|
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. ... |
18-441 |
1.45e-170 |
|
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: 490.02 E-value: 1.45e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 18 RLRRLDETAEIVVFERSGYVSYANCGLPYYIGGVITDKEELTLQTPESFWQRFRVDMRVRHEVTAIHPAEKTVDVRNLAT 97
Cdd:TIGR03385 5 RVRRLDKESDIIVFEKTEDVSFANCGLPYVIGGVIDDRNKLLAYTPEVFIKKRGIDVKTNHEVIEVNDERQTVVVRNNKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 98 GETFTESYDKLVLSPGARPTQPALPGVGIDRLFTLRTVEDTLKIREFIEQHHPRSAVLAGGGFIGVELMENLRELGIDVT 177
Cdd:TIGR03385 85 NETYEESYDYLILSPGASPIVPNIEGINLDIVFTLRNLEDTDAIKQYIDKNKVENVVIIGGGYIGIEMAEALRERGKNVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 178 VVQRPRQLLNPL-DADMAAFLHAKLRQKGVRLHLGCTVEgfAANGDRVNVLLKDEAPLTADMVVLAIGVTPDTGLAKAAG 256
Cdd:TIGR03385 165 LIHRSERILNKLfDEEMNQIVEEELKKHEINLRLNEEVD--SIEGEERVKVFTSGGVYQADMVILATGIKPNSELAKDSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 257 LELGIKGSILVNDRMETSAPDIYAVGDAVQVKHFVTGQDTLLSLAGPANKQGRIAADNICGGDSRYPGSQGSSVIKVFDM 336
Cdd:TIGR03385 243 LKLGETGAIWVNEKFQTSVPNIYAAGDVAESHNIITKKPAWVPLAWGANKMGRIAGENIAGNDIEFKGVLGTNITKFFDL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 337 TIATTGVNEKTAKQAGIDCDKVYLSPMSHAGYYPGGKVMTLKVVFEKGTYRLLGAQIVGYEGVDKRIDVLATAIHAGLSA 416
Cdd:TIGR03385 323 TIASTGVTENEAKKLNIDYKTVFVKAKTHANYYPGNSPLHLKLIYEKDTRRILGAQAVGKEGADKRIDVLAAAIMAGLTV 402
|
410 420
....*....|....*....|....*
gi 646496747 417 LQLKDLDLAYAPPYSSAKDPVNMAG 441
Cdd:TIGR03385 403 KDLFFFELAYAPPYSRVWDPLNMAG 427
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
21-342 |
3.80e-139 |
|
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: 405.73 E-value: 3.80e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 21 RLDETAEIVVFERSGYVSYANCGLPYYIGGVITDKEELTLQTPESFwQRFRVDMRVRHEVTAIHPAEKTVDVRnlaTGET 100
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESF-ERKGIDVRTGTEVTAIDPEAKTVTLR---DGET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 101 ftESYDKLVLSPGARPTQPALPGVGIDRLFTLRTVEDTLKIREFIEQHHPRSAVLAGGGFIGVELMENLRELGIDVTVVQ 180
Cdd:COG0446 77 --LSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 181 RPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANgDRVNVLLKDEAPLTADMVVLAIGVTPDTGLAKAAGLELG 260
Cdd:COG0446 155 RAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGD-DKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 261 IKGSILVNDRMETSAPDIYAVGDAVQVKHFVTGQDTLLSLAGPANKQGRIAADNICGGDSRYPGsQGSSVIKVFDMTIAT 340
Cdd:COG0446 234 ERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPG-LGTFISKVFDLCIAS 312
|
..
gi 646496747 341 TG 342
Cdd:COG0446 313 TG 314
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
1-441 |
4.97e-132 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 392.48 E-value: 4.97e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 1 MKVIIVGGVAGGATAAARLRRLDETAEIVVFERSGYVSYANCGLPYYIGGVITDKEELTLQTPESFWQRfRVDMRVRHEV 80
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIKS-GIDVKTEHEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 81 TAIHPAEKTVDVRNLATGETFTESYDKLVLSPGARPTQPALPGVGIDRLFTLRTVEDTLKIREFIEQHHPRSAVLAGGGF 160
Cdd:PRK09564 80 VKVDAKNKTITVKNLKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEIKNIVIIGAGF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 161 IGVELMENLRELGIDVTVVQRP-RQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANgDRVNVLLKDEAPLTADMV 239
Cdd:PRK09564 160 IGLEAVEAAKHLGKNVRIIQLEdRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGE-DKVEGVVTDKGEYEADVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 240 VLAIGVTPDTGLAKAAGLELGIKGSILVNDRMETSAPDIYAVGDAVQVKHFVTGQDTLLSLAGPANKQGRIAADNICGGD 319
Cdd:PRK09564 239 IVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGRH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 320 SRYPGSQGSSVIKVFDMTIATTGVNEKTAKQAGIDCDKVYLSPMSHAGYYPGGKVMTLKVVFEKGTYRLLGAQIVGYEGV 399
Cdd:PRK09564 319 VSFKGTLGSACIKVLDLEAARTGLTEEEAKKLGIDYKTVFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQIIGKKGA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 646496747 400 DKRIDVLATAIHAGLSALQLKDLDLAYAPPYSSAKDPVNMAG 441
Cdd:PRK09564 399 VLRIDALAVAIYAKLTTQELGMMDFCYAPPFARTWDALNVAG 440
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
1-442 |
4.42e-118 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 356.40 E-value: 4.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 1 MKVIIVGGVAGGATAAARLRRLDETAEIVVFERSGYVSYANCGLPYYIGGVITDKEELTLQTPESFWQRFRVDMRVRHEV 80
Cdd:PRK13512 2 PKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALAYTPEKFYDRKQITVKTYHEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 81 TAIHPAEKTVDVRNLATGETFTESYDKLVLSPGARPTQPALPGvgiDRLFTLRTVEDTLKIREFIEQHHPRSAVLAGGGF 160
Cdd:PRK13512 82 IAINDERQTVTVLNRKTNEQFEESYDKLILSPGASANSLGFES---DITFTLRNLEDTDAIDQFIKANQVDKALVVGAGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 161 IGVELMENLRELGIDVTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVegfaangDRVN---VLLKDEAPLTAD 237
Cdd:PRK13512 159 ISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEI-------DAINgneVTFKSGKVEHYD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 238 MVVLAIGVTPDTGLAKAAGLELGIKGSILVNDRMETSAPDIYAVGDAVQVKHFVTGQDTLLSLAGPANKQGRIAADNICG 317
Cdd:PRK13512 232 MIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLAWGAHRAASIVAEQIAG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 318 GDS-RYPGSQGSSVIKVFDMTIATTGVNEKTAKQagIDCDKVYLSPMSHAGYYPGGKVMTLKVVFEKGTYRLLGAQIVGY 396
Cdd:PRK13512 312 NDTiEFKGFLGNNIVKFFDYTFASVGVKPNELKQ--FDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNRKILRAAAVGK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 646496747 397 EGVDKRIDVLATAIHAGLSALQLKDLDLAYAPPYSSAKDPVNMAGF 442
Cdd:PRK13512 390 EGADKRIDVLSMAMMNQLTVDELTEFEVAYAPPYSHPKDLINMIGY 435
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
19-395 |
5.00e-101 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 311.31 E-value: 5.00e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 19 LRRLDETAEIVVFERSGYVSYANCGLPYYIGGviTDKEELTLQTPESFWQRFRVDMRVRHEVTAIHPAEKTVDvrnLATG 98
Cdd:COG1251 20 LRKLDPDGEITVIGAEPHPPYNRPPLSKVLAG--ETDEEDLLLRPADFYEENGIDLRLGTRVTAIDRAARTVT---LADG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 99 ETFteSYDKLVLSPGARPTQPALPGVGIDRLFTLRTVEDTLKIREFIEQHhpRSAVLAGGGFIGVELMENLRELGIDVTV 178
Cdd:COG1251 95 ETL--PYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPG--KRVVVIGGGLIGLEAAAALRKRGLEVTV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 179 VQRPRQLLNP-LDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAIGVTPDTGLAKAAGL 257
Cdd:COG1251 171 VERAPRLLPRqLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPNTELARAAGL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 258 ELGikGSILVNDRMETSAPDIYAVGDAVQVKHFVTGQDTLLSLAgPANKQGRIAADNICGGDSRYPGSQGSSVIKVFDMT 337
Cdd:COG1251 251 AVD--RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRVLELVA-PAYEQARVAAANLAGGPAAYEGSVPSTKLKVFGVD 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 646496747 338 IATTGVNEktakqagiDCDKVYLSPMSHAGYYpggkvmtLKVVFEKGtyRLLGAQIVG 395
Cdd:COG1251 328 VASAGDAE--------GDEEVVVRGDPARGVY-------KKLVLRDG--RLVGAVLVG 368
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
18-283 |
3.11e-59 |
|
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: 199.08 E-value: 3.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 18 RLRRLDetAEIVVFERSGYVSYANCGLPYYIGGVITDKEELTL-------QTPESFWQRFRVDMRVRHEVTAIHPAEKTV 90
Cdd:pfam07992 18 TLAQLG--GKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLwadlykrKEEVVKKLNNGIEVLLGTEVVSIDPGAKKV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 91 DVRNLATGETFTESYDKLVLSPGARPTQPALPGVGIDRLFTLRTVEDTLKIREfieQHHPRSAVLAGGGFIGVELMENLR 170
Cdd:pfam07992 96 VLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRL---KLLPKRVVVVGGGYIGVELAAALA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 171 ELGIDVTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAIGVTPDTG 250
Cdd:pfam07992 173 KLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVVAIGRRPNTE 252
|
250 260 270
....*....|....*....|....*....|...
gi 646496747 251 LAKAAGLELGIKGSILVNDRMETSAPDIYAVGD 283
Cdd:pfam07992 253 LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGD 285
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
87-421 |
2.70e-55 |
|
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: 192.99 E-value: 2.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 87 EKTVDVRNlatGETFTesYDKLVLSPGARPTQPALPGVGIDRLFTLRTVedtLKIREFieqhhPRSAVLAGGGFIGVELM 166
Cdd:COG1249 118 PHTVEVTG---GETLT--ADHIVIATGSRPRVPPIPGLDEVRVLTSDEA---LELEEL-----PKSLVVIGGGYIGLEFA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 167 ENLRELGIDVTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKD---EAPLTADMVVLAI 243
Cdd:COG1249 185 QIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDgggEEAVEADKVLVAT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 244 GVTPDT---GLAkAAGLELGIKGSILVNDRMETSAPDIYAVGDavqvkhfVTGQdtlLSLAGPANKQGRIAADNICGGDS 320
Cdd:COG1249 265 GRRPNTdglGLE-AAGVELDERGGIKVDEYLRTSVPGIYAIGD-------VTGG---PQLAHVASAEGRVAAENILGKKP 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 321 RYpgsqgssvikvFDMT-----------IATTGVNEKTAKQAGIDCdKVYLSPMSHAGYypgGKVM-----TLKVVFEKG 384
Cdd:COG1249 334 RP-----------VDYRaipsvvftdpeIASVGLTEEEAREAGIDV-KVGKFPFAANGR---ALALgetegFVKLIADAE 398
|
330 340 350
....*....|....*....|....*....|....*..
gi 646496747 385 TYRLLGAQIVGyEGVDKRIDVLATAIHAGLSALQLKD 421
Cdd:COG1249 399 TGRILGAHIVG-PHAGELIHEAALAMEMGLTVEDLAD 434
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
19-342 |
1.89e-46 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 174.25 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 19 LRRLDETAEIVVFERSGYVSYANCGLPYYIGGViTDKEELTLQTpESFWQRFRVDMRVRHEVTAIHPAEKTVdvrnlATG 98
Cdd:TIGR02374 18 LKLNRHMFEITIFGEEPHPNYNRILLSSVLQGE-ADLDDITLNS-KDWYEKHGITLYTGETVIQIDTDQKQV-----ITD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 99 ETFTESYDKLVLSPGARPTQPALPGVGIDRLFTLRTVEDTLKIREfIEQHHPRSAVLaGGGFIGVELMENLRELGIDVTV 178
Cdd:TIGR02374 91 AGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMA-MAQRFKKAAVI-GGGLLGLEAAVGLQNLGMDVSV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 179 VQ-RPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAIGVTPDTGLAKAAGL 257
Cdd:TIGR02374 169 IHhAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 258 ELGikGSILVNDRMETSAPDIYAVGDAVQVKHFVTGqdtllsLAGPANKQGRIAADNICGGDSR-YPGSQGSSVIKVFDM 336
Cdd:TIGR02374 249 KVN--RGIIVNDSMQTSDPDIYAVGECAEHNGRVYG------LVAPLYEQAKVLADHICGVECEeYEGSDLSAKLKLLGV 320
|
....*.
gi 646496747 337 TIATTG 342
Cdd:TIGR02374 321 DVWSAG 326
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
106-429 |
1.12e-40 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 153.41 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 106 DKLVLSPGARptQPALPGV---GIDRLFTLRTVedtLKIREFieqhhPRSAVLAGGGFIGVELMENLRELGIDVTVVQRP 182
Cdd:PRK06292 132 KNIVIATGSR--VPPIPGVwliLGDRLLTSDDA---FELDKL-----PKSLAVIGGGVIGLELGQALSRLGVKVTVFERG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 183 RQLLNPLDADMAAFLHAKLRQKgVRLHLGCTVEGFAANGDRVNVLLKDEAP---LTADMVVLAIGVTPDT---GLAKaAG 256
Cdd:PRK06292 202 DRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGGKtetIEADYVLVATGRRPNTdglGLEN-TG 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 257 LELGIKGSILVNDRMETSAPDIYAVGDAVqvkhfvtgQDTLLSLAgpANKQGRIAADNICGGDSRY------PGSqgssv 330
Cdd:PRK06292 280 IELDERGRPVVDEHTQTSVPGIYAAGDVN--------GKPPLLHE--AADEGRIAAENAAGDVAGGvryhpiPSV----- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 331 ikVF-DMTIATTGVNEKTAKQAGIDcdkvYLS---PMSHAGYypgGKVMT-----LKVVFEKGTYRLLGAQIVGyEGVDK 401
Cdd:PRK06292 345 --VFtDPQIASVGLTEEELKAAGID----YVVgevPFEAQGR---ARVMGkndgfVKVYADKKTGRLLGAHIIG-PDAEH 414
|
330 340
....*....|....*....|....*...
gi 646496747 402 RIDVLATAIHAGLSALQLkdLDLAYAPP 429
Cdd:PRK06292 415 LIHLLAWAMQQGLTVEDL--LRMPFYHP 440
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
87-418 |
1.69e-39 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 149.97 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 87 EKTVDVrnlaTGETFTesYDKLVLSPGARPTQPALPGVGIDRLFTLRTVEDTLKIrefieqhhPRSAVLAGGGFIGVELM 166
Cdd:PRK06370 122 PNTVRV----GGETLR--AKRIFINTGARAAIPPIPGLDEVGYLTNETIFSLDEL--------PEHLVIIGGGYIGLEFA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 167 ENLRELGIDVTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLK---DEAPLTADMVVLAI 243
Cdd:PRK06370 188 QMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDcngGAPEITGSHILVAV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 244 GVTPDT---GLAkAAGLELGIKGSILVNDRMETSAPDIYAVGDAVQvkhfvTGQDTLLSLAgpankQGRIAADNICGGDS 320
Cdd:PRK06370 268 GRVPNTddlGLE-AAGVETDARGYIKVDDQLRTTNPGIYAAGDCNG-----RGAFTHTAYN-----DARIVAANLLDGGR 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 321 RypgsqgssviKVFDMT----------IATTGVNEKTAKQAGIDCDkVYLSPMSHAGYypggKVMT------LKVVFEKG 384
Cdd:PRK06370 337 R----------KVSDRIvpyatytdppLARVGMTEAEARKSGRRVL-VGTRPMTRVGR----AVEKgetqgfMKVVVDAD 401
|
330 340 350
....*....|....*....|....*....|....*.
gi 646496747 385 TYRLLGAQIVGYEGvDKRIDVLATAIHAG--LSALQ 418
Cdd:PRK06370 402 TDRILGATILGVHG-DEMIHEILDAMYAGapYTTLS 436
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
77-395 |
1.18e-38 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 147.60 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 77 RHEVTAIH-----PAEKTVDVRNLATGETFTesYDKLVLSPGARPTqpALPGVGIDRLfTLRTVEDTLKIrefieQHHPR 151
Cdd:PRK06416 104 KNKVDIIRgeaklVDPNTVRVMTEDGEQTYT--AKNIILATGSRPR--ELPGIEIDGR-VIWTSDEALNL-----DEVPK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 152 SAVLAGGGFIGVELMENLRELGIDVTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKD- 230
Cdd:PRK06416 174 SLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQTDDGVTVTLEDg 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 231 --EAPLTADMVVLAIGVTPDTglaKAAGLE-LGIK---GSILVNDRMETSAPDIYAVGDavqvkhfVTGQdtlLSLAGPA 304
Cdd:PRK06416 254 gkEETLEADYVLVAVGRRPNT---ENLGLEeLGVKtdrGFIEVDEQLRTNVPNIYAIGD-------IVGG---PMLAHKA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 305 NKQGRIAADNICGGDS--RYpgsqgSSVIKV-F-DMTIATTGVNEKTAKQAGIDCdKVYLSPMshAGyypGGKVMTL--- 377
Cdd:PRK06416 321 SAEGIIAAEAIAGNPHpiDY-----RGIPAVtYtHPEVASVGLTEAKAKEEGFDV-KVVKFPF--AG---NGKALALget 389
|
330 340
....*....|....*....|..
gi 646496747 378 ----KVVFEKGTYRLLGAQIVG 395
Cdd:PRK06416 390 dgfvKLIFDKKDGEVLGAHMVG 411
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
69-315 |
2.09e-37 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 142.58 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 69 RFRVDmrvrhEVTAIHPAEKTVDvrnLATGETFteSYDKLVLSPGARPTQPALPGVGiDRLFTLRTVEDTLKIRE----F 144
Cdd:COG1252 72 RFIQG-----EVTGIDPEARTVT---LADGRTL--SYDYLVIATGSVTNFFGIPGLA-EHALPLKTLEDALALRErllaA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 145 IEQHHPRSA---VLAGGGFIGVELMENLREL--------GID-----VTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRL 208
Cdd:COG1252 141 FERAERRRLltiVVVGGGPTGVELAGELAELlrkllrypGIDpdkvrITLVEAGPRILPGLGEKLSEAAEKELEKRGVEV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 209 HLGCTVEGFAANGdrvnVLLKDEAPLTADMVVLAIGVTPdTGLAKAAGLELGIKGSILVNDRMET-SAPDIYAVGDAVQV 287
Cdd:COG1252 221 HTGTRVTEVDADG----VTLEDGEEIPADTVIWAAGVKA-PPLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAV 295
|
250 260
....*....|....*....|....*....
gi 646496747 288 KHfvtGQDTLLS-LAGPANKQGRIAADNI 315
Cdd:COG1252 296 PD---PDGKPVPkTAQAAVQQAKVLAKNI 321
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
456-545 |
8.55e-35 |
|
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: 126.23 E-value: 8.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 456 FPEDVDALPRDGsVTLLDVRTPGEYADGHAEGFVNLPVDDLRERLREVPVGKPVYVICQSGLRSYIACRILAQQGFKCYN 535
Cdd:cd01524 2 QWHELDNYRADG-VTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFKVKN 80
|
90
....*....|
gi 646496747 536 LSGGWRLYET 545
Cdd:cd01524 81 LDGGYKTYST 90
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
19-320 |
1.21e-34 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 134.66 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 19 LRRLDETAEIVVFERSGYVSYANCGLPYyiggVITDK---EELTLQTPESFWQRFRVDMRVRHEVTAIHPAEKTVdvrnL 95
Cdd:PRK04965 21 IRKQDAHIPITLITADSGDEYNKPDLSH----VFSQGqraDDLTRQSAGEFAEQFNLRLFPHTWVTDIDAEAQVV----K 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 96 ATGETFteSYDKLVLSPGARPTQPALPGVGidRLFTL------RTVEDTLkirefieqHHPRSAVLAGGGFIGVELMENL 169
Cdd:PRK04965 93 SQGNQW--QYDKLVLATGASAFVPPIPGRE--LMLTLnsqqeyRAAETQL--------RDAQRVLVVGGGLIGTELAMDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 170 RELGIDVTVVQRPRQLL-NPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAIGVTPD 248
Cdd:PRK04965 161 CRAGKAVTLVDNAASLLaSLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAAAGLRPN 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 646496747 249 TGLAKAAGLELGiKGsILVNDRMETSAPDIYAVGDAV----QVKHFVtgQDTLLSlagpANkqgrIAADNICGGDS 320
Cdd:PRK04965 241 TALARRAGLAVN-RG-IVVDSYLQTSAPDIYALGDCAeingQVLPFL--QPIQLS----AM----ALAKNLLGQNT 304
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
72-420 |
2.33e-32 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 129.51 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 72 VDMR----VRHEVTAIHPA-----EKTVDVRNLAtGETFTESYDKLVLSPGARPTQPAlpgvGIDrlFTLRTVEDTLKIR 142
Cdd:PRK05249 97 VEVRrgqyERNRVDLIQGRarfvdPHTVEVECPD-GEVETLTADKIVIATGSRPYRPP----DVD--FDHPRIYDSDSIL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 143 EFieQHHPRSAVLAGGGFIGVELMENLRELGIDVTVVQRPRQLLNPLDADMA-AFLHAkLRQKGVRLHLGCTVEGFAANG 221
Cdd:PRK05249 170 SL--DHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISdALSYH-LRDSGVTIRHNEEVEKVEGGD 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 222 DRVNVLLKDEAPLTADMVVLAIGVTPDT---GLAkAAGLELGIKGSILVNDRMETSAPDIYAVGDavqvkhfVTGqdtLL 298
Cdd:PRK05249 247 DGVIVHLKSGKKIKADCLLYANGRTGNTdglNLE-NAGLEADSRGQLKVNENYQTAVPHIYAVGD-------VIG---FP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 299 SLAGPANKQGRIAADNICGGDSRypgsqgsSVIKVFDMTIATT------GVNEKTAKQAGID--CDKVYLSPMSHaGYYP 370
Cdd:PRK05249 316 SLASASMDQGRIAAQHAVGEATA-------HLIEDIPTGIYTIpeissvGKTEQELTAAKVPyeVGRARFKELAR-AQIA 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 646496747 371 GGKVMTLKVVFEKGTYRLLGAQIVGYEgvdkridvlATA-IHAGLSALQLK 420
Cdd:PRK05249 388 GDNVGMLKILFHRETLEILGVHCFGER---------ATEiIHIGQAIMEQK 429
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
87-413 |
2.95e-32 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 129.12 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 87 EKTVDVrnlaTGETFTEsyDKLVLSPGARPTQPALPGV--GI--DRLFTLRTVedtlkirefieqhhPRSAVLAGGGFIG 162
Cdd:PRK06116 120 AHTVEV----NGERYTA--DHILIATGGRPSIPDIPGAeyGItsDGFFALEEL--------------PKRVAVVGAGYIA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 163 VELMENLRELGIDVTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGD-RVNVLLKDEAPLTADMVVL 241
Cdd:PRK06116 180 VEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADgSLTLTLEDGETLTVDCLIW 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 242 AIGVTPDT---GLAkAAGLELGIKGSILVNDRMETSAPDIYAVGDavqvkhfVTGQdtlLSLAGPANKQGRIAADNICGG 318
Cdd:PRK06116 260 AIGREPNTdglGLE-NAGVKLNEKGYIIVDEYQNTNVPGIYAVGD-------VTGR---VELTPVAIAAGRRLSERLFNN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 319 DS-RYPG-SQGSSVikVFDM-TIATTGVNEKTA-KQAGIDCDKVYLS---PMSHAgyYPGGKVMTL-KVVFEKGTYRLLG 390
Cdd:PRK06116 329 KPdEKLDySNIPTV--VFSHpPIGTVGLTEEEArEQYGEDNVKVYRSsftPMYTA--LTGHRQPCLmKLVVVGKEEKVVG 404
|
330 340
....*....|....*....|...
gi 646496747 391 AQIVGYeGVDKRIDVLATAIHAG 413
Cdd:PRK06116 405 LHGIGF-GADEMIQGFAVAIKMG 426
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
457-541 |
1.40e-30 |
|
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: 115.06 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 457 PEDVDALPRDGSVTLLDVRTPGEYADGHAEGFVNLPVDDLRERLREVPVGKPVYVICQSGLRSYIACRILAQQGFK-CYN 535
Cdd:COG0607 8 PAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTnVYN 87
|
....*.
gi 646496747 536 LSGGWR 541
Cdd:COG0607 88 LAGGIE 93
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
90-416 |
3.04e-30 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 123.53 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 90 VDVRNLATGETFTESYDKLVLSPGARPTqpaLPGVGIDRLFTLRTVEDTLKIREFieqhhPRSAVLAGGGFIGVELMENL 169
Cdd:PRK07846 114 IGPKTLRTGDGEEITADQVVIAAGSRPV---IPPVIADSGVRYHTSDTIMRLPEL-----PESLVIVGGGFIAAEFAHVF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 170 RELGIDVTVVQRPRQLLNPLDADMAAFLhAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAIGVTPDT 249
Cdd:PRK07846 186 SALGVRVTVVNRSGRLLRHLDDDISERF-TELASKRWDVRLGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGRVPNG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 250 GL--AKAAGLELGIKGSILVNDRMETSAPDIYAVGDA---VQVKHFvtgqdtllslagpANKQGRIAADNICGGDS---- 320
Cdd:PRK07846 265 DLldAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVsspYQLKHV-------------ANHEARVVQHNLLHPDDlias 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 321 --RYPGSqgssviKVF-DMTIATTGVNEKTAKQAGIDCdKVYLSPMSHAGYypgGKVMT-----LKVVFEKGTYRLLGAQ 392
Cdd:PRK07846 332 dhRFVPA------AVFtHPQIASVGLTENEARAAGLDI-TVKVQNYGDVAY---GWAMEdttgfVKLIADRDTGRLLGAH 401
|
330 340
....*....|....*....|....
gi 646496747 393 IVGYEGvDKRIDVLATAIHAGLSA 416
Cdd:PRK07846 402 IIGPQA-STLIQPLIQAMSFGLDA 424
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
19-325 |
1.04e-29 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 120.80 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 19 LRRLDETAEIVVFERSGYVSYANCGLPYYIggVITDKEELTLQTPESFWQRFRVDMRVRHEVTAIHPAEKTVdvrNLATG 98
Cdd:PRK09754 22 LRQQGFTGELHLFSDERHLPYERPPLSKSM--LLEDSPQLQQVLPANWWQENNVHLHSGVTIKTLGRDTREL---VLTNG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 99 ETFteSYDKLVLSPGARPTQ-PALPGVGiDRLFTLRTVEDTLKIREFIEQHhpRSAVLAGGGFIGVELMENLRELGIDVT 177
Cdd:PRK09754 97 ESW--HWDQLFIATGAAARPlPLLDALG-ERCFTLRHAGDAARLREVLQPE--RSVVIVGAGTIGLELAASATQRRCKVT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 178 VVQRPRQLLN----PLDADmaaFLHAKLRQKGVRLHLGCTVEGfAANGDRVNVLLKDEAPLTADMVVLAIGVTPDTGLAK 253
Cdd:PRK09754 172 VIELAATVMGrnapPPVQR---YLLQRHQQAGVRILLNNAIEH-VVDGEKVELTLQSGETLQADVVIYGIGISANDQLAR 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 646496747 254 AAGLElgIKGSILVNDRMETSAPDIYAVGDaVQVKHFVTGQDTLLSLAGPANKQGRIAADNICGGDSRYPGS 325
Cdd:PRK09754 248 EANLD--TANGIVIDEACRTCDPAIFAGGD-VAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPP 316
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
87-463 |
1.55e-28 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 119.87 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 87 EKTVDVRnLATGETFTESYDKLVLSPGARPTQPALPGVGiDRLFTLRT---VEDTLKirefieqhhPRSAVLaGGGFIGV 163
Cdd:PRK13748 216 DQTLIVR-LNDGGERVVAFDRCLIATGASPAVPPIPGLK-ETPYWTSTealVSDTIP---------ERLAVI-GSSVVAL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 164 ELMENLRELGIDVTVVQRpRQLLNPLDADMAAFLHAKLRQKGVRLhLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAI 243
Cdd:PRK13748 284 ELAQAFARLGSKVTILAR-STLFFREDPAIGEAVTAAFRAEGIEV-LEHTQASQVAHVDGEFVLTTGHGELRADKLLVAT 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 244 GVTPDT-GLA-KAAGLELGIKGSILVNDRMETSAPDIYAVGDAVQVKHFVTgqdtllsLAGPAnkqGRIAADNICGGDSR 321
Cdd:PRK13748 362 GRAPNTrSLAlDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVY-------VAAAA---GTRAAINMTGGDAA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 322 YPGSQGSSVikVF-DMTIATTGVNEKTAKQAGIDCDKVYLS----PMSHAGYYPGGKVmtlKVVFEKGTYRLLGAQIVGY 396
Cdd:PRK13748 432 LDLTAMPAV--VFtDPQVATVGYSEAEAHHDGIETDSRTLTldnvPRALANFDTRGFI---KLVIEEGSGRLIGVQAVAP 506
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 646496747 397 EGvDKRIDVLATAIHAGLSALQLKDLDLayapPYSSakdpvnmagfMIENLShgLVEQFFPEDVDAL 463
Cdd:PRK13748 507 EA-GELIQTAALAIRNRMTVQELADQLF----PYLT----------MVEGLK--LAAQTFNKDVKQL 556
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
24-342 |
4.80e-28 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 119.45 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 24 ETAEIVVFERSGYVSYANCGLPYYIGGviTDKEELTLqTPESFWQRFRVDMRVRHEVTAIHPAEKTVdvrNLATGETFte 103
Cdd:PRK14989 29 ANFDITVFCEEPRIAYDRVHLSSYFSH--HTAEELSL-VREGFYEKHGIKVLVGERAITINRQEKVI---HSSAGRTV-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 104 SYDKLVLSPGARPTQPALPGVGIDRLFTLRTVEDTLKIREFIEQhhPRSAVLAGGGFIGVELMENLRELGIDVTVVQ-RP 182
Cdd:PRK14989 101 FYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARR--SKRGAVVGGGLLGLEAAGALKNLGVETHVIEfAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 183 RQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGD--RVNVLLKDEAPLTADMVVLAIGVTPDTGLAKAAGLELG 260
Cdd:PRK14989 179 MLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVeaRKTMRFADGSELEVDFIVFSTGIRPQDKLATQCGLAVA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 261 IKGSILVNDRMETSAPDIYAVGDAvqvkhfVTGQDTLLSLAGPANKQGRIAADNICGGDSRYPGSQGSSVIKVFDMTIAT 340
Cdd:PRK14989 259 PRGGIVINDSCQTSDPDIYAIGEC------ASWNNRVFGLVAPGYKMAQVAVDHLLGSENAFEGADLSAKLKLLGVDVGG 332
|
..
gi 646496747 341 TG 342
Cdd:PRK14989 333 IG 334
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
120-397 |
4.25e-24 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 105.39 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 120 ALPGVGIDRlftlRTVEDTLKIREFIEQhhPRSAVLAGGGFIGVELMENLRELGIDVTVVQRPRQLLNPLDADMAAFLHA 199
Cdd:PRK06327 159 HLPGVPFDN----KIILDNTGALNFTEV--PKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 200 KLRQKGVRLHLGCTVEGFAANGDRVNVLLKD----EAPLTADMVVLAIGVTPDT-GL-AKAAGLELGIKGSILVNDRMET 273
Cdd:PRK06327 233 AFTKQGLDIHLGVKIGEIKTGGKGVSVAYTDadgeAQTLEVDKLIVSIGRVPNTdGLgLEAVGLKLDERGFIPVDDHCRT 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 274 SAPDIYAVGDavqvkhfVTGQDTllsLAGPANKQGRIAADNICGGDSRYPGSQGSSVIKVFDmTIATTGVNEKTAKQAGI 353
Cdd:PRK06327 313 NVPNVYAIGD-------VVRGPM---LAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSP-EIAWVGKTEQQLKAEGV 381
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 646496747 354 DCdKVYLSPMSHAGY-----YPGGKVmtlKVVFEKGTYRLLGAQIVGYE 397
Cdd:PRK06327 382 EY-KAGKFPFMANGRalamgEPDGFV---KIIADAKTDEILGVHVIGPN 426
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
459-539 |
1.28e-23 |
|
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: 95.06 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 459 DVDALPRDGSVTLLDVRTPGEYADGHAEGFVNLPVDDLRER--LREVPVGKPVYVICQSGLRSYIACRILAQQGF-KCYN 535
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERaaLLELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYN 80
|
....
gi 646496747 536 LSGG 539
Cdd:cd00158 81 LEGG 84
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
106-421 |
1.40e-21 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 97.39 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 106 DKLVLSPGARPTQPALPGVGidrlfTLRTVEDTLKIREFIEQhhPRSAVLAGGGFIGVELMENLRELGIDVTVVQRPRQL 185
Cdd:PRK08010 121 EKIFINTGAQTVVPPIPGIT-----TTPGVYDSTGLLNLKEL--PGHLGILGGGYIGVEFASMFANFGSKVTILEAASLF 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 186 LNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVlLKDEAPLTADMVVLAIGVTPDT-GL-AKAAGLELGIKG 263
Cdd:PRK08010 194 LPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQV-HSEHAQLAVDALLIASGRQPATaSLhPENAGIAVNERG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 264 SILVNDRMETSAPDIYAVGDavqvkhfVTG--QDTLLSLagpanKQGRIAADNICGGDSRYPGSQGSSVIKVFdMT--IA 339
Cdd:PRK08010 273 AIVVDKYLHTTADNIWAMGD-------VTGglQFTYISL-----DDYRIVRDELLGEGKRSTDDRKNVPYSVF-MTppLS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 340 TTGVNEKTAKQAGIDCDKVYLsPMSHagyYPGGKVM-----TLKVVFEKGTYRLLGAQIVGYEGvDKRIDVLATAIHAGL 414
Cdd:PRK08010 340 RVGMTEEQARESGADIQVVTL-PVAA---IPRARVMndtrgVLKAIVDNKTQRILGASLLCVDS-HEMINIVKMVMDAGL 414
|
....*..
gi 646496747 415 SALQLKD 421
Cdd:PRK08010 415 PYSILRD 421
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
331-433 |
1.15e-19 |
|
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: 84.53 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 331 IKVFDMTIATTGVNEKTAKQAGIDCD--KVYLSPMSHAGYYPGGKVMtLKVVFEKGTYRLLGAQIVGYeGVDKRIDVLAT 408
Cdd:pfam02852 4 VVFTDPEIASVGLTEEEAKEKGGEVKvgKFPFAANGRALAYGDTDGF-VKLVADRETGKILGAHIVGP-NAGELIQEAAL 81
|
90 100
....*....|....*....|....*
gi 646496747 409 AIHAGLSALQLkDLDLAYAPPYSSA 433
Cdd:pfam02852 82 AIKMGATVEDL-ANTIHIHPTLSEA 105
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
89-395 |
3.27e-19 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 90.65 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 89 TVDVRNLaTGETFTESYDKLVLSPGARPTQPALPG--VGIdrlftlrTVEDTLKIREFieqhhPRSAVLAGGGFIGVELM 166
Cdd:PLN02507 153 EVEVTQL-DGTKLRYTAKHILIATGSRAQRPNIPGkeLAI-------TSDEALSLEEL-----PKRAVVLGGGYIAVEFA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 167 ENLRELGIDVTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAIGVT 246
Cdd:PLN02507 220 SIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHGEEFVADVVLFATGRA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 247 PDT---GLaKAAGLELGIKGSILVNDRMETSAPDIYAVGDavqvkhfVTGQdtlLSLAGPANKQGRIAADNICGGDSRYP 323
Cdd:PLN02507 300 PNTkrlNL-EAVGVELDKAGAVKVDEYSRTNIPSIWAIGD-------VTNR---INLTPVALMEGTCFAKTVFGGQPTKP 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 646496747 324 GSQGSSViKVFDM-TIATTGVNEKTA-KQAGIDCdKVYLS---PMSHAgyYPGGKVMT-LKVVFEKGTYRLLGAQIVG 395
Cdd:PLN02507 369 DYENVAC-AVFCIpPLSVVGLSEEEAvEQAKGDI-LVFTSsfnPMKNT--ISGRQEKTvMKLIVDAETDKVLGASMCG 442
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
106-410 |
2.12e-18 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 87.88 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 106 DKLVLSPGARPTQPALPGvgidrLFTLRTVEDTLKIREFieQHHPRSAVLAGGGFIGVELMENLRELGIDVTVVQRPRQL 185
Cdd:PRK07251 120 ETIVINTGAVSNVLPIPG-----LADSKHVYDSTGIQSL--ETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 186 LNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEApLTADMVVLAIGVTPDT---GLAKAAgLELGIK 262
Cdd:PRK07251 193 LPREEPSVAALAKQYMEEDGITFLLNAHTTEVKNDGDQVLVVTEDET-YRFDALLYATGRKPNTeplGLENTD-IELTER 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 263 GSILVNDRMETSAPDIYAVGDavqvkhfVTG--QDTLLSLagpanKQGRIAAdNICGGDSRYPGSQGSSVIKVFDMT--I 338
Cdd:PRK07251 271 GAIKVDDYCQTSVPGVFAVGD-------VNGgpQFTYISL-----DDFRIVF-GYLTGDGSYTLEDRGNVPTTMFITppL 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 646496747 339 ATTGVNEKTAKQAGIDCDK----VYLSPMSHAGYYPGGkvmTLKVVFEKGTYRLLGAQIVGyEGVDKRIDVLATAI 410
Cdd:PRK07251 338 SQVGLTEKEAKEAGLPYAVkellVAAMPRAHVNNDLRG---AFKVVVNTETKEILGATLFG-EGSQEIINLITMAM 409
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
152-231 |
2.74e-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: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 152 SAVLAGGGFIGVELMENLRELGIDVTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDE 231
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTDG 80
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
68-289 |
5.84e-18 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 84.79 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 68 QRFRVDMrVRHEVTAIHPAEKTVDVrNLATGETFTEsyDKLVLSPGARPTQPALPGVgidRLFTLRTVE--DTLKIREFI 145
Cdd:COG0492 68 ERFGAEI-LLEEVTSVDKDDGPFRV-TTDDGTEYEA--KAVIIATGAGPRKLGLPGE---EEFEGRGVSycATCDGFFFR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 146 EQHhprsAVLAGGGFIGVELMENLRELGIDVTVVQRPRQLlnPLDADMAAFLHAKlrqKGVRLHLGCTVEGFAANgDRVN 225
Cdd:COG0492 141 GKD----VVVVGGGDSALEEALYLTKFASKVTLIHRRDEL--RASKILVERLRAN---PKIEVLWNTEVTEIEGD-GRVE 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 226 -VLLKD-----EAPLTADMVVLAIGVTPDTGLAKAAGLELGIKGSILVNDRMETSAPDIYAVGDAVQVKH 289
Cdd:COG0492 211 gVTLKNvktgeEKELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKY 280
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
94-361 |
1.25e-16 |
|
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: 82.59 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 94 NLATGETFTESYdkLVLSPGARPTQPALPG---VGI--DRLFTLRTVedtlkirefieqhhPRSAVLAGGGFIGVELMEN 168
Cdd:TIGR01438 135 KKGKEKIYSAER--FLIATGERPRYPGIPGakeLCItsDDLFSLPYC--------------PGKTLVVGASYVALECAGF 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 169 LRELGIDVTVVQRpRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTA---DMVVLAIGV 245
Cdd:TIGR01438 199 LAGIGLDVTVMVR-SILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEeeyDTVLLAIGR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 246 TPDTglaKAAGLE-LGIK-----GSILVNDRMETSAPDIYAVGDAVQVKhfvtgqdtlLSLAGPANKQGRIAADNICGgd 319
Cdd:TIGR01438 278 DACT---RKLNLEnVGVKinkktGKIPADEEEQTNVPYIYAVGDILEDK---------PELTPVAIQAGRLLAQRLFK-- 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 646496747 320 srypgsqGSSVIKVFDmTIATT----------GVNEKTAKQA-GIDCDKVYLS 361
Cdd:TIGR01438 344 -------GSTVICDYE-NVPTTvftpleygacGLSEEKAVEKfGEENVEVFHS 388
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
77-315 |
1.40e-16 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 82.12 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 77 RHEVTAIHPAEKTVDVRNLATGE-----TFTESYDKLVLSPGARPTQPALPGVgIDRLFTLRTVEDTLKIREFIEQHHPR 151
Cdd:PTZ00318 81 RAVVYDVDFEEKRVKCGVVSKSNnanvnTFSVPYDKLVVAHGARPNTFNIPGV-EERAFFLKEVNHARGIRKRIVQCIER 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 152 ---------------SAVLAGGGFIGVELMENLRELGID--------------VTVVQRPRQLLNPLDADMAAFLHAKLR 202
Cdd:PTZ00318 160 aslpttsveerkrllHFVVVGGGPTGVEFAAELADFFRDdvrnlnpelveeckVTVLEAGSEVLGSFDQALRKYGQRRLR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 203 QKGVRLHLGCTVEGFAANgdrvNVLLKDEAPLTADMVVLAIGVTPDTgLAKAAGLELGIKGSILVNDRMETS-APDIYAV 281
Cdd:PTZ00318 240 RLGVDIRTKTAVKEVLDK----EVVLKDGEVIPTGLVVWSTGVGPGP-LTKQLKVDKTSRGRISVDDHLRVKpIPNVFAL 314
|
250 260 270
....*....|....*....|....*....|....
gi 646496747 282 GDAVQVKhfvtgQDTLLSLAGPANKQGRIAADNI 315
Cdd:PTZ00318 315 GDCAANE-----ERPLPTLAQVASQQGVYLAKEF 343
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
108-443 |
1.67e-16 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 82.74 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 108 LVLSPGARPTQPALPGVgidrlftlrtvEDTLKIREFIEQHHPRSAVLAGGGFIGVELMENLRELGIDVTVVQRPRQLLN 187
Cdd:PTZ00058 206 ILIAVGNKPIFPDVKGK-----------EFTISSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLR 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 188 PLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDR-VNVLLKD-EAPLTADMVVLAIGVTPDTglaKAAGLE----LGI 261
Cdd:PTZ00058 275 KFDETIINELENDMKKNNINIITHANVEEIEKVKEKnLTIYLSDgRKYEHFDYVIYCVGRSPNT---EDLNLKalniKTP 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 262 KGSILVNDRMETSAPDIYAVGDAVQVKHFVTGQDTLL------------------------SLAGPANKQGRIAADNICG 317
Cdd:PTZ00058 352 KGYIKVDDNQRTSVKHIYAVGDCCMVKKNQEIEDLNLlklyneepylkkkentsgesyynvQLTPVAINAGRLLADRLFG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 318 GDSRYPGSQGSSVIKVFDMTIATTGVNEKTA-KQAGIDCDKVYLSPMSHAGYY-----PGGKVMT-LKVVFEKGTYRLLG 390
Cdd:PTZ00058 432 PFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAiDIYGKENVKIYESRFTNLFFSvydmdPAQKEKTyLKLVCVGKEELIKG 511
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 646496747 391 AQIVGYeGVDKRIDVLATAIHAGLSAlqlKDLDLAYAPPYSSAKDPVNMAGFM 443
Cdd:PTZ00058 512 LHIVGL-NADEILQGFAVALKMNATK---ADFDETIPIHPTAAEEFVTMAPWM 560
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
89-311 |
4.09e-16 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 81.06 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 89 TVDVRnLATGETFTESYDKLVLSPGARPTQpaLPGVGID--RLFTLRTVEDtlkIREFieqhhPRSAVLAGGGFIGVELM 166
Cdd:PRK07845 125 RVKVT-TADGGEETLDADVVLIATGASPRI--LPTAEPDgeRILTWRQLYD---LDEL-----PEHLIVVGSGVTGAEFA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 167 ENLRELGIDVTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAIGVT 246
Cdd:PRK07845 194 SAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVERTGDGVVVTLTDGRTVEGSHALMAVGSV 273
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 646496747 247 PDT---GLAKAaGLELGIKGSILVnDRME-TSAPDIYAVGDavqvkhfVTGqdtLLSLAGPANKQGRIA 311
Cdd:PRK07845 274 PNTaglGLEEA-GVELTPSGHITV-DRVSrTSVPGIYAAGD-------CTG---VLPLASVAAMQGRIA 330
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
466-541 |
1.19e-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: 72.49 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 466 DGSVTLLDVRTPGEYADGHAEGFVNLPVDDLRERLREVPV--------------GKPVYVICQSGLRSYIACRILAQQGF 531
Cdd:smart00450 2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIlefeellkrlgldkDKPVVVYCRSGNRSAKAAWLLRELGF 81
|
90
....*....|.
gi 646496747 532 K-CYNLSGGWR 541
Cdd:smart00450 82 KnVYLLDGGYK 92
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
466-540 |
5.97e-15 |
|
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: 70.59 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 466 DGSVTLLDVRTPGEYADGHAEGFVNLPVDDLR----------ERLREVPVGKPVYVICQSGLRSYIACRILAQQGF-KCY 534
Cdd:pfam00581 3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSlpplpllellEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYkNVY 82
|
....*.
gi 646496747 535 NLSGGW 540
Cdd:pfam00581 83 VLDGGF 88
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
471-543 |
7.16e-14 |
|
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: 67.80 E-value: 7.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 471 LLDVRTPGEYADGHAEGFVNLPVDDLRERLREVPVG---KPVYVICQSGLRSYIACRILAQQGF-KCYNLSGG---WRLY 543
Cdd:cd01528 20 LIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSDnpdKDIVVLCHHGGRSMQVAQWLLRQGFeNVYNLQGGidaWSLE 99
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
106-395 |
8.68e-14 |
|
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: 73.85 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 106 DKLVLSPGARPTQPALPGVgidrlftlrtvEDTLKIRE-FIEQHHPRSAVLAGGGFIGVE---LMENLRELGIDVTVVQR 181
Cdd:TIGR01423 153 EHILLATGSWPQMLGIPGI-----------EHCISSNEaFYLDEPPRRVLTVGGGFISVEfagIFNAYKPRGGKVTLCYR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 182 PRQLLNPLDADMAAFLHAKLRQKG--VRLHLGCTVEGFAANGDRvNVLLKDEAPLTADMVVLAIGVTPDTGLAK--AAGL 257
Cdd:TIGR01423 222 NNMILRGFDSTLRKELTKQLRANGinIMTNENPAKVTLNADGSK-HVTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 258 ELGIKGSILVNDRMETSAPDIYAVGDavqvkhfVTGQdtlLSLAGPANKQGRIAADNICGGDSRyPGSQGSSVIKVFDM- 336
Cdd:TIGR01423 301 ELTKKGAIQVDEFSRTNVPNIYAIGD-------VTDR---VMLTPVAINEGAAFVDTVFGNKPR-KTDHTRVASAVFSIp 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 646496747 337 TIATTGVNEKTAKQAgIDCDKVYLS---PMSHAGYYPGGKVMTLKVVFEKGTYRLLGAQIVG 395
Cdd:TIGR01423 370 PIGTCGLVEEDAAKK-FEKVAVYESsftPLMHNISGSKYKKFVAKIVTNHADGTVLGVHLLG 430
|
|
| SelU |
COG2603 |
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ... |
461-553 |
1.18e-10 |
|
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: 63.25 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 461 DALPRDGSVTLLDVRTPGEYADGHAEGFVNLPV-DD---------------------------------LRERLREVPVG 506
Cdd:COG2603 9 DFLELLDDDPLIDVRSPVEFAEGHIPGAINLPLlDDeeraevgtcykqqgpfaaiklghalvsgklaahREEAWAFAPKH 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 646496747 507 KPVYVIC-QSGLRSYIACRILAQQGFKCYNLSGGWRLYETVVRDRTAA 553
Cdd:COG2603 89 PRPLVYCwRGGLRSGSVAQWLREAGIDVPRLEGGYKAYRRFVLDELER 136
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
108-426 |
1.49e-10 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 63.78 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 108 LVLSPGARPTQPAlpGVGIDRlFTLRTVEDTLKIREFieqhhPRSAVLAGGGFIGVELMENLRELGIDVTVVQRPRQLLN 187
Cdd:PTZ00153 278 IIIATGSTPNIPD--NIEVDQ-KSVFTSDTAVKLEGL-----QNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 188 PLDADMAA-FLHAKLRQKGVRLHLGCTVEGFAA-----------------NGDRVNVLLKDEAPLTADMVVLAIGVTPDT 249
Cdd:PTZ00153 350 LLDADVAKyFERVFLKSKPVRVHLNTLIEYVRAgkgnqpviighserqtgESDGPKKNMNDIKETYVDSCLVATGRKPNT 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 250 glaKAAGLE-LGI---KGSILVNDRMETSAPD------IYAVGDAvqvkhfvTGQdtlLSLAGPANKQGRIAADNICGGD 319
Cdd:PTZ00153 430 ---NNLGLDkLKIqmkRGFVSVDEHLRVLREDqevydnIFCIGDA-------NGK---QMLAHTASHQALKVVDWIEGKG 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 320 SRY----PGSQGSSVIKVFDM--------TIATTGVNEKTAKQAG-----------------IDCD-KVYLSPMSHAGYY 369
Cdd:PTZ00153 497 KENvninVENWASKPIIYKNIpsvcyttpELAFIGLTEKEAKELYppdnvgveisfykanskVLCEnNISFPNNSKNNSY 576
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 646496747 370 PGGKVMT-------LKVVFEKGTYRLLGAQIVGYEGVDkridvlatAIHAGLSALQLK--DLDLAY 426
Cdd:PTZ00153 577 NKGKYNTvdntegmVKIVYLKDTKEILGMFIVGSYASI--------LIHEGVLAINLKlsVKDLAH 634
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
175-315 |
1.98e-10 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 62.89 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 175 DVTVVQRPRQllnpldADMAA----FLHAKlrQKGVRLHLGCTVEGFAANGD--------------------RVNVLLKD 230
Cdd:PRK11749 299 SVTIVYRRGR------EEMPAseeeVEHAK--EEGVEFEWLAAPVEILGDEGrvtgvefvrmelgepdasgrRRVPIEGS 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 231 EAPLTADMVVLAIGVTPDT-GLAKAAGLELGIKGSILVNDR-METSAPDIYAVGDAvqvkhfVTGQDTLLSlagpANKQG 308
Cdd:PRK11749 371 EFTLPADLVIKAIGQTPNPlILSTTPGLELNRWGTIIADDEtGRTSLPGVFAGGDI------VTGAATVVW----AVGDG 440
|
....*..
gi 646496747 309 RIAADNI 315
Cdd:PRK11749 441 KDAAEAI 447
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
448-539 |
2.02e-10 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 62.58 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 448 SHGLVEQFFPEDVDALPRDgsVTLLDVRTPGEYADGHAEGFVNLPVDDLRERLR--EVPVGKPVYVICQSGLRSYIACRI 525
Cdd:PRK05597 256 SGGFGEVLDVPRVSALPDG--VTLIDVREPSEFAAYSIPGAHNVPLSAIREGANppSVSAGDEVVVYCAAGVRSAQAVAI 333
|
90
....*....|....*
gi 646496747 526 LAQQGFK-CYNLSGG 539
Cdd:PRK05597 334 LERAGYTgMSSLDGG 348
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
234-315 |
3.03e-10 |
|
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: 62.46 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 234 LTADMVVLAIGVTPDT-GLAKAAGLELGIKGSILVNDR-METSAPDIYAVGDAvqvkhfVTGQDTLLSlagpANKQGRIA 311
Cdd:COG0493 358 LPADLVILAIGQTPDPsGLEEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDA------VRGPSLVVW----AIAEGRKA 427
|
....
gi 646496747 312 ADNI 315
Cdd:COG0493 428 ARAI 431
|
|
| glpE |
PRK00162 |
thiosulfate sulfurtransferase GlpE; |
457-541 |
6.23e-10 |
|
thiosulfate sulfurtransferase GlpE;
Pssm-ID: 178908 [Multi-domain] Cd Length: 108 Bit Score: 56.57 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 457 PEDVDALPRDGSVTLLDVRTPGEYADGHAEGFVNLPVDDLRERLREVPVGKPVYVICQSGLRSYIACRILAQQGF-KCYN 535
Cdd:PRK00162 9 VEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQQGFdVVYS 88
|
....*....
gi 646496747 536 LSGG---WR 541
Cdd:PRK00162 89 IDGGfeaWR 97
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
80-439 |
7.56e-10 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 61.43 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 80 VTAIHPAEKTVDVRNLAT-GETFTESYdkLVLSPGARPTQPALPGV--GIDRLFTLRTVEDTLKIrefieqhhprsaVLA 156
Cdd:PLN02546 193 VTLIEGRGKIVDPHTVDVdGKLYTARN--ILIAVGGRPFIPDIPGIehAIDSDAALDLPSKPEKI------------AIV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 157 GGGFIGVELMENLRELGIDVTVVQRPRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTA 236
Cdd:PLN02546 259 GGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTVEG 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 237 -DMVVLAIGVTPDTglaKAAGLE-LGIK----GSILVNDRMETSAPDIYAVGDavqvkhfVTGQdtlLSLAGPANKQGRI 310
Cdd:PLN02546 339 fSHVMFATGRKPNT---KNLGLEeVGVKmdknGAIEVDEYSRTSVPSIWAVGD-------VTDR---INLTPVALMEGGA 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 311 AADNICGGDSRYPGSQGSSViKVFDM-TIATTGVNEKTAKQAGIDCDkVYLS---PMSHAGYYPGGKVMtLKVVFEKGTY 386
Cdd:PLN02546 406 LAKTLFGNEPTKPDYRAVPS-AVFSQpPIGQVGLTEEQAIEEYGDVD-VFTAnfrPLKATLSGLPDRVF-MKLIVCAKTN 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 646496747 387 RLLGAQIVGyEGVDKRIDVLATAIHAGLSAlqlKDLDLAYAPPYSSAKDPVNM 439
Cdd:PLN02546 483 KVLGVHMCG-EDAPEIIQGFAVAVKAGLTK---ADFDATVGIHPTAAEEFVTM 531
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
457-541 |
1.53e-09 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 60.03 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 457 PEDVDALPRDGSVtLLDVRTPGEYADGHAEGFVNLPVDDLRERLRE-VP-VGKPVYVICQSGLRSYIACRILAQQGF-KC 533
Cdd:PRK08762 7 PAEARARAAQGAV-LIDVREAHERASGQAEGALRIPRGFLELRIEThLPdRDREIVLICASGTRSAHAAATLRELGYtRV 85
|
90
....*....|.
gi 646496747 534 YNLSGG---WR 541
Cdd:PRK08762 86 ASVAGGfsaWK 96
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
458-541 |
5.84e-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: 53.81 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 458 EDVDALPR-DGSVTLLDVRTPGEYADGHAEGFVNLPVDDLRERL------------REVPV-GKPVYVICQSGLRSYIAC 523
Cdd:cd01519 4 EEVKNLPNpHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALalseeefekkygFPKPSkDKELIFYCKAGVRSKAAA 83
|
90
....*....|....*....
gi 646496747 524 RILAQQGFK-CYNLSGGWR 541
Cdd:cd01519 84 ELARSLGYEnVGNYPGSWL 102
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
219-315 |
9.92e-09 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 58.21 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 219 ANGDRVNVLLK-DEAPLTADMVVLAIGVTPDTGLAKAA-GLELGIKGSILVNDRMETSAPDIYAVGDAvqvkhfVTGQDT 296
Cdd:PRK12778 657 ASGRRRPVAIPgSTFTVDVDLVIVSVGVSPNPLVPSSIpGLELNRKGTIVVDEEMQSSIPGIYAGGDI------VRGGAT 730
|
90
....*....|....*....
gi 646496747 297 LLSLAGpankQGRIAADNI 315
Cdd:PRK12778 731 VILAMG----DGKRAAAAI 745
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
87-285 |
1.13e-08 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 57.53 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 87 EKTVDVRNLATGETFTESYdkLVLSPGARPTQP-ALPG-----VGIDRLFTLRTVedtlkirefieqhhPRSAVLAGGGF 160
Cdd:PTZ00052 129 EHTVSYGDNSQEETITAKY--ILIATGGRPSIPeDVPGakeysITSDDIFSLSKD--------------PGKTLIVGASY 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 161 IGVELMENLRELGIDVTVVQRpRQLLNPLDADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVV 240
Cdd:PTZ00052 193 IGLETAGFLNELGFDVTVAVR-SIPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIKVLFSDGTTELFDTVL 271
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 646496747 241 LAIGVTPDTGLAK--AAGLELGIKGSILVNDRMeTSAPDIYAVGDAV 285
Cdd:PTZ00052 272 YATGRKPDIKGLNlnAIGVHVNKSNKIIAPNDC-TNIPNIFAVGDVV 317
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
78-315 |
1.51e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 56.54 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 78 HEVTAIHPAEKTVDVrnlatgETFTESYDKLVLSPGA----RPTQP--ALPGV--GIDRLFTLRTVEDTLKIREFIEQHH 149
Cdd:PRK12770 98 HEEEGDEFVERIVSL------EELVKKYDAVLIATGTwksrKLGIPgeDLPGVysALEYLFRIRAAKLGYLPWEKVPPVE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 150 PRSAVLAGGGFIGVELMENLRELGID-VTVV-QRPRQllnplDADMAAFLHAKLRQKGVRLHLGCT-------------- 213
Cdd:PRK12770 172 GKKVVVVGAGLTAVDAALEAVLLGAEkVYLAyRRTIN-----EAPAGKYEIERLIARGVEFLELVTpvriigegrvegve 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 214 ------VEGFAANGDRVNVLLKDEAPLTADMVVLAIGVTPDTGLAK-AAGLELGIKGSILVNDRMETSAPDIYAVGDAvq 286
Cdd:PRK12770 247 lakmrlGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKeCLGIELNRKGEIVVDEKHMTSREGVFAAGDV-- 324
|
250 260
....*....|....*....|....*....
gi 646496747 287 vkhfVTGQdtllSLAGPANKQGRIAADNI 315
Cdd:PRK12770 325 ----VTGP----SKIGKAIKSGLRAAQSI 345
|
|
| PRK11784 |
PRK11784 |
tRNA 2-selenouridine synthase; Provisional |
458-561 |
3.10e-08 |
|
tRNA 2-selenouridine synthase; Provisional
Pssm-ID: 236982 [Multi-domain] Cd Length: 345 Bit Score: 55.61 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 458 EDVDALPRDGsVTLLDVRTPGEYADGHAEGFVNLPV-DD-----------------------------LRERLREV---- 503
Cdd:PRK11784 6 QDFRALFLND-TPLIDVRSPIEFAEGHIPGAINLPLlNDeeraevgtcykqqgqfaaialghalvagnIAAHREEAwadf 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 646496747 504 -PVGKPVYVIC-QSGLRSYIACRILAQQGFKCYNLSGGWRLYETVVRDRT-AAQEAWP----CGM 561
Cdd:PRK11784 85 pRANPRGLLYCwRGGLRSGSVQQWLKEAGIDVPRLEGGYKAYRRFVIDTLeEAPAQFPlvvlGGN 149
|
|
| RHOD_1 |
cd01522 |
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ... |
463-539 |
4.94e-08 |
|
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: 51.56 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 463 LPRDGSVTLLDVRTPGE-YADGHAEGFVNLPVDD----------LRERLREVPVGKPVYVICQSGLRSYIACRILAQQGF 531
Cdd:cd01522 10 LQADPQAVLVDVRTEAEwKFVGGVPDAVHVAWQVypdmeinpnfLAELEEKVGKDRPVLLLCRSGNRSIAAAEAAAQAGF 89
|
....*....
gi 646496747 532 K-CYNLSGG 539
Cdd:cd01522 90 TnVYNVLEG 98
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
457-539 |
5.99e-08 |
|
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: 50.89 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 457 PEDVDALPRDGSVTLLDVRTPGEY-ADGHAEGFVNLPVDDLRERL-REVPV-------GKPVYVICQSGLRSYIACRILA 527
Cdd:cd01447 3 PEDARALLGSPGVLLVDVRDPRELeRTGMIPGAFHAPRGMLEFWAdPDSPYhkpafaeDKPFVFYCASGWRSALAGKTLQ 82
|
90
....*....|...
gi 646496747 528 QQGFK-CYNLSGG 539
Cdd:cd01447 83 DMGLKpVYNIEGG 95
|
|
| RHOD_YbbB |
cd01520 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ... |
458-543 |
6.35e-08 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.
Pssm-ID: 238778 [Multi-domain] Cd Length: 128 Bit Score: 51.53 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 458 EDVDALpRDGSVTLLDVRTPGEYADGHAEGFVNLPV--DDLRERL--------REVPV---------------------- 505
Cdd:cd01520 4 EDLLAL-RKADGPLIDVRSPKEFFEGHLPGAINLPLldDEERALVgtlykqqgREAAIelglelvsgklkrilneawear 82
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 646496747 506 ---GKPVYVIC-QSGLRSYIACRILAQQGFKCYNLSGGWRLY 543
Cdd:cd01520 83 lerDPKLLIYCaRGGMRSQSLAWLLESLGIDVPLLEGGYKAY 124
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
96-315 |
7.33e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 55.12 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 96 ATGETFTESYDKLVLSPGArptQPA---------LPGV--GIDrlFtLRTVEDTlkirefiEQHHP-RSAVLAGGGFIGV 163
Cdd:PRK12814 270 ITLEELQKEFDAVLLAVGA---QKAskmgipgeeLPGVisGID--F-LRNVALG-------TALHPgKKVVVIGGGNTAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 164 ELMENLRELGID-VTVVQRPRQllnpldADMAAFlHAKLRQ---KGVRLHLGC------TVEGFA-------------AN 220
Cdd:PRK12814 337 DAARTALRLGAEsVTILYRRTR------EEMPAN-RAEIEEalaEGVSLRELAapvsieRSEGGLeltaikmqqgepdES 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 221 GDRVNVLLK-DEAPLTADMVVLAIGVTPDTGLAKAAGLELGIKGSILVNDR-METSAPDIYAVGDAvqvkhfVTGQDTll 298
Cdd:PRK12814 410 GRRRPVPVEgSEFTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVDPEtLQTSVAGVFAGGDC------VTGADI-- 481
|
250
....*....|....*..
gi 646496747 299 slAGPANKQGRIAADNI 315
Cdd:PRK12814 482 --AINAVEQGKRAAHAI 496
|
|
| tRNA_sel_U_synt |
TIGR03167 |
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ... |
470-551 |
9.41e-08 |
|
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274463 [Multi-domain] Cd Length: 311 Bit Score: 54.14 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 470 TLLDVRTPGEYADGHAEGFVNLPV--DDLRER-------------------------------LREVPVGKP-VYVIC-Q 514
Cdd:TIGR03167 4 PLIDVRSPAEFAEGHLPGAINLPLlnDEERAEvgtlykqvgpfaaiklglalvspnlaahveqWRAFADGPPqPLLYCwR 83
|
90 100 110
....*....|....*....|....*....|....*..
gi 646496747 515 SGLRSYIACRILAQQGFKCYNLSGGWRLYETVVRDRT 551
Cdd:TIGR03167 84 GGMRSGSLAWLLAQIGFRVPRLEGGYKAYRRFVIDQL 120
|
|
| RHOD_Lact_B |
cd01523 |
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ... |
457-539 |
1.42e-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: 49.80 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 457 PEDV-DALPRDGSVTLLDVRTPGEYADGHAEGFVNLPVDDLRER--------LREVPVGKPVYVICQSGLRSYIACRILA 527
Cdd:cd01523 3 PEDLyARLLAGQPLFILDVRNESDYERWKIDGENNTPYFDPYFDfleieediLDQLPDDQEVTVICAKEGSSQFVAELLA 82
|
90
....*....|..
gi 646496747 528 QQGFKCYNLSGG 539
Cdd:cd01523 83 ERGYDVDYLAGG 94
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
457-541 |
1.77e-07 |
|
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: 49.18 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 457 PEDVDALPRDGS-VTLLDVRTPGEYAD--GHAEGFVNLPVDDLRERLREVPVGKPVYVICQSGLRSYIACRILAQQGFK- 532
Cdd:cd01444 4 VDELAELLAAGEaPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAGFTd 83
|
90
....*....|..
gi 646496747 533 CYNLSGG---WR 541
Cdd:cd01444 84 VRSLAGGfeaWR 95
|
|
| 4RHOD_Repeat_3 |
cd01534 |
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ... |
464-539 |
6.93e-07 |
|
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 3rd repeat which does not contain the putative catalytic Cys residue.
Pssm-ID: 238792 [Multi-domain] Cd Length: 95 Bit Score: 47.46 E-value: 6.93e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 646496747 464 PRDGSVTLLDVRTPGEYADGHAEGFVNLPVDDLRERLRE-VPV-GKPVYVICQSGLRSYIACRILAQQGFKCYNLSGG 539
Cdd:cd01534 12 EGDRTVYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHfAPVrGARIVLADDDGVRADMTASWLAQMGWEVYVLEGG 89
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
458-540 |
3.41e-06 |
|
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: 46.09 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 458 EDVDALPRDGSVTLLDVRTPGEYA-----------DGHAEGFVNLP-------------VDDLRERLREVPV--GKPVYV 511
Cdd:cd01449 4 EEVLANLDSGDVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPwtslldedgtfksPEELRALFAALGItpDKPVIV 83
|
90 100 110
....*....|....*....|....*....|..
gi 646496747 512 ICQSGLRS---YIACRILAQQGFKCYNlsGGW 540
Cdd:cd01449 84 YCGSGVTAcvlLLALELLGYKNVRLYD--GSW 113
|
|
| PRK10287 |
PRK10287 |
thiosulfate:cyanide sulfurtransferase; Provisional |
472-539 |
5.56e-06 |
|
thiosulfate:cyanide sulfurtransferase; Provisional
Pssm-ID: 182356 [Multi-domain] Cd Length: 104 Bit Score: 45.22 E-value: 5.56e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 472 LDVRTPGEYADGHAEGFVNLPVDDLRERLREVPVGK--PVYVICQSGLRSYIACRILAQQGFKCYNLSGG 539
Cdd:PRK10287 24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKndTVKLYCNAGRQSGQAKEILSEMGYTHAENAGG 93
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
457-539 |
6.87e-06 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 48.30 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 457 PEDVDALPRDGSVTLLDVRTPGEYADGHAEGFVNLPVDDLRERLREV------PVGKPVYVICQSGLRSYIACRILAQQG 530
Cdd:PRK00142 116 PKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPPWVeenldpLKDKKVVMYCTGGIRCEKASAWMKHEG 195
|
90
....*....|
gi 646496747 531 FK-CYNLSGG 539
Cdd:PRK00142 196 FKeVYQLEGG 205
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
157-282 |
6.95e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 47.99 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 157 GGGFIGVELMENLRELGIDVTVVQRpRQLLNPLDADMAA--------FLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLL 228
Cdd:pfam13738 162 GGYNSAVDAALELVRKGARVTVLYR-GSEWEDRDSDPSYslspdtlnRLEELVKNGKIKAHFNAEVKEITEVDVSYKVHT 240
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 646496747 229 KDEAPLTADM-VVLAIGVTPDTGLAKAAGLELGIKGSILVNDR-METSAPDIYAVG 282
Cdd:pfam13738 241 EDGRKVTSNDdPILATGYHPDLSFLKKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
457-539 |
7.55e-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: 44.88 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 457 PEDVDALPRDGSVTLLDVRTPGEYADGHAEGFVNLPVDDLRERLREV------PVGKPVYVICQSGLRSYIACRILAQQG 530
Cdd:cd01518 6 PAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLdenldlLKGKKVLMYCTGGIRCEKASAYLKERG 85
|
90
....*....|
gi 646496747 531 FK-CYNLSGG 539
Cdd:cd01518 86 FKnVYQLKGG 95
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
147-258 |
8.56e-06 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 47.65 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 147 QHHPRSAVLAGGgfIGVELMENLRELGIDVTVVQRPRQ--LLNPLD-----------------ADMAAFLHAKLRQKGVR 207
Cdd:COG0644 25 GSFPGDKICGGG--LLPRALEELEPLGLDEPLERPVRGarFYSPGGksvelppgrgggyvvdrARFDRWLAEQAEEAGAE 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 646496747 208 LHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAIGVTpdTGLAKAAGLE 258
Cdd:COG0644 103 VRTGTRVTDVLRDDGRVVVRTGDGEEIRADYVVDADGAR--SLLARKLGLK 151
|
|
| RHOD_ThiF |
cd01526 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ... |
470-532 |
9.74e-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: 44.99 E-value: 9.74e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 646496747 470 TLLDVRTPGEYADGHAEGFVNLPVDDLRERLREVPVG----------KPVYVICQSGLRSYIACRILAQQGFK 532
Cdd:cd01526 26 VLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLqelpldndkdSPIYVVCRRGNDSQTAVRKLKELGLE 98
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
164-267 |
1.25e-05 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 47.59 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 164 ELMENLRELGIDVTVVQRP--RQLLNPLDAD------------------MAAFLHAKLRQKGVRLHLGCTVEGFAANGDR 223
Cdd:COG0665 104 AEAEALRALGLPVELLDAAelREREPGLGSPdyagglydpddghvdpakLVRALARAARAAGVRIREGTPVTGLEREGGR 183
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 646496747 224 VNVLLKDEAPLTADMVVLAIGV-TPDtgLAKAAGLELGI---KGSILV 267
Cdd:COG0665 184 VTGVRTERGTVRADAVVLAAGAwSAR--LLPMLGLRLPLrpvRGYVLV 229
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
197-276 |
1.29e-05 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 47.87 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 197 LHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAIGVTpDTGLAKAAGLELGI---KG-SILVNDRME 272
Cdd:PRK00711 207 LAAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTGGGVITADAYVVALGSY-STALLKPLGVDIPVyplKGySLTVPITDE 285
|
....
gi 646496747 273 TSAP 276
Cdd:PRK00711 286 DRAP 289
|
|
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
458-519 |
1.65e-05 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 46.71 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 458 EDVDALPRDGSVTLLDVRTPGEYAdGHAEGF----------VNLP-------------VDDLRERLREVPV--GKPVYVI 512
Cdd:COG2897 143 DEVLAALGDPDAVLVDARSPERYR-GEVEPIdpraghipgaVNLPwtdlldedgtfksAEELRALFAALGIdpDKPVITY 221
|
....*..
gi 646496747 513 CQSGLRS 519
Cdd:COG2897 222 CGSGVRA 228
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
191-242 |
2.49e-05 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 46.47 E-value: 2.49e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 646496747 191 ADMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLA 242
Cdd:COG0654 104 ADLERALLEAARALGVELRFGTEVTGLEQDADGVTVTLADGRTLRADLVVGA 155
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
231-315 |
2.82e-05 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 46.70 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 231 EAPLTADMVVLAIG-VTPDTGLAKAAGLELGIKGSILVNDR-METSAPDIYAVGDAvqvkhfVTGQdtllSLAGPANKQG 308
Cdd:PRK12810 384 EFVLPADLVLLAMGfTGPEAGLLAQFGVELDERGRVAAPDNaYQTSNPKVFAAGDM------RRGQ----SLVVWAIAEG 453
|
....*..
gi 646496747 309 RIAADNI 315
Cdd:PRK12810 454 RQAARAI 460
|
|
| RHOD_YgaP |
cd01527 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ... |
457-539 |
3.37e-05 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, and similar uncharacterized putative rhodanese-related sulfurtransferases.
Pssm-ID: 238785 [Multi-domain] Cd Length: 99 Bit Score: 42.86 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 457 PEDVDALPRDGSVtLLDVRTPGEYADGHAEGFVNLPVDDLRERLREVPVGKPVYVICQSGLRSYIACRILAQ-QGFKCYN 535
Cdd:cd01527 6 PNDACELLAQGAV-LVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIFHCRSGMRTQQNAERLAAiSAGEAYV 84
|
....
gi 646496747 536 LSGG 539
Cdd:cd01527 85 LEGG 88
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
64-285 |
4.55e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 46.30 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 64 ESFWQRFRVDMRVRHEVTAihpaektvdvrnlatgETFTESYDKLVLSPG---ARPTQpaLPGVG----IDRLFTLRTVE 136
Cdd:PRK13984 344 EALGVKIHLNTRVGKDIPL----------------EELREKHDAVFLSTGftlGRSTR--IPGTDhpdvIQALPLLREIR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 137 DTLKiREFIEQHHPRSAVLAGGGFIGVELMENLRELG------IDVTVVQRPRQLlNPLDADMAAFLHAKlrQKGVRLHL 210
Cdd:PRK13984 406 DYLR-GEGPKPKIPRSLVVIGGGNVAMDIARSMARLQkmeygeVNVKVTSLERTF-EEMPADMEEIEEGL--EEGVVIYP 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 211 G-------------------CTVEGFAANGdRVNVLL--KDEAPLTADMVVLAIGVTPDTGLAK---AAGLELgIKGSIL 266
Cdd:PRK13984 482 GwgpmevviendkvkgvkfkKCVEVFDEEG-RFNPKFdeSDQIIVEADMVVEAIGQAPDYSYLPeelKSKLEF-VRGRIL 559
|
250
....*....|....*....
gi 646496747 267 VNDRMETSAPDIYAVGDAV 285
Cdd:PRK13984 560 TNEYGQTSIPWLFAGGDIV 578
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
234-315 |
1.25e-04 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 44.87 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 234 LTADMVVLAIGVTPDT-GLAKAAGLELGiKGSILVND-RMETSAPDIYAVGDAVQVKHFVTgqdtllslagPANKQGRIA 311
Cdd:PRK12771 367 LEADLVVLAIGQDIDSaGLESVPGVEVG-RGVVQVDPnFMMTGRPGVFAGGDMVPGPRTVT----------TAIGHGKKA 435
|
....
gi 646496747 312 ADNI 315
Cdd:PRK12771 436 ARNI 439
|
|
| PRK07411 |
PRK07411 |
molybdopterin-synthase adenylyltransferase MoeB; |
469-539 |
1.26e-04 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 44.34 E-value: 1.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 646496747 469 VTLLDVRTPGEYADGHAEGFVNLPVDDLR-----ERLREVPVGKPVYVICQSGLRSYIACRILAQQGFKCYNLSGG 539
Cdd:PRK07411 300 FVLIDVRNPNEYEIARIPGSVLVPLPDIEngpgvEKVKELLNGHRLIAHCKMGGRSAKALGILKEAGIEGTNVKGG 375
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
234-315 |
1.32e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 44.62 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 234 LTADMVVLAIGVTPDTGLAKAA-GLELGIKGSILVN-DRMETSAPDIYAVGDAvqvkhfVTGQDTLLSLAGpankQGRIA 311
Cdd:PRK12831 383 LEVDTVIMSLGTSPNPLISSTTkGLKINKRGCIVADeETGLTSKEGVFAGGDA------VTGAATVILAMG----AGKKA 452
|
....
gi 646496747 312 ADNI 315
Cdd:PRK12831 453 AKAI 456
|
|
| COG3453 |
COG3453 |
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ... |
457-519 |
1.84e-04 |
|
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only];
Pssm-ID: 442676 [Multi-domain] Cd Length: 125 Bit Score: 41.36 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 457 PEDVDALPRDGSVTLLDVRTPGEYADGH----------AEG--FVNLPV----------DDLRERLREVPvgKPVYVICQ 514
Cdd:COG3453 16 PEDLAALAAAGFKTVINLRPDGEEPDQPaaadeaaaaeAAGleYVHIPVtggaitdedvEAFAAALAAAP--GPVLAHCR 93
|
....*
gi 646496747 515 SGLRS 519
Cdd:COG3453 94 SGTRS 98
|
|
| 4RHOD_Repeats |
cd01529 |
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ... |
471-542 |
1.86e-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: 40.74 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 471 LLDVRTPGEYADGHAEGFVNLPVDDLRERLREVPV------GKPVYVICQSGLRSYIACRILAQQGFK----CYNLSGGW 540
Cdd:cd01529 15 LLDVRAEDEYAAGHLPGKRSIPGAALVLRSQELQAleapgrATRYVLTCDGSLLARFAAQELLALGGKpvalLDGGTSAW 94
|
..
gi 646496747 541 RL 542
Cdd:cd01529 95 VA 96
|
|
| RHOD_PspE2 |
cd01521 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ... |
468-541 |
4.93e-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: 40.03 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 468 SVTLLDVRTPGEYADGHAEGFVNLPVDDLRER-LREVPVGKPVYVICQSglrsyIACRI-------LAQQGFKCYNLSGG 539
Cdd:cd01521 25 DFVLVDVRSAEAYARGHVPGAINLPHREICENaTAKLDKEKLFVVYCDG-----PGCNGatkaalkLAELGFPVKEMIGG 99
|
....*
gi 646496747 540 ---WR 541
Cdd:cd01521 100 ldwWK 104
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
200-284 |
1.16e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 41.77 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 200 KLRQKGVRLHLGCTVEGFAANGDRVNV-----LLKDEAPLTADMVVLAIGVTPDTG---LAKAAGLELGIKGSILVNDR- 270
Cdd:COG1148 359 RAREDGVRFIRGRVAEIEEDEGGKLVVtvedtLLGEPVEIEADLVVLATGMVPSEDneeLAKLLKLPLDQDGFFLEAHPk 438
|
90
....*....|....*..
gi 646496747 271 ---METSAPDIYAVGDA 284
Cdd:COG1148 439 lrpVETATDGIFLAGAA 455
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
471-532 |
1.52e-03 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 41.23 E-value: 1.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 646496747 471 LLDVRTPGEYADGHAEGFVNLPVDDLR--ERLREVPVGKPVYVICQSGLRSYIACRILAQQGFK 532
Cdd:PRK07878 306 LIDVREPVEWDIVHIPGAQLIPKSEILsgEALAKLPQDRTIVLYCKTGVRSAEALAALKKAGFS 369
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
72-284 |
4.86e-03 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 39.76 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 72 VDMRVRHEVTAIHPAEKTVDVRnLATGETFTEsyDKLVLSPGARPTQPALPGvgidrlftlrtvEDtlkirEFIEQH--- 148
Cdd:PRK15317 281 VDIMNLQRASKLEPAAGLIEVE-LANGAVLKA--KTVILATGARWRNMNVPG------------ED-----EYRNKGvay 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 149 --H---P-----RSAVLaGGGFIGVELmenlrelGID-------VTVVQrprqLLNPLDADmaAFLHAKLRQKG-VRLHL 210
Cdd:PRK15317 341 cpHcdgPlfkgkRVAVI-GGGNSGVEA-------AIDlagivkhVTVLE----FAPELKAD--QVLQDKLRSLPnVTIIT 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 646496747 211 GCTVEGFAANGDRVNVL-LKD-----EAPLTADMVVLAIGVTPDTGLAKAAgLELGIKGSILVNDRMETSAPDIYAVGDA 284
Cdd:PRK15317 407 NAQTTEVTGDGDKVTGLtYKDrttgeEHHLELEGVFVQIGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDC 485
|
|
| PRK06847 |
PRK06847 |
hypothetical protein; Provisional |
192-245 |
9.52e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235874 [Multi-domain] Cd Length: 375 Bit Score: 38.70 E-value: 9.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 646496747 192 DMAAFLHAKLRQKGVRLHLGCTVEGFAANGDRVNVLLKDEAPLTADMVVLAIGV 245
Cdd:PRK06847 108 ALARILADAARAAGADVRLGTTVTAIEQDDDGVTVTFSDGTTGRYDLVVGADGL 161
|
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| |
