|
Name |
Accession |
Description |
Interval |
E-value |
| CoA_CoA_reduc |
TIGR03385 |
CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1. ... |
25-454 |
1.12e-128 |
|
CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1.14), as characterized in Staphylococcus aureus, Pyrococcus horikoshii, and Borrelia burgdorferi, and inferred in several other species on the basis of high levels of CoA and an absence of glutathione as a protective thiol. [Cellular processes, Detoxification]
Pssm-ID: 163244 [Multi-domain] Cd Length: 427 Bit Score: 383.32 E-value: 1.12e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 25 SAAARARRLDETASIVVLEQSEYVSFANCGLPYHLSGEIESRDALLLHTPQSLRAALALDVRTGSRVTAIDRAARTVTVT 104
Cdd:TIGR03385 1 SAASRVRRLDKESDIIVFEKTEDVSFANCGLPYVIGGVIDDRNKLLAYTPEVFIKKRGIDVKTNHEVIEVNDERQTVVVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 105 HADG--TYELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALTARvaaLPADGPRRAVVVGAGFIGLEAVEALA 182
Cdd:TIGR03385 81 NNKTneTYEESYDYLILSPGASPIVPNIEGINLDIVFTLRNLEDTDAIKQY---IDKNKVENVVIIGGGYIGIEMAEALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 183 ARGLEVALVELADHVL-PPLDAELAPLLADELRAHGVALHLGVSASAVTSTDdgaALVTLSDGTRLPADVVVVNVGVRPA 261
Cdd:TIGR03385 158 ERGKNVTLIHRSERILnKLFDEEMNQIVEEELKKHEINLRLNEEVDSIEGEE---RVKVFTSGGVYQADMVILATGIKPN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 262 SDLARDAGLELGARGAIKVDADQRTSDPYVWAVGDAVEVTQAVTGDTGPVPLAGPANRQGRRAADAMLGRRTTPQApVLG 341
Cdd:TIGR03385 235 SELAKDSGLKLGETGAIWVNEKFQTSVPNIYAAGDVAESHNIITKKPAWVPLAWGANKMGRIAGENIAGNDIEFKG-VLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 342 TAIVRVFGLTAAVTGASQATLARAGVEHETVRIHAGHHAGYFPGAEQVHLVASFAPD-GRLLGAQAVGREGVDKRIDVLA 420
Cdd:TIGR03385 314 TNITKFFDLTIASTGVTENEAKKLNIDYKTVFVKAKTHANYYPGNSPLHLKLIYEKDtRRILGAQAVGKEGADKRIDVLA 393
|
410 420 430
....*....|....*....|....*....|....
gi 502880639 421 TALRAGMTADDLAELELAYAPPYGAAKDPVNMLG 454
Cdd:TIGR03385 394 AAIMAGLTVKDLFFFELAYAPPYSRVWDPLNMAG 427
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
32-356 |
1.00e-111 |
|
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: 336.01 E-value: 1.00e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 32 RLDETASIVVLEQSEYVSFANCGLPYHLSGEIESRDALLLHTPQSLRAAlALDVRTGSRVTAIDRAARTVTVThaDGTyE 111
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERK-GIDVRTGTEVTAIDPEAKTVTLR--DGE-T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 112 LPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALtarVAALPADGPRRAVVVGAGFIGLEAVEALAARGLEVALV 191
Cdd:COG0446 77 LSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADAL---REALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 192 ELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAalVTLSDGTRLPADVVVVNVGVRPASDLARDAGLE 271
Cdd:COG0446 154 ERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDKVA--VTLTDGEEIPADLVVVAPGVRPNTELAKDAGLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 272 LGARGAIKVDADQRTSDPYVWAVGDAVEVTQAVTGDTGPVPLAGPANRQGRRAADAMLGRRTTPQApvLGTAIVRVFGLT 351
Cdd:COG0446 232 LGERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPG--LGTFISKVFDLC 309
|
....*
gi 502880639 352 AAVTG 356
Cdd:COG0446 310 IASTG 314
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
24-458 |
2.28e-105 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 323.92 E-value: 2.28e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 24 MSAAARARRLDETASIVVLEQSEYVSFANCGLPYHLSGEIESRDALLLHTPQSLRAAlALDVRTGSRVTAIDRAARTVTV 103
Cdd:PRK09564 13 MSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIKS-GIDVKTEHEVVKVDAKNKTITV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 104 TH--ADGTYELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALTArvaALPADGPRRAVVVGAGFIGLEAVEAL 181
Cdd:PRK09564 92 KNlkTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKE---LLKDEEIKNIVIIGAGFIGLEAVEAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 182 AARGLEVALVELADHVLP-PLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAALVTlsDGTRLPADVVVVNVGVRP 260
Cdd:PRK09564 169 KHLGKNVRIIQLEDRILPdSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVT--DKGEYEADVVIVATGVKP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 261 ASDLARDAGLELGARGAIKVDADQRTSDPYVWAVGDAVEVTQAVTGDTGPVPLAGPANRQGRRAADAMLGRRtTPQAPVL 340
Cdd:PRK09564 247 NTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGRH-VSFKGTL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 341 GTAIVRVFGLTAAVTGASQATLARAGVEHETVRIHAGHHAGYFPGAEQVHLVASFAPDGR-LLGAQAVGREGVDKRIDVL 419
Cdd:PRK09564 326 GSACIKVLDLEAARTGLTEEEAKKLGIDYKTVFIKDKNHTNYYPGQEDLYVKLIYEADTKvILGGQIIGKKGAVLRIDAL 405
|
410 420 430
....*....|....*....|....*....|....*....
gi 502880639 420 ATALRAGMTADDLAELELAYAPPYGAAKDPVNMLGFVAQ 458
Cdd:PRK09564 406 AVAIYAKLTTQELGMMDFCYAPPFARTWDALNVAGNVAK 444
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
27-458 |
5.40e-90 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 283.98 E-value: 5.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 27 AARARRLDETASIVVLEQSEYVSFANCGLPYHLSGEIESRDALLLHTPQSLRAALALDVRTGSRVTAIDRAARTVTVTH- 105
Cdd:PRK13512 17 ASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALAYTPEKFYDRKQITVKTYHEVIAINDERQTVTVLNr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 106 -ADGTYELPYDALLLAPGAVAVRPPvegLDHPAVHALRTIPDLDALTARVAALPADgprRAVVVGAGFIGLEAVEALAAR 184
Cdd:PRK13512 97 kTNEQFEESYDKLILSPGASANSLG---FESDITFTLRNLEDTDAIDQFIKANQVD---KALVVGAGYISLEVLENLYER 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 185 GLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVtstdDGAAlVTLSDGTRLPADVVVVNVGVRPASDL 264
Cdd:PRK13512 171 GLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAI----NGNE-VTFKSGKVEHYDMIIEGVGTHPNSKF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 265 ARDAGLELGARGAIKVDADQRTSDPYVWAVGDAVEVTQAVTGDTGPVPLAGPANRQGRRAADAMLGRRTTPQAPVLGTAI 344
Cdd:PRK13512 246 IESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGFLGNNI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 345 VRVFGLTAAVTGASQATLARAGVEHetVRIHAGHHAGYFPGAEQVHLVASFAPD-GRLLGAQAVGREGVDKRIDVLATAL 423
Cdd:PRK13512 326 VKFFDYTFASVGVKPNELKQFDYKM--VEVTQGAHANYYPGNSPLHLRVYYDTSnRKILRAAAVGKEGADKRIDVLSMAM 403
|
410 420 430
....*....|....*....|....*....|....*
gi 502880639 424 RAGMTADDLAELELAYAPPYGAAKDPVNMLGFVAQ 458
Cdd:PRK13512 404 MNQLTVDELTEFEVAYAPPYSHPKDLINMIGYKAK 438
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
24-431 |
5.74e-81 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 259.30 E-value: 5.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 24 MSAAARARRLDETASIVVLEQSEYVSFANCGLPYHLSGEIEsRDALLLHtPQSLRAALALDVRTGSRVTAIDRAARTVTV 103
Cdd:COG1251 14 VRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETD-EEDLLLR-PADFYEENGIDLRLGTRVTAIDRAARTVTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 104 thADGTyELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALTARvaalpADGPRRAVVVGAGFIGLEAVEALAA 183
Cdd:COG1251 92 --ADGE-TLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAA-----LAPGKRVVVIGGGLIGLEAAAALRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 184 RGLEVALVELADHVLPP-LDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAAlVTLSDGTRLPADVVVVNVGVRPAS 262
Cdd:COG1251 164 RGLEVTVVERAPRLLPRqLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTG-VRLADGEELPADLVVVAIGVRPNT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 263 DLARDAGLELGaRGaIKVDADQRTSDPYVWAVGDAVEVTQAVTGDTgPVPLAGPANRQGRRAADAMLGRRTTPQAPVLGT 342
Cdd:COG1251 243 ELARAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEHPGPVYGRR-VLELVAPAYEQARVAAANLAGGPAAYEGSVPST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 343 aIVRVFGLTAAVTGASQATlaragvEHETVRIHAGhhAGYFpgaeqVHLVASfapDGRLLGAQAVGREgvdKRIDVLATA 422
Cdd:COG1251 320 -KLKVFGVDVASAGDAEGD------EEVVVRGDPA--RGVY-----KKLVLR---DGRLVGAVLVGDT---SDAGALRQL 379
|
....*....
gi 502880639 423 LRAGMTADD 431
Cdd:COG1251 380 IKNGRPLPP 388
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
24-296 |
8.06e-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: 174.04 E-value: 8.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 24 MSAAARARRLDetASIVVLEQSEYVSFANCGLPYHLSGEIESRDALLL-------HTPQSLRAALALDVRTGSRVTAIDR 96
Cdd:pfam07992 13 LAAALTLAQLG--GKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLwadlykrKEEVVKKLNNGIEVLLGTEVVSIDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 97 AARTVTVTH--ADGTYELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALTArvaalpADGPRRAVVVGAGFIG 174
Cdd:pfam07992 91 GAKKVVLEElvDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRL------KLLPKRVVVVGGGYIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 175 LEAVEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAAlVTLSDGTRLPADVVVV 254
Cdd:pfam07992 165 VELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVE-VILKDGTEIDADLVVV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 502880639 255 NVGVRPASDLARDAGLELGARGAIKVDADQRTSDPYVWAVGD 296
Cdd:pfam07992 244 AIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGD 285
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
98-434 |
5.20e-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: 156.79 E-value: 5.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 98 ARTVTVThadGTYELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALtarvaalpadgPRRAVVVGAGFIGLEA 177
Cdd:COG1249 118 PHTVEVT---GGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEALELEEL-----------PKSLVVIGGGYIGLEF 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 178 VEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAAlVTLSDG---TRLPADVVVV 254
Cdd:COG1249 184 AQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVT-VTLEDGggeEAVEADKVLV 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 255 NVGVRPASD---LARdAGLELGARGAIKVDADQRTSDPYVWAVGDAvevtqavtgdTGPVPLAGPANRQGRRAADAMLGR 331
Cdd:COG1249 263 ATGRRPNTDglgLEA-AGVELDERGGIKVDEYLRTSVPGIYAIGDV----------TGGPQLAHVASAEGRVAAENILGK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 332 rttPQAPVLGTAIVR-VFglT----AAVtGASQATLARAGVEHETVR---------IHAGHHAGYfpgaeqVHLVASfAP 397
Cdd:COG1249 332 ---KPRPVDYRAIPSvVF--TdpeiASV-GLTEEEAREAGIDVKVGKfpfaangraLALGETEGF------VKLIAD-AE 398
|
330 340 350
....*....|....*....|....*....|....*..
gi 502880639 398 DGRLLGAQAVGrEGVDKRIDVLATALRAGMTADDLAE 434
Cdd:COG1249 399 TGRILGAHIVG-PHAGELIHEAALAMEMGLTVEDLAD 434
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
87-361 |
3.36e-38 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 149.98 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 87 TGSRVTAIDRAARTVtVTHADGTyeLPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALTArvaalPADGPRRAV 166
Cdd:TIGR02374 73 TGETVIQIDTDQKQV-ITDAGRT--LSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMA-----MAQRFKKAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 167 VVGAGFIGLEAVEALAARGLEVALVELADHVLP-PLDAELAPLLADELRAHGVALHLGvSASAVTSTDDGAALVTLSDGT 245
Cdd:TIGR02374 145 VIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAkQLDQTAGRLLQRELEQKGLTFLLE-KDTVEIVGATKADRIRFKDGS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 246 RLPADVVVVNVGVRPASDLARDAGLELGarGAIKVDADQRTSDPYVWAVGDAVEVTQAVTGdtgpvpLAGPANRQGRRAA 325
Cdd:TIGR02374 224 SLEADLIVMAAGIRPNDELAVSAGIKVN--RGIIVNDSMQTSDPDIYAVGECAEHNGRVYG------LVAPLYEQAKVLA 295
|
250 260 270
....*....|....*....|....*....|....*..
gi 502880639 326 DAMLGRRTTP-QAPVLGTAIvRVFGLTAAVTGASQAT 361
Cdd:TIGR02374 296 DHICGVECEEyEGSDLSAKL-KLLGVDVWSAGDAQET 331
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
24-326 |
6.43e-36 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 138.34 E-value: 6.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 24 MSAAAR-ARRLDETASIVVLEQSEYVSFANcGLPYHLSGEIESRDALLlhtpqSLRAALA---LDVRTGsRVTAIDRAAR 99
Cdd:COG1252 14 LEAARRlRKKLGGDAEVTLIDPNPYHLFQP-LLPEVAAGTLSPDDIAI-----PLRELLRragVRFIQG-EVTGIDPEAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 100 TVTVthADGTyELPYDALLLAPGAVAVRPPVEGLDHPAvHALRTIPDL----DALTARVAALPADGPRRAVVVGAGFIGL 175
Cdd:COG1252 87 TVTL--ADGR-TLSYDYLVIATGSVTNFFGIPGLAEHA-LPLKTLEDAlalrERLLAAFERAERRRLLTIVVVGGGPTGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 176 EAVEALAAR-------------GLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVtsTDDGaalVTLS 242
Cdd:COG1252 163 ELAGELAELlrkllrypgidpdKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEV--DADG---VTLE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 243 DGTRLPADVVVVNVGVRpASDLARDAGLELGARGAIKVDADQRT-SDPYVWAVGDAVEVTQAvtGDTGPVPLAGPANRQG 321
Cdd:COG1252 238 DGEEIPADTVIWAAGVK-APPLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDP--DGKPVPKTAQAAVQQA 314
|
....*
gi 502880639 322 RRAAD 326
Cdd:COG1252 315 KVLAK 319
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
67-300 |
2.93e-28 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 116.55 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 67 DALLLHTPQSLRAALALDVRTGSRVTAIDRAARTVTVthADGTYelPYDALLLAPGAVAVRPPVEGLDHpavhalrtIPD 146
Cdd:PRK04965 57 DDLTRQSAGEFAEQFNLRLFPHTWVTDIDAEAQVVKS--QGNQW--QYDKLVLATGASAFVPPIPGREL--------MLT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 147 LDALTA-RVAALPADGPRRAVVVGAGFIGLEAVEALAARGLEVALVELADHVLPPL-DAELAPLLADELRAHGVALHLGV 224
Cdd:PRK04965 125 LNSQQEyRAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLmPPEVSSRLQHRLTEMGVHLLLKS 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502880639 225 SASAVTSTDDGAAlVTLSDGTRLPADVVVVNVGVRPASDLARDAGLELGaRGaIKVDADQRTSDPYVWAVGDAVEV 300
Cdd:PRK04965 205 QLQGLEKTDSGIR-ATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVN-RG-IVVDSYLQTSAPDIYALGDCAEI 277
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
84-344 |
2.19e-27 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 115.25 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 84 DVRTG----SRVTAIDRAAR-----TVTVTHADGTYE-LPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALtar 153
Cdd:PRK05249 98 EVRRGqyerNRVDLIQGRARfvdphTVEVECPDGEVEtLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSILSLDHL--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 154 vaalpadgPRRAVVVGAGFIGLEAVEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTD 233
Cdd:PRK05249 175 --------PRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 234 DGaALVTLSDGTRLPADVVVVNVGVRPASD-LARD-AGLELGARGAIKVDADQRTSDPYVWAVGDAVevtqavtgdtGPV 311
Cdd:PRK05249 247 DG-VIVHLKSGKKIKADCLLYANGRTGNTDgLNLEnAGLEADSRGQLKVNENYQTAVPHIYAVGDVI----------GFP 315
|
250 260 270
....*....|....*....|....*....|...
gi 502880639 312 PLAGPANRQGRRAADAMLGRRTTPQAPVLGTAI 344
Cdd:PRK05249 316 SLASASMDQGRIAAQHAVGEATAHLIEDIPTGI 348
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
82-334 |
4.34e-27 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 116.37 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 82 ALDVRTGSRVTAIDRAARTVtvtHADGTYELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALTArvaalPADG 161
Cdd:PRK14989 73 GIKVLVGERAITINRQEKVI---HSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEA-----CARR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 162 PRRAVVVGAGFIGLEAVEALAARGLEVALVELAdhvlPPLDAE-LAPLLADELRAH----GVALHLGVSASAVTST-DDG 235
Cdd:PRK14989 145 SKRGAVVGGGLLGLEAAGALKNLGVETHVIEFA----PMLMAEqLDQMGGEQLRRKiesmGVRVHTSKNTLEIVQEgVEA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 236 AALVTLSDGTRLPADVVVVNVGVRPASDLARDAGLELGARGAIKVDADQRTSDPYVWAVGDAVEVTQAVTGdtgpvpLAG 315
Cdd:PRK14989 221 RKTMRFADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECASWNNRVFG------LVA 294
|
250
....*....|....*....
gi 502880639 316 PANRQGRRAADAMLGRRTT 334
Cdd:PRK14989 295 PGYKMAQVAVDHLLGSENA 313
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
97-435 |
2.09e-25 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 109.47 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 97 AARTVTVTHADGTYELPYDALLLAPGAVAVRPPVEGLDHpavhalRTIPDLD-ALTarvaalPADGPRRAVVVGAGFIGL 175
Cdd:PRK06416 118 DPNTVRVMTEDGEQTYTAKNIILATGSRPRELPGIEIDG------RVIWTSDeALN------LDEVPKSLVVIGGGYIGV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 176 EAVEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAAlVTLSDGTR---LPADVV 252
Cdd:PRK06416 186 EFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQTDDGVT-VTLEDGGKeetLEADYV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 253 VVNVGVRPASDlarDAGLE-LG---ARGAIKVDADQRTSDPYVWAVGDAVevtqavtgdtGPVPLAGPANRQGRRAADAM 328
Cdd:PRK06416 265 LVAVGRRPNTE---NLGLEeLGvktDRGFIEVDEQLRTNVPNIYAIGDIV----------GGPMLAHKASAEGIIAAEAI 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 329 LGRrttpQAPVLGTAIVRVfglT-----AAVTGASQATLARAGVEHETVRIhaghhagYFPG-----AEQ-----VHLVA 393
Cdd:PRK06416 332 AGN----PHPIDYRGIPAV---TythpeVASVGLTEAKAKEEGFDVKVVKF-------PFAGngkalALGetdgfVKLIF 397
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 502880639 394 SfAPDGRLLGAQAVGREgVDKRIDVLATALRAGMTADDLAEL 435
Cdd:PRK06416 398 D-KKDGEVLGAHMVGAR-ASELIQEAQLAINWEATPEDLALT 437
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
162-434 |
7.35e-23 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 101.79 E-value: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 162 PRRAVVVGAGFIGLEAVEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHgVALHLGVSASAVTSTDDGAALVTL 241
Cdd:PRK06292 169 PKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 242 SDG--TRLPADVVVVNVGVRPASDL--ARDAGLELGARGAIKVDADQRTSDPYVWAVGDavevtqaVTGDTgpvPLAGPA 317
Cdd:PRK06292 248 KGGktETIEADYVLVATGRRPNTDGlgLENTGIELDERGRPVVDEHTQTSVPGIYAAGD-------VNGKP---PLLHEA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 318 NRQGRRAADAMLGRRTTPQ--APVLGTaivrVFglT---AAVTGASQATLARAGVEHETvrihaghhaGYFPGAEQ---- 388
Cdd:PRK06292 318 ADEGRIAAENAAGDVAGGVryHPIPSV----VF--TdpqIASVGLTEEELKAAGIDYVV---------GEVPFEAQgrar 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 502880639 389 --------VHLVASfAPDGRLLGAQAVGREGvDKRIDVLATALRAGMTADDLAE 434
Cdd:PRK06292 383 vmgkndgfVKVYAD-KKTGRLLGAHIIGPDA-EHLIHLLAWAMQQGLTVEDLLR 434
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
463-554 |
3.98e-22 |
|
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: 91.18 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 463 GTMPQWTVAEVDAVMASH--LVLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVrdaADGRPVAVHCASGVRAHIATRVV 540
Cdd:COG0607 1 ASVKEISPAELAELLESEdaVLLDVREPEEFAAGHIPGAINIPLGELAERLDEL---PKDKPIVVYCASGGRSAQAAALL 77
|
90
....*....|....*
gi 502880639 541 LAAGLD-ARNLSGGW 554
Cdd:COG0607 78 RRAGYTnVYNLAGGI 92
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
83-330 |
9.00e-21 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 94.61 E-value: 9.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 83 LDVRTGSRVTAIDRAARTVTVTHADgtyELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALtaRVAALPAdgp 162
Cdd:PRK09754 73 VHLHSGVTIKTLGRDTRELVLTNGE---SWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARL--REVLQPE--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 163 RRAVVVGAGFIGLEAVEALAARGLEVALVELADHVL----PPLdaeLAPLLADELRAHGVALHLGvsaSAVTSTDDGAAL 238
Cdd:PRK09754 145 RSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMgrnaPPP---VQRYLLQRHQQAGVRILLN---NAIEHVVDGEKV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 239 V-TLSDGTRLPADVVVVNVGVRPASDLARDAGLElgARGAIKVDADQRTSDPYVWAVGDaVEVTQAVTGDTGPVPLAGPA 317
Cdd:PRK09754 219 ElTLQSGETLQADVVIYGIGISANDQLAREANLD--TANGIVIDEACRTCDPAIFAGGD-VAITRLDNGALHRCESWENA 295
|
250
....*....|...
gi 502880639 318 NRQGRRAADAMLG 330
Cdd:PRK09754 296 NNQAQIAAAAMLG 308
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
467-553 |
1.85e-20 |
|
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: 86.17 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 467 QWTvaEVDAVMASHLVL-DVRSRAEFAGGHLEGALNVPHTELRDRLDEV-RDaadgRPVAVHCASGVRAHIATRVVLAAG 544
Cdd:cd01524 2 QWH--ELDNYRADGVTLiDVRTPQEFEKGHIKGAINIPLDELRDRLNELpKD----KEIIVYCAVGLRGYIAARILTQNG 75
|
....*....
gi 502880639 545 LDARNLSGG 553
Cdd:cd01524 76 FKVKNLDGG 84
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
115-431 |
4.50e-19 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 89.83 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 115 DALLLAPGAVAVRPPVEGLDHpavhalrTIP-----DLDALtarvaalpadgPRRAVVVGAGFIGLEAVEALAARGLEVA 189
Cdd:PRK06116 133 DHILIATGGRPSIPDIPGAEY-------GITsdgffALEEL-----------PKRVAVVGAGYIAVEFAGVLNGLGSETH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 190 LVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAALVTLSDGTRLPADVVVVNVGVRPASD---LAR 266
Cdd:PRK06116 195 LFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTLEDGETLTVDCLIWAIGREPNTDglgLEN 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 267 dAGLELGARGAIKVDADQRTSDPYVWAVGD---AVEVTqavtgdtgPVPLAgpanrQGRRAADAMLGRRTT--------P 335
Cdd:PRK06116 275 -AGVKLNEKGYIIVDEYQNTNVPGIYAVGDvtgRVELT--------PVAIA-----AGRRLSERLFNNKPDekldysniP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 336 QA----PVLGTAivrvfGLTAAvtgASQATLARAGVEHETVRIHAGHHAgyFPGAEQ---VHLVASfAPDGRLLGAQAVG 408
Cdd:PRK06116 341 TVvfshPPIGTV-----GLTEE---EAREQYGEDNVKVYRSSFTPMYTA--LTGHRQpclMKLVVV-GKEEKVVGLHGIG 409
|
330 340
....*....|....*....|...
gi 502880639 409 rEGVDKRIDVLATALRAGMTADD 431
Cdd:PRK06116 410 -FGADEMIQGFAVAIKMGATKAD 431
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
87-297 |
4.82e-19 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 90.26 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 87 TGSRVTAIDRAAR-----TVTVTHADGTyELPYDA--LLLAPGAVAVRPPVEGldhpavHALrtipdldALTARVAALPA 159
Cdd:PLN02507 135 ANAGVKLYEGEGKivgpnEVEVTQLDGT-KLRYTAkhILIATGSRAQRPNIPG------KEL-------AITSDEALSLE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 160 DGPRRAVVVGAGFIGLEAVEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAALV 239
Cdd:PLN02507 201 ELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVI 280
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 240 TlSDGTRLPADVVVVNVGVRPASDLA--RDAGLELGARGAIKVDADQRTSDPYVWAVGDA 297
Cdd:PLN02507 281 T-DHGEEFVADVVLFATGRAPNTKRLnlEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV 339
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
75-296 |
1.08e-18 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 89.11 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 75 QSLRAALALDVRTGsrvTAIDRAARTVTVTHAdgtyELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALtarv 154
Cdd:PRK06370 102 QWLRGLEGVDVFRG---HARFESPNTVRVGGE----TLRAKRIFINTGARAAIPPIPGLDEVGYLTNETIFSLDEL---- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 155 aalpadgPRRAVVVGAGFIGLEAVEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDD 234
Cdd:PRK06370 171 -------PEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGD 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502880639 235 GAA--LVTLSDGTRLPADVVVVNVGVRPASD---LARdAGLELGARGAIKVDADQRTSDPYVWAVGD 296
Cdd:PRK06370 244 GIAvgLDCNGGAPEITGSHILVAVGRVPNTDdlgLEA-AGVETDARGYIKVDDQLRTTNPGIYAAGD 309
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
115-297 |
1.15e-18 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 88.86 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 115 DALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALtarvaalpadgPRRAVVVGAGFIGLEAVEALAARGLEVALVELA 194
Cdd:PRK07846 130 DQVVIAAGSRPVIPPVIADSGVRYHTSDTIMRLPEL-----------PESLVIVGGGFIAAEFAHVFSALGVRVTVVNRS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 195 DHVLPPLDAELAPLLADELRAHgVALHLGVSASAVTSTDDGAALvTLSDGTRLPADVVVVNVGVRPASDL--ARDAGLEL 272
Cdd:PRK07846 199 GRLLRHLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSGVTL-RLDDGSTVEADVLLVATGRVPNGDLldAAAAGVDV 276
|
170 180
....*....|....*....|....*
gi 502880639 273 GARGAIKVDADQRTSDPYVWAVGDA 297
Cdd:PRK07846 277 DEDGRVVVDEYQRTSAEGVFALGDV 301
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
164-244 |
2.61e-18 |
|
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: 79.56 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 164 RAVVVGAGFIGLEAVEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGaALVTLSD 243
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDG-VVVVLTD 79
|
.
gi 502880639 244 G 244
Cdd:pfam00070 80 G 80
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
90-374 |
3.39e-17 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 84.14 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 90 RVTAIDRAARTVTVTHADGT-YELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALtarvaalpadgPRRAVVV 168
Cdd:PRK07845 115 RLIDPGLGPHRVKVTTADGGeETLDADVVLIATGASPRILPTAEPDGERILTWRQLYDLDEL-----------PEHLIVV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 169 GAGFIGLEAVEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGaALVTLSDGTRLP 248
Cdd:PRK07845 184 GSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVERTGDG-VVVTLTDGRTVE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 249 ADVVVVNVGVRP-ASDLA-RDAGLELGARGAIKVDADQRTSDPYVWAVGDAvevtqavtgdTGPVPLAGPANRQGRRAAD 326
Cdd:PRK07845 263 GSHALMAVGSVPnTAGLGlEEAGVELTPSGHITVDRVSRTSVPGIYAAGDC----------TGVLPLASVAAMQGRIAMY 332
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 502880639 327 AMLGRRTTPQApvLGTAIVRVFglTA---AVTGASQATLARAGVEHETVRI 374
Cdd:PRK07845 333 HALGEAVSPLR--LKTVASNVF--TRpeiATVGVSQAAIDSGEVPARTVML 379
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
481-553 |
1.80e-16 |
|
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: 74.64 E-value: 1.80e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502880639 481 LVLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAADgRPVAVHCASGVRAHIATRVVLAAGL-DARNLSGG 553
Cdd:cd00158 12 VLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKD-KPIVVYCRSGNRSARAAKLLRKAGGtNVYNLEGG 84
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
112-332 |
2.45e-16 |
|
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: 81.94 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 112 LPYDALLLAPGAVAVRPPVEGLDHpavhalrtipdldALTARVAALPADGPRRAVVVGAGFIGLE---AVEALAARGLEV 188
Cdd:TIGR01423 150 LQAEHILLATGSWPQMLGIPGIEH-------------CISSNEAFYLDEPPRRVLTVGGGFISVEfagIFNAYKPRGGKV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 189 ALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAALVTLSDGTRLPADVVVVNVGVRPAS-DLARD 267
Cdd:TIGR01423 217 TLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESGKTLDVDVVMMAIGRVPRTqTLQLD 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502880639 268 -AGLELGARGAIKVDADQRTSDPYVWAVGDAvevtqavtgdTGPVPLAGPANRQGRRAADAMLGRR 332
Cdd:TIGR01423 297 kVGVELTKKGAIQVDEFSRTNVPNIYAIGDV----------TDRVMLTPVAINEGAAFVDTVFGNK 352
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
90-306 |
3.10e-16 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 79.78 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 90 RVTAIDRAARTVTVTHADGTyELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIPDLDALTARvaalpadGpRRAVVVG 169
Cdd:COG0492 78 EVTSVDKDDGPFRVTTDDGT-EYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFR-------G-KDVVVVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 170 AGFIGLEAVEALAARGLEVALVeladHVLPPLDAElaPLLADELRAH-GVALHLGVSASAVTSTD--DGAALVTLSDGT- 245
Cdd:COG0492 149 GGDSALEEALYLTKFASKVTLI----HRRDELRAS--KILVERLRANpKIEVLWNTEVTEIEGDGrvEGVTLKNVKTGEe 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502880639 246 -RLPADVVVVNVGVRPASDLARDAGLELGARGAIKVDADQRTSDPYVWAVGDAV--EVTQAVTG 306
Cdd:COG0492 223 kELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRdyKYRQAATA 286
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
162-434 |
5.12e-16 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 80.74 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 162 PRRAVVVGAGFIGLEAVEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAAlVTL 241
Cdd:PRK06327 183 PKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVS-VAY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 242 SDGT----RLPADVVVVNVGVRPASD--LARDAGLELGARGAIKVDADQRTSDPYVWAVGDAVEvtqavtgdtGPVpLAG 315
Cdd:PRK06327 262 TDADgeaqTLEVDKLIVSIGRVPNTDglGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVR---------GPM-LAH 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 316 PANRQGRRAADAMLGrrttpQAPVLGTAIVRVFGLTA---AVTGASQATLARAGVEHEtvrihaghhAGYFPGAEQVHLV 392
Cdd:PRK06327 332 KAEEEGVAVAERIAG-----QKGHIDYNTIPWVIYTSpeiAWVGKTEQQLKAEGVEYK---------AGKFPFMANGRAL 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 502880639 393 ASFAPDG-----------RLLGAQAVGrEGVDKRIDVLATALRAGMTADDLAE 434
Cdd:PRK06327 398 AMGEPDGfvkiiadaktdEILGVHVIG-PNASELIAEAVVAMEFKASSEDIAR 449
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
87-296 |
1.29e-15 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 79.41 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 87 TGSRVTAIDRAAR-----TVTVTHADGTYELPYDALLLAPGAVAVRPPVEGLDHPA-VHALRTIPDLDALtarvaalpad 160
Cdd:PRK07251 87 AGSGVDLYDAEAHfvsnkVIEVQAGDEKIELTAETIVINTGAVSNVLPIPGLADSKhVYDSTGIQSLETL---------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 161 gPRRAVVVGAGFIGLEAVEALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVtSTDDGAALVT 240
Cdd:PRK07251 157 -PERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEV-KNDGDQVLVV 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502880639 241 LSDGTrLPADVVVVNVGVRPASDlarDAGLE-----LGARGAIKVDADQRTSDPYVWAVGD 296
Cdd:PRK07251 235 TEDET-YRFDALLYATGRKPNTE---PLGLEntdieLTERGAIKVDDYCQTSVPGVFAVGD 291
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
478-554 |
2.28e-15 |
|
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: 71.72 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 478 ASHLVLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAAD-----------GRPVAVHCASGVRAHIATRVVLAAGL- 545
Cdd:smart00450 3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFeellkrlgldkDKPVVVYCRSGNRSAKAAWLLRELGFk 82
|
....*....
gi 502880639 546 DARNLSGGW 554
Cdd:smart00450 83 NVYLLDGGY 91
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
481-554 |
1.86e-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: 69.05 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 481 LVLDVRSRAEFAGGHLEGALNVPHTELRDR-------LDEVRDAADGRPVAVHCASGVRAHIATRVVLAAGL-DARNLSG 552
Cdd:pfam00581 7 VLIDVRPPEEYAKGHIPGAVNVPLSSLSLPplpllelLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYkNVYVLDG 86
|
..
gi 502880639 553 GW 554
Cdd:pfam00581 87 GF 88
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
98-434 |
1.50e-13 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 73.26 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 98 ARTVTVTHADGT-YELPYDALLLAPGAVAVRPPVEGLDhpavhalrtipDLDALTARVAALPADGPRRAVVVGAGFIGLE 176
Cdd:PRK13748 216 DQTLIVRLNDGGeRVVAFDRCLIATGASPAVPPIPGLK-----------ETPYWTSTEALVSDTIPERLAVIGSSVVALE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 177 AVEALAARGLEVALveLADHVL-PPLDAELAPLLADELRAHGVALHLGVSASAVTStDDGAALVTLSDGTrLPADVVVVN 255
Cdd:PRK13748 285 LAQAFARLGSKVTI--LARSTLfFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAH-VDGEFVLTTGHGE-LRADKLLVA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 256 VGVRP-ASDLARDA-GLELGARGAIKVDADQRTSDPYVWAVGDAVEVTQAVTgdtgpvpLAGPAnrqGRRAA------DA 327
Cdd:PRK13748 361 TGRAPnTRSLALDAaGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVY-------VAAAA---GTRAAinmtggDA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 328 MLGRRTTPqapvlgtAIVRVFGLTAAVtGASQATLARAGVEHET--------VRIHAGHHAGYFpgaeqVHLVASfAPDG 399
Cdd:PRK13748 431 ALDLTAMP-------AVVFTDPQVATV-GYSEAEAHHDGIETDSrtltldnvPRALANFDTRGF-----IKLVIE-EGSG 496
|
330 340 350
....*....|....*....|....*....|....*
gi 502880639 400 RLLGAQAVGREGvDKRIDVLATALRAGMTADDLAE 434
Cdd:PRK13748 497 RLIGVQAVAPEA-GELIQTAALAIRNRMTVQELAD 530
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
100-362 |
8.40e-13 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 70.43 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 100 TVTVTHADGTYELPYDALLLAPGAVAVRPPVEGLDH-PAVHALRTIPDLDALTARVAalpadgprravVVGAGFIGLEAV 178
Cdd:PRK08010 106 SLRVHRPEGNLEIHGEKIFINTGAQTVVPPIPGITTtPGVYDSTGLLNLKELPGHLG-----------ILGGGYIGVEFA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 179 EALAARGLEVALVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVtSTDDGAALVTLSDGTRLpADVVVVNVGV 258
Cdd:PRK08010 175 SMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERI-SHHENQVQVHSEHAQLA-VDALLIASGR 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 259 RPASD--LARDAGLELGARGAIKVDADQRTSDPYVWAVGD---AVEVTQAVTGDTGPV--PLAGpanrQGRRAADamlGR 331
Cdd:PRK08010 253 QPATAslHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDvtgGLQFTYISLDDYRIVrdELLG----EGKRSTD---DR 325
|
250 260 270
....*....|....*....|....*....|.
gi 502880639 332 RTTPQAPVLGTAIVRVfGLTAAVTGASQATL 362
Cdd:PRK08010 326 KNVPYSVFMTPPLSRV-GMTEEQARESGADI 355
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
468-554 |
1.00e-09 |
|
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: 56.12 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 468 WTVAEVDAVMASH---LVLDVRSRAEFAGGHLEGALNVPHTELRDRLD-----------EVRDAADGrPVAVHCASGVRA 533
Cdd:cd01519 1 YSFEEVKNLPNPHpnkVLIDVREPEELKTGKIPGAINIPLSSLPDALAlseeefekkygFPKPSKDK-ELIFYCKAGVRS 79
|
90 100
....*....|....*....|..
gi 502880639 534 HIATRVVLAAGL-DARNLSGGW 554
Cdd:cd01519 80 KAAAELARSLGYeNVGNYPGSW 101
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
117-296 |
6.40e-09 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 58.73 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 117 LLLAPGAVAVRPPVEGLDHpavhALRTIPDLDaltarvaaLPADgPRRAVVVGAGFIGLEAVEALAARGLEVALVELADH 196
Cdd:PLN02546 220 ILIAVGGRPFIPDIPGIEH----AIDSDAALD--------LPSK-PEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 197 VLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAALVTLSDGTRLPADVVVVNVGVRPAS-DLA-RDAGLELGA 274
Cdd:PLN02546 287 VLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTVEGFSHVMFATGRKPNTkNLGlEEVGVKMDK 366
|
170 180
....*....|....*....|..
gi 502880639 275 RGAIKVDADQRTSDPYVWAVGD 296
Cdd:PLN02546 367 NGAIEVDEYSRTSVPSIWAVGD 388
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
117-302 |
1.52e-08 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 57.32 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 117 LLLAPGAVAVRPPVEGLDHpavhalrTIPDLDALTARvaalpadGPRRAVVVGAGFIGLEAVEALAARGLEVALVELADH 196
Cdd:PTZ00058 206 ILIAVGNKPIFPDVKGKEF-------TISSDDFFKIK-------EAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNR 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 197 VLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDGAALVTLSDGTR-LPADVVVVNVGVRP-ASDLARDAGLELGA 274
Cdd:PTZ00058 272 LLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKyEHFDYVIYCVGRSPnTEDLNLKALNIKTP 351
|
170 180
....*....|....*....|....*...
gi 502880639 275 RGAIKVDADQRTSDPYVWAVGDAVEVTQ 302
Cdd:PTZ00058 352 KGYIKVDDNQRTSVKHIYAVGDCCMVKK 379
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
469-554 |
4.11e-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: 51.86 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 469 TVAEVDAVMASH--LVLDVRSRAEFAG-----------GHLEGALNVPHT-------------ELRDRLDEVRDAADgRP 522
Cdd:cd01449 2 TAEEVLANLDSGdvQLVDARSPERFRGevpeprpglrsGHIPGAVNIPWTslldedgtfkspeELRALFAALGITPD-KP 80
|
90 100 110
....*....|....*....|....*....|...
gi 502880639 523 VAVHCASGVRA-HIATRVVLAAGLDARNLSGGW 554
Cdd:cd01449 81 VIVYCGSGVTAcVLLLALELLGYKNVRLYDGSW 113
|
|
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
470-554 |
4.70e-08 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 54.41 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 470 VAEVDAVMA-----SHLVLDVRSRAEFAG---------GHLEGALNVPHT-------------ELRDRLDEVrDAADGRP 522
Cdd:COG2897 139 LADADEVLAalgdpDAVLVDARSPERYRGevepidpraGHIPGAVNLPWTdlldedgtfksaeELRALFAAL-GIDPDKP 217
|
90 100 110
....*....|....*....|....*....|....*
gi 502880639 523 VAVHCASGVRA-HIAtrVVL-AAGL-DARNLSGGW 554
Cdd:COG2897 218 VITYCGSGVRAaHTW--LALeLLGYpNVRLYDGSW 250
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
342-446 |
1.47e-07 |
|
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: 49.86 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 342 TAIVRVFGLTAAVTGASQATLARAGVEHETVRIHAGH--HAGYFPGAE-QVHLVASfAPDGRLLGAQAVGrEGVDKRIDV 418
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAAngRALAYGDTDgFVKLVAD-RETGKILGAHIVG-PNAGELIQE 78
|
90 100
....*....|....*....|....*...
gi 502880639 419 LATALRAGMTADDLAeLELAYAPPYGAA 446
Cdd:pfam02852 79 AALAIKMGATVEDLA-NTIHIHPTLSEA 105
|
|
| PLN02160 |
PLN02160 |
thiosulfate sulfurtransferase |
470-558 |
3.00e-07 |
|
thiosulfate sulfurtransferase
Pssm-ID: 177819 [Multi-domain] Cd Length: 136 Bit Score: 49.70 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 470 VAEVDAVMAS-HLVLDVRSRAEFAGGHLEGA--------LNVPHTELRDR--LDEVR---DAADGrpVAVHCASGVRAHI 535
Cdd:PLN02160 19 VSQAKTLLQSgHQYLDVRTQDEFRRGHCEAAkivnipymLNTPQGRVKNQefLEQVSsllNPADD--ILVGCQSGARSLK 96
|
90 100
....*....|....*....|....
gi 502880639 536 ATRVVLAAG-LDARNLSGGWISLV 558
Cdd:PLN02160 97 ATTELVAAGyKKVRNKGGGYLAWV 120
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
465-553 |
3.72e-07 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 52.32 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 465 MPQWTVAEVDAVMASHLVL-DVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAADgRPVAVHCASGVRAHIATRVVLAA 543
Cdd:PRK08762 2 IREISPAEARARAAQGAVLiDVREAHERASGQAEGALRIPRGFLELRIETHLPDRD-REIVLICASGTRSAHAAATLREL 80
|
90
....*....|.
gi 502880639 544 GL-DARNLSGG 553
Cdd:PRK08762 81 GYtRVASVAGG 91
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
156-319 |
4.67e-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: 52.55 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 156 ALPADgPRRAVVVGAGFIGLEAVEALAARGLEVAlVELADHVLPPLDAELAPLLADELRAHGVALHLGVSASAVTSTDDg 235
Cdd:TIGR01438 175 SLPYC-PGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEA- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 236 AALVTLSDGTRLPADVVVVNVGVRPASDLARDAGLE-LGAR-----GAIKVDADQRTSDPYVWAVGDAVEVTQAVTgdtg 309
Cdd:TIGR01438 252 KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLEnVGVKinkktGKIPADEEEQTNVPYIYAVGDILEDKPELT---- 327
|
170
....*....|
gi 502880639 310 pvPLAGPANR 319
Cdd:TIGR01438 328 --PVAIQAGR 335
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
114-328 |
5.71e-07 |
|
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: 52.06 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 114 YDALLLAPGAVAVRP-PVEGLDHPAVHA----LRTIpdldALTARVAALPADGpRRAVVVGAGFIGLEAVeALAAR--GL 186
Cdd:COG0493 207 FDAVFLATGAGKPRDlGIPGEDLKGVHSamdfLTAV----NLGEAPDTILAVG-KRVVVIGGGNTAMDCA-RTALRlgAE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 187 EVALVELADHV-LPPLDAELapllaDELRAHGVALHLGVSASAVTSTDDGA--ALVTL--------SDGTR--------- 246
Cdd:COG0493 281 SVTIVYRRTREeMPASKEEV-----EEALEEGVEFLFLVAPVEIIGDENGRvtGLECVrmelgepdESGRRrpvpiegse 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 247 --LPADVVVVNVGVRPASD-LARDAGLELGARGAIKVDA-DQRTSDPYVWAVGDAV----EVTQAVtgdtgpvplagpan 318
Cdd:COG0493 356 ftLPADLVILAIGQTPDPSgLEEELGLELDKRGTIVVDEeTYQTSLPGVFAGGDAVrgpsLVVWAI-------------- 421
|
250
....*....|
gi 502880639 319 RQGRRAADAM 328
Cdd:COG0493 422 AEGRKAARAI 431
|
|
| RHOD_ThiF |
cd01526 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ... |
478-553 |
1.76e-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: 47.30 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 478 ASHLVLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAADGR-------PVAVHCASGVRAHIATRVVLAAGLDA--R 548
Cdd:cd01526 23 KKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLQELPldndkdsPIYVVCRRGNDSQTAVRKLKELGLERfvR 102
|
....*
gi 502880639 549 NLSGG 553
Cdd:cd01526 103 DIIGG 107
|
|
| Acr2p |
cd01531 |
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ... |
482-553 |
2.57e-06 |
|
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.
Pssm-ID: 238789 [Multi-domain] Cd Length: 113 Bit Score: 46.64 E-value: 2.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502880639 482 VLDVRsRAEFAGGHLEGALNVPHTELRDRLDEVRDAADG---RPVAVHCA-SGVRAHIATRvVLAAGLDARNLSGG 553
Cdd:cd01531 22 VVDVR-DEDYAGGHIKGSWHYPSTRFKAQLNQLVQLLSGskkDTVVFHCAlSQVRGPSAAR-KFLRYLDEEDLETS 95
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
467-553 |
4.81e-06 |
|
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: 45.46 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 467 QWTVAEVDAVMASH----LVLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAADGRPVAVHCASGVRAHIATRVVLA 542
Cdd:cd01528 1 QISVAELAEWLADEreepVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLR 80
|
90
....*....|..
gi 502880639 543 AGLDA-RNLSGG 553
Cdd:cd01528 81 QGFENvYNLQGG 92
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
114-328 |
4.88e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 49.02 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 114 YDALLLAPGAVAVRP-PVEGLDHPAVHalrtiPDLDALTA-RVAALPADGP--RRAVVVGAGFIGLEAV----------- 178
Cdd:PRK11749 226 YDAVFIGTGAGLPRFlGIPGENLGGVY-----SAVDFLTRvNQAVADYDLPvgKRVVVIGGGNTAMDAArtakrlgaesv 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 179 --------EALAARGLEVAL-----VELADHVlppldaelAPL--LADELRAHGVAL---HLGVSasavtsTDDGAALVT 240
Cdd:PRK11749 301 tivyrrgrEEMPASEEEVEHakeegVEFEWLA--------APVeiLGDEGRVTGVEFvrmELGEP------DASGRRRVP 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 241 LSDGTR-LPADVVVVNVGVRPASDLARDA-GLELGARGAIKVD-ADQRTSDPYVWAVGDAVE----VTQAVtgdtgpvpl 313
Cdd:PRK11749 367 IEGSEFtLPADLVIKAIGQTPNPLILSTTpGLELNRWGTIIADdETGRTSLPGVFAGGDIVTgaatVVWAV--------- 437
|
250
....*....|....*
gi 502880639 314 agpanRQGRRAADAM 328
Cdd:PRK11749 438 -----GDGKDAAEAI 447
|
|
| SelU |
COG2603 |
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ... |
469-554 |
1.51e-05 |
|
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442015 [Multi-domain] Cd Length: 341 Bit Score: 47.46 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 469 TVAEVDAVMASHLVLDVRSRAEFAGGHLEGALNVP------------------------------HTELRDRLDEVRDAA 518
Cdd:COG2603 6 TLDDFLELLDDDPLIDVRSPVEFAEGHIPGAINLPllddeeraevgtcykqqgpfaaiklghalvSGKLAAHREEAWAFA 85
|
90 100 110
....*....|....*....|....*....|....*...
gi 502880639 519 DGRP-VAVHCA-SGVRAHIATRVVLAAGLDARNLSGGW 554
Cdd:COG2603 86 PKHPrPLVYCWrGGLRSGSVAQWLREAGIDVPRLEGGY 123
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
470-553 |
4.83e-05 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 45.63 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 470 VAEVDAVMASHLVLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAAdGRPVAVHCASGVRAHIATRVVLAAGL-DAR 548
Cdd:PRK05597 265 VPRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSA-GDEVVVYCAAGVRSAQAVAILERAGYtGMS 343
|
....*
gi 502880639 549 NLSGG 553
Cdd:PRK05597 344 SLDGG 348
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
469-553 |
7.97e-05 |
|
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: 42.03 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 469 TVAEVDAVMASH--LVLDVRSRAEF-AGGHLEGALNVPHTELRDRLDEVRDAAD-----GRPVAVHCASGVRAHIATRVV 540
Cdd:cd01447 2 SPEDARALLGSPgvLLVDVRDPRELeRTGMIPGAFHAPRGMLEFWADPDSPYHKpafaeDKPFVFYCASGWRSALAGKTL 81
|
90
....*....|....
gi 502880639 541 LAAGLD-ARNLSGG 553
Cdd:cd01447 82 QDMGLKpVYNIEGG 95
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
114-328 |
8.67e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 45.49 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 114 YDALLLAPGA-VAVRPPVEGLDHPAVhalrtIPDLDALtARVAALPADGPRRAVVVGAGfiGLEAVEAlaARgleVALVE 192
Cdd:PRK12814 279 FDAVLLAVGAqKASKMGIPGEELPGV-----ISGIDFL-RNVALGTALHPGKKVVVIGG--GNTAIDA--AR---TALRL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 193 LADHV----------LPPLDAELapllaDELRAHGVALHLGVSASAVTSTDDGAALVTL--------SDGTRLP------ 248
Cdd:PRK12814 346 GAESVtilyrrtreeMPANRAEI-----EEALAEGVSLRELAAPVSIERSEGGLELTAIkmqqgepdESGRRRPvpvegs 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 249 -----ADVVVVNVGVRPASDLARDAGLELGARGAIKVD-ADQRTSDPYVWAVGDAVevtqavtgdTGPvPLAGPANRQGR 322
Cdd:PRK12814 421 eftlqADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVDpETLQTSVAGVFAGGDCV---------TGA-DIAINAVEQGK 490
|
....*.
gi 502880639 323 RAADAM 328
Cdd:PRK12814 491 RAAHAI 496
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
114-328 |
1.31e-04 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 44.21 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 114 YDALLLAPGAVAVRPP-VEGLDHPAVHalrtiPDLDAL----TARVAALPADGP-----RRAVVVGAGfigLEAVE-ALA 182
Cdd:PRK12770 119 YDAVLIATGTWKSRKLgIPGEDLPGVY-----SALEYLfrirAAKLGYLPWEKVppvegKKVVVVGAG---LTAVDaALE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 183 ARGLEVALVELADHvlppLDAELAPLLADE---LRAHGVALHLGVSASAVTStDDGAALVTL-------SDGTR------ 246
Cdd:PRK12770 191 AVLLGAEKVYLAYR----RTINEAPAGKYEierLIARGVEFLELVTPVRIIG-EGRVEGVELakmrlgePDESGrprpvp 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 247 -------LPADVVVVNVGVRPASDLARDA-GLELGARGAIKVDADQRTSDPYVWAVGDAVevtqavtgdTGPvPLAGPAN 318
Cdd:PRK12770 266 ipgsefvLEADTVVFAIGEIPTPPFAKEClGIELNRKGEIVVDEKHMTSREGVFAAGDVV---------TGP-SKIGKAI 335
|
250
....*....|
gi 502880639 319 RQGRRAADAM 328
Cdd:PRK12770 336 KSGLRAAQSI 345
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
481-537 |
2.18e-04 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 43.68 E-value: 2.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 481 LVLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAAD---GRPVAVHCASGVRAHIAT 537
Cdd:PRK00142 129 VFIDMRNDYEYEIGHFENAIEPDIETFREFPPWVEENLDplkDKKVVMYCTGGIRCEKAS 188
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
70-299 |
2.18e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 44.04 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 70 LLHTPQSLRAALALDVRTG---SRVTAIDRAARTV---TVTHADGTYELPYDA--LLLAPGAvavRPpvegldhpavhal 141
Cdd:PTZ00052 93 LVTTVQNHIRSLNFSYRTGlrsSKVEYINGLAKLKdehTVSYGDNSQEETITAkyILIATGG---RP------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 142 rTIPDlDALTARVAALPADG-------PRRAVVVGAGFIGLEAVEALAARGLEVAlVELADHVLPPLDAELAPLLADELR 214
Cdd:PTZ00052 157 -SIPE-DVPGAKEYSITSDDifslskdPGKTLIVGASYIGLETAGFLNELGFDVT-VAVRSIPLRGFDRQCSEKVVEYMK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 215 AHGVALHLGVSASAVTSTDDGAAlVTLSDGTRLPADVVVVNVGVRPASDlardaGLELGARG------AIKVDADQRTSD 288
Cdd:PTZ00052 234 EQGTLFLEGVVPINIEKMDDKIK-VLFSDGTTELFDTVLYATGRKPDIK-----GLNLNAIGvhvnksNKIIAPNDCTNI 307
|
250
....*....|.
gi 502880639 289 PYVWAVGDAVE 299
Cdd:PTZ00052 308 PNIFAVGDVVE 318
|
|
| RHOD_PspE2 |
cd01521 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ... |
481-553 |
2.36e-04 |
|
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: 40.80 E-value: 2.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502880639 481 LVLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAadGRPVAVHCAsGVRAHIATRVVLA---AGLDARNLSGG 553
Cdd:cd01521 27 VLVDVRSAEAYARGHVPGAINLPHREICENATAKLDK--EKLFVVYCD-GPGCNGATKAALKlaeLGFPVKEMIGG 99
|
|
| 4RHOD_Repeats |
cd01529 |
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ... |
482-556 |
2.47e-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: 40.35 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 482 VLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAA---DGRPVAVHCASGVRAHIATRVVLAAGLDA----RNLSGGW 554
Cdd:cd01529 15 LLDVRAEDEYAAGHLPGKRSIPGAALVLRSQELQALEapgRATRYVLTCDGSLLARFAAQELLALGGKPvallDGGTSAW 94
|
..
gi 502880639 555 IS 556
Cdd:cd01529 95 VA 96
|
|
| RHOD_Lact_B |
cd01523 |
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ... |
482-555 |
2.98e-04 |
|
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: 40.17 E-value: 2.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502880639 482 VLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAA-----DGRPVAVHCASGVRAHIATRVVLAAGLDARNLSGGWI 555
Cdd:cd01523 18 ILDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDIldqlpDDQEVTVICAKEGSSQFVAELLAERGYDVDYLAGGMK 96
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
469-553 |
3.05e-04 |
|
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: 39.94 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 469 TVAEVDAVMASH---LVLDVRSRAEFAG--GHLEGALNVPHtelrDRLDE-VRDAADGRPVAVHCASGVRAHIATRVVLA 542
Cdd:cd01444 3 SVDELAELLAAGeapVLLDVRDPASYAAlpDHIPGAIHLDE----DSLDDwLGDLDRDRPVVVYCYHGNSSAQLAQALRE 78
|
90
....*....|..
gi 502880639 543 AG-LDARNLSGG 553
Cdd:cd01444 79 AGfTDVRSLAGG 90
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
481-553 |
3.86e-04 |
|
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: 39.87 E-value: 3.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502880639 481 LVLDVRSRAEFAGGHLEGALNVPHTELRD---RLDEVRDAADGRPVAVHCASGVRAHIATRVVLAAGL-DARNLSGG 553
Cdd:cd01518 19 VLLDVRNDYEYDIGHFKGAVNPDVDTFREfpfWLDENLDLLKGKKVLMYCTGGIRCEKASAYLKERGFkNVYQLKGG 95
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
269-328 |
8.52e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 42.42 E-value: 8.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 269 GLELGARGAIKVDADQRTSDPYVWAVGDAveVTQAVTgdtgpVPLAGPAnrqGRRAADAM 328
Cdd:PRK12778 696 GLELNRKGTIVVDEEMQSSIPGIYAGGDI--VRGGAT-----VILAMGD---GKRAAAAI 745
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
474-554 |
1.28e-03 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 40.85 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 474 DAVMASH----LVLDVRSRAEFAG-----------GHLEGALNVPHTEL--------RDRLDEVRDAAD---GRPVAVHC 527
Cdd:PRK11493 159 DVLLASHektaQIVDARPAARFNAevdeprpglrrGHIPGALNVPWTELvregelktTDELDAIFFGRGvsfDRPIIASC 238
|
90 100 110
....*....|....*....|....*....|.
gi 502880639 528 ASGVRAHIatrVVLA-AGLDARNLS---GGW 554
Cdd:PRK11493 239 GSGVTAAV---VVLAlATLDVPNVKlydGAW 266
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
167-331 |
1.48e-03 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 41.44 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 167 VVGAGFIGLEAVEALAARGLEVALVELADHVLPPLDAELAPLLADE-LRAHGVALHLGVSASAVTSTDDGAAL-VTLSDG 244
Cdd:PTZ00153 317 IVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLDADVAKYFERVfLKSKPVRVHLNTLIEYVRAGKGNQPViIGHSER 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 245 T----RLPADVVVVNVGVRPASDL--------ARDAGLE-LGA---RGAIKVDADQRT--SDP----YVWAVGDAvevtq 302
Cdd:PTZ00153 397 QtgesDGPKKNMNDIKETYVDSCLvatgrkpnTNNLGLDkLKIqmkRGFVSVDEHLRVlrEDQevydNIFCIGDA----- 471
|
170 180
....*....|....*....|....*....
gi 502880639 303 avtgdTGPVPLAGPANRQGRRAADAMLGR 331
Cdd:PTZ00153 472 -----NGKQMLAHTASHQALKVVDWIEGK 495
|
|
| 4RHOD_Repeat_2 |
cd01533 |
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ... |
466-554 |
2.16e-03 |
|
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue.
Pssm-ID: 238791 [Multi-domain] Cd Length: 109 Bit Score: 37.82 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 466 PQWTVAEVDAVMASH---LVLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVrdAADGR-PVAVHCASGVRAHIATRVVL 541
Cdd:cd01533 10 PSVSADELAALQARGaplVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGEL--APDPRtPIVVNCAGRTRSIIGAQSLI 87
|
90
....*....|....*...
gi 502880639 542 AAGLD-----ARNLSGGW 554
Cdd:cd01533 88 NAGLPnpvaaLRNGTQGW 105
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
74-145 |
2.51e-03 |
|
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: 40.59 E-value: 2.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502880639 74 PQSLRAAL-ALDVRTGSRVTAIDRAARTVTVTHADGTyELPYDALLLAPGAVAVRPPVEGLDHPAVHALRTIP 145
Cdd:COG1232 213 VEALAEALeAGEIRLGTRVTAIEREGGGWRVTTSDGE-TIEADAVVSATPAPALARLLAPLPPEVAAALAGIP 284
|
|
| Cdc25_Acr2p |
cd01443 |
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ... |
481-529 |
2.91e-03 |
|
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).
Pssm-ID: 238720 [Multi-domain] Cd Length: 113 Bit Score: 37.77 E-value: 2.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 502880639 481 LVLDVRsRAEFAGGHLEGALNVPHTELRDRLDEVRDA--ADGRPVAV-HCAS 529
Cdd:cd01443 25 VVVDLR-RDDYEGGHIKGSINLPAQSCYQTLPQVYALfsLAGVKLAIfYCGS 75
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
154-548 |
4.15e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 40.24 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 154 VAALPADGPRRAVVVGAGFIGLEAVEALAARGLEVALVeladHVLPPLDAELAPLLAD--ELRAHGV-----ALHLGVSA 226
Cdd:COG3321 783 VEALLADGVRVFLEVGPGPVLTGLVRQCLAAAGDAVVL----PSLRRGEDELAQLLTAlaQLWVAGVpvdwsALYPGRGR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 227 SAVT--------STDDGAALVTLSDGTRLPADVVVVNVGVRPASDLARDAGLELGARGAIKVDADQRTSDPYVWAVGDAV 298
Cdd:COG3321 859 RRVPlptypfqrEDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAA 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 299 EVTQAVTGDTGPVPLAGPANRQGRRAADAMLGRRTTPQAPVLGTAIVRVFGLTAAVTGASQATLARAGVEHETVRIHAGH 378
Cdd:COG3321 939 AAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAA 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 379 HAGYFPGAEQVHLVASFAPDGRLLGAQAVGREGVDKRIDVLATALRAGMTADDLAELELAYAPPYGAAKDPVNMLGFVAQ 458
Cdd:COG3321 1019 AALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALA 1098
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 459 NVLDGTMPQWTVAEVDAVMASHLVLDVRSRAEFAGGHLEGALNVPHTELRDRLDEVRDAADGRPVAVHCASGVRAHIATR 538
Cdd:COG3321 1099 LAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALA 1178
|
410
....*....|
gi 502880639 539 VVLAAGLDAR 548
Cdd:COG3321 1179 LALAAALAAA 1188
|
|
| PRK11784 |
PRK11784 |
tRNA 2-selenouridine synthase; Provisional |
480-503 |
4.56e-03 |
|
tRNA 2-selenouridine synthase; Provisional
Pssm-ID: 236982 [Multi-domain] Cd Length: 345 Bit Score: 39.43 E-value: 4.56e-03
10 20
....*....|....*....|....
gi 502880639 480 HLVLDVRSRAEFAGGHLEGALNVP 503
Cdd:PRK11784 16 TPLIDVRSPIEFAEGHIPGAINLP 39
|
|
| RHOD_1 |
cd01522 |
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ... |
483-554 |
5.54e-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: 36.92 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502880639 483 LDVRSRAEFAG-GHLEGALNV-----PHTELRDR-LDEVRDAAD-GRPVAVHCASGVRAHIATRVVLAAG---------- 544
Cdd:cd01522 19 VDVRTEAEWKFvGGVPDAVHVawqvyPDMEINPNfLAELEEKVGkDRPVLLLCRSGNRSIAAAEAAAQAGftnvynvleg 98
|
90
....*....|....*..
gi 502880639 545 ----LDA---RNLSGGW 554
Cdd:cd01522 99 fegdLDAaghRGGVNGW 115
|
|
| |
