypdpkdiFLEIYYAPD 380
Cdd:PRK05249 335 EATaHLIEDIPTGI-----YTipeISSVGKTEQELTAAKVPYEvgrarfkelARAQIAGDNVG--------MLKILFHRE 401
|
330
....*....|..
gi 2175630195 381 TGVLLGAEMIGE 392
Cdd:PRK05249 402 TLEILGVHCFGE 413
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
455-542 |
2.70e-19 |
|
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.
Pssm-ID: 238089 [Multi-domain] Cd Length: 89 Bit Score: 82.73 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 455 QAENLIDKQELLtILDVRSPLEIQNnGAIEGSVNIPLDELRNRI--EELDPSQPMLVYCAKGLRGYLSSLILAHHGFDTI 532
Cdd:cd00158 1 ELKELLDDEDAV-LLDVREPEEYAA-GHIPGAINIPLSELEERAalLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNV 78
|
90
....*....|
gi 2175630195 533 YNLAGGYTAW 542
Cdd:cd00158 79 YNLEGGMLAW 88
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
87-391 |
5.88e-19 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 89.82 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 87 DPDAHEVRTHKDS--YKYDKLIVATGGRAFLPP-IKgIDNyenwafaKTIEDFDEITKKGVIKEadHITIVGAGLIGLET 163
Cdd:PRK06416 118 DPNTVRVMTEDGEqtYTAKNIILATGSRPRELPgIE-IDG-------RVIWTSDEALNLDEVPK--SLVVIGGGYIGVEF 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 164 AE---NLihaGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEV--NAESNELVLSNGERFNT---DFM 235
Cdd:PRK06416 188 ASayaSL---GAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVeqTDDGVTVTLEDGGKEETleaDYV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 236 LVSISVKPNTEI--LVEKGAKhLPNGALIVNEYMETSLADIYAAGDCAAIPNLliqesgwfpmgTHsnKA---GRVAGAN 310
Cdd:PRK06416 265 LVAVGRRPNTENlgLEELGVK-TDRGFIEVDEQLRTNVPNIYAIGDIVGGPML-----------AH--KAsaeGIIAAEA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 311 AAGAQE----------TFSggygtsimqlfDYTIARTGLGPKELAKRGVPFESSM---------IIAGTTPGfypdpkdi 371
Cdd:PRK06416 331 IAGNPHpidyrgipavTYT-----------HPEVASVGLTEAKAKEEGFDVKVVKfpfagngkaLALGETDG-------- 391
|
330 340
....*....|....*....|
gi 2175630195 372 FLEIYYAPDTGVLLGAEMIG 391
Cdd:PRK06416 392 FVKLIFDKKDGEVLGAHMVG 411
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
47-286 |
1.08e-17 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 85.59 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 47 IPYTMSGKIKSRDKLMVVSPEL--LENRFkvdlhLNEPVIDIDPDAHEVRTHKDS-----------YKYDKLIVATGGRA 113
Cdd:PTZ00318 51 LPQTTTGTLEFRSICEPVRPALakLPNRY-----LRAVVYDVDFEEKRVKCGVVSksnnanvntfsVPYDKLVVAHGARP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 114 FLPPIKGIDNYENwaFAKTIEDFDEITKKGV--IKEAD-------------HITIVGAGLIGLETAENL----------- 167
Cdd:PTZ00318 126 NTFNIPGVEERAF--FLKEVNHARGIRKRIVqcIERASlpttsveerkrllHFVVVGGGPTGVEFAAELadffrddvrnl 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 168 ---IHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNaeSNELVLSNGERFNTDFMLVSISVKPN 244
Cdd:PTZ00318 204 npeLVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVL--DKEVVLKDGEVIPTGLVVWSTGVGPG 281
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2175630195 245 TeILVEKGAKHLPNGALIVNEYMETS-LADIYAAGDCAAIPNL 286
Cdd:PTZ00318 282 P-LTKQLKVDKTSRGRISVDDHLRVKpIPNVFALGDCAANEER 323
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
103-279 |
3.53e-17 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 84.03 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 103 DKLIVATGGRAFLPPIKGIDNYENWAFAKTIEDFDEITKKgvikeadhITIVGAGLIGLETAENLIHAGKKVTVVELSDH 182
Cdd:PRK07251 120 ETIVINTGAVSNVLPIPGLADSKHVYDSTGIQSLETLPER--------LGIIGGGNIGLEFAGLYNKLGSKVTVLDAAST 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 183 VLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNAESNELVLS-NGERFNTDFMLVSISVKPNTEIL-VEKGA-KHLPNG 259
Cdd:PRK07251 192 ILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKNDGDQVLVVtEDETYRFDALLYATGRKPNTEPLgLENTDiELTERG 271
|
170 180
....*....|....*....|
gi 2175630195 260 ALIVNEYMETSLADIYAAGD 279
Cdd:PRK07251 272 AIKVDDYCQTSVPGVFAVGD 291
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
89-286 |
1.17e-16 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 82.51 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 89 DAHEVRTHKDSYKYDKLIVATGGRAFLPPIKG----IDNyeNWAFAktiedFDEITKKgvikeadhITIVGAGLIGLETA 164
Cdd:PRK06116 119 DAHTVEVNGERYTADHILIATGGRPSIPDIPGaeygITS--DGFFA-----LEELPKR--------VAVVGAGYIAVEFA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 165 eNLIHA-GKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNAESN---ELVLSNGERFNTDFMLVSIS 240
Cdd:PRK06116 184 -GVLNGlGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADgslTLTLEDGETLTVDCLIWAIG 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2175630195 241 VKPNTEIL-VEK-GAKHLPNGALIVNEYMETSLADIYAAGDCAAIPNL 286
Cdd:PRK06116 263 REPNTDGLgLENaGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVEL 310
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
451-542 |
6.29e-15 |
|
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.
Pssm-ID: 238724 [Multi-domain] Cd Length: 103 Bit Score: 70.53 E-value: 6.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 451 VNVTQAENLIDKQELLtILDVRSPLEIQNNGAIEGSVNIPLDELRNRIE--------ELDPSQPMLVYCAKGLRGYLSSL 522
Cdd:cd01447 1 LSPEDARALLGSPGVL-LVDVRDPRELERTGMIPGAFHAPRGMLEFWADpdspyhkpAFAEDKPFVFYCASGWRSALAGK 79
|
90 100
....*....|....*....|
gi 2175630195 523 ILAHHGFDTIYNLAGGYTAW 542
Cdd:cd01447 80 TLQDMGLKPVYNIEGGFKDW 99
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
103-391 |
1.55e-14 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 76.12 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 103 DKLIVATGGRAFLPPIKGIDNyenwafaKTIED------FDEITKKgvikeadhITIVGAGLIGLETAENLIHAGKKVTV 176
Cdd:PRK06327 147 KHVIIATGSEPRHLPGVPFDN-------KIILDntgalnFTEVPKK--------LAVIGAGVIGLELGSVWRRLGAEVTI 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 177 VELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNAESNELVLS------NGERFNTDFMLVSISVKPNTE-ILV 249
Cdd:PRK06327 212 LEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAytdadgEAQTLEVDKLIVSIGRVPNTDgLGL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 250 EK-GAKHLPNGALIVNEYMETSLADIYAAGDCAaipnlliqeSGWfpMGTHsnKA---GRVAGANAAGAQETFSggYGT- 324
Cdd:PRK06327 292 EAvGLKLDERGFIPVDDHCRTNVPNVYAIGDVV---------RGP--MLAH--KAeeeGVAVAERIAGQKGHID--YNTi 356
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2175630195 325 -SIMqlfdYT---IARTGLGPKELAKRGVPFEssmiiAGTTPgFYPDPK-------DIFLEIYYAPDTGVLLGAEMIG 391
Cdd:PRK06327 357 pWVI----YTspeIAWVGKTEQQLKAEGVEYK-----AGKFP-FMANGRalamgepDGFVKIIADAKTDEILGVHVIG 424
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
468-542 |
2.22e-14 |
|
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.
Pssm-ID: 425764 [Multi-domain] Cd Length: 92 Bit Score: 68.66 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 468 ILDVRSPLEIqNNGAIEGSVNIP----------LDELRNRIEELDPSQPMLVYCAKGLRGYLSSLILAHHGFDTIYNLAG 537
Cdd:pfam00581 8 LIDVRPPEEY-AKGHIPGAVNVPlsslslpplpLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLDG 86
|
....*
gi 2175630195 538 GYTAW 542
Cdd:pfam00581 87 GFEAW 91
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
103-391 |
2.71e-14 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 74.99 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 103 DKLIVATGGRAFLPPI---KGIDNYENwafaKTIEDFDEITKkgvikeadHITIVGAGLIGLETAENLIHAGKKVTVVEL 179
Cdd:PRK07846 130 DQVVIAAGSRPVIPPViadSGVRYHTS----DTIMRLPELPE--------SLVIVGGGFIAAEFAHVFSALGVRVTVVNR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 180 SDHVLVNWD----KKFTqmaanELVRNGVDLKLGVSVIEV--NAESNELVLSNGERFNTDFMLVSISVKPNTEIL-VEK- 251
Cdd:PRK07846 198 SGRLLRHLDddisERFT-----ELASKRWDVRLGRNVVGVsqDGSGVTLRLDDGSTVEADVLLVATGRVPNGDLLdAAAa 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 252 GAKHLPNGALIVNEYMETSLADIYAAGDCAAiPNLLiqesgwfpmgTH-SNKAGRVAGANAAGAQEtfsggygtsiMQLF 330
Cdd:PRK07846 273 GVDVDEDGRVVVDEYQRTSAEGVFALGDVSS-PYQL----------KHvANHEARVVQHNLLHPDD----------LIAS 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2175630195 331 DY-----------TIARTGLGPKELAKRGVPFESSMI-IAGTTPGFYPDPKDIFLEIYYAPDTGVLLGAEMIG 391
Cdd:PRK07846 332 DHrfvpaavfthpQIASVGLTENEARAAGLDITVKVQnYGDVAYGWAMEDTTGFVKLIADRDTGRLLGAHIIG 404
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
89-279 |
4.99e-14 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 74.28 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 89 DAHEVRTHKDS----YKYDKLIVATGGRAFLPPIKGIdnyenwafAKTIEDFDEITKKGVIKEADHITIVGAGLIGLETA 164
Cdd:PRK08010 103 NNHSLRVHRPEgnleIHGEKIFINTGAQTVVPPIPGI--------TTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 165 ENLIHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNAESNEL-VLSNGERFNTDFMLVSISVKP 243
Cdd:PRK08010 175 SMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVqVHSEHAQLAVDALLIASGRQP 254
|
170 180 190
....*....|....*....|....*....|....*...
gi 2175630195 244 NTEILVEKGAKHLPN--GALIVNEYMETSLADIYAAGD 279
Cdd:PRK08010 255 ATASLHPENAGIAVNerGAIVVDKYLHTTADNIWAMGD 292
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-227 |
6.03e-14 |
|
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: 67.23 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 150 HITIVGAGLIGLETAENLIHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSV--IEVNAESNELVLSNG 227
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVeaIEGNGDGVVVVLTDG 80
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
89-284 |
1.04e-13 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 73.65 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 89 DAHE--VRTHKDSYK---YDKLIVATGGRAFLPPIKGIDNYENWAFAKTIEDfDEITKkgvikeadHITIVGAGLIGLET 163
Cdd:PRK13748 215 DDQTliVRLNDGGERvvaFDRCLIATGASPAVPPIPGLKETPYWTSTEALVS-DTIPE--------RLAVIGSSVVALEL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 164 AENLIHAGKKVTVveLSDHVLVNWDKKFTQMAANELVRN-GVDLKLGVSVIEVNAESNELVLSNGE-RFNTDFMLVSISV 241
Cdd:PRK13748 286 AQAFARLGSKVTI--LARSTLFFREDPAIGEAVTAAFRAeGIEVLEHTQASQVAHVDGEFVLTTGHgELRADKLLVATGR 363
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2175630195 242 KPNTEILV--EKGAKHLPNGALIVNEYMETSLADIYAAGDCAAIP 284
Cdd:PRK13748 364 APNTRSLAldAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP 408
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
466-542 |
1.05e-13 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 67.10 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 466 LTILDVRSPLEIqNNGAIEGSVNIPLDELRNRIEE--------------LDPSQPMLVYCAKGLRGYLSSLILAHHGFDT 531
Cdd:smart00450 5 VVLLDVRSPEEY-EGGHIPGAVNIPLSELLDRRGEldilefeellkrlgLDKDKPVVVYCRSGNRSAKAAWLLRELGFKN 83
|
90
....*....|.
gi 2175630195 532 IYNLAGGYTAW 542
Cdd:smart00450 84 VYLLDGGYKEW 94
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
450-542 |
1.53e-13 |
|
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.
Pssm-ID: 238786 [Multi-domain] Cd Length: 101 Bit Score: 66.65 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 450 EVNVTQ-AENLIDKQELLTILDVRSPLEIQNnGAIEGSVNIPLDELRNRIEELD---PSQPMLVYCAKGLRGYLSSLILA 525
Cdd:cd01528 1 QISVAElAEWLADEREEPVLIDVREPEELEI-AFLPGFLHLPMSEIPERSKELDsdnPDKDIVVLCHHGGRSMQVAQWLL 79
|
90
....*....|....*..
gi 2175630195 526 HHGFDTIYNLAGGYTAW 542
Cdd:cd01528 80 RQGFENVYNLQGGIDAW 96
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
450-544 |
2.30e-13 |
|
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.
Pssm-ID: 238721 [Multi-domain] Cd Length: 96 Bit Score: 66.13 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 450 EVNVTQAENLIDKQELLTILDVRSPLEI-QNNGAIEGSVNIPLDELRNRIEELDPSQPMLVYCAKGLRGYLSSLILAHHG 528
Cdd:cd01444 1 RISVDELAELLAAGEAPVLLDVRDPASYaALPDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80
|
90
....*....|....*.
gi 2175630195 529 FDTIYNLAGGYTAWDR 544
Cdd:cd01444 81 FTDVRSLAGGFEAWRR 96
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
450-545 |
9.25e-13 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 70.04 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 450 EVNVTQAENLIDKQELLtiLDVRSPLEIQNnGAIEGSVNIPLDELRNRIEE--LDPSQPMLVYCAKGLRGYLSSLILAHH 527
Cdd:PRK08762 4 EISPAEARARAAQGAVL--IDVREAHERAS-GQAEGALRIPRGFLELRIEThlPDRDREIVLICASGTRSAHAAATLREL 80
|
90
....*....|....*...
gi 2175630195 528 GFDTIYNLAGGYTAWDRM 545
Cdd:PRK08762 81 GYTRVASVAGGFSAWKDA 98
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
71-278 |
3.76e-11 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 64.17 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 71 NRFKVDLHLNEPVIDIDPDAH--EVRTHKDSYKYDKLIVATG--GRAFLPPI--KGIDNYEnwafaktIEDFDEITKKGV 144
Cdd:pfam13738 86 DHFELPINLFEEVTSVKKEDDgfVVTTSKGTYQARYVIIATGefDFPNKLGVpeLPKHYSY-------VKDFHPYAGQKV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 145 IkeadhitIVGAGLIGLETAENLIHAGKKVTVV----ELSDHV--LVNWDKKFTQMAANELVRNG-VDLKLGVSVIEVNA 217
Cdd:pfam13738 159 V-------VIGGYNSAVDAALELVRKGARVTVLyrgsEWEDRDsdPSYSLSPDTLNRLEELVKNGkIKAHFNAEVKEITE 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2175630195 218 ESNELVL--SNGERFNT-DFMLVSISVKPNTEILVEKGAKHLPNGALIVN-EYMETSLADIYAAG 278
Cdd:pfam13738 232 VDVSYKVhtEDGRKVTSnDDPILATGYHPDLSFLKKGLFELDEDGRPVLTeETESTNVPGLFLAG 296
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
330-429 |
4.45e-11 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 59.87 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 330 FDYTIARTGLGPKELAKRGVPFES-SMIIAGTTPGFYPDPKDIFLEIYYAPDTGVLLGAEMIGeKGVDKRVDVLSTAIYA 408
Cdd:pfam02852 7 TDPEIASVGLTEEEAKEKGGEVKVgKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVG-PNAGELIQEAALAIKM 85
|
90 100
....*....|....*....|.
gi 2175630195 409 KLTIHDLpRLDLAYAPPFSPA 429
Cdd:pfam02852 86 GATVEDL-ANTIHIHPTLSEA 105
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
467-542 |
7.56e-11 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 63.74 E-value: 7.56e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2175630195 467 TILDVRSPLEIQNnGAIEGSVNIPLDELRNRI--EELDPSQPMLVYCAKGLRGYLSSLILAHHGFDTIYNLAGGYTAW 542
Cdd:PRK05597 276 TLIDVREPSEFAA-YSIPGAHNVPLSAIREGAnpPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGW 352
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
97-279 |
9.09e-11 |
|
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: 64.22 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 97 KDSYKYDKLIVATGGRAFLPPIKGIDN--YENWAFAktiedFDEITKKgvikeadhITIVGAGLIGLETAeNLIHA---- 170
Cdd:TIGR01423 147 KERLQAEHILLATGSWPQMLGIPGIEHciSSNEAFY-----LDEPPRR--------VLTVGGGFISVEFA-GIFNAykpr 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 171 GKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKL--GVSVIEVNAE-SNELVLSNGERFNTDFMLVSISVKPNTEI 247
Cdd:TIGR01423 213 GGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTneNPAKVTLNADgSKHVTFESGKTLDVDVVMMAIGRVPRTQT 292
|
170 180 190
....*....|....*....|....*....|....
gi 2175630195 248 LV--EKGAKHLPNGALIVNEYMETSLADIYAAGD 279
Cdd:TIGR01423 293 LQldKVGVELTKKGAIQVDEFSRTNVPNIYAIGD 326
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
89-286 |
1.01e-10 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 64.07 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 89 DAHEVR-THKD----SYKYDKLIVATGGRAFLPPIKGIDnyenwaFAKTIED---FDEITKKGVIkeadhitiVGAGLIG 160
Cdd:PLN02507 150 GPNEVEvTQLDgtklRYTAKHILIATGSRAQRPNIPGKE------LAITSDEalsLEELPKRAVV--------LGGGYIA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 161 LETAENLIHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNAESNEL--VLSNGERFNTDFMLVS 238
Cdd:PLN02507 216 VEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIkvITDHGEEFVADVVLFA 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2175630195 239 ISVKPNTEIL-VEKGAKHLPN-GALIVNEYMETSLADIYAAGDCAAIPNL 286
Cdd:PLN02507 296 TGRAPNTKRLnLEAVGVELDKaGAVKVDEYSRTNIPSIWAIGDVTNRINL 345
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
55-280 |
1.56e-09 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 60.40 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 55 IKSRDKLMVVSPELLENRFKVDLHLNEPVIDIDPDAHEVRTHKDSYKY---DKLIVATGGRAFLPPIKGIDNyenwafak 131
Cdd:PTZ00058 153 FEGKGSLLSENQVLIKKVSQVDGEADESDDDEVTIVSAGVSQLDDGQViegKNILIAVGNKPIFPDVKGKEF-------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 132 TIeDFDEITKkgvIKEADHITIVGAGLIGLETAENLIHAGKKVTVVELSDHVLVNWDKKFTQMAANELVRNGVDL--KLG 209
Cdd:PTZ00058 225 TI-SSDDFFK---IKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELENDMKKNNINIitHAN 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2175630195 210 VSVIEVNAESNELVL--SNGERFNTDFMLVSISVKPNTEILVEKGAKHL-PNGALIVNEYMETSLADIYAAGDC 280
Cdd:PTZ00058 301 VEEIEKVKEKNLTIYlsDGRKYEHFDYVIYCVGRSPNTEDLNLKALNIKtPKGYIKVDDNQRTSVKHIYAVGDC 374
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
89-286 |
7.99e-09 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 58.35 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 89 DAHEVRTHKDSYKYDKLIVATGGRAFLPPIKGIDNYenwafaktiedFDEITKKGVIKEADHITIVGAGLIGLETAEnlI 168
Cdd:PLN02546 204 DPHTVDVDGKLYTARNILIAVGGRPFIPDIPGIEHA-----------IDSDAALDLPSKPEKIAIVGGGYIALEFAG--I 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 169 HAGKK--VTVVELSDHVLVNWDKKFTQMAANELVRNGVDLKLGVS---VIEVNAESNELVLSNGERFNTDFMLVSISVKP 243
Cdd:PLN02546 271 FNGLKsdVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESpqaIIKSADGSLSLKTNKGTVEGFSHVMFATGRKP 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2175630195 244 NTEIL--VEKGAKHLPNGALIVNEYMETSLADIYAAGDCAAIPNL 286
Cdd:PLN02546 351 NTKNLglEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINL 395
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
467-542 |
2.27e-08 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.
Pssm-ID: 238777 [Multi-domain] Cd Length: 106 Bit Score: 51.89 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 467 TILDVRSPLEIQNnGAIEGSVNIPLDELRN--RIEELD-----------PSQPMLVYCAKGLRGYLSSLILAHHGFDTIY 533
Cdd:cd01519 17 VLIDVREPEELKT-GKIPGAINIPLSSLPDalALSEEEfekkygfpkpsKDKELIFYCKAGVRSKAAAELARSLGYENVG 95
|
....*....
gi 2175630195 534 NLAGGYTAW 542
Cdd:cd01519 96 NYPGSWLDW 104
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
451-542 |
4.18e-08 |
|
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.
Pssm-ID: 238726 [Multi-domain] Cd Length: 118 Bit Score: 51.48 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 451 VNVTQAENLIDKQELlTILDVRS----------PLEIQNNGAIEGSVNIP-------------LDELRNRIEEL--DPSQ 505
Cdd:cd01449 1 VTAEEVLANLDSGDV-QLVDARSperfrgevpePRPGLRSGHIPGAVNIPwtslldedgtfksPEELRALFAALgiTPDK 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 2175630195 506 PMLVYCAKGLRGYLSSLILAHHGFDTIYNLAGGYTAW 542
Cdd:cd01449 80 PVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| glpE |
PRK00162 |
thiosulfate sulfurtransferase GlpE; |
448-544 |
3.32e-07 |
|
thiosulfate sulfurtransferase GlpE;
Pssm-ID: 178908 [Multi-domain] Cd Length: 108 Bit Score: 48.86 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 448 FIEVNVTQAENLIDKQELLtILDVRSPLEIQNnGAIEGSVNIPLDELRNRIEELDPSQPMLVYCAKGLRGYLSSLILAHH 527
Cdd:PRK00162 4 FECINVEQAHQKLQEGGAV-LVDIRDPQSFAM-GHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQQ 81
|
90
....*....|....*..
gi 2175630195 528 GFDTIYNLAGGYTAWDR 544
Cdd:PRK00162 82 GFDVVYSIDGGFEAWRR 98
|
|
| RHOD_Lact_B |
cd01523 |
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ... |
454-544 |
9.12e-07 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.
Pssm-ID: 238781 [Multi-domain] Cd Length: 100 Bit Score: 47.49 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 454 TQAENL---IDKQELLTILDVRSPLEIQNNgAIEGSVNIP--------LDELRNRIEELDPSQPMLVYCAKGLRGYLSSL 522
Cdd:cd01523 1 LDPEDLyarLLAGQPLFILDVRNESDYERW-KIDGENNTPyfdpyfdfLEIEEDILDQLPDDQEVTVICAKEGSSQFVAE 79
|
90 100
....*....|....*....|..
gi 2175630195 523 ILAHHGFDTIYnLAGGYTAWDR 544
Cdd:cd01523 80 LLAERGYDVDY-LAGGMKAWSE 100
|
|
| RHOD_ThiF |
cd01526 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ... |
451-542 |
1.11e-06 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.
Pssm-ID: 238784 [Multi-domain] Cd Length: 122 Bit Score: 47.69 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 451 VNVTQAENLIDKQELLTILDVRSPLEIQNnGAIEGSVNIPLDELRNRIEEL----------DPSQPMLVYCAKGLRGYLS 520
Cdd:cd01526 10 VSVKDYKNILQAGKKHVLLDVRPKVHFEI-CRLPEAINIPLSELLSKAAELkslqelpldnDKDSPIYVVCRRGNDSQTA 88
|
90 100
....*....|....*....|...
gi 2175630195 521 SLILAHHGFD-TIYNLAGGYTAW 542
Cdd:cd01526 89 VRKLKELGLErFVRDIIGGLKAW 111
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
455-538 |
9.24e-06 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.
Pssm-ID: 238776 [Multi-domain] Cd Length: 101 Bit Score: 44.49 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 455 QAENLIDKQELLtILDVRSPLEIQNnGAIEGSVNIPLDELRNRIEELDPS------QPMLVYCAKGLRGYLSSLILAHHG 528
Cdd:cd01518 8 EWNELLEDPEVV-LLDVRNDYEYDI-GHFKGAVNPDVDTFREFPFWLDENldllkgKKVLMYCTGGIRCEKASAYLKERG 85
|
90
....*....|
gi 2175630195 529 FDTIYNLAGG 538
Cdd:cd01518 86 FKNVYQLKGG 95
|
|
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
455-542 |
1.10e-05 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 47.09 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 455 QAENLIDKQELL--------TILDVRSPLE--------IQNNGAIEGSVNIP-------------LDELRNRIEEL--DP 503
Cdd:COG2897 135 DPELLADADEVLaalgdpdaVLVDARSPERyrgevepiDPRAGHIPGAVNLPwtdlldedgtfksAEELRALFAALgiDP 214
|
90 100 110
....*....|....*....|....*....|....*....
gi 2175630195 504 SQPMLVYCAKGLRGYLSSLILAHHGFDTIYNLAGGYTAW 542
Cdd:COG2897 215 DKPVITYCGSGVRAAHTWLALELLGYPNVRLYDGSWSEW 253
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
451-542 |
6.50e-05 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 45.47 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 451 VNVTQAENLIDKQELLTILDVRSPLEIQNNgAIEGSVNIPLDELRN--RIEELDPSQPMLVYCAKGLRGYLSSLILAHHG 528
Cdd:PRK07878 289 ITPRELKEWLDSGKKIALIDVREPVEWDIV-HIPGAQLIPKSEILSgeALAKLPQDRTIVLYCKTGVRSAEALAALKKAG 367
|
90
....*....|....
gi 2175630195 529 FDTIYNLAGGYTAW 542
Cdd:PRK07878 368 FSDAVHLQGGVVAW 381
|
|
| PRK10287 |
PRK10287 |
thiosulfate:cyanide sulfurtransferase; Provisional |
469-538 |
6.90e-05 |
|
thiosulfate:cyanide sulfurtransferase; Provisional
Pssm-ID: 182356 [Multi-domain] Cd Length: 104 Bit Score: 42.14 E-value: 6.90e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2175630195 469 LDVRSPLEIQNNgAIEGSVNIPLDELRNRIEEL--DPSQPMLVYCAKGLRGYLSSLILAHHGFDTIYNlAGG 538
Cdd:PRK10287 24 IDVRVPEQYQQE-HVQGAINIPLKEVKERIATAvpDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAEN-AGG 93
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
150-334 |
1.50e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 44.38 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 150 HITIVGAGLIGLETAENLihAG--KKVTVVELSDhvlvnwdkkftQMAANE-LVRngvdlKL----GVSVIeVNAESNEl 222
Cdd:PRK15317 353 RVAVIGGGNSGVEAAIDL--AGivKHVTVLEFAP-----------ELKADQvLQD-----KLrslpNVTII-TNAQTTE- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 223 VLSNGERFN----------------TDFMLVSISVKPNTEILveKGAKHL-PNGALIVNEYMETSLADIYAAGDCAAIPN 285
Cdd:PRK15317 413 VTGDGDKVTgltykdrttgeehhleLEGVFVQIGLVPNTEWL--KGTVELnRRGEIIVDARGATSVPGVFAAGDCTTVPY 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2175630195 286 LLIQESgwfpMGthsnkagrvAGANAA-GAqetfsggygtsimqlFDYTI 334
Cdd:PRK15317 491 KQIIIA----MG---------EGAKAAlSA---------------FDYLI 512
|
|
| 4RHOD_Repeats |
cd01529 |
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ... |
456-542 |
3.41e-04 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.
Pssm-ID: 238787 [Multi-domain] Cd Length: 96 Bit Score: 39.97 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 456 AENLIDKQELLTILDVRSPLEIQNnGAIEGSVNIPLDELRNRIEEL------DPSQPMLVYCAKGLRGYLSSLILAHHGF 529
Cdd:cd01529 3 ADWLGEHEPGTALLDVRAEDEYAA-GHLPGKRSIPGAALVLRSQELqaleapGRATRYVLTCDGSLLARFAAQELLALGG 81
|
90
....*....|...
gi 2175630195 530 DTIYNLAGGYTAW 542
Cdd:cd01529 82 KPVALLDGGTSAW 94
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
86-281 |
1.04e-03 |
|
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: 41.76 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 86 IDPD---AHEVRTHKDSYKYDKLIVATGGRAFLPPIKGIDNYenwafakTIEDFDEITKKgviKEADHITIVGAGLIGLE 162
Cdd:TIGR01438 125 VDKHrikATNKKGKEKIYSAERFLIATGERPRYPGIPGAKEL-------CITSDDLFSLP---YCPGKTLVVGASYVALE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 163 TAENLIHAGKKVTVVELSDhVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNA-ESNELVLSNG------ERFNTdfM 235
Cdd:TIGR01438 195 CAGFLAGIGLDVTVMVRSI-LLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQiEAKVLVEFTDstngieEEYDT--V 271
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2175630195 236 LVSISVKPNTEI--LVEKGAK-HLPNGALIVNEYMETSLADIYAAGDCA 281
Cdd:TIGR01438 272 LLAIGRDACTRKlnLENVGVKiNKKTGKIPADEEEQTNVPYIYAVGDIL 320
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
89-281 |
1.74e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 40.96 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 89 DAHEVR----THKDSYKYDKLIVATGGRAFLPpikgiDNYENwAFAKTIEDFDEITKKgviKEADHITIVGAGLIGLETA 164
Cdd:PTZ00052 128 DEHTVSygdnSQEETITAKYILIATGGRPSIP-----EDVPG-AKEYSITSDDIFSLS---KDPGKTLIVGASYIGLETA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 165 ENLIHAGKKVTVVELSDhVLVNWDKKFTQMAANELVRNGVDLKLGVSVIEVNAESNEL--VLSNG--ERFNTdfMLVSIS 240
Cdd:PTZ00052 199 GFLNELGFDVTVAVRSI-PLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIkvLFSDGttELFDT--VLYATG 275
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2175630195 241 VKPNTEIL-VEKGAKHLPNGALIVNEYMETSLADIYAAGDCA 281
Cdd:PTZ00052 276 RKPDIKGLnLNAIGVHVNKSNKIIAPNDCTNIPNIFAVGDVV 317
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
450-538 |
1.94e-03 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 40.60 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 450 EVNvtqaeNLIDKQELLtILDVRSPLEIQNnGAIEGSVNIPLDELRNRIEE----LDPSQ--PMLVYCAKGLRGYLSSLI 523
Cdd:PRK00142 118 EVN-----ELLDDPDVV-FIDMRNDYEYEI-GHFENAIEPDIETFREFPPWveenLDPLKdkKVVMYCTGGIRCEKASAW 190
|
90
....*....|....*
gi 2175630195 524 LAHHGFDTIYNLAGG 538
Cdd:PRK00142 191 MKHEGFKEVYQLEGG 205
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
150-178 |
1.96e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 40.66 E-value: 1.96e-03
10 20
....*....|....*....|....*....
gi 2175630195 150 HITIVGAGLIGLETAENLIHAGKKVTVVE 178
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLE 32
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
150-183 |
2.67e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 40.29 E-value: 2.67e-03
10 20 30
....*....|....*....|....*....|....
gi 2175630195 150 HITIVGAGLIGLETAENLIHAGKKVTVVELSDHV 183
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVTVLEARDRV 42
|
|
| RHOD_1 |
cd01522 |
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ... |
454-539 |
2.78e-03 |
|
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.
Pssm-ID: 238780 [Multi-domain] Cd Length: 117 Bit Score: 37.69 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 454 TQAENLIDKQELLTILDVRSPLEIQNNGAIEGSVNIPLDEL----RN-----RIEEL-DPSQPMLVYCAKGLRGYLSSLI 523
Cdd:cd01522 4 AEAWALLQADPQAVLVDVRTEAEWKFVGGVPDAVHVAWQVYpdmeINpnflaELEEKvGKDRPVLLLCRSGNRSIAAAEA 83
|
90
....*....|....*.
gi 2175630195 524 LAHHGFDTIYNLAGGY 539
Cdd:cd01522 84 AAQAGFTNVYNVLEGF 99
|
|
| RHOD_PspE2 |
cd01521 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ... |
466-544 |
3.02e-03 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.
Pssm-ID: 238779 [Multi-domain] Cd Length: 110 Bit Score: 37.72 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 466 LTILDVRSPlEIQNNGAIEGSVNIPLDEL-RNRIEELDPSQPMLVYCAkGLRGYLS---SLILAHHGFDtIYNLAGGYTA 541
Cdd:cd01521 26 FVLVDVRSA-EAYARGHVPGAINLPHREIcENATAKLDKEKLFVVYCD-GPGCNGAtkaALKLAELGFP-VKEMIGGLDW 102
|
...
gi 2175630195 542 WDR 544
Cdd:cd01521 103 WKR 105
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
150-183 |
3.32e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 39.87 E-value: 3.32e-03
10 20 30
....*....|....*....|....*....|....
gi 2175630195 150 HITIVGAGLIGLETAENLIHAGKKVTVVELSDHV 183
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQL 34
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
100-279 |
4.23e-03 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 39.90 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 100 YKYDKLIVATGGRAFLPpikgiDNYEnwafaktIEDFDEITKKGVIKEA---DHITIVGAGLIGLETAENLIHAGKKVTV 176
Cdd:PTZ00153 273 FKVKNIIIATGSTPNIP-----DNIE-------VDQKSVFTSDTAVKLEglqNYMGIVGMGIIGLEFMDIYTALGSEVVS 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175630195 177 VELSDHVLVNWDKKFTQMAANELVRNG-VDLKLGVSVIEVNAESNELVL-----------SNGERFNT--------DFML 236
Cdd:PTZ00153 341 FEYSPQLLPLLDADVAKYFERVFLKSKpVRVHLNTLIEYVRAGKGNQPViighserqtgeSDGPKKNMndiketyvDSCL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2175630195 237 VSISVKPNTEIL-VEKGAKHLPNGALIVNEYMETSLAD------IYAAGD 279
Cdd:PTZ00153 421 VATGRKPNTNNLgLDKLKIQMKRGFVSVDEHLRVLREDqevydnIFCIGD 470
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
6-36 |
4.29e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 39.65 E-value: 4.29e-03
10 20 30
....*....|....*....|....*....|.
gi 2175630195 6 IIIIGGLSAGPSAAAKARRTDENAEIILFEK 36
Cdd:PRK08275 12 ILVIGGGTAGPMAAIKAKERNPALRVLLLEK 42
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
141-178 |
7.62e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 38.51 E-value: 7.62e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2175630195 141 KKGVIKEADHITIVGAGLIGLETAENLIHAGKKVTVVE 178
Cdd:COG0569 88 ERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVID 125
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
147-178 |
9.78e-03 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 38.62 E-value: 9.78e-03
10 20 30
....*....|....*....|....*....|..
gi 2175630195 147 EADHItIVGAGLIGLETAENLIHAGKKVTVVE 178
Cdd:COG3573 5 DADVI-VVGAGLAGLVAAAELADAGRRVLLLD 35
|
|
| |
