|
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. ... |
143-566 |
3.74e-152 |
|
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: 455.74 E-value: 3.74e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 143 RLRRIDEKAEIILFEKGQNISYANCGLPYYIGGVIKERENLFVQTPEKFGRLLNLDVRVQSEVLSIDRSDKQIRVRE-AN 221
Cdd:TIGR03385 5 RVRRLDKESDIIVFEKTEDVSFANCGLPYVIGGVIDDRNKLLAYTPEVFIKKRGIDVKTNHEVIEVNDERQTVVVRNnKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 222 GREYSEHYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYLDTHKVKRATVVGGGFIGLEMAENLHARGIAVN 301
Cdd:TIGR03385 85 NETYEESYDYLILSPGASPIVPNIEGINLDIVFTLRNLEDTDAIKQYIDKNKVENVVIIGGGYIGIEMAEALRERGKNVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 302 VIEMAPQV-MAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTasLDSGEKIEAELILLSIGVRPNTKLAADAQ 380
Cdd:TIGR03385 165 LIHRSERIlNKLFDEEMNQIVEEELKKHEINLRLNEEVDSIEGEERVKV--FTSGGVYQADMVILATGIKPNSELAKDSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 381 LAIGPARGIQVNEYLQTSDPDIYAIGDAIEYPHPLTGKPWTNFLAGPANRQGRIVADNMHGQTLrSYEGAIGTAIAKIFD 460
Cdd:TIGR03385 243 LKLGETGAIWVNEKFQTSVPNIYAAGDVAESHNIITKKPAWVPLAWGANKMGRIAGENIAGNDI-EFKGVLGTNITKFFD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 461 LTVAATGLPAKALKREGLPYESVTVQPNSHAGYYPNAYPLTLKITFHPESGMLYGAQCVGIEGVDKRIDSIAQIIKRKGG 540
Cdd:TIGR03385 322 LTIASTGVTENEAKKLNIDYKTVFVKAKTHANYYPGNSPLHLKLIYEKDTRRILGAQAVGKEGADKRIDVLAAAIMAGLT 401
|
410 420
....*....|....*....|....*.
gi 543985159 541 ITDLMQTEQAYAPPFSSAKDPVALAG 566
Cdd:TIGR03385 402 VKDLFFFELAYAPPYSRVWDPLNMAG 427
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
146-467 |
9.94e-141 |
|
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: 421.91 E-value: 9.94e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 146 RIDEKAEIILFEKGQNISYANCGLPYYIGGVIKERENLFVQTPEKFGRLlNLDVRVQSEVLSIDRSDKQIRVReaNGREY 225
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERK-GIDVRTGTEVTAIDPEAKTVTLR--DGETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 226 SehYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYLDTHKVKRATVVGGGFIGLEMAENLHARGIAVNVIEM 305
Cdd:COG0446 78 S--YDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 306 APQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVlTASLDSGEKIEAELILLSIGVRPNTKLAADAQLAIGP 385
Cdd:COG0446 156 APRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDKV-AVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 386 ARGIQVNEYLQTSDPDIYAIGDAIEYPHPLTGKPWTNFLAGPANRQGRIVADNMHGQTLRsYEGaIGTAIAKIFDLTVAA 465
Cdd:COG0446 235 RGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAP-FPG-LGTFISKVFDLCIAS 312
|
..
gi 543985159 466 TG 467
Cdd:COG0446 313 TG 314
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
143-569 |
1.97e-104 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 331.75 E-value: 1.97e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 143 RLRRIDEKAEIILFEKGQNISYANCGLPYYIGGVIKERENLFVQTPEKFGRLLNLDVRVQSEVLSIDRSDKQIRVREANG 222
Cdd:PRK13512 19 QIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALAYTPEKFYDRKQITVKTYHEVIAINDERQTVTVLNRKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 223 REY-SEHYDKLLLSPGALPFVPPLpgvDSPGVFTLRNVEDTDAIKSYLDTHKVKRATVVGGGFIGLEMAENLHARGIAVN 301
Cdd:PRK13512 99 NEQfEESYDKLILSPGASANSLGF---ESDITFTLRNLEDTDAIDQFIKANQVDKALVVGAGYISLEVLENLYERGLHPT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 302 VIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRgevlTASLDSGEKIEAELILLSIGVRPNTKLAADAQL 381
Cdd:PRK13512 176 LIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGN----EVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 382 AIGPARGIQVNEYLQTSDPDIYAIGDAIE--YPHplTGKPWTNFLAGPANRQGRIVADNMHGQTLRSYEGAIGTAIAKIF 459
Cdd:PRK13512 252 KLDDKGFIPVNDKFETNVPNIYAIGDIITshYRH--VDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGFLGNNIVKFF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 460 DLTVAATGLPAKALKRegLPYESVTVQPNSHAGYYPNAYPLTLKITFHPESGMLYGAQCVGIEGVDKRIDSIAQIIKRKG 539
Cdd:PRK13512 330 DYTFASVGVKPNELKQ--FDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNRKILRAAAVGKEGADKRIDVLSMAMMNQL 407
|
410 420 430
....*....|....*....|....*....|
gi 543985159 540 GITDLMQTEQAYAPPFSSAKDPVALAGYVA 569
Cdd:PRK13512 408 TVDELTEFEVAYAPPYSHPKDLINMIGYKA 437
|
|
| YrkE |
COG2210 |
Peroxiredoxin family protein [Energy production and conversion]; |
784-938 |
2.18e-83 |
|
Peroxiredoxin family protein [Energy production and conversion];
Pssm-ID: 441812 Cd Length: 156 Bit Score: 265.15 E-value: 2.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 784 KGKTFILFSDDLDKALATFVLANGAAAMGQPVTIFFTFWGLNAIKKPHAVKAKKDIWGKMFGMMLPKNSKGLGLSKMNMF 863
Cdd:COG2210 2 KKLTIIVFSGDLDKAYAALILANGAAAMGKEVTIFFTFWGLNALRKDKKDSLKKPLGNPMFGMMMPKGPPKLPLSKPGMG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543985159 864 GLGAKMMRMVMKEKHVDSLESMRKQALENGVEFIACQMSMDVMGINREELLDEVSIGGVATYMNRAEEANINLFI 938
Cdd:COG2210 82 GLGTKMMKKRMKKKGVASLEELLELAKELGVKLYACQMSMDLMGIKKEELIDGVEIGGAATFLEEAEEADINLFI 156
|
|
| DrsE_2 |
pfam13686 |
DsrE/DsrF/DrsH-like family; DsrE is a small soluble protein involved in intracellular sulfur ... |
783-937 |
2.41e-68 |
|
DsrE/DsrF/DrsH-like family; DsrE is a small soluble protein involved in intracellular sulfur reduction. The family also includes YrkE proteins.
Pssm-ID: 433404 Cd Length: 156 Bit Score: 224.50 E-value: 2.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 783 AKGKTFILFS-DDLDKALATFVLANGAAAMGQPVTIFFTFWGLNAIKKPHAVKAKKDIWGKMFGMMLPKNSKGLGLSKMN 861
Cdd:pfam13686 1 ENKKTIIIFSkGTDDKAYAAFIIANGAAAMGMEVTMFFTFWGLNLLRKPEKVKVKKKPLEKMFGPMMPRGSKKLPLSKMN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543985159 862 MFGLGAKMMRMVMKEKHVDSLESMRKQALENGVEFIACQMSMDVMGINREELLDEVSIGGVATYMNRAEEANINLF 937
Cdd:pfam13686 81 MGGIGTKMMKKVMKDKGVPSLEELLEMAQEKGVKLVACTMTMDLMGIKKEELIDGVEIAGAATYLGDAEESDVNLF 156
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
143-407 |
3.69e-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: 204.47 E-value: 3.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 143 RLRRidEKAEIILFEKGQNISYANCGLPYYIGGVIKERENL-----FVQTPEKFGRLLNLDVRV--QSEVLSIDRSDKQI 215
Cdd:pfam07992 18 TLAQ--LGGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIAslwadLYKRKEEVVKKLNNGIEVllGTEVVSIDPGAKKV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 216 RV---REANGREYSehYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYLdthKVKRATVVGGGFIGLEMAEN 292
Cdd:pfam07992 96 VLeelVDGDGETIT--YDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKL---LPKRVVVVGGGYIGVELAAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 293 LHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEKIEAELILLSIGVRPN 372
Cdd:pfam07992 171 LAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVVAIGRRPN 250
|
250 260 270
....*....|....*....|....*....|....*
gi 543985159 373 TKLAADAQLAIGPARGIQVNEYLQTSDPDIYAIGD 407
Cdd:pfam07992 251 TELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGD 285
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
577-670 |
2.24e-43 |
|
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: 152.04 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 577 MKPLHWREMkevDPNRVTLIDARPRQAYEIEHIPGAISMPVEEIRARIGEIPHDKPIYVYCAVGMRGYFASNILRQCGFs 656
Cdd:cd01524 1 VQWHELDNY---RADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGF- 76
|
90
....*....|....
gi 543985159 657 NVRNLIGGYRLYST 670
Cdd:cd01524 77 KVKNLDGGYKTYST 90
|
|
| SirA_RHOD_Pry_redox |
cd03420 |
SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown ... |
700-768 |
2.06e-37 |
|
SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown function. Other domains include RHOD (rhodanese homology domain), and Pry_redox (pyridine nucleotide-disulphide oxidoreductase) as well as a C-terminal domain that corresponds to COG2210. This fold is referred to as a two-layered alpha/beta sandwich, structurally similar to that of translation initiation factor 3.
Pssm-ID: 239512 Cd Length: 69 Bit Score: 134.43 E-value: 2.06e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543985159 700 EVDACGMSCPGPILKLKQSIDQIAVGEQLCILATDPGFARDAQAWCDTTGHNLIRQETIKGKYKVTIEK 768
Cdd:cd03420 1 EVDACGLQCPGPILKLKKEIDKLQDGEQLEVKASDPGFARDAQAWCKSTGNTLISLETEKGKVKAVIEK 69
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
575-681 |
8.88e-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: 113.91 E-value: 8.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 575 GRMKPLHWREMKE-VDPNRVTLIDARPRQAYEIEHIPGAISMPVEEIRARIGEIPHDKPIYVYCAVGMRGYFASNILRQC 653
Cdd:COG0607 1 ASVKEISPAELAElLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80
|
90 100
....*....|....*....|....*...
gi 543985159 654 GFSNVRNLIGGYRlystitaDYSSAGQP 681
Cdd:COG0607 81 GYTNVYNLAGGIE-------AWKAAGLP 101
|
|
| TusA |
COG0425 |
Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ... |
701-770 |
2.95e-23 |
|
Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ribosomal structure and biogenesis, Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440194 Cd Length: 70 Bit Score: 93.72 E-value: 2.95e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 701 VDACGMSCPGPILKLKQSIDQIAVGEQLCILATDPGFARDAQAWCDTTGHNLIRQETIKGKYKVTIEKTA 770
Cdd:COG0425 1 LDARGLSCPLPVLKTKKALEELKPGEVLEVLADDPGAVEDIPAWCRETGHELLSVEEEGGVYRILIRKGG 70
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
589-669 |
3.95e-21 |
|
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: 89.06 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 589 DPNRVTLIDARPRQAYEIEHIPGAISMPVEEIRARIGE--------------IPHDKPIYVYCAVGMRGYFASNILRQCG 654
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeellkrlgLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90
....*....|....*
gi 543985159 655 FSNVRNLIGGYRLYS 669
Cdd:smart00450 81 FKNVYLLDGGYKEWS 95
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
591-665 |
7.51e-19 |
|
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: 82.15 E-value: 7.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 591 NRVTLIDARPRQAYEIEHIPGAISMPVE----------EIRARIGEIPHDKPIYVYCAVGMRGYFASNILRQCGFSNVRN 660
Cdd:pfam00581 4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSslslpplpllELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYV 83
|
....*
gi 543985159 661 LIGGY 665
Cdd:pfam00581 84 LDGGF 88
|
|
| TusA |
pfam01206 |
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. |
700-763 |
3.14e-17 |
|
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases.
Pssm-ID: 426125 Cd Length: 64 Bit Score: 76.46 E-value: 3.14e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543985159 700 EVDACGMSCPGPILKLKQSIDQIAVGEQLCILATDPGFARDAQAWCDTTGHNLIRQETIKGKYK 763
Cdd:pfam01206 1 TLDLRGLACPMPLLKTKKALKKLKPGEVLEVLADDPGAVEDIPRWAKETGHEVLEVEEEDGEYR 64
|
|
| DUF1661 |
pfam07877 |
Protein of unknown function (DUF1661); This is a family containing bacterial proteins of ... |
1-31 |
1.45e-12 |
|
Protein of unknown function (DUF1661); This is a family containing bacterial proteins of unknown function. Many of the proteins in this family are hypothetical.
Pssm-ID: 285160 Cd Length: 31 Bit Score: 62.51 E-value: 1.45e-12
10 20 30
....*....|....*....|....*....|.
gi 543985159 1 MVREAKNLRARTKKFSLHIFRKHAPQSEDFR 31
Cdd:pfam07877 1 LVREFKNSRAKTKKFSRHFFRKYAPQSGDFR 31
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
584-705 |
1.11e-11 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 67.73 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 584 EMKEVDPNRVTLIDARPRQAYEIEHIPGAISMPVEEIRARI-GEIP-HDKPIYVYCAVGMRGYFASNILRQCGFSNVRNL 661
Cdd:PRK08762 9 EARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIeTHLPdRDREIVLICASGTRSAHAAATLRELGYTRVASV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 543985159 662 IGGyrlystiTADYSSAGQP-ATAQLPA---KDSPSSHTQVPEVDACG 705
Cdd:PRK08762 89 AGG-------FSAWKDAGLPlERPRLLTdeqDERYSRHLRLPEVGEEG 129
|
|
| PRK00299 |
PRK00299 |
sulfurtransferase TusA; |
689-768 |
1.64e-11 |
|
sulfurtransferase TusA;
Pssm-ID: 178967 Cd Length: 81 Bit Score: 60.81 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 689 KDSPSSHTQVpeVDACGMSCPGPILKLKQSIDQIAVGEQLCILATDPGFARDAQAWCDTTGHNLIRQETIKGKYKVTIEK 768
Cdd:PRK00299 2 TDLFSSPDHT--LDALGLRCPEPVMMVRKTVRNMQPGETLLIIADDPATTRDIPSFCRFMDHELLAQETEQLPYRYLIRK 79
|
|
| selenium_YedF |
TIGR03527 |
selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in ... |
701-789 |
9.88e-04 |
|
selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in size, and include the uncharacterized YedF protein of Escherichia coli. This family shares an N-terminal domain, modeled by pfam01206, with the sulfurtransferase TusA (also called SirA). The C-terminal domain includes a typical redox-active disulfide motif, CGXC. This protein family found only among those genomes that also carry the selenium donor protein SelD, and its connection to selenium metabolism is indicated by the method of partial phylogenetic profiling vs. SelD. Its gene typically is found next to selD. Members of this family are found even when selenocysteine and selenouridine biosynthesis pathways are, except for SelD, completely absent, as in Enterococcus faecalis. Its role in selenium metabolism is unclear, but may include either detoxification or a role in labile selenoprotein biosynthesis.
Pssm-ID: 274630 [Multi-domain] Cd Length: 194 Bit Score: 41.46 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 701 VDACGMSCPGPILKLKQSIDQIAVGEQLCILaTDPGFARDaqawcdttghNLIRQETIKGkYKVTIEKtacKEEGTCVNE 780
Cdd:TIGR03527 1 IDARGLACPQPVILTKKALDELGEEGVLTVI-VDNEAAKE----------NVSKFATSLG-YEVEVEE---KEEGYWILI 65
|
....*....
gi 543985159 781 TpaKGKTFI 789
Cdd:TIGR03527 66 I--KKGEGA 72
|
|
| |
|
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. ... |
143-566 |
3.74e-152 |
|
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: 455.74 E-value: 3.74e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 143 RLRRIDEKAEIILFEKGQNISYANCGLPYYIGGVIKERENLFVQTPEKFGRLLNLDVRVQSEVLSIDRSDKQIRVRE-AN 221
Cdd:TIGR03385 5 RVRRLDKESDIIVFEKTEDVSFANCGLPYVIGGVIDDRNKLLAYTPEVFIKKRGIDVKTNHEVIEVNDERQTVVVRNnKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 222 GREYSEHYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYLDTHKVKRATVVGGGFIGLEMAENLHARGIAVN 301
Cdd:TIGR03385 85 NETYEESYDYLILSPGASPIVPNIEGINLDIVFTLRNLEDTDAIKQYIDKNKVENVVIIGGGYIGIEMAEALRERGKNVT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 302 VIEMAPQV-MAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTasLDSGEKIEAELILLSIGVRPNTKLAADAQ 380
Cdd:TIGR03385 165 LIHRSERIlNKLFDEEMNQIVEEELKKHEINLRLNEEVDSIEGEERVKV--FTSGGVYQADMVILATGIKPNSELAKDSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 381 LAIGPARGIQVNEYLQTSDPDIYAIGDAIEYPHPLTGKPWTNFLAGPANRQGRIVADNMHGQTLrSYEGAIGTAIAKIFD 460
Cdd:TIGR03385 243 LKLGETGAIWVNEKFQTSVPNIYAAGDVAESHNIITKKPAWVPLAWGANKMGRIAGENIAGNDI-EFKGVLGTNITKFFD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 461 LTVAATGLPAKALKREGLPYESVTVQPNSHAGYYPNAYPLTLKITFHPESGMLYGAQCVGIEGVDKRIDSIAQIIKRKGG 540
Cdd:TIGR03385 322 LTIASTGVTENEAKKLNIDYKTVFVKAKTHANYYPGNSPLHLKLIYEKDTRRILGAQAVGKEGADKRIDVLAAAIMAGLT 401
|
410 420
....*....|....*....|....*.
gi 543985159 541 ITDLMQTEQAYAPPFSSAKDPVALAG 566
Cdd:TIGR03385 402 VKDLFFFELAYAPPYSRVWDPLNMAG 427
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
146-467 |
9.94e-141 |
|
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: 421.91 E-value: 9.94e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 146 RIDEKAEIILFEKGQNISYANCGLPYYIGGVIKERENLFVQTPEKFGRLlNLDVRVQSEVLSIDRSDKQIRVReaNGREY 225
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERK-GIDVRTGTEVTAIDPEAKTVTLR--DGETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 226 SehYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYLDTHKVKRATVVGGGFIGLEMAENLHARGIAVNVIEM 305
Cdd:COG0446 78 S--YDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 306 APQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVlTASLDSGEKIEAELILLSIGVRPNTKLAADAQLAIGP 385
Cdd:COG0446 156 APRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDKV-AVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 386 ARGIQVNEYLQTSDPDIYAIGDAIEYPHPLTGKPWTNFLAGPANRQGRIVADNMHGQTLRsYEGaIGTAIAKIFDLTVAA 465
Cdd:COG0446 235 RGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAP-FPG-LGTFISKVFDLCIAS 312
|
..
gi 543985159 466 TG 467
Cdd:COG0446 313 TG 314
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
143-569 |
1.97e-104 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 331.75 E-value: 1.97e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 143 RLRRIDEKAEIILFEKGQNISYANCGLPYYIGGVIKERENLFVQTPEKFGRLLNLDVRVQSEVLSIDRSDKQIRVREANG 222
Cdd:PRK13512 19 QIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALAYTPEKFYDRKQITVKTYHEVIAINDERQTVTVLNRKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 223 REY-SEHYDKLLLSPGALPFVPPLpgvDSPGVFTLRNVEDTDAIKSYLDTHKVKRATVVGGGFIGLEMAENLHARGIAVN 301
Cdd:PRK13512 99 NEQfEESYDKLILSPGASANSLGF---ESDITFTLRNLEDTDAIDQFIKANQVDKALVVGAGYISLEVLENLYERGLHPT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 302 VIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRgevlTASLDSGEKIEAELILLSIGVRPNTKLAADAQL 381
Cdd:PRK13512 176 LIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGN----EVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 382 AIGPARGIQVNEYLQTSDPDIYAIGDAIE--YPHplTGKPWTNFLAGPANRQGRIVADNMHGQTLRSYEGAIGTAIAKIF 459
Cdd:PRK13512 252 KLDDKGFIPVNDKFETNVPNIYAIGDIITshYRH--VDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGFLGNNIVKFF 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 460 DLTVAATGLPAKALKRegLPYESVTVQPNSHAGYYPNAYPLTLKITFHPESGMLYGAQCVGIEGVDKRIDSIAQIIKRKG 539
Cdd:PRK13512 330 DYTFASVGVKPNELKQ--FDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNRKILRAAAVGKEGADKRIDVLSMAMMNQL 407
|
410 420 430
....*....|....*....|....*....|
gi 543985159 540 GITDLMQTEQAYAPPFSSAKDPVALAGYVA 569
Cdd:PRK13512 408 TVDELTEFEVAYAPPYSHPKDLINMIGYKA 437
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
144-520 |
4.64e-102 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 324.02 E-value: 4.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 144 LRRIDEKAEIILFEKGQNISYANCGLPYYIGGVIKErENLFVQTPEKFGRLlNLDVRVQSEVLSIDRSDKQIRVreANGR 223
Cdd:COG1251 20 LRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDE-EDLLLRPADFYEEN-GIDLRLGTRVTAIDRAARTVTL--ADGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 224 EYseHYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYLDTHKvkRATVVGGGFIGLEMAENLHARGIAVNVI 303
Cdd:COG1251 96 TL--PYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGK--RVVVIGGGLIGLEAAAALRKRGLEVTVV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 304 EMAPQVMAPV-DFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEKIEAELILLSIGVRPNTKLAADAQLA 382
Cdd:COG1251 172 ERAPRLLPRQlDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPNTELARAAGLA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 383 IGpaRGIQVNEYLQTSDPDIYAIGDAIEYPHPLTGKPwTNFLAGPANRQGRIVADNMHGQTlRSYEGAIGTAIAKIFDLT 462
Cdd:COG1251 252 VD--RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGRR-VLELVAPAYEQARVAAANLAGGP-AAYEGSVPSTKLKVFGVD 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 543985159 463 VAATGLPAkalkreglPYESVTVQPNSHAGYYpnaypltLKITFhpESGMLYGAQCVG 520
Cdd:COG1251 328 VASAGDAE--------GDEEVVVRGDPARGVY-------KKLVL--RDGRLVGAVLVG 368
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
126-569 |
6.81e-100 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 320.06 E-value: 6.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 126 MRYVIVGGVAGGATAAARLRRIDEKAEIILFEKGQNISYANCGLPYYIGGVIKERENLFVQTPEKFGRLlNLDVRVQSEV 205
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIKS-GIDVKTEHEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 206 LSIDRSDKQIRVRE-ANGREYSEHYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYLDTHKVKRATVVGGGF 284
Cdd:PRK09564 80 VKVDAKNKTITVKNlKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEIKNIVIIGAGF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 285 IGLEMAENLHARGIAVNVIEMAPQVMAPV-DFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEkIEAELI 363
Cdd:PRK09564 160 IGLEAVEAAKHLGKNVRIIQLEDRILPDSfDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGE-YEADVV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 364 LLSIGVRPNTKLAADAQLAIGPARGIQVNEYLQTSDPDIYAIGDAIEYPHPLTGKPWTNFLAGPANRQGRIVADNMHGQT 443
Cdd:PRK09564 239 IVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGRH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 444 LrSYEGAIGTAIAKIFDLTVAATGLPAKALKREGLPYESVTVQPNSHAGYYPNAYPLTLKITFHPESGMLYGAQCVGIEG 523
Cdd:PRK09564 319 V-SFKGTLGSACIKVLDLEAARTGLTEEEAKKLGIDYKTVFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQIIGKKG 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 543985159 524 VDKRIDSIAQIIKRKGGITDLMQTEQAYAPPFSSAKDPVALAGYVA 569
Cdd:PRK09564 398 AVLRIDALAVAIYAKLTTQELGMMDFCYAPPFARTWDALNVAGNVA 443
|
|
| YrkE |
COG2210 |
Peroxiredoxin family protein [Energy production and conversion]; |
784-938 |
2.18e-83 |
|
Peroxiredoxin family protein [Energy production and conversion];
Pssm-ID: 441812 Cd Length: 156 Bit Score: 265.15 E-value: 2.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 784 KGKTFILFSDDLDKALATFVLANGAAAMGQPVTIFFTFWGLNAIKKPHAVKAKKDIWGKMFGMMLPKNSKGLGLSKMNMF 863
Cdd:COG2210 2 KKLTIIVFSGDLDKAYAALILANGAAAMGKEVTIFFTFWGLNALRKDKKDSLKKPLGNPMFGMMMPKGPPKLPLSKPGMG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543985159 864 GLGAKMMRMVMKEKHVDSLESMRKQALENGVEFIACQMSMDVMGINREELLDEVSIGGVATYMNRAEEANINLFI 938
Cdd:COG2210 82 GLGTKMMKKRMKKKGVASLEELLELAKELGVKLYACQMSMDLMGIKKEELIDGVEIGGAATFLEEAEEADINLFI 156
|
|
| DrsE_2 |
pfam13686 |
DsrE/DsrF/DrsH-like family; DsrE is a small soluble protein involved in intracellular sulfur ... |
783-937 |
2.41e-68 |
|
DsrE/DsrF/DrsH-like family; DsrE is a small soluble protein involved in intracellular sulfur reduction. The family also includes YrkE proteins.
Pssm-ID: 433404 Cd Length: 156 Bit Score: 224.50 E-value: 2.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 783 AKGKTFILFS-DDLDKALATFVLANGAAAMGQPVTIFFTFWGLNAIKKPHAVKAKKDIWGKMFGMMLPKNSKGLGLSKMN 861
Cdd:pfam13686 1 ENKKTIIIFSkGTDDKAYAAFIIANGAAAMGMEVTMFFTFWGLNLLRKPEKVKVKKKPLEKMFGPMMPRGSKKLPLSKMN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543985159 862 MFGLGAKMMRMVMKEKHVDSLESMRKQALENGVEFIACQMSMDVMGINREELLDEVSIGGVATYMNRAEEANINLF 937
Cdd:pfam13686 81 MGGIGTKMMKKVMKDKGVPSLEELLEMAQEKGVKLVACTMTMDLMGIKKEELIDGVEIAGAATYLGDAEESDVNLF 156
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
143-407 |
3.69e-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: 204.47 E-value: 3.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 143 RLRRidEKAEIILFEKGQNISYANCGLPYYIGGVIKERENL-----FVQTPEKFGRLLNLDVRV--QSEVLSIDRSDKQI 215
Cdd:pfam07992 18 TLAQ--LGGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIAslwadLYKRKEEVVKKLNNGIEVllGTEVVSIDPGAKKV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 216 RV---REANGREYSehYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYLdthKVKRATVVGGGFIGLEMAEN 292
Cdd:pfam07992 96 VLeelVDGDGETIT--YDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKL---LPKRVVVVGGGYIGVELAAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 293 LHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEKIEAELILLSIGVRPN 372
Cdd:pfam07992 171 LAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVVAIGRRPN 250
|
250 260 270
....*....|....*....|....*....|....*
gi 543985159 373 TKLAADAQLAIGPARGIQVNEYLQTSDPDIYAIGD 407
Cdd:pfam07992 251 TELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGD 285
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
196-467 |
7.80e-52 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 195.43 E-value: 7.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 196 NLDVRVQSEVLSIDRSDKQirVREANGREYSehYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYldTHKVK 275
Cdd:TIGR02374 68 GITLYTGETVIQIDTDQKQ--VITDAGRTLS--YDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAM--AQRFK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 276 RATVVGGGFIGLEMAENLHARGIAVNVIEMAPQVMA-PVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDS 354
Cdd:TIGR02374 142 KAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAkQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 355 GEKIEAELILLSIGVRPNTKLAADAQLAIGpaRGIQVNEYLQTSDPDIYAIGDAIEYPHPLTGkpwtnfLAGPANRQGRI 434
Cdd:TIGR02374 222 GSSLEADLIVMAAGIRPNDELAVSAGIKVN--RGIIVNDSMQTSDPDIYAVGECAEHNGRVYG------LVAPLYEQAKV 293
|
250 260 270
....*....|....*....|....*....|...
gi 543985159 435 VADNMHGQTLRSYEGAIGTAIAKIFDLTVAATG 467
Cdd:TIGR02374 294 LADHICGVECEEYEGSDLSAKLKLLGVDVWSAG 326
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
211-547 |
6.04e-48 |
|
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: 177.59 E-value: 6.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 211 SDKQIRVreANGREYSehYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVedtdaiksyLDTHKV-KRATVVGGGFIGLEM 289
Cdd:COG1249 117 DPHTVEV--TGGETLT--ADHIVIATGSRPRVPPIPGLDEVRVLTSDEA---------LELEELpKSLVVIGGGYIGLEF 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 290 AENLHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEK---IEAELILLS 366
Cdd:COG1249 184 AQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDGGGeeaVEADKVLVA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 367 IGVRPNTK---LAAdAQLAIGPARGIQVNEYLQTSDPDIYAIGDAieyphplTGKPWtnfLAGPANRQGRIVADNMHGQT 443
Cdd:COG1249 264 TGRRPNTDglgLEA-AGVELDERGGIKVDEYLRTSVPGIYAIGDV-------TGGPQ---LAHVASAEGRVAAENILGKK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 444 LRSYE-GAIGTAiakIF-DLTVAATGLPAKALKREGLPYESVTVQpnshagYYPNAYPLT-------LKITFHPESGMLY 514
Cdd:COG1249 333 PRPVDyRAIPSV---VFtDPEIASVGLTEEEAREAGIDVKVGKFP------FAANGRALAlgetegfVKLIADAETGRIL 403
|
330 340 350
....*....|....*....|....*....|...
gi 543985159 515 GAQCVGiEGVDKRIDSIAQIIKRKGGITDLMQT 547
Cdd:COG1249 404 GAHIVG-PHAGELIHEAALAMEMGLTVEDLADT 435
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
181-410 |
3.87e-46 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 170.10 E-value: 3.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 181 ENLFVQTPEKFGRLLNLDVRVQSEVLSIDRSDKQIRvreANGREYseHYDKLLLSPGALPFVPPLPGVDSpgVFTLRNVE 260
Cdd:PRK04965 57 DDLTRQSAGEFAEQFNLRLFPHTWVTDIDAEAQVVK---SQGNQW--QYDKLVLATGASAFVPPIPGREL--MLTLNSQQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 261 DTDAIKSYLDThkVKRATVVGGGFIGLEMAENLHARGIAVNVIEMAPQVMA---PVDFSMAtiVHAHLQEKGIGLYLGKA 337
Cdd:PRK04965 130 EYRAAETQLRD--AQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLAslmPPEVSSR--LQHRLTEMGVHLLLKSQ 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543985159 338 VKSIEKRGEVLTASLDSGEKIEAELILLSIGVRPNTKLAADAQLAIGpaRGIQVNEYLQTSDPDIYAIGDAIE 410
Cdd:PRK04965 206 LQGLEKTDSGIRATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVN--RGIVVDSYLQTSAPDIYALGDCAE 276
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
577-670 |
2.24e-43 |
|
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: 152.04 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 577 MKPLHWREMkevDPNRVTLIDARPRQAYEIEHIPGAISMPVEEIRARIGEIPHDKPIYVYCAVGMRGYFASNILRQCGFs 656
Cdd:cd01524 1 VQWHELDNY---RADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGF- 76
|
90
....*....|....
gi 543985159 657 NVRNLIGGYRLYST 670
Cdd:cd01524 77 KVKNLDGGYKTYST 90
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
142-475 |
8.14e-39 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 149.13 E-value: 8.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 142 ARLRR-IDEKAEIILFEKGqniSYANC--GLPYYIGGVIKEREnlfVQTPekFGRLL-NLDVR-VQSEVLSIDRSDKQIR 216
Cdd:COG1252 18 RRLRKkLGGDAEVTLIDPN---PYHLFqpLLPEVAAGTLSPDD---IAIP--LRELLrRAGVRfIQGEVTGIDPEARTVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 217 VreANGREYSehYDKLLLSPGALPFVPPLPGVDsPGVFTLRNVEDTDAIKSYLDThKVKRAT--------VVGGGFIGLE 288
Cdd:COG1252 90 L--ADGRTLS--YDYLVIATGSVTNFFGIPGLA-EHALPLKTLEDALALRERLLA-AFERAErrrlltivVVGGGPTGVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 289 MA-------------ENLHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGevltASLDSG 355
Cdd:COG1252 164 LAgelaellrkllryPGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADG----VTLEDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 356 EKIEAELILLSIGVRPNtKLAADAQLAIGPARGIQVNEYLQT-SDPDIYAIGDAIEYPHPlTGKPW--TnflAGPANRQG 432
Cdd:COG1252 240 EEIPADTVIWAAGVKAP-PLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDP-DGKPVpkT---AQAAVQQA 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 543985159 433 RIVADN----MHGQTLRSYEG-------AIG--TAIAKIFDLTVaaTGLPAKALKR 475
Cdd:COG1252 315 KVLAKNiaalLRGKPLKPFRYrdkgclaSLGrgAAVADVGGLKL--SGFLAWLLKR 368
|
|
| SirA_RHOD_Pry_redox |
cd03420 |
SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown ... |
700-768 |
2.06e-37 |
|
SirA_RHOD_Pry_redox. SirA-like domain located within a multidomain protein of unknown function. Other domains include RHOD (rhodanese homology domain), and Pry_redox (pyridine nucleotide-disulphide oxidoreductase) as well as a C-terminal domain that corresponds to COG2210. This fold is referred to as a two-layered alpha/beta sandwich, structurally similar to that of translation initiation factor 3.
Pssm-ID: 239512 Cd Length: 69 Bit Score: 134.43 E-value: 2.06e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543985159 700 EVDACGMSCPGPILKLKQSIDQIAVGEQLCILATDPGFARDAQAWCDTTGHNLIRQETIKGKYKVTIEK 768
Cdd:cd03420 1 EVDACGLQCPGPILKLKKEIDKLQDGEQLEVKASDPGFARDAQAWCKSTGNTLISLETEKGKVKAVIEK 69
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
196-467 |
5.18e-37 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 150.27 E-value: 5.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 196 NLDVRVQSEVLSIDRSDKQIRvrEANGREYseHYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYldTHKVK 275
Cdd:PRK14989 73 GIKVLVGERAITINRQEKVIH--SSAGRTV--FYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEAC--ARRSK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 276 RATVVGGGFIGLEMAENLHARGIAVNVIEMAPQVMAP-VDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVL--TASL 352
Cdd:PRK14989 147 RGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEqLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEArkTMRF 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 353 DSGEKIEAELILLSIGVRPNTKLAADAQLAIGPARGIQVNEYLQTSDPDIYAIGDAIEYPHPLTGkpwtnfLAGPANRQG 432
Cdd:PRK14989 227 ADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECASWNNRVFG------LVAPGYKMA 300
|
250 260 270
....*....|....*....|....*....|....*
gi 543985159 433 RIVADNMHGQTLRsYEGAIGTAIAKIFDLTVAATG 467
Cdd:PRK14989 301 QVAVDHLLGSENA-FEGADLSAKLKLLGVDVGGIG 334
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
210-565 |
1.85e-34 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 138.16 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 210 RSDKQIRVREANGREYSEhYDKLLLSPGALPFVPPLP-GVDSPGVFTlrnveDTDAIKSyldTHKVKRATVVGGGFIGLE 288
Cdd:TIGR01350 114 LDPGTVSVTGENGEETLE-AKNIIIATGSRPRSLPGPfDFDGKVVIT-----STGALNL---EEVPESLVIIGGGVIGIE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 289 MAENLHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSG--EKIEAELILLS 366
Cdd:TIGR01350 185 FASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTYENKGGetETLTGEKVLVA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 367 IGVRPNTKLAADAQLAIG--PARGIQVNEYLQTSDPDIYAIGDAIeyphpltGKPwtnFLAGPANRQGRIVADNMHGQTl 444
Cdd:TIGR01350 265 VGRKPNTEGLGLEKLGVEldERGRIVVDEYMRTNVPGIYAIGDVI-------GGP---MLAHVASHEGIVAAENIAGKE- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 445 rSYEGAIGTAIAKIF-DLTVAATGLPAKALKREGLPYESVTVQ--PNSHAGYYPNAYPLtLKITFHPESGMLYGAQCVGI 521
Cdd:TIGR01350 334 -PAHIDYDAVPSVIYtDPEVASVGLTEEQAKEAGYDVKIGKFPfaANGKALALGETDGF-VKIIADKKTGEILGAHIIGP 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 543985159 522 EGVDkRIDSIAQIIKRKGGITDLMQTEQAYaPPFSSAKDPVALA 565
Cdd:TIGR01350 412 HATE-LISEAALAMELEGTVEELARTIHPH-PTLSEAIKEAALA 453
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
214-547 |
7.83e-34 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 136.04 E-value: 7.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 214 QIRVREANG-REYS-EHydkLLLSPGALPFVppLPGVDSPGvftlRNVED-TDAIKsyLDtHKVKRATVVGGGFIGLEMA 290
Cdd:PRK06416 121 TVRVMTEDGeQTYTaKN---IILATGSRPRE--LPGIEIDG----RVIWTsDEALN--LD-EVPKSLVVIGGGYIGVEFA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 291 ENLHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEK---IEAELILLSI 367
Cdd:PRK06416 189 SAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQTDDGVTVTLEDGGKeetLEADYVLVAV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 368 GVRPNTKLAADAQLAIGPARG-IQVNEYLQTSDPDIYAIGDAieyphplTGKPWtnfLAGPANRQGRIVADNMHGQTL-- 444
Cdd:PRK06416 269 GRRPNTENLGLEELGVKTDRGfIEVDEQLRTNVPNIYAIGDI-------VGGPM---LAHKASAEGIIAAEAIAGNPHpi 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 445 --RSYEGAIGTaiakifDLTVAATGL-PAKAlKREGLPYESVTvqpnshagyYP---NAYPLTL-------KITFHPESG 511
Cdd:PRK06416 339 dyRGIPAVTYT------HPEVASVGLtEAKA-KEEGFDVKVVK---------FPfagNGKALALgetdgfvKLIFDKKDG 402
|
330 340 350
....*....|....*....|....*....|....*.
gi 543985159 512 MLYGAQCVGIEgVDKRIDSIAQIIKRKGGITDLMQT 547
Cdd:PRK06416 403 EVLGAHMVGAR-ASELIQEAQLAINWEATPEDLALT 437
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
144-441 |
2.82e-33 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 133.13 E-value: 2.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 144 LRRIDEKAEIILFEKGQNISYANCGLPYYIggVIKERENLFVQTPEKFGRLLNLDVRVQSEVLSIDRSDKQIRVreANGR 223
Cdd:PRK09754 22 LRQQGFTGELHLFSDERHLPYERPPLSKSM--LLEDSPQLQQVLPANWWQENNVHLHSGVTIKTLGRDTRELVL--TNGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 224 EYseHYDKLLLSPGALpfVPPLPGVDSPG--VFTLRNVEDTDAIKSYLdtHKVKRATVVGGGFIGLEMAENLHARGIAVN 301
Cdd:PRK09754 98 SW--HWDQLFIATGAA--ARPLPLLDALGerCFTLRHAGDAARLREVL--QPERSVVIVGAGTIGLELAASATQRRCKVT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 302 VIEMAPQVM---APvDFSMATIVHAHlQEKGIGLYLGKAVKSIEKrGEVLTASLDSGEKIEAELILLSIGVRPNTKLAAD 378
Cdd:PRK09754 172 VIELAATVMgrnAP-PPVQRYLLQRH-QQAGVRILLNNAIEHVVD-GEKVELTLQSGETLQADVVIYGIGISANDQLARE 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543985159 379 AQLAIgpARGIQVNEYLQTSDPDIYAIGDAIEYPHPlTG-----KPWTNflagpANRQGRIVADNMHG 441
Cdd:PRK09754 249 ANLDT--ANGIVIDEACRTCDPAIFAGGDVAITRLD-NGalhrcESWEN-----ANNQAQIAAAAMLG 308
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
214-520 |
1.14e-30 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 126.81 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 214 QIRVREANGREYSEHYDKLLLSPGALPFVPPlpGVDspgvFTLRNVEDTDAIKSyLDtHKVKRATVVGGGFIGLEMAENL 293
Cdd:PRK05249 123 TVEVECPDGEVETLTADKIVIATGSRPYRPP--DVD----FDHPRIYDSDSILS-LD-HLPRSLIIYGAGVIGCEYASIF 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 294 HARGIAVNVIEMAPQvmaPVDFSMATIVHA---HLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEKIEAELILLSIGVR 370
Cdd:PRK05249 195 AALGVKVTLINTRDR---LLSFLDDEISDAlsyHLRDSGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLYANGRT 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 371 PNTK--------LAADAqlaigpaRG-IQVNEYLQTSDPDIYAIGDAIEYPHpltgkpwtnfLAGPANRQGRIVADNMHG 441
Cdd:PRK05249 272 GNTDglnlenagLEADS-------RGqLKVNENYQTAVPHIYAVGDVIGFPS----------LASASMDQGRIAAQHAVG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 442 QTLRSYEGAIGTAIAKIFDL-TVAATglpAKALKREGLPYESvtvqpnSHAGYYPNA--------YPLtLKITFHPESGM 512
Cdd:PRK05249 335 EATAHLIEDIPTGIYTIPEIsSVGKT---EQELTAAKVPYEV------GRARFKELAraqiagdnVGM-LKILFHRETLE 404
|
....*...
gi 543985159 513 LYGAQCVG 520
Cdd:PRK05249 405 ILGVHCFG 412
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
211-547 |
1.19e-30 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 126.45 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 211 SDKQIRVreaNGREYseHYDKLLLSPGALpfVPPLPGVD---------SPGVFTLRNVEdtdaiksyldthkvKRATVVG 281
Cdd:PRK06292 118 DPNTVEV---NGERI--EAKNIVIATGSR--VPPIPGVWlilgdrlltSDDAFELDKLP--------------KSLAVIG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 282 GGFIGLEMAENLHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKgIGLYLGKAVKSIEKRGEVLTASLDSGEK---I 358
Cdd:PRK06292 177 GGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGGKtetI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 359 EAELILLSIGVRPNTKLAADAQLAIGP-ARG-IQVNEYLQTSDPDIYAIGDAieyphplTGKPwtnFLAGPANRQGRIVA 436
Cdd:PRK06292 256 EADYVLVATGRRPNTDGLGLENTGIELdERGrPVVDEHTQTSVPGIYAAGDV-------NGKP---PLLHEAADEGRIAA 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 437 DN-MHGQTLRSYEGAIGTAiakIF-DLTVAATGLPAKALKREGLPYESVTV----QPNSHA-----GYypnaypltLKIT 505
Cdd:PRK06292 326 ENaAGDVAGGVRYHPIPSV---VFtDPQIASVGLTEEELKAAGIDYVVGEVpfeaQGRARVmgkndGF--------VKVY 394
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 543985159 506 FHPESGMLYGAQCVGIEGvDKRIDSIAQIIKRKGGITDLMQT 547
Cdd:PRK06292 395 ADKKTGRLLGAHIIGPDA-EHLIHLLAWAMQQGLTVEDLLRM 435
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
575-681 |
8.88e-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: 113.91 E-value: 8.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 575 GRMKPLHWREMKE-VDPNRVTLIDARPRQAYEIEHIPGAISMPVEEIRARIGEIPHDKPIYVYCAVGMRGYFASNILRQC 653
Cdd:COG0607 1 ASVKEISPAELAElLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80
|
90 100
....*....|....*....|....*...
gi 543985159 654 GFSNVRNLIGGYRlystitaDYSSAGQP 681
Cdd:COG0607 81 GYTNVYNLAGGIE-------AWKAAGLP 101
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
211-547 |
4.20e-29 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 121.85 E-value: 4.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 211 SDKQIRVreaNGREYseHYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYLdthkvkraTVVGGGFIGLEMA 290
Cdd:PRK06370 121 SPNTVRV---GGETL--RAKRIFINTGARAAIPPIPGLDEVGYLTNETIFSLDELPEHL--------VIIGGGYIGLEFA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 291 ENLHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDS---GEKIEAELILLSI 367
Cdd:PRK06370 188 QMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDCnggAPEITGSHILVAV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 368 GVRPNTK---LAAdAQLAIGPARGIQVNEYLQTSDPDIYAIGDaieyphpLTGKP-WTNFlagpANRQGRIVADNMHGQT 443
Cdd:PRK06370 268 GRVPNTDdlgLEA-AGVETDARGYIKVDDQLRTTNPGIYAAGD-------CNGRGaFTHT----AYNDARIVAANLLDGG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 444 LRSYEGAIgTAIAKIFDLTVAATGLPAKALKREGLPYESVTVqPNSH----------AGYypnaypltLKITFHPESGML 513
Cdd:PRK06370 336 RRKVSDRI-VPYATYTDPPLARVGMTEAEARKSGRRVLVGTR-PMTRvgravekgetQGF--------MKVVVDADTDRI 405
|
330 340 350
....*....|....*....|....*....|....
gi 543985159 514 YGAQCVGIEGvDKRIDSIAQIIKRKGGITDLMQT 547
Cdd:PRK06370 406 LGATILGVHG-DEMIHEILDAMYAGAPYTTLSRA 438
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
588-666 |
2.89e-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: 94.67 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 588 VDPNRVTLIDARPRQAYEIEHIPGAISMPVEEIRARIG--EIPHDKPIYVYCAVGMRGYFASNILRQCGFSNVRNLIGGY 665
Cdd:cd00158 6 LDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGGM 85
|
.
gi 543985159 666 R 666
Cdd:cd00158 86 L 86
|
|
| TusA |
COG0425 |
Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ... |
701-770 |
2.95e-23 |
|
Sulfur carrier protein TusA (tRNA thiolation, molybdenum cofactor biosynthesis) [Translation, ribosomal structure and biogenesis, Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440194 Cd Length: 70 Bit Score: 93.72 E-value: 2.95e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 701 VDACGMSCPGPILKLKQSIDQIAVGEQLCILATDPGFARDAQAWCDTTGHNLIRQETIKGKYKVTIEKTA 770
Cdd:COG0425 1 LDARGLSCPLPVLKTKKALEELKPGEVLEVLADDPGAVEDIPAWCRETGHELLSVEEEGGVYRILIRKGG 70
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
235-480 |
3.01e-21 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 98.07 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 235 SPGALPFVPplpgvdspgvFTLRNVEDTDAIksyLDTHKV-KRATVVGGGFIGLEMAENLHARGIAVNVIEMAPQVMAPV 313
Cdd:PRK06327 156 EPRHLPGVP----------FDNKIILDNTGA---LNFTEVpKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 314 DFSMATIVHAHLQEKGIGLYLGKAVKSIE--KRGEVLTASLDSGE--KIEAELILLSIGVRPNTK-LAADAQLAIGPARG 388
Cdd:PRK06327 223 DEQVAKEAAKAFTKQGLDIHLGVKIGEIKtgGKGVSVAYTDADGEaqTLEVDKLIVSIGRVPNTDgLGLEAVGLKLDERG 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 389 -IQVNEYLQTSDPDIYAIGDaieyphpLTGKPWtnfLAGPANRQGRIVADNMHGQTLRSYEGAIGTAIakifdLT---VA 464
Cdd:PRK06327 303 fIPVDDHCRTNVPNVYAIGD-------VVRGPM---LAHKAEEEGVAVAERIAGQKGHIDYNTIPWVI-----YTspeIA 367
|
250
....*....|....*.
gi 543985159 465 ATGLPAKALKREGLPY 480
Cdd:PRK06327 368 WVGKTEQQLKAEGVEY 383
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
589-669 |
3.95e-21 |
|
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: 89.06 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 589 DPNRVTLIDARPRQAYEIEHIPGAISMPVEEIRARIGE--------------IPHDKPIYVYCAVGMRGYFASNILRQCG 654
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeellkrlgLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90
....*....|....*
gi 543985159 655 FSNVRNLIGGYRLYS 669
Cdd:smart00450 81 FKNVYLLDGGYKEWS 95
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
219-409 |
8.94e-21 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 96.38 E-value: 8.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 219 EANGREYSEhyDKLLLSPGALPFVPPLPG----VDSPGVFTLrnvedtdaiksyldTHKVKRATVVGGGFIGLEMAENLH 294
Cdd:PRK06116 124 EVNGERYTA--DHILIATGGRPSIPDIPGaeygITSDGFFAL--------------EELPKRVAVVGAGYIAVEFAGVLN 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 295 ARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGE-VLTASLDSGEKIEAELILLSIGVRPNT 373
Cdd:PRK06116 188 GLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADgSLTLTLEDGETLTVDCLIWAIGREPNT 267
|
170 180 190
....*....|....*....|....*....|....*....
gi 543985159 374 K---LAAdAQLAIGPARGIQVNEYLQTSDPDIYAIGDAI 409
Cdd:PRK06116 268 DglgLEN-AGVKLNEKGYIIVDEYQNTNVPGIYAVGDVT 305
|
|
| SirA_YedF_YeeD |
cd00291 |
SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and ... |
700-768 |
2.16e-20 |
|
SirA, YedF, and YeeD. Two-layered alpha/beta sandwich domain. SirA (also known as UvrY, and YhhP) belongs to a family of bacterial two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.
Pssm-ID: 238180 Cd Length: 69 Bit Score: 85.68 E-value: 2.16e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543985159 700 EVDACGMSCPGPILKLKQSIDQIAVGEQLCILATDPGFARDAQAWCDTTGHNLIRQETIKGKYKVTIEK 768
Cdd:cd00291 1 TLDLRGLPCPLPVLKTKKALEKLKSGEVLEVLLDDPGAVEDIPAWAKETGHEVLEVEEEGGVYRILIRK 69
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
181-413 |
2.95e-19 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 89.41 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 181 ENLFVQTpEKFGrllnLDVRVQsEVLSIDRSDKQIRVREANGREYseHYDKLLLSPGALPFVPPLPGVDSpgvFTLRNVe 260
Cdd:COG0492 61 ERLREQA-ERFG----AEILLE-EVTSVDKDDGPFRVTTDDGTEY--EAKAVIIATGAGPRKLGLPGEEE---FEGRGV- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 261 dtdaikSY---LDTHKV--KRATVVGGGFIGLEMAENLHARGIAVNVIEMAPQVMApvdfsmativHAHLQEK-----GI 330
Cdd:COG0492 129 ------SYcatCDGFFFrgKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRA----------SKILVERlranpKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 331 GLYLGKAVKSIEKRG---EVLTASLDSGEK--IEAELILLSIGVRPNTKLAADAQLAIGPARGIQVNEYLQTSDPDIYAI 405
Cdd:COG0492 193 EVLWNTEVTEIEGDGrveGVTLKNVKTGEEkeLEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAA 272
|
....*...
gi 543985159 406 GDAIEYPH 413
Cdd:COG0492 273 GDVRDYKY 280
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
591-665 |
7.51e-19 |
|
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: 82.15 E-value: 7.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 591 NRVTLIDARPRQAYEIEHIPGAISMPVE----------EIRARIGEIPHDKPIYVYCAVGMRGYFASNILRQCGFSNVRN 660
Cdd:pfam00581 4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSslslpplpllELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYV 83
|
....*
gi 543985159 661 LIGGY 665
Cdd:pfam00581 84 LDGGF 88
|
|
| COG2044 |
COG2044 |
Predicted peroxiredoxin, DsrE/DsrF-like family [General function prediction only]; |
792-933 |
1.63e-18 |
|
Predicted peroxiredoxin, DsrE/DsrF-like family [General function prediction only];
Pssm-ID: 441647 Cd Length: 121 Bit Score: 82.25 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 792 SDDLDKALATFVLANGAAAMGQPVTIFFTFWGLNAIKKPHAVKakkdiwgkmfgmmlpknskglglskmnmfglgakmmr 871
Cdd:COG2044 13 PDDPERATMAFVLAAAAAAMGAEVTIFLTGEGVRLAKKGVAEK------------------------------------- 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543985159 872 mvMKEKHVDSLESMRKQALENGVEFIACQMSMDVMGINREELLDEVSIGGVATYMNRAEEAN 933
Cdd:COG2044 56 --IRAPGGPPLADLLEEAIEAGVKVYVCEPCLKARGLTEEDLIPGVEIAGAADFAELALEAD 115
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
230-520 |
3.50e-18 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 88.47 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 230 DKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKsyldthkvKRATVVGGGFIGLEMAENLHARGIAVNVIEMAPQV 309
Cdd:PRK07846 130 DQVVIAAGSRPVIPPVIADSGVRYHTSDTIMRLPELP--------ESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 310 MAPVDfsmATIVHA--HLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEKIEAELILLSIGVRPNTKL--AADAQLAIGP 385
Cdd:PRK07846 202 LRHLD---DDISERftELASKRWDVRLGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGRVPNGDLldAAAAGVDVDE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 386 ARGIQVNEYLQTSDPDIYAIGDaIEYPHPLTGKpwtnflagpANRQGRIVADNM-HGQTLRSYE-----GAIGTaiakif 459
Cdd:PRK07846 279 DGRVVVDEYQRTSAEGVFALGD-VSSPYQLKHV---------ANHEARVVQHNLlHPDDLIASDhrfvpAAVFT------ 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543985159 460 DLTVAATGLPAKALKREGLPYeSVTVQPnshagYYPNAYPLTLKITFH-------PESGMLYGAQCVG 520
Cdd:PRK07846 343 HPQIASVGLTENEARAAGLDI-TVKVQN-----YGDVAYGWAMEDTTGfvkliadRDTGRLLGAHIIG 404
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
211-520 |
4.44e-18 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 87.88 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 211 SDKQIRVREANGREYSEHyDKLLLSPGALPFVPPLPGVDspgvfTLRNVEDTDAIKSyLDTHKvKRATVVGGGFIGLEMA 290
Cdd:PRK07251 102 SNKVIEVQAGDEKIELTA-ETIVINTGAVSNVLPIPGLA-----DSKHVYDSTGIQS-LETLP-ERLGIIGGGNIGLEFA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 291 eNLHAR-GIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGE--VLTAsldSGEKIEAELILLSI 367
Cdd:PRK07251 174 -GLYNKlGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKNDGDqvLVVT---EDETYRFDALLYAT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 368 GVRPNTklaADAQL-----AIGPARGIQVNEYLQTSDPDIYAIGDaieyphpLTGKPWTNFLagpANRQGRIVADNMHGQ 442
Cdd:PRK07251 250 GRKPNT---EPLGLentdiELTERGAIKVDDYCQTSVPGVFAVGD-------VNGGPQFTYI---SLDDFRIVFGYLTGD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 443 TLRSYE--GAIGTAIakIFDLTVAATGLPAKALKREGLPYES----VTVQPNSHA-GYYPNAYpltlKITFHPESGMLYG 515
Cdd:PRK07251 317 GSYTLEdrGNVPTTM--FITPPLSQVGLTEKEAKEAGLPYAVkellVAAMPRAHVnNDLRGAF----KVVVNTETKEILG 390
|
....*
gi 543985159 516 AQCVG 520
Cdd:PRK07251 391 ATLFG 395
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
276-355 |
1.10e-17 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 78.40 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 276 RATVVGGGFIGLEMAENLHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSG 355
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTDG 80
|
|
| TusA |
pfam01206 |
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases. |
700-763 |
3.14e-17 |
|
Sulfurtransferase TusA; This family includes the TusA sulfurtransferases.
Pssm-ID: 426125 Cd Length: 64 Bit Score: 76.46 E-value: 3.14e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543985159 700 EVDACGMSCPGPILKLKQSIDQIAVGEQLCILATDPGFARDAQAWCDTTGHNLIRQETIKGKYK 763
Cdd:pfam01206 1 TLDLRGLACPMPLLKTKKALKKLKPGEVLEVLADDPGAVEDIPRWAKETGHEVLEVEEEDGEYR 64
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
196-407 |
8.30e-16 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 80.83 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 196 NLDVrVQSEVLSIDrsDKQIRVREAnGREYSEHYDKLLLSPGALPFVPPLPGVDS-PGVFtlrnveDTDAIKSYldTHKV 274
Cdd:PRK08010 91 NIDV-IDGQAEFIN--NHSLRVHRP-EGNLEIHGEKIFINTGAQTVVPPIPGITTtPGVY------DSTGLLNL--KELP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 275 KRATVVGGGFIGLEMAENLHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSI-EKRGEVLTASLD 353
Cdd:PRK08010 159 GHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERIsHHENQVQVHSEH 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 543985159 354 SGEKIEAelILLSIGVRPNTK--LAADAQLAIGPARGIQVNEYLQTSDPDIYAIGD 407
Cdd:PRK08010 239 AQLAVDA--LLIASGRQPATAslHPENAGIAVNERGAIVVDKYLHTTADNIWAMGD 292
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
275-408 |
1.30e-15 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 80.63 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 275 KRATVVGGGFIGLEMAENLHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDS 354
Cdd:PLN02507 204 KRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDH 283
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 543985159 355 GEKIEAELILLSIGVRPNTKLA--ADAQLAIGPARGIQVNEYLQTSDPDIYAIGDA 408
Cdd:PLN02507 284 GEEFVADVVLFATGRAPNTKRLnlEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV 339
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
202-441 |
3.15e-14 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 75.96 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 202 QSEVLSIDRSDKQIRVREANGREY------SEHYDKLLLSPGALPFVPPLPGVDSpGVFTLRNVEDTDAIKSYL------ 269
Cdd:PTZ00318 81 RAVVYDVDFEEKRVKCGVVSKSNNanvntfSVPYDKLVVAHGARPNTFNIPGVEE-RAFFLKEVNHARGIRKRIvqcier 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 270 ------DTHKVKRAT---VVGGGFIGLEMAENLH------ARGI--------AVNVIEMAPQVMAPVDFSMATIVHAHLQ 326
Cdd:PTZ00318 160 aslpttSVEERKRLLhfvVVGGGPTGVEFAAELAdffrddVRNLnpelveecKVTVLEAGSEVLGSFDQALRKYGQRRLR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 327 EKGIGLYLGKAVKSIEKRgEVLTaslDSGEKIEAELILLSIGV--RPNTKlaadaQLAIGP-ARG-IQVNEYLQTSD-PD 401
Cdd:PTZ00318 240 RLGVDIRTKTAVKEVLDK-EVVL---KDGEVIPTGLVVWSTGVgpGPLTK-----QLKVDKtSRGrISVDDHLRVKPiPN 310
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 543985159 402 IYAIGD--AIE-YPHPLTgkpwtnflAGPANRQGRIVADNMHG 441
Cdd:PTZ00318 311 VFALGDcaANEeRPLPTL--------AQVASQQGVYLAKEFNN 345
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
453-558 |
1.19e-12 |
|
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: 64.88 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 453 TAIAKIFDLTVAATGLPAKALKREGLPYESVTVQ--PNSHAGYYPNAYPLtLKITFHPESGMLYGAQCVGiEGVDKRIDS 530
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPfaANGRALAYGDTDGF-VKLVADRETGKILGAHIVG-PNAGELIQE 78
|
90 100
....*....|....*....|....*...
gi 543985159 531 IAQIIKRKGGITDLMQTeQAYAPPFSSA 558
Cdd:pfam02852 79 AALAIKMGATVEDLANT-IHIHPTLSEA 105
|
|
| DUF1661 |
pfam07877 |
Protein of unknown function (DUF1661); This is a family containing bacterial proteins of ... |
1-31 |
1.45e-12 |
|
Protein of unknown function (DUF1661); This is a family containing bacterial proteins of unknown function. Many of the proteins in this family are hypothetical.
Pssm-ID: 285160 Cd Length: 31 Bit Score: 62.51 E-value: 1.45e-12
10 20 30
....*....|....*....|....*....|.
gi 543985159 1 MVREAKNLRARTKKFSLHIFRKHAPQSEDFR 31
Cdd:pfam07877 1 LVREFKNSRAKTKKFSRHFFRKYAPQSGDFR 31
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
589-666 |
1.64e-12 |
|
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: 64.20 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 589 DPNRVTLIDARPRQAYE--IEHIPGAISMPVEEIRARIGEIPHDKPIYVYCAVGMRGYFASNILRQCGFSNVRNLIGGYR 666
Cdd:cd01444 13 AGEAPVLLDVRDPASYAalPDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAGFTDVRSLAGGFE 92
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
210-544 |
8.05e-12 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 69.02 E-value: 8.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 210 RSDKQIRVREANGREYSEHYDKLLLSPGALPFVPPLPGV-DSPgVFTlrnveDTDAIKSyldTHKVKRATVVGGGFIGLE 288
Cdd:PRK13748 214 KDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLkETP-YWT-----STEALVS---DTIPERLAVIGSSVVALE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 289 MAENLHARGIAVNVIEMApQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEkIEAELILLSIG 368
Cdd:PRK13748 285 LAQAFARLGSKVTILARS-TLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHVDGEFVLTTGHGE-LRADKLLVATG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 369 VRPNT-KLAADAQ-LAIGPARGIQVNEYLQTSDPDIYAIGDAieyphplTGKPWTNFLAGPAnrqGRIVADNMHGQtlrs 446
Cdd:PRK13748 363 RAPNTrSLALDAAgVTVNAQGAIVIDQGMRTSVPHIYAAGDC-------TDQPQFVYVAAAA---GTRAAINMTGG---- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 447 yEGAIG-TAI-AKIF-DLTVAATGLPAKALKREGLPYESVTVQ----PNSHAGYYPNAYpltLKITFHPESGMLYGAQCV 519
Cdd:PRK13748 429 -DAALDlTAMpAVVFtDPQVATVGYSEAEAHHDGIETDSRTLTldnvPRALANFDTRGF---IKLVIEEGSGRLIGVQAV 504
|
330 340
....*....|....*....|....*
gi 543985159 520 GIEGvDKRIDSIAQIIKRKGGITDL 544
Cdd:PRK13748 505 APEA-GELIQTAALAIRNRMTVQEL 528
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
584-705 |
1.11e-11 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 67.73 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 584 EMKEVDPNRVTLIDARPRQAYEIEHIPGAISMPVEEIRARI-GEIP-HDKPIYVYCAVGMRGYFASNILRQCGFSNVRNL 661
Cdd:PRK08762 9 EARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIeTHLPdRDREIVLICASGTRSAHAAATLRELGYTRVASV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 543985159 662 IGGyrlystiTADYSSAGQP-ATAQLPA---KDSPSSHTQVPEVDACG 705
Cdd:PRK08762 89 AGG-------FSAWKDAGLPlERPRLLTdeqDERYSRHLRLPEVGEEG 129
|
|
| SirA |
cd03423 |
SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators ... |
700-768 |
1.22e-11 |
|
SirA (also known as UvrY, and YhhP) belongs to a family of two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is thought to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.
Pssm-ID: 239515 Cd Length: 69 Bit Score: 60.84 E-value: 1.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543985159 700 EVDACGMSCPGPILKLKQSIDQIAVGEQLCILATDPGFARDAQAWCDTTGHNLIRQETIKGKYKVTIEK 768
Cdd:cd03423 1 ILDTRGLRCPEPVMMLHKKVRKMKPGDTLLVLATDPSTTRDIPKFCTFLGHELLAQETEDEPYRYLIRK 69
|
|
| PRK00299 |
PRK00299 |
sulfurtransferase TusA; |
689-768 |
1.64e-11 |
|
sulfurtransferase TusA;
Pssm-ID: 178967 Cd Length: 81 Bit Score: 60.81 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 689 KDSPSSHTQVpeVDACGMSCPGPILKLKQSIDQIAVGEQLCILATDPGFARDAQAWCDTTGHNLIRQETIKGKYKVTIEK 768
Cdd:PRK00299 2 TDLFSSPDHT--LDALGLRCPEPVMMVRKTVRNMQPGETLLIIADDPATTRDIPSFCRFMDHELLAQETEQLPYRYLIRK 79
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
221-407 |
5.41e-11 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 66.44 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 221 NGREYSEHYdkLLLSPGALPFVPPLPGVDspgvftlrNVEDTDAIksyLD-THKVKRATVVGGGFIGLEMAENLHARGIA 299
Cdd:PLN02546 211 DGKLYTARN--ILIAVGGRPFIPDIPGIE--------HAIDSDAA---LDlPSKPEKIAIVGGGYIALEFAGIFNGLKSD 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 300 VNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEKIEA-ELILLSIGVRPNTKLAAD 378
Cdd:PLN02546 278 VHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTVEGfSHVMFATGRKPNTKNLGL 357
|
170 180 190
....*....|....*....|....*....|.
gi 543985159 379 AQLAIGPAR--GIQVNEYLQTSDPDIYAIGD 407
Cdd:PLN02546 358 EEVGVKMDKngAIEVDEYSRTSVPSIWAVGD 388
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
595-669 |
1.16e-10 |
|
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: 59.33 E-value: 1.16e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543985159 595 LIDARPRQAYEIEHIPGAISMPVEEIRARIGEIP---HDKPIYVYCAVGMRGY-FASNILRQcGFSNVRNLIGGYRLYS 669
Cdd:cd01528 20 LIDVREPEELEIAFLPGFLHLPMSEIPERSKELDsdnPDKDIVVLCHHGGRSMqVAQWLLRQ-GFENVYNLQGGIDAWS 97
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
205-407 |
1.59e-10 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 64.61 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 205 VLSIDRSDKQIRVREangREYSEHydkLLLSPGALPFVPPLPGVDspgvftlRNVEDTDAIksYLDtHKVKRATVVGGGF 284
Cdd:TIGR01423 134 VLVRESADPKSAVKE---RLQAEH---ILLATGSWPQMLGIPGIE-------HCISSNEAF--YLD-EPPRRVLTVGGGF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 285 IGLEMAENLHA---RGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGE-VLTASLDSGEKIEA 360
Cdd:TIGR01423 198 ISVEFAGIFNAykpRGGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADgSKHVTFESGKTLDV 277
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 543985159 361 ELILLSIGVRPNTKlaaDAQLA-----IGPARGIQVNEYLQTSDPDIYAIGD 407
Cdd:TIGR01423 278 DVVMMAIGRVPRTQ---TLQLDkvgveLTKKGAIQVDEFSRTNVPNIYAIGD 326
|
|
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
584-660 |
1.61e-10 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 62.50 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 584 EMKE-VDPNRVTLIDARPRQAY--EIE-------HIPGAISMP-------------VEEIRARIGE--IPHDKPIYVYCA 638
Cdd:COG2897 144 EVLAaLGDPDAVLVDARSPERYrgEVEpidpragHIPGAVNLPwtdlldedgtfksAEELRALFAAlgIDPDKPVITYCG 223
|
90 100
....*....|....*....|....*
gi 543985159 639 VGMRG---YFAsniLRQCGFSNVRN 660
Cdd:COG2897 224 SGVRAahtWLA---LELLGYPNVRL 245
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
221-441 |
1.62e-10 |
|
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: 64.49 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 221 NGREYSEHYDKLLLSPGALPFVPPLPG-----VDSPGVFTLRNVEDtdaiksyldthkvkRATVVGGGFIGLEMAENLHA 295
Cdd:TIGR01438 136 KGKEKIYSAERFLIATGERPRYPGIPGakelcITSDDLFSLPYCPG--------------KTLVVGASYVALECAGFLAG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 296 RGIAVNVIeMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRG-EVLTASLDSGEKIEAEL--ILLSIGVRPN 372
Cdd:TIGR01438 202 IGLDVTVM-VRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEaKVLVEFTDSTNGIEEEYdtVLLAIGRDAC 280
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543985159 373 T-KLAAD-AQLAIGPARG-IQVNEYLQTSDPDIYAIGDAIEyphpltGKPWtnfLAGPANRQGRIVADNMHG 441
Cdd:TIGR01438 281 TrKLNLEnVGVKINKKTGkIPADEEEQTNVPYIYAVGDILE------DKPE---LTPVAIQAGRLLAQRLFK 343
|
|
| RHOD_ThiF |
cd01526 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ... |
594-670 |
2.30e-10 |
|
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: 58.86 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 594 TLIDARPRQAYEIEHIPGAISMPVEEIRARIGEIPH----------DKPIYVYCAVGMRGYFASNILRQCGFS-NVRNLI 662
Cdd:cd01526 26 VLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSlqelpldndkDSPIYVVCRRGNDSQTAVRKLKELGLErFVRDII 105
|
....*...
gi 543985159 663 GGYRLYST 670
Cdd:cd01526 106 GGLKAWAD 113
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
582-660 |
3.43e-10 |
|
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: 58.41 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 582 WREMKE-VDPNRVTLIDARPRQAYEIE-----------HIPGAISMP-------------VEEIRARIGE--IPHDKPIY 634
Cdd:cd01449 3 AEEVLAnLDSGDVQLVDARSPERFRGEvpeprpglrsgHIPGAVNIPwtslldedgtfksPEELRALFAAlgITPDKPVI 82
|
90 100
....*....|....*....|....*....
gi 543985159 635 VYCAVGMRG---YFAsniLRQCGFSNVRN 660
Cdd:cd01449 83 VYCGSGVTAcvlLLA---LELLGYKNVRL 108
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
212-408 |
4.12e-10 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 63.78 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 212 DKQIRVREANGREYseHYDKLLLSPGALPFVPPLPGVDSPGVFTLRNVEDTDAIKSYLdthkvkraTVVGGGFIGLEMAE 291
Cdd:PTZ00153 260 DKNTIKSEKSGKEF--KVKNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYM--------GIVGMGIIGLEFMD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 292 NLHARGIAVNVIEMAPQVMAPVDFSMATIVH-AHLQEKGIGLYLGKAVKSI-----------------EKRGEVLTASLD 353
Cdd:PTZ00153 330 IYTALGSEVVSFEYSPQLLPLLDADVAKYFErVFLKSKPVRVHLNTLIEYVragkgnqpviighserqTGESDGPKKNMN 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543985159 354 SGEKIEAELILLSIGVRPNTKLAADAQLAIGPARG-IQVNEYLQTSDPD------IYAIGDA 408
Cdd:PTZ00153 410 DIKETYVDSCLVATGRKPNTNNLGLDKLKIQMKRGfVSVDEHLRVLREDqevydnIFCIGDA 471
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
587-666 |
1.01e-09 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.
Pssm-ID: 238777 [Multi-domain] Cd Length: 106 Bit Score: 56.51 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 587 EVDPNrVTLIDARPRQAYEIEHIPGAISMPV-----------EEIRARIGEI--PHDKPIYVYCAVGMRGYFASNILRQC 653
Cdd:cd01519 11 NPHPN-KVLIDVREPEELKTGKIPGAINIPLsslpdalalseEEFEKKYGFPkpSKDKELIFYCKAGVRSKAAAELARSL 89
|
90
....*....|...
gi 543985159 654 GFSNVRNLIGGYR 666
Cdd:cd01519 90 GYENVGNYPGSWL 102
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
232-409 |
1.34e-09 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 61.94 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 232 LLLSPGALPFVPPLPGVDspgvftlrNVEDTDaikSYLDTHKVKRATVVGGGFIGLEMAENLHARGIAVNVIEMAPQVMA 311
Cdd:PTZ00058 206 ILIAVGNKPIFPDVKGKE--------FTISSD---DFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLR 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 312 PVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGE--VLTASLDSGEKIEAELILLSIGVRPNTK-LAADAQLAIGPARG 388
Cdd:PTZ00058 275 KFDETIINELENDMKKNNINIITHANVEEIEKVKEknLTIYLSDGRKYEHFDYVIYCVGRSPNTEdLNLKALNIKTPKGY 354
|
170 180
....*....|....*....|.
gi 543985159 389 IQVNEYLQTSDPDIYAIGDAI 409
Cdd:PTZ00058 355 IKVDDNQRTSVKHIYAVGDCC 375
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
541-664 |
2.61e-09 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 60.11 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 541 ITDLMQTEQayappFSSA-KDPVALAgyVADNIITgrmkPLHWREMKEVDPNrVTLIDARPRQAYEIEHIPGAISMPVEE 619
Cdd:PRK07878 263 ITELIDYEA-----FCGVvSDEAQQA--AAGSTIT----PRELKEWLDSGKK-IALIDVREPVEWDIVHIPGAQLIPKSE 330
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 543985159 620 IRA--RIGEIPHDKPIYVYCAVGMRGYFASNILRQCGFSNVRNLIGG 664
Cdd:PRK07878 331 ILSgeALAKLPQDRTIVLYCKTGVRSAEALAALKKAGFSDAVHLQGG 377
|
|
| PRK10287 |
PRK10287 |
thiosulfate:cyanide sulfurtransferase; Provisional |
596-663 |
8.72e-09 |
|
thiosulfate:cyanide sulfurtransferase; Provisional
Pssm-ID: 182356 [Multi-domain] Cd Length: 104 Bit Score: 54.08 E-value: 8.72e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 596 IDARPRQAYEIEHIPGAISMPVEEIRARIGEIPHDK--PIYVYCAVGMRGYFASNILRQCGFSNVRNLIG 663
Cdd:PRK10287 24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKndTVKLYCNAGRQSGQAKEILSEMGYTHAENAGG 93
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
193-485 |
9.03e-09 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 58.72 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 193 RLLNLDVRV---QSEVLSIDRSDKQIRVREANGREYSEHYDKLLLSPGALPFVppLPGVDSPG--VFTLRNVEDTDAiks 267
Cdd:PRK07845 101 RLEREGVRViagRGRLIDPGLGPHRVKVTTADGGEETLDADVVLIATGASPRI--LPTAEPDGerILTWRQLYDLDE--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 268 yLDTHKVkratVVGGGFIGLEMAENLHARGIAVNVIEMAPQVMAPVDFSMATIVHAHLQEKGIGLyLGKA-VKSIEKRGE 346
Cdd:PRK07845 176 -LPEHLI----VVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTV-LKRSrAESVERTGD 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 347 VLTASLDSGEKIEAELILLSIGVRPNTK---LAaDAQLAIGPARGIQVNEYLQTSDPDIYAIGDAieyphplTGK-Pwtn 422
Cdd:PRK07845 250 GVVVTLTDGRTVEGSHALMAVGSVPNTAglgLE-EAGVELTPSGHITVDRVSRTSVPGIYAAGDC-------TGVlP--- 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543985159 423 fLAGPANRQGRIVadnM-HgqtlrsyegAIGTAIAKIFDLTVAAT----------GLPAKALKREGLPYESVTV 485
Cdd:PRK07845 319 -LASVAAMQGRIA---MyH---------ALGEAVSPLRLKTVASNvftrpeiatvGVSQAAIDSGEVPARTVML 379
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
526-665 |
1.39e-08 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 57.96 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 526 KRIDSIAQIIKRKGGITDLMQTEQAYAPPFSSAKDPVAL-AGYVADNIITGRMKPLHWREMKEVdPNRVTLIDARPRQAY 604
Cdd:PRK05597 208 KLITGVGTPLIGKLGYYDSLDGTWEYIPVVGNPAVLERVrGSTPVHGISGGFGEVLDVPRVSAL-PDGVTLIDVREPSEF 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543985159 605 EIEHIPGAISMPVEEIRAriGEIPHD----KPIYVYCAVGMRGYFASNILRQCGFSNVRNLIGGY 665
Cdd:PRK05597 287 AAYSIPGAHNVPLSAIRE--GANPPSvsagDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGI 349
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
227-440 |
7.15e-08 |
|
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: 55.91 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 227 EHYDKLLLSPGA-LPFVPPLPGVDSPGVFT----LRNVEDTDAIKSYLDTHKvkRATVVGGGFIGLEMAenlharGIA-- 299
Cdd:COG0493 205 EEFDAVFLATGAgKPRDLGIPGEDLKGVHSamdfLTAVNLGEAPDTILAVGK--RVVVIGGGNTAMDCA------RTAlr 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 300 -----VNVIEMAPQVMAPvdFSMATIVHAHlqEKGIGLYLGKAVKSIEKR--GEV---------LTASLDSG-------- 355
Cdd:COG0493 277 lgaesVTIVYRRTREEMP--ASKEEVEEAL--EEGVEFLFLVAPVEIIGDenGRVtglecvrmeLGEPDESGrrrpvpie 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 356 ---EKIEAELILLSIGVRPNTK-LAADAQLAIGPARGIQVNE-YLQTSDPDIYAIGDAIEYPHPLTGkpwtnflagpANR 430
Cdd:COG0493 353 gseFTLPADLVILAIGQTPDPSgLEEELGLELDKRGTIVVDEeTYQTSLPGVFAGGDAVRGPSLVVW----------AIA 422
|
250
....*....|
gi 543985159 431 QGRIVADNMH 440
Cdd:COG0493 423 EGRKAARAID 432
|
|
| RHOD_PspE2 |
cd01521 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ... |
593-664 |
4.00e-07 |
|
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: 49.27 E-value: 4.00e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543985159 593 VTLIDARPRQAYEIEHIPGAISMPVEEIRARIGE-IPHDKPIYVYCA-VGMRGYFASNI-LRQCGFSnVRNLIGG 664
Cdd:cd01521 26 FVLVDVRSAEAYARGHVPGAINLPHREICENATAkLDKEKLFVVYCDgPGCNGATKAALkLAELGFP-VKEMIGG 99
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
593-665 |
2.23e-06 |
|
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: 47.04 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 593 VTLIDAR-PRqayEIEH---IPGAISMPVEEIRARIG-EIPH-------DKPIYVYCAVGMRGYFASNILRQCGFSNVRN 660
Cdd:cd01447 15 VLLVDVRdPR---ELERtgmIPGAFHAPRGMLEFWADpDSPYhkpafaeDKPFVFYCASGWRSALAGKTLQDMGLKPVYN 91
|
....*
gi 543985159 661 LIGGY 665
Cdd:cd01447 92 IEGGF 96
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
578-664 |
2.37e-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: 46.80 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 578 KPLHWREMKEvDPNrVTLIDARPRQAYEIEHIPGAISMPVEEIR------ARIGEIPHDKPIYVYCAVGMRGYFASNILR 651
Cdd:cd01518 5 SPAEWNELLE-DPE-VVLLDVRNDYEYDIGHFKGAVNPDVDTFRefpfwlDENLDLLKGKKVLMYCTGGIRCEKASAYLK 82
|
90
....*....|...
gi 543985159 652 QCGFSNVRNLIGG 664
Cdd:cd01518 83 ERGFKNVYQLKGG 95
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
589-666 |
5.52e-06 |
|
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.
Pssm-ID: 238725 [Multi-domain] Cd Length: 122 Bit Score: 46.46 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 589 DPNrVTLIDAR-------PRQAYEIEHIPGAISMPVEEIRARIGEIPH-------------------DKPIYVYCAVGMr 642
Cdd:cd01448 13 DPD-VRILDARwylpdrdGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHmlpspeefaellgslgisnDDTVVVYDDGGG- 90
|
90 100
....*....|....*....|....*..
gi 543985159 643 gYFASN---ILRQCGFSNVRNLIGGYR 666
Cdd:cd01448 91 -FFAARawwTLRYFGHENVRVLDGGLQ 116
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
570-664 |
9.73e-06 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 48.69 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 570 DNIITGR-MKPLHWREMKEvDPNrVTLIDARPRQAYEIEHIPGAISMPVEEIRARIGEI------PHDKPIYVYCAVGMR 642
Cdd:PRK00142 106 PLENVGTyLKPKEVNELLD-DPD-VVFIDMRNDYEYEIGHFENAIEPDIETFREFPPWVeenldpLKDKKVVMYCTGGIR 183
|
90 100
....*....|....*....|..
gi 543985159 643 GYFASNILRQCGFSNVRNLIGG 664
Cdd:PRK00142 184 CEKASAWMKHEGFKEVYQLEGG 205
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
227-440 |
2.21e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 47.87 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 227 EHYDKLLLSPGA-LPFVPPLPGVDSPGVFT----LRNVedtDAIKSYLDTHKVKRATVVGGGFIGLEM--------AEN- 292
Cdd:PRK11749 224 AGYDAVFIGTGAgLPRFLGIPGENLGGVYSavdfLTRV---NQAVADYDLPVGKRVVVIGGGNTAMDAartakrlgAESv 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 293 --LHARGIAvnviEM-ApqvmapvdfSMATIVHAhlQEKGIGLYLGKAVKSIEKRGEVLTA----------SLDSGEK-- 357
Cdd:PRK11749 301 tiVYRRGRE----EMpA---------SEEEVEHA--KEEGVEFEWLAAPVEILGDEGRVTGvefvrmelgePDASGRRrv 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 358 --------IEAELILLSIGVRPNTKLAADAQ-LAIGPARGIQVNE-YLQTSDPDIYAIGDAIeyphplTGKP---Wtnfl 424
Cdd:PRK11749 366 piegseftLPADLVIKAIGQTPNPLILSTTPgLELNRWGTIIADDeTGRTSLPGVFAGGDIV------TGAAtvvW---- 435
|
250
....*....|....*.
gi 543985159 425 agpANRQGRIVADNMH 440
Cdd:PRK11749 436 ---AVGDGKDAAEAIH 448
|
|
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
589-665 |
1.80e-04 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 44.40 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 589 DPNrVTLIDAR-----PRQAYEIEHIPGAISMPVE-EIRARIGEIPH-------------------DKPIYVYCAVGM-- 641
Cdd:COG2897 7 DPD-VVILDVRwdlpdGRAAYEAGHIPGAVFLDLDtDLSDPRSPGRHplpspeafaallgalgisnDTTVVVYDDGGGlf 85
|
90 100
....*....|....*....|....*.
gi 543985159 642 --RGYFasnILRQCGFSNVRNLIGGY 665
Cdd:COG2897 86 aaRAWW---LLRYAGHEDVRVLDGGL 108
|
|
| 4RHOD_Repeat_2 |
cd01533 |
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ... |
593-657 |
3.31e-04 |
|
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue.
Pssm-ID: 238791 [Multi-domain] Cd Length: 109 Bit Score: 40.91 E-value: 3.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543985159 593 VTLIDARPRQAYEIEHIPGAISMPVEEIRARIGEI-PHDK-PIYVYCAVGMRGYFASNILRQCGFSN 657
Cdd:cd01533 27 LVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELaPDPRtPIVVNCAGRTRSIIGAQSLINAGLPN 93
|
|
| 4RHOD_Repeats |
cd01529 |
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ... |
595-664 |
3.50e-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: 3.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543985159 595 LIDARPRQAYEIEHIPGAISMPVEEIRARIGEIPH------DKPIYVYCAVGMRGYFASNILRQCGFSNVRNLIGG 664
Cdd:cd01529 15 LLDVRAEDEYAAGHLPGKRSIPGAALVLRSQELQAleapgrATRYVLTCDGSLLARFAAQELLALGGKPVALLDGG 90
|
|
| PRK07411 |
PRK07411 |
molybdopterin-synthase adenylyltransferase MoeB; |
593-669 |
4.76e-04 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 43.57 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 593 VTLIDARPRQAYEIEHIPGAISMPVEEIR-----ARIGEIPHDKPIYVYCAVGMRGYFASNILRQCGFSNVrNLIGGYRL 667
Cdd:PRK07411 300 FVLIDVRNPNEYEIARIPGSVLVPLPDIEngpgvEKVKELLNGHRLIAHCKMGGRSAKALGILKEAGIEGT-NVKGGITA 378
|
..
gi 543985159 668 YS 669
Cdd:PRK07411 379 WS 380
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
279-443 |
4.89e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 43.66 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 279 VVGGGFIGLEMAENLHARGIAVNViEMAPQVMAPVDFSMATIVHAHLQEKGIGLYLGKAVKSIEKRGEVLTASLDSGEKI 358
Cdd:PTZ00052 187 IVGASYIGLETAGFLNELGFDVTV-AVRSIPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIKVLFSDGTTE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 359 EAELILLSIGVRPNTKLAADAQLaigparGIQVNEYLQ-------TSDPDIYAIGDAIEyphpltGKPWtnfLAGPANRQ 431
Cdd:PTZ00052 266 LFDTVLYATGRKPDIKGLNLNAI------GVHVNKSNKiiapndcTNIPNIFAVGDVVE------GRPE---LTPVAIKA 330
|
170
....*....|..
gi 543985159 432 GRIVADNMHGQT 443
Cdd:PTZ00052 331 GILLARRLFKQS 342
|
|
| glpE |
PRK00162 |
thiosulfate sulfurtransferase GlpE; |
595-668 |
5.19e-04 |
|
thiosulfate sulfurtransferase GlpE;
Pssm-ID: 178908 [Multi-domain] Cd Length: 108 Bit Score: 40.39 E-value: 5.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543985159 595 LIDARPRQAYEIEHIPGAISMPVEEIRARIGEIPHDKPIYVYCAVGMRGYFASNILRQCGFSNVRNLIGGYRLY 668
Cdd:PRK00162 23 LVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQQGFDVVYSIDGGFEAW 96
|
|
| COG1416 |
COG1416 |
Intracellular sulfur oxidation protein, DsrE/DsrF family [Inorganic ion transport and ... |
863-931 |
5.50e-04 |
|
Intracellular sulfur oxidation protein, DsrE/DsrF family [Inorganic ion transport and metabolism];
Pssm-ID: 441026 Cd Length: 139 Bit Score: 41.08 E-value: 5.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543985159 863 FGLGAKMMRmvmkeKHVDSLESMRKQALENGVEFIACQMSMDVMGINREELLDEVSI--GGVATYMNRAEE 931
Cdd:COG1416 67 HGPGIKLLL-----KDNNPLAERIAALAEKGVKFVACGNTLKARGIDKDDLLPGVEVvpSGVVELAELQQE 132
|
|
| DrsE |
pfam02635 |
DsrE/DsrF-like family; DsrE is a small soluble protein involved in intracellular sulfur ... |
786-932 |
6.41e-04 |
|
DsrE/DsrF-like family; DsrE is a small soluble protein involved in intracellular sulfur reduction. This family also includes DsrF.
Pssm-ID: 426894 Cd Length: 117 Bit Score: 40.40 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 786 KTFILFSD---DLDKALATFVLANGAAAMGQPVTIFFTFWGLNAIKKPHAVKAKKDiwgkmfgmmlpknskglglskmnm 862
Cdd:pfam02635 2 KVFIVVTSgpyGTEAAREALDLALAAAALGHDVAVFFHGDGVLNLLKGQEPNPIGE------------------------ 57
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543985159 863 fglgakmmrmvmkekhvDSLESMRKQALENGVEFIACQMSMDVMGINREELLD-EVSIGGVATYMNRAEEA 932
Cdd:pfam02635 58 -----------------KNLAELLKALAEYGVKVYVCGQSLKARGITEDELLGvGVEVSGLGELAELQLEG 111
|
|
| SirA_like_N |
cd03421 |
SirA_like_N, a protein of unknown function with an N-terminal SirA-like domain. The SirA, ... |
700-726 |
7.11e-04 |
|
SirA_like_N, a protein of unknown function with an N-terminal SirA-like domain. The SirA, YedF, YeeD protein family is present in bacteria as well as archaea. SirA (also known as UvrY, and YhhP) belongs to a family of a two-component response regulators that controls secondary metabolism and virulence. The other member of this two-component system is a sensor kinase called BarA which phosphorylates SirA. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. YhhP is suggested to be important for normal cell division and growth in rich nutrient medium. Moreover, despite a low primary sequence similarity, the YccP structure closely resembles the non-homologous C-terminal RNA-binding domain of E. coli translation initiation factor IF3. The signature CPxP motif serves to stabilize the N-terminal helix as part of the N-capping box and might be important in mRNA-binding.
Pssm-ID: 239513 Cd Length: 67 Bit Score: 38.72 E-value: 7.11e-04
10 20
....*....|....*....|....*..
gi 543985159 700 EVDACGMSCPGPILKLKQSIDQIAVGE 726
Cdd:cd03421 1 TIDARGLACPQPVIKTKKALELEAGGE 27
|
|
| selenium_YedF |
TIGR03527 |
selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in ... |
701-789 |
9.88e-04 |
|
selenium metabolism protein YedF; Members of this protein family are about 200 amino acids in size, and include the uncharacterized YedF protein of Escherichia coli. This family shares an N-terminal domain, modeled by pfam01206, with the sulfurtransferase TusA (also called SirA). The C-terminal domain includes a typical redox-active disulfide motif, CGXC. This protein family found only among those genomes that also carry the selenium donor protein SelD, and its connection to selenium metabolism is indicated by the method of partial phylogenetic profiling vs. SelD. Its gene typically is found next to selD. Members of this family are found even when selenocysteine and selenouridine biosynthesis pathways are, except for SelD, completely absent, as in Enterococcus faecalis. Its role in selenium metabolism is unclear, but may include either detoxification or a role in labile selenoprotein biosynthesis.
Pssm-ID: 274630 [Multi-domain] Cd Length: 194 Bit Score: 41.46 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 701 VDACGMSCPGPILKLKQSIDQIAVGEQLCILaTDPGFARDaqawcdttghNLIRQETIKGkYKVTIEKtacKEEGTCVNE 780
Cdd:TIGR03527 1 IDARGLACPQPVILTKKALDELGEEGVLTVI-VDNEAAKE----------NVSKFATSLG-YEVEVEE---KEEGYWILI 65
|
....*....
gi 543985159 781 TpaKGKTFI 789
Cdd:TIGR03527 66 I--KKGEGA 72
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
227-409 |
4.98e-03 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 40.88 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 227 EHYDKLLLSPGA-LPFVPPLPGVDSPGVFT----LRNVEDTDAIKSYLDTHKV--KRATVVGGGFIGLEMAENLHARGI- 298
Cdd:PRK12778 516 EGFKGIFIASGAgLPNFMNIPGENSNGVMSsneyLTRVNLMDAASPDSDTPIKfgKKVAVVGGGNTAMDSARTAKRLGAe 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 299 AVNVIEMAPQVMAPvdfSMATIVHaHLQEKGIG-LYLGKAVKSI-EKRGEVLTASL---------DSG-----------E 356
Cdd:PRK12778 596 RVTIVYRRSEEEMP---ARLEEVK-HAKEEGIEfLTLHNPIEYLaDEKGWVKQVVLqkmelgepdASGrrrpvaipgstF 671
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 543985159 357 KIEAELILLSIGVRPNTKL-AADAQLAIGPARGIQVNEYLQTSDPDIYAIGDAI 409
Cdd:PRK12778 672 TVDVDLVIVSVGVSPNPLVpSSIPGLELNRKGTIVVDEEMQSSIPGIYAGGDIV 725
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
224-412 |
5.18e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 40.52 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 224 EYSEHYDKLLLSPG-ALPFVPPLPGVDSPGVFT----LRNVED---TDAIKSYLDthkvKRATVVGGGFIGLEMAENLhA 295
Cdd:PRK13984 364 ELREKHDAVFLSTGfTLGRSTRIPGTDHPDVIQalplLREIRDylrGEGPKPKIP----RSLVVIGGGNVAMDIARSM-A 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 296 R---------GIAVNVIEMAPQVMaPVDfsMATIVHAhlQEKGIGLYLGKA-VKSIEKRGEV-----------------L 348
Cdd:PRK13984 439 RlqkmeygevNVKVTSLERTFEEM-PAD--MEEIEEG--LEEGVVIYPGWGpMEVVIENDKVkgvkfkkcvevfdeegrF 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543985159 349 TASLDSGEKI--EAELILLSIGVRPNTK-LAADAQLAIGPARG-IQVNEYLQTSDPDIYAIGDAIEYP 412
Cdd:PRK13984 514 NPKFDESDQIivEADMVVEAIGQAPDYSyLPEELKSKLEFVRGrILTNEYGQTSIPWLFAGGDIVHGP 581
|
|
| IucD |
COG3486 |
Lysine/ornithine N-monooxygenase [Secondary metabolites biosynthesis, transport and catabolism] ... |
198-296 |
9.34e-03 |
|
Lysine/ornithine N-monooxygenase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442709 [Multi-domain] Cd Length: 440 Bit Score: 39.38 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543985159 198 DVRVQSEVLSIDRSDKQ----IRVREANGREYSEHYDKLLLSPGALPFVPP-LPGVDSPGVFT----LRNVEDTdaiksy 268
Cdd:COG3486 114 NVRFGTEVEAVEYDDDAgafrVTVRDGTGERETYRARNLVLGTGTRPYLPEcFRGLPGERVFHsseyLHRKEDL------ 187
|
90 100
....*....|....*....|....*...
gi 543985159 269 ldtHKVKRATVVGGGFIGLEMAENLHAR 296
Cdd:COG3486 188 ---QAAKRVTVVGSGQSAAEIFLDLLRR 212
|
|
| |
