|
Name |
Accession |
Description |
Interval |
E-value |
| COG3581 |
COG3581 |
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function ... |
1062-1468 |
7.09e-121 |
|
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only];
Pssm-ID: 442800 Cd Length: 407 Bit Score: 384.19 E-value: 7.09e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 1062 TRHILAPYFTEYLTPLLPPLCRLIGWDVEVLPPGDAESAEYGLKYANNEVCYPATLIVGDFVKALRSGRYNPDQVSVVMT 1141
Cdd:COG3581 3 TMTILFPHMGPIHFRLLKAAFRGLGYEVEVLPPPDKETLELGLKYVNNDACYPLKIVLGQLIEALESGKYDPDATAIVMT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 1142 QTGGQCRATNYAALIRRALDANGFGQVPLITLgvatSAEDEDKNQDGTLNVPWLRLAptiVTTFLYGDAISKMYHasvvR 1221
Cdd:COG3581 83 GTGGPCRAGNYIELLRKALKDAGYPDVPVISL----NPQGLEFNPGFKLTLKLLKRA---WKAIVYGDLLEKLLY----R 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 1222 LRPDALRvtgpfANAAEALREKYLRLAAEPILKNRPGRLMELIGEAAEAFDAI--TEDREVPAVGIVGEIFLKFNPFAHQ 1299
Cdd:COG3581 152 TRPYEKN-----KGSADRLYEKWLEKLEEALESGSLKELKKLLKEIVKEFDAIplDEDEKKPRVGIVGEIYVKLEPFANN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 1300 FIADKIISRGIEVVPALLSPFFLQNFVNVIvEKHMGLRCSNVPDFVIRSIYSLIWRREKQINRVASRFRYFRPFTNIFEE 1379
Cdd:COG3581 227 NIEKFLEEEGAEVVRPPLSDWILYNLYNRK-FKAKELGGSKKSRLKKKLAIKVLEKYRKPIKKALRKSLRFEPPPDIKEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 1380 AKDVDGVVSLAAQFGEGWLLPSDIISMVRQGVTNVASLQPFGCIANhVVSKGIEKRLKRRFPELNLVSLDFDSGVSSVNV 1459
Cdd:COG3581 306 AEAAKPYLSLGNIGGEGWLLIGEMVELIKEGYDGIICLQPFGCMPN-IVAKGILKKLRRDYPEIPILTLDYDEGASEVNQ 384
|
....*....
gi 433303179 1460 TNRLLLFLD 1468
Cdd:COG3581 385 LTRLEAFLD 393
|
|
| COG3580 |
COG3580 |
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function ... |
679-1019 |
9.46e-110 |
|
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only];
Pssm-ID: 442799 Cd Length: 343 Bit Score: 351.06 E-value: 9.46e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 679 LFDRPAIPANSSaklpattagPRRLVAIPRVLNMYEDYPFWHALFTTAGFEVMLSSESvfSR--YEAALgSVMSDNICFP 756
Cdd:COG3580 1 LFDYKPLPPEKA---------MRGTIGIPRALNYYEYYPFWKTFFTELGFEVVLSPPT--NKeiYEKGI-EIASDEACYP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 757 AKLVHAHVKELDERlsAPDmpagaFIFMPYVVYERQDDARNTNSYNCPIVSAYSDVIRSAMTLHA---RLDSPVINFRDE 833
Cdd:COG3580 69 AKLAHGHVADLLDK--GVD-----YIFYPRIVSEPKEDEGADNHYNCPKVQGYPEVIKANIDEEEkgiPFISPFLNLDDK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 834 KLLVRQLTGYL-RGLGIDRQTIRRACRQAAAAQDEYTRLVRQKALDLLAASRREGRLTILLAGRPYHT-DPLIQHKLSDM 911
Cdd:COG3580 142 ELLAKRLYEELgKGLGISKKEIKRAVEKAWEAQRAFRRDLRKKGEEILEELKENGEKGIVLLGRPYHIyDPEINHGIPEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 912 IASLGVNVISEDVVRGD-LSVGTGNTRIVRQWAYMNRIIKAGQWCAEQPDdLHFVQMTSFGCGPDSFIQDEIRSIMKEHG 990
Cdd:COG3580 222 LRSLGVAVLTEDSLPHLgEDLSARPLRKNLQWTYHSRLLGAAKFVARHPN-LDGIQLTSFGCGPDSVTTDLVEEILERSG 300
|
330 340
....*....|....*....|....*....
gi 433303179 991 KPYTLLKIDDVSNIGSLKLRVRSLVESLR 1019
Cdd:COG3580 301 KPYLLLKIDEHSNEGGVKTRLEAFLDALK 329
|
|
| ASKHA_NBD_O66634-like_rpt2 |
cd24035 |
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ... |
335-600 |
4.88e-108 |
|
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the second copy of the BcrAD/BadFG-like domain.
Pssm-ID: 466885 Cd Length: 258 Bit Score: 342.98 E-value: 4.88e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 335 VVGIDSGSTTTKLVAVRARGEqqgqLVFSDYSMNLGNPIKAVAEGLRRLQTAADENGTdlrIVGSCSTGYGEELIKTAFG 414
Cdd:cd24035 1 YLGIDVGSTTTKAVLIDEDGE----ILASVYLRTKGNPIEAVKKGLKELREQLPEKVV---IVGVGTTGSGRELLKDALG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 415 LDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVDGGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAGLACR 494
Cdd:cd24035 74 ADVVKVEITAHATAALHFDPDVDTIFEIGGQDSKYISLKNGVVKDFAMNEACSAGTGSFLEEQAKSLGIPIEEFAELALK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 495 GTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNCLYKVLklhGNDNLGNRIVVQGGTMKNDSVVRAFELL 574
Cdd:cd24035 154 AKNPPDLGSRCTVFMESDIKQAQQEGASKEDISAGLAYSVVKNYLNKVV---GGRNLGKKIVFQGGTFLNKAVLAAFEQV 230
|
250 260
....*....|....*....|....*.
gi 433303179 575 TGTEVARSNMPEMMGAYGCALHAIEQ 600
Cdd:cd24035 231 TGKEIIVPPHPGLMGAYGAALLAKEE 256
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
331-603 |
1.90e-107 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 341.31 E-value: 1.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 331 MEEVVVGIDSGSTTTKLVAVrargEQQGQLVFSDYSMNLGNPIKAVAEGLRRLQTAAdeNGTDLRIVGSCSTGYGEELIK 410
Cdd:COG1924 1 QGMIYLGIDIGSTTTKAVLL----DEDGEILASAYLPTGGDPLEAAKEALKELLEEA--GLKREDIAGVVATGYGRVLIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 411 TAFgLDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVDGGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAG 490
Cdd:COG1924 75 AAF-ADKVVTEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLEDGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 491 LACRGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNCLYKVLKLHgndnLGNRIVVQGGTMKNDSVVRA 570
Cdd:COG1924 154 LALKAKNPVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVG----IGEPVVFQGGVAKNDGVVRA 229
|
250 260 270
....*....|....*....|....*....|...
gi 433303179 571 FELLTGTEVARSNMPEMMGAYGCALHAIEQLHA 603
Cdd:COG1924 230 LEKELGKEVIVPPIPQLMGALGAALLAREKVKK 262
|
|
| ASKHA_NBD_O66634-like_rpt1 |
cd24034 |
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ... |
6-263 |
1.03e-86 |
|
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the first copy of the BcrAD/BadFG-like domain.
Pssm-ID: 466884 [Multi-domain] Cd Length: 258 Bit Score: 283.33 E-value: 1.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 6 RVGLDVGSTTAKIAVLDHDDRLVYSRYERHNAKVNELVHNYLHEIRQQLGDVRLRLCVTGSVGMSAAEQLGAEFVQEVVA 85
Cdd:cd24034 1 YLGIDIGSTTVKAVVLDEKGNIVFSDYERHFGNPREALLELLEEIKERLGDEIARIAVTGSGGRGLAELLGLPFVQEVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 86 ATVFARHRHPEAKALIDIGGEDAKVVFFNGQ--SMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQSTHLYPMAA 163
Cdd:cd24034 81 IEAAVKHLHPDARTVIEIGGEDFKLIELDGDgkLKDFRMNSKCAAGTGAFIDQQARRLGLSLEELAELALKAEPPAPIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 164 RCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLSHGCDFTPPILLCGGPLTFLPSLRKAFADYLELSttDFIVV 243
Cdd:cd24034 161 RCSVFAKSDMIHLQNKGVPKEDIAAGLCRAVARNVIATLAKGREIEGPVILVGGVATNNAVLREAFEELLGDE--ELIVP 238
|
250 260
....*....|....*....|
gi 433303179 244 HEGNLIPAIGCAIRAGQSDS 263
Cdd:cd24034 239 EHAEYFEALGAALYALEEGS 258
|
|
| DUF2229 |
pfam09989 |
CoA enzyme activase uncharacterized domain (DUF2229); Members of this family include various ... |
704-922 |
4.81e-74 |
|
CoA enzyme activase uncharacterized domain (DUF2229); Members of this family include various bacterial hypothetical proteins, as well as CoA enzyme activases. The exact function of this domain has not, as yet, been defined.
Pssm-ID: 462935 Cd Length: 213 Bit Score: 245.53 E-value: 4.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 704 VAIPRVLNMYEDYPFWHALFTTAGFEVMLSSESVFSRYEAALGSVMSDNICFPAKLVHAHVKELDERlsAPDmpagaFIF 783
Cdd:pfam09989 1 IGIPRALNMYEYYPFWHTFFTELGFRVVLSPPSSKEIYEKGIETIPSETVCYPAKLAHGHVADLLKK--GVD-----YIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 784 MPYVVYERQDDARNTNSYNCPIVSAYSDVIRSAMTLHA---RLDSPVINFRDEKLLVRQLtgyLRGLGIDRQTIRRACRQ 860
Cdd:pfam09989 74 YPCIVYEPREEDDADNHYNCPIVQGYPEVIKNNMDEREegiRFLSPFLDLDDGKLLAKQL---FEELGISKKEIKRAVEK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433303179 861 AAAAQDEYTRLVRQKALDLLAASRREGRLTILLAGRPYHT-DPLIQHKLSDMIASLGVNVISE 922
Cdd:pfam09989 151 ALEAQEAFKEDLRKKGEEILEYLEENGKKGIVLAGRPYHIyDPEINHGIPELLASLGVAVLTE 213
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
3-256 |
9.13e-48 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 171.83 E-value: 9.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 3 KTYRVGLDVGSTTAKIAVLDHDDRLVYSRYERHNAKVNELVHNYLHEIRQQLGDVR---LRLCVTGSvGMSAAEQLGAEF 79
Cdd:COG1924 2 GMIYLGIDIGSTTTKAVLLDEDGEILASAYLPTGGDPLEAAKEALKELLEEAGLKRediAGVVATGY-GRVLIGAAFADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 80 VQ-EVVAATVFARHRHPEAKALIDIGGEDAKVVFF-NGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQSTH 157
Cdd:COG1924 81 VVtEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLeDGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELALKAKN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 158 LYPMAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQtVTTLSHGCDFTPPILLCGGplTFL-PSLRKAFADYLEls 236
Cdd:COG1924 161 PVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKR-VLNLVKRVGIGEPVVFQGG--VAKnDGVVRALEKELG-- 235
|
250 260
....*....|....*....|
gi 433303179 237 tTDFIVVHEGNLIPAIGCAI 256
Cdd:COG1924 236 -KEVIVPPIPQLMGALGAAL 254
|
|
| CoA_E_activ |
TIGR00241 |
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ... |
334-595 |
2.15e-29 |
|
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.
Pssm-ID: 129344 Cd Length: 248 Bit Score: 118.36 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 334 VVVGIDSGSTTTKLVAVRargeqQGQLV---FSDYSMNLGNPIKAVAEGLRRLQTAADEngtdlrIVGSCSTGYGEELIK 410
Cdd:TIGR00241 1 ISLGIDSGSTTTKMVLME-----DGKVIgykWLDTTPVIEETARAILEALKEAGIGLEP------IDKIVATGYGRHKVG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 411 TAfglDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVDGGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAG 490
Cdd:TIGR00241 70 FA---DKIVTEISCHGKGANYLAPEARGVIDIGGQDSKVIKIDDGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 491 LACRGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNCLYKVLKLHGNDNlgnrIVVQGGTMKNDSVVRA 570
Cdd:TIGR00241 147 LAEKADRKAKISSMCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAP----IVFTGGVSKNKGLVKA 222
|
250 260
....*....|....*....|....*
gi 433303179 571 FELLTGTEVARSNMPEMMGAYGCAL 595
Cdd:TIGR00241 223 LEKKLGMKVITPPEPQIVGAVGAAL 247
|
|
| CoA_E_activ |
TIGR00241 |
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ... |
5-256 |
4.17e-29 |
|
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.
Pssm-ID: 129344 Cd Length: 248 Bit Score: 117.59 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 5 YRVGLDVGSTTAKIAVLDhDDRLVYSRYERHNAKVNE---LVHNYLHEIRQQLGDVRlRLCVTG----SVGmsaaeqlGA 77
Cdd:TIGR00241 1 ISLGIDSGSTTTKMVLME-DGKVIGYKWLDTTPVIEEtarAILEALKEAGIGLEPID-KIVATGygrhKVG-------FA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 78 EFVQ-EVVAATVFARHRHPEAKALIDIGGEDAKVV-FFNGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQS 155
Cdd:TIGR00241 72 DKIVtEISCHGKGANYLAPEARGVIDIGGQDSKVIkIDDGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 156 THLYPMAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLSHgCDFTPPILLCGGpLTFLPSLRKAFADYLEL 235
Cdd:TIGR00241 152 DRKAKISSMCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQR-LKIEAPIVFTGG-VSKNKGLVKALEKKLGM 229
|
250 260
....*....|....*....|.
gi 433303179 236 sttDFIVVHEGNLIPAIGCAI 256
Cdd:TIGR00241 230 ---KVITPPEPQIVGAVGAAL 247
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
336-597 |
1.59e-26 |
|
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.
Pssm-ID: 396441 [Multi-domain] Cd Length: 271 Bit Score: 110.91 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 336 VGIDSGSTTTKLVAVRARGEQQGQLVF-SDYSMNLG--NPIKAVAEGLRRLQTAADENGTDLRIVGSCSTGYGEELIKTA 412
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGRAIAgSANFESVGveAAERNLKDAITEALEEAGLKLDDIEYMFLGLTGYGRAGVDGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 413 FGLDSGIIETMAHYRAAARLMPDVSF---ILDIGGQDMKAIFVDGGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFA 489
Cdd:pfam01869 81 FGKDIVREEITVHADGAVALAPGTRGedgVIDIGGTGSKVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARALGAVVRELD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 490 GLACRGT-HPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNcLYKVLKLHGNDnlGNRIVVQGGTMKNDSVV 568
Cdd:pfam01869 161 GLAPKTTlNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALR-VAALAKRLGFV--PDEVVLTGGVAKNAGLV 237
|
250 260 270
....*....|....*....|....*....|....
gi 433303179 569 RAFELLTGTEVAR-----SNMPEMMGAYGCALHA 597
Cdd:pfam01869 238 KALRDYLKENILGvkvnvHPDPQYAGAIGAALLA 271
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
7-234 |
2.28e-14 |
|
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.
Pssm-ID: 396441 [Multi-domain] Cd Length: 271 Bit Score: 75.08 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 7 VGLDVGSTTAKIAVLDHDDRLVY------SRYERHNAK-----VNELVHNYLHEIRQQLGDVRLRLCVTGSVGMSAAEQl 75
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGraiagsANFESVGVEaaernLKDAITEALEEAGLKLDDIEYMFLGLTGYGRAGVDG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 76 gaEFVQEVVAATVFARHR--------HPEAKALIDIGGEDAKVVFFNGQSME-LRMNGNCAGGTGAFIDQMSVLMGCDNA 146
Cdd:pfam01869 80 --HFGKDIVREEITVHADgavalapgTRGEDGVIDIGGTGSKVIGLDGGKVVrFGGNGQCAGGEGSFLEIAARALGAVVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 147 RLDELARQST-HLYPMAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLSHGCDFTPPILLCGGplTFLPS- 224
Cdd:pfam01869 158 ELDGLAPKTTlNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRLGFVPDEVVLTGG--VAKNAg 235
|
250
....*....|
gi 433303179 225 LRKAFADYLE 234
Cdd:pfam01869 236 LVKALRDYLK 245
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG3581 |
COG3581 |
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function ... |
1062-1468 |
7.09e-121 |
|
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only];
Pssm-ID: 442800 Cd Length: 407 Bit Score: 384.19 E-value: 7.09e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 1062 TRHILAPYFTEYLTPLLPPLCRLIGWDVEVLPPGDAESAEYGLKYANNEVCYPATLIVGDFVKALRSGRYNPDQVSVVMT 1141
Cdd:COG3581 3 TMTILFPHMGPIHFRLLKAAFRGLGYEVEVLPPPDKETLELGLKYVNNDACYPLKIVLGQLIEALESGKYDPDATAIVMT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 1142 QTGGQCRATNYAALIRRALDANGFGQVPLITLgvatSAEDEDKNQDGTLNVPWLRLAptiVTTFLYGDAISKMYHasvvR 1221
Cdd:COG3581 83 GTGGPCRAGNYIELLRKALKDAGYPDVPVISL----NPQGLEFNPGFKLTLKLLKRA---WKAIVYGDLLEKLLY----R 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 1222 LRPDALRvtgpfANAAEALREKYLRLAAEPILKNRPGRLMELIGEAAEAFDAI--TEDREVPAVGIVGEIFLKFNPFAHQ 1299
Cdd:COG3581 152 TRPYEKN-----KGSADRLYEKWLEKLEEALESGSLKELKKLLKEIVKEFDAIplDEDEKKPRVGIVGEIYVKLEPFANN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 1300 FIADKIISRGIEVVPALLSPFFLQNFVNVIvEKHMGLRCSNVPDFVIRSIYSLIWRREKQINRVASRFRYFRPFTNIFEE 1379
Cdd:COG3581 227 NIEKFLEEEGAEVVRPPLSDWILYNLYNRK-FKAKELGGSKKSRLKKKLAIKVLEKYRKPIKKALRKSLRFEPPPDIKEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 1380 AKDVDGVVSLAAQFGEGWLLPSDIISMVRQGVTNVASLQPFGCIANhVVSKGIEKRLKRRFPELNLVSLDFDSGVSSVNV 1459
Cdd:COG3581 306 AEAAKPYLSLGNIGGEGWLLIGEMVELIKEGYDGIICLQPFGCMPN-IVAKGILKKLRRDYPEIPILTLDYDEGASEVNQ 384
|
....*....
gi 433303179 1460 TNRLLLFLD 1468
Cdd:COG3581 385 LTRLEAFLD 393
|
|
| COG3580 |
COG3580 |
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function ... |
679-1019 |
9.46e-110 |
|
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only];
Pssm-ID: 442799 Cd Length: 343 Bit Score: 351.06 E-value: 9.46e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 679 LFDRPAIPANSSaklpattagPRRLVAIPRVLNMYEDYPFWHALFTTAGFEVMLSSESvfSR--YEAALgSVMSDNICFP 756
Cdd:COG3580 1 LFDYKPLPPEKA---------MRGTIGIPRALNYYEYYPFWKTFFTELGFEVVLSPPT--NKeiYEKGI-EIASDEACYP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 757 AKLVHAHVKELDERlsAPDmpagaFIFMPYVVYERQDDARNTNSYNCPIVSAYSDVIRSAMTLHA---RLDSPVINFRDE 833
Cdd:COG3580 69 AKLAHGHVADLLDK--GVD-----YIFYPRIVSEPKEDEGADNHYNCPKVQGYPEVIKANIDEEEkgiPFISPFLNLDDK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 834 KLLVRQLTGYL-RGLGIDRQTIRRACRQAAAAQDEYTRLVRQKALDLLAASRREGRLTILLAGRPYHT-DPLIQHKLSDM 911
Cdd:COG3580 142 ELLAKRLYEELgKGLGISKKEIKRAVEKAWEAQRAFRRDLRKKGEEILEELKENGEKGIVLLGRPYHIyDPEINHGIPEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 912 IASLGVNVISEDVVRGD-LSVGTGNTRIVRQWAYMNRIIKAGQWCAEQPDdLHFVQMTSFGCGPDSFIQDEIRSIMKEHG 990
Cdd:COG3580 222 LRSLGVAVLTEDSLPHLgEDLSARPLRKNLQWTYHSRLLGAAKFVARHPN-LDGIQLTSFGCGPDSVTTDLVEEILERSG 300
|
330 340
....*....|....*....|....*....
gi 433303179 991 KPYTLLKIDDVSNIGSLKLRVRSLVESLR 1019
Cdd:COG3580 301 KPYLLLKIDEHSNEGGVKTRLEAFLDALK 329
|
|
| ASKHA_NBD_O66634-like_rpt2 |
cd24035 |
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ... |
335-600 |
4.88e-108 |
|
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the second copy of the BcrAD/BadFG-like domain.
Pssm-ID: 466885 Cd Length: 258 Bit Score: 342.98 E-value: 4.88e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 335 VVGIDSGSTTTKLVAVRARGEqqgqLVFSDYSMNLGNPIKAVAEGLRRLQTAADENGTdlrIVGSCSTGYGEELIKTAFG 414
Cdd:cd24035 1 YLGIDVGSTTTKAVLIDEDGE----ILASVYLRTKGNPIEAVKKGLKELREQLPEKVV---IVGVGTTGSGRELLKDALG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 415 LDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVDGGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAGLACR 494
Cdd:cd24035 74 ADVVKVEITAHATAALHFDPDVDTIFEIGGQDSKYISLKNGVVKDFAMNEACSAGTGSFLEEQAKSLGIPIEEFAELALK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 495 GTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNCLYKVLklhGNDNLGNRIVVQGGTMKNDSVVRAFELL 574
Cdd:cd24035 154 AKNPPDLGSRCTVFMESDIKQAQQEGASKEDISAGLAYSVVKNYLNKVV---GGRNLGKKIVFQGGTFLNKAVLAAFEQV 230
|
250 260
....*....|....*....|....*.
gi 433303179 575 TGTEVARSNMPEMMGAYGCALHAIEQ 600
Cdd:cd24035 231 TGKEIIVPPHPGLMGAYGAALLAKEE 256
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
331-603 |
1.90e-107 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 341.31 E-value: 1.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 331 MEEVVVGIDSGSTTTKLVAVrargEQQGQLVFSDYSMNLGNPIKAVAEGLRRLQTAAdeNGTDLRIVGSCSTGYGEELIK 410
Cdd:COG1924 1 QGMIYLGIDIGSTTTKAVLL----DEDGEILASAYLPTGGDPLEAAKEALKELLEEA--GLKREDIAGVVATGYGRVLIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 411 TAFgLDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVDGGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAG 490
Cdd:COG1924 75 AAF-ADKVVTEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLEDGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 491 LACRGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNCLYKVLKLHgndnLGNRIVVQGGTMKNDSVVRA 570
Cdd:COG1924 154 LALKAKNPVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVG----IGEPVVFQGGVAKNDGVVRA 229
|
250 260 270
....*....|....*....|....*....|...
gi 433303179 571 FELLTGTEVARSNMPEMMGAYGCALHAIEQLHA 603
Cdd:COG1924 230 LEKELGKEVIVPPIPQLMGALGAALLAREKVKK 262
|
|
| ASKHA_NBD_O66634-like_rpt1 |
cd24034 |
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ... |
6-263 |
1.03e-86 |
|
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the first copy of the BcrAD/BadFG-like domain.
Pssm-ID: 466884 [Multi-domain] Cd Length: 258 Bit Score: 283.33 E-value: 1.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 6 RVGLDVGSTTAKIAVLDHDDRLVYSRYERHNAKVNELVHNYLHEIRQQLGDVRLRLCVTGSVGMSAAEQLGAEFVQEVVA 85
Cdd:cd24034 1 YLGIDIGSTTVKAVVLDEKGNIVFSDYERHFGNPREALLELLEEIKERLGDEIARIAVTGSGGRGLAELLGLPFVQEVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 86 ATVFARHRHPEAKALIDIGGEDAKVVFFNGQ--SMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQSTHLYPMAA 163
Cdd:cd24034 81 IEAAVKHLHPDARTVIEIGGEDFKLIELDGDgkLKDFRMNSKCAAGTGAFIDQQARRLGLSLEELAELALKAEPPAPIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 164 RCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLSHGCDFTPPILLCGGPLTFLPSLRKAFADYLELSttDFIVV 243
Cdd:cd24034 161 RCSVFAKSDMIHLQNKGVPKEDIAAGLCRAVARNVIATLAKGREIEGPVILVGGVATNNAVLREAFEELLGDE--ELIVP 238
|
250 260
....*....|....*....|
gi 433303179 244 HEGNLIPAIGCAIRAGQSDS 263
Cdd:cd24034 239 EHAEYFEALGAALYALEEGS 258
|
|
| DUF2229 |
pfam09989 |
CoA enzyme activase uncharacterized domain (DUF2229); Members of this family include various ... |
704-922 |
4.81e-74 |
|
CoA enzyme activase uncharacterized domain (DUF2229); Members of this family include various bacterial hypothetical proteins, as well as CoA enzyme activases. The exact function of this domain has not, as yet, been defined.
Pssm-ID: 462935 Cd Length: 213 Bit Score: 245.53 E-value: 4.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 704 VAIPRVLNMYEDYPFWHALFTTAGFEVMLSSESVFSRYEAALGSVMSDNICFPAKLVHAHVKELDERlsAPDmpagaFIF 783
Cdd:pfam09989 1 IGIPRALNMYEYYPFWHTFFTELGFRVVLSPPSSKEIYEKGIETIPSETVCYPAKLAHGHVADLLKK--GVD-----YIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 784 MPYVVYERQDDARNTNSYNCPIVSAYSDVIRSAMTLHA---RLDSPVINFRDEKLLVRQLtgyLRGLGIDRQTIRRACRQ 860
Cdd:pfam09989 74 YPCIVYEPREEDDADNHYNCPIVQGYPEVIKNNMDEREegiRFLSPFLDLDDGKLLAKQL---FEELGISKKEIKRAVEK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 433303179 861 AAAAQDEYTRLVRQKALDLLAASRREGRLTILLAGRPYHT-DPLIQHKLSDMIASLGVNVISE 922
Cdd:pfam09989 151 ALEAQEAFKEDLRKKGEEILEYLEENGKKGIVLAGRPYHIyDPEINHGIPELLASLGVAVLTE 213
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
3-256 |
9.13e-48 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 171.83 E-value: 9.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 3 KTYRVGLDVGSTTAKIAVLDHDDRLVYSRYERHNAKVNELVHNYLHEIRQQLGDVR---LRLCVTGSvGMSAAEQLGAEF 79
Cdd:COG1924 2 GMIYLGIDIGSTTTKAVLLDEDGEILASAYLPTGGDPLEAAKEALKELLEEAGLKRediAGVVATGY-GRVLIGAAFADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 80 VQ-EVVAATVFARHRHPEAKALIDIGGEDAKVVFF-NGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQSTH 157
Cdd:COG1924 81 VVtEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLeDGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELALKAKN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 158 LYPMAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQtVTTLSHGCDFTPPILLCGGplTFL-PSLRKAFADYLEls 236
Cdd:COG1924 161 PVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKR-VLNLVKRVGIGEPVVFQGG--VAKnDGVVRALEKELG-- 235
|
250 260
....*....|....*....|
gi 433303179 237 tTDFIVVHEGNLIPAIGCAI 256
Cdd:COG1924 236 -KEVIVPPIPQLMGALGAAL 254
|
|
| ASKHA_NBD_BcrAD_BadFG-like |
cd24002 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ... |
7-255 |
1.09e-46 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ATPase family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL, Methanocaldococcus jannaschii protein MJ0800, and Aquifex aeolicus hypothetical protein O66634, are also includes in this family. The members of the O66634-like group contain two copies of the BcrAD/BadFG-like region suggesting that they may structurally dimerize. The BcrAD/BadFG-like ATPase family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466852 [Multi-domain] Cd Length: 255 Bit Score: 168.38 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 7 VGLDVGSTTAKIAVLDHDDRLVYSRYERHNAKVN---ELVHNYLHEIRQQLGDVRLRLCVTGSVGMSAAEQ--LGAEFVQ 81
Cdd:cd24002 2 LGLDIGSTTSKAVLLDEGKNIVATEYERSGTGTSgpiEAVKKTLEKFLLEKGVKEEDIACTGVTGYGRVELfiDGDKQIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 82 EVVAATVFARHRHPEAKALIDIGGEDAKVVFF--NGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQSTHLY 159
Cdd:cd24002 82 EVSAHARGANHIYPDARTIIDVGGQDAKVIILdeNGQMKNFKMNDKCAAGTGAFLDSMANKLNVKVEELADVKMNSKKEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 160 PMAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLSHGCDFTPPILLCGGPLTFlPSLRKAFADYlelsTTD 239
Cdd:cd24002 162 SVSSTCAVFAETDINSFQSRGAPKEDIIAGLHKAVALRVMSLVGRLGVPKKDVVLQGGVARN-SAVVRALEEI----INN 236
|
250
....*....|....*..
gi 433303179 240 FIVVHE-GNLIPAIGCA 255
Cdd:cd24002 237 EIIVPEiAQVMGALGAA 253
|
|
| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
335-596 |
1.61e-46 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.
Pssm-ID: 466886 [Multi-domain] Cd Length: 250 Bit Score: 167.72 E-value: 1.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 335 VVGIDSGSTTTKLVAVRARGEqqgqLVFSDYSMNLGNPIKAVAEGLRRLQTAADENGTDLRIVgsCSTGYGEELIKTAfg 414
Cdd:cd24036 1 FAGIDVGSTTTKAVILDDKGK----ILGKAVIRTGTDPEKTAERALEEALEEAGLSREDIEYI--VATGYGRNSVPFA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 415 lDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVD-GGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAGLAC 493
Cdd:cd24036 73 -DKTITEITCHARGAHFLFPEARTVIDIGGQDSKVIRLDeDGKVLDFAMNDKCAAGTGRFLEVMARRLEVSLEELGELAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 494 RGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRnclyKVLKLHGNDNLGNRIVVQGGTMKNDSVVRAFEL 573
Cdd:cd24036 152 KSTNPVEISSTCTVFAESEVISLIAEGVPKEDIIAGIHNSIAK----RVAALAKRVGVEDPVVLTGGVAKNPGVVKALEE 227
|
250 260
....*....|....*....|...
gi 433303179 574 LTGTEVARSNMPEMMGAYGCALH 596
Cdd:cd24036 228 KLGVEVIVPPNPQLVGALGAALL 250
|
|
| ASKHA_NBD_O66634-like_rpt1 |
cd24034 |
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ... |
335-600 |
4.54e-43 |
|
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the first copy of the BcrAD/BadFG-like domain.
Pssm-ID: 466884 [Multi-domain] Cd Length: 258 Bit Score: 158.14 E-value: 4.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 335 VVGIDSGSTTTKLVAVrargEQQGQLVFSDYSMNLGNPIKAVAEGLRRLqtaadENGTDLRIVGSCSTGYGEELIKTAFG 414
Cdd:cd24034 1 YLGIDIGSTTVKAVVL----DEKGNIVFSDYERHFGNPREALLELLEEI-----KERLGDEIARIAVTGSGGRGLAELLG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 415 LdSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVDG-GAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAGLAC 493
Cdd:cd24034 72 L-PFVQEVVAIEAAVKHLHPDARTVIEIGGEDFKLIELDGdGKLKDFRMNSKCAAGTGAFIDQQARRLGLSLEELAELAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 494 RGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNclYKVLKLHGNDnLGNRIVVQGGTMKNDSVVRAF-- 571
Cdd:cd24034 151 KAEPPAPIAGRCSVFAKSDMIHLQNKGVPKEDIAAGLCRAVARN--VIATLAKGRE-IEGPVILVGGVATNNAVLREAfe 227
|
250 260
....*....|....*....|....*....
gi 433303179 572 ELLTGTEVARSNMPEMMGAYGCALHAIEQ 600
Cdd:cd24034 228 ELLGDEELIVPEHAEYFEALGAALYALEE 256
|
|
| ASKHA_NBD_BcrAD_BadFG-like |
cd24002 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ... |
336-595 |
1.12e-38 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ATPase family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL, Methanocaldococcus jannaschii protein MJ0800, and Aquifex aeolicus hypothetical protein O66634, are also includes in this family. The members of the O66634-like group contain two copies of the BcrAD/BadFG-like region suggesting that they may structurally dimerize. The BcrAD/BadFG-like ATPase family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466852 [Multi-domain] Cd Length: 255 Bit Score: 145.27 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 336 VGIDSGSTTTKLVAVrargEQQGQLVFSDYSMNLGN---PIKAVAEGLRRLQTAADEngTDLRIVGSCSTGYGEELIktA 412
Cdd:cd24002 2 LGLDIGSTTSKAVLL----DEGKNIVATEYERSGTGtsgPIEAVKKTLEKFLLEKGV--KEEDIACTGVTGYGRVEL--F 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 413 FGLDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVDGGAVVRM-ELNEACSSGCGTFIQTFATNLGYRVQDFAGL 491
Cdd:cd24002 74 IDGDKQISEVSAHARGANHIYPDARTIIDVGGQDAKVIILDENGQMKNfKMNDKCAAGTGAFLDSMANKLNVKVEELADV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 492 ACRGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNCLYKVLKLHgndNLGNRIVVQGGTMKNDSVVRAF 571
Cdd:cd24002 154 KMNSKKEVSVSSTCAVFAETDINSFQSRGAPKEDIIAGLHKAVALRVMSLVGRLG---VPKKDVVLQGGVARNSAVVRAL 230
|
250 260
....*....|....*....|....
gi 433303179 572 ELLTGTEVARSNMPEMMGAYGCAL 595
Cdd:cd24002 231 EEIINNEIIVPEIAQVMGALGAAL 254
|
|
| ASKHA_NBD_O66634-like_rpt2 |
cd24035 |
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ... |
7-258 |
1.77e-38 |
|
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the second copy of the BcrAD/BadFG-like domain.
Pssm-ID: 466885 Cd Length: 258 Bit Score: 144.98 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 7 VGLDVGSTTAKIAVLDHDDRLVYSRYERHNAKVNELVHNYLHEIRQQLGD--VRLRLCVTGSVGMSAAEQLGAEFVQ-EV 83
Cdd:cd24035 2 LGIDVGSTTTKAVLIDEDGEILASVYLRTKGNPIEAVKKGLKELREQLPEkvVIVGVGTTGSGRELLKDALGADVVKvEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 84 VAATVFARHRHPEAKALIDIGGEDAKVVFF-NGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQSTHLYPMA 162
Cdd:cd24035 82 TAHATAALHFDPDVDTIFEIGGQDSKYISLkNGVVKDFAMNEACSAGTGSFLEEQAKSLGIPIEEFAELALKAKNPPDLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 163 ARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLSHGCDFTPPILLCGGpltflPSLRKAFADYLELSTTDFIV 242
Cdd:cd24035 162 SRCTVFMESDIKQAQQEGASKEDISAGLAYSVVKNYLNKVVGGRNLGKKIVFQGG-----TFLNKAVLAAFEQVTGKEII 236
|
250
....*....|....*..
gi 433303179 243 VH-EGNLIPAIGCAIRA 258
Cdd:cd24035 237 VPpHPGLMGAYGAALLA 253
|
|
| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
7-256 |
4.18e-36 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.
Pssm-ID: 466886 [Multi-domain] Cd Length: 250 Bit Score: 137.67 E-value: 4.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 7 VGLDVGSTTAKIAVLDHDDRLVYSRYER----HNAKVNELVHNYLHEIRQQLGDVRlRLCVTG----SVGMsAAEQlgae 78
Cdd:cd24036 2 AGIDVGSTTTKAVILDDKGKILGKAVIRtgtdPEKTAERALEEALEEAGLSREDIE-YIVATGygrnSVPF-ADKT---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 79 fVQEVVAATVFARHRHPEAKALIDIGGEDAKV--VFFNGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQST 156
Cdd:cd24036 76 -ITEITCHARGAHFLFPEARTVIDIGGQDSKVirLDEDGKVLDFAMNDKCAAGTGRFLEVMARRLEVSLEELGELALKST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 157 HLYPMAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQtVTTLSHGCDFTPPILLCGGpLTFLPSLRKAFADYLELS 236
Cdd:cd24036 155 NPVEISSTCTVFAESEVISLIAEGVPKEDIIAGIHNSIAKR-VAALAKRVGVEDPVVLTGG-VAKNPGVVKALEEKLGVE 232
|
250 260
....*....|....*....|
gi 433303179 237 TtdfIVVHEGNLIPAIGCAI 256
Cdd:cd24036 233 V---IVPPNPQLVGALGAAL 249
|
|
| ASKHA_NBD_benz_CoA_BzdP |
cd24107 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar ... |
7-258 |
7.05e-36 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar proteins; bzd-type benzoyl-CoA reductase BzdP is encoded by the gene bzdP from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdP may function the same as the D subunit of benzoyl-CoA reductase BcrD from Thauera aromatica and benzoyl-CoA reductase BadG from Rhodopseudomonas palustris.
Pssm-ID: 466957 [Multi-domain] Cd Length: 250 Bit Score: 137.29 E-value: 7.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 7 VGLDVGSTTAKIAVLDHDDRLVYSRYE---RHNAKVNELVHNYLHEIRQQLGDVRlRLCVTGSvGMSAAeQLGAEFVQEV 83
Cdd:cd24107 2 AGIDVGSKFTKAVILEDGEILAKAIVPtgfDVAKAAERALDEALAAAGISRDDVK-KIVATGA-GRKLV-SFADDTVTEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 84 VAATVFARHRHPEAKALIDIGGEDAKVVFF--NGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQSTHLYPM 161
Cdd:cd24107 79 VCAAKGAYFLFPSARTVIDVGAEEGRAIKLdeNGKVVDFAQNDKCAAGAGAFLEAMSRALEVPLEELGELSLKSTKKIPM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 162 AARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQtVTTLSHGCDFTPPILLCGGpLTFLPSLRKAFADYLElstTDFI 241
Cdd:cd24107 159 NAQCAVFAESEVVSLIHAGTPKEDIAAAVHDAIASR-IASMVRRVGIEDDVALIGG-VAKNPGFVESLKELLG---KEVL 233
|
250
....*....|....*..
gi 433303179 242 VVHEGNLIPAIGCAIRA 258
Cdd:cd24107 234 VPEDPEYVGALGAALIA 250
|
|
| ASKHA_NBD_YjiL-like |
cd24109 |
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ... |
335-595 |
1.64e-34 |
|
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YjiL, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.
Pssm-ID: 466959 [Multi-domain] Cd Length: 243 Bit Score: 133.09 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 335 VVGIDSGSTTTKLVAVrargEQQGQLVFSDYSmNLGNPIKAVAEGLRRLqtAADENGTDLRIVgscSTGYGEELIKTAfg 414
Cdd:cd24109 1 YIGIDIGSRATKIALF----EDDKILEKFVIP-TGWFYKEYGRRIIKEL--LEDINYEDDKIV---ATGYGRNNLDFA-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 415 lDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVDGGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAGLACR 494
Cdd:cd24109 69 -DKTITEITAHAKGARYLTGKDFTVIDIGGQDTKVIKVENGKVIDFIMNDKCAAGTGRFLENMANILGISLEEISKYAED 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 495 GThPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRnclyKVLKL---HGNDNlgnrIVVQGGTMKNDSVVRAF 571
Cdd:cd24109 148 PE-PLSISSTCAVFAESEVISLIAEGVSRERIAAGVNYSIAK----RVAPLlnrLKSPP----IVLTGGVARNKAIIELL 218
|
250 260
....*....|....*....|....
gi 433303179 572 ELLTGTEVARSNMPEMMGAYGCAL 595
Cdd:cd24109 219 EKRLGAEVIVPELPQFAGAIGAAL 242
|
|
| ASKHA_NBD_HgdC_HadI-like |
cd24103 |
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ... |
336-601 |
4.66e-34 |
|
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily includes a group of proteins such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). HgdC (EC 3.6.1.-), also called (R)-2-hydroxyglutaryl-CoA dehydratase activase, (R)-2-hydroxyglutaryl-CoA dehydratase (component A), ATP-coupled electron transfer protein HgdC, or activator of (R)-2-hydroxyglutaryl-CoA dehydratase, is involved in the fermentation of L-glutamate via the hydroxyglutarate pathway. HgdC (CompA) has a very low ATPase activity. Its role is to activate dehydratase HgdA-HgdB complex and then maintain an appropriate redox state via an ATP-dependent electron transfer. The dehydratase requires only catalytic amounts of ATP and substoichiometric amounts of HgdC (CompA) to be functional. HadI is involved in the reductive branch of L-leucine fermentation. It is required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. FldI (EC 3.6.1.-), also called initiator of phenyllactate dehydratase, is involved in the fermentation of L-phenylalanine via a Stickland reaction. It is required for the activation of the (R)-phenyllactate dehydratase complex FldABC. Only in the oxidized state, FldI exhibits significant ATPase activity, which appears to be essential for unidirectional electron transfer. LcdC, also called lactoyl-CoA dehydratase component E I, is required for the activation of lactoyl-CoA dehydratase. HadI, FldI and LcdC are extremely sensitive towards oxygen.
Pssm-ID: 466953 Cd Length: 255 Bit Score: 132.15 E-value: 4.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 336 VGIDSGSTTTKLVAVRARGEQQGQLVfsdYSMNLGN--PIKAVAEGLrrlqtaADENGTDLRIVGSCSTGYGEELIKTAf 413
Cdd:cd24103 2 MGIDIGSTASKCVILKDGKEIVAQSV---ISVGTGTsgPARALEEVL------EKAGLAKEDIAYTVATGYGRNSFEGA- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 414 glDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVDG-GAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAGLA 492
Cdd:cd24103 72 --DKQISELSCHARGVNFLLPEVRTIIDIGGQDVKVLKLDDnGRLLNFVMNDKCAAGTGRFLDVMARVLEVKVSELGELD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 493 CRGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRnclyKVLKLHGNDNLGNRIVVQGGTMKNDSVVRAFE 572
Cdd:cd24103 150 AQSTNPVSISSTCTVFAESEVISQLSEGAKIPDIIAGIHTSVAS----RVAGLAKRVGIEKDVVMTGGVAQNSGVVRAME 225
|
250 260
....*....|....*....|....*....
gi 433303179 573 LLTGTEVARSNMPEMMGAYGCALHAIEQL 601
Cdd:cd24103 226 EELGTEIIVSPNPQLTGALGAALYAYEKA 254
|
|
| ASKHA_NBD_benz_CoA_BzdP |
cd24107 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar ... |
335-597 |
5.29e-32 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar proteins; bzd-type benzoyl-CoA reductase BzdP is encoded by the gene bzdP from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdP may function the same as the D subunit of benzoyl-CoA reductase BcrD from Thauera aromatica and benzoyl-CoA reductase BadG from Rhodopseudomonas palustris.
Pssm-ID: 466957 [Multi-domain] Cd Length: 250 Bit Score: 126.12 E-value: 5.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 335 VVGIDSGSTTTKLVAVRargeqQGQLVFSDYSMNLGNPIKAVAEGLRRLQTAADENGTDLRivGSCSTGYGEELIKTAfg 414
Cdd:cd24107 1 TAGIDVGSKFTKAVILE-----DGEILAKAIVPTGFDVAKAAERALDEALAAAGISRDDVK--KIVATGAGRKLVSFA-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 415 lDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVD-GGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAGLAC 493
Cdd:cd24107 72 -DDTVTEVVCAAKGAYFLFPSARTVIDVGAEEGRAIKLDeNGKVVDFAQNDKCAAGAGAFLEAMSRALEVPLEELGELSL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 494 RGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNCLYKVLKLhgndNLGNRIVVQGGTMKNDSVVRAFEL 573
Cdd:cd24107 151 KSTKKIPMNAQCAVFAESEVVSLIHAGTPKEDIAAAVHDAIASRIASMVRRV----GIEDDVALIGGVAKNPGFVESLKE 226
|
250 260
....*....|....*....|....
gi 433303179 574 LTGTEVARSNMPEMMGAYGCALHA 597
Cdd:cd24107 227 LLGKEVLVPEDPEYVGALGAALIA 250
|
|
| ASKHA_NBD_benz_CoA_BcrA_BadF |
cd24104 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ... |
335-599 |
9.44e-32 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar proteins; Benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit A of benzoyl-CoA reductase.
Pssm-ID: 466954 Cd Length: 253 Bit Score: 125.48 E-value: 9.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 335 VVGIDSGSTTTKLVAVRARGEQQGQLVfsdysMNLGNPIKAVAEGLRR--LQTAADENGTDLRIVGscsTGYGEelIKTA 412
Cdd:cd24104 1 AAGVDVGSTQTKAVIIDEDGEIVGRGL-----TNTGANVVVAAERAFReaIEEAGIKEEEVEYVVG---TGYGR--YKVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 413 FGlDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVD-GGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAGL 491
Cdd:cd24104 71 FG-NAQRTEISCHARGAHHMFPNTRTVLDIGGQDTKAIRVDeTGEVVDFVMNDKCAAGTGRFLGYAADALGIPLDELGPL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 492 ACRGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRnclyKVLKLHGNDNLGNRIVVQGGTMKNDSVVRAF 571
Cdd:cd24104 150 ALKSTKPVRISSTCTVFAESEIRSWLALGKKREDILGGVHRAIAA----RAVSLIRRVGIEPEFTFTGGVARNEAMVKAL 225
|
250 260
....*....|....*....|....*...
gi 433303179 572 ELLTGTEVARSNMPEMMGAYGCALHAIE 599
Cdd:cd24104 226 EELLGVKINVSPDSHFMGALGAALFALE 253
|
|
| CoA_E_activ |
TIGR00241 |
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ... |
334-595 |
2.15e-29 |
|
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.
Pssm-ID: 129344 Cd Length: 248 Bit Score: 118.36 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 334 VVVGIDSGSTTTKLVAVRargeqQGQLV---FSDYSMNLGNPIKAVAEGLRRLQTAADEngtdlrIVGSCSTGYGEELIK 410
Cdd:TIGR00241 1 ISLGIDSGSTTTKMVLME-----DGKVIgykWLDTTPVIEETARAILEALKEAGIGLEP------IDKIVATGYGRHKVG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 411 TAfglDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVDGGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAG 490
Cdd:TIGR00241 70 FA---DKIVTEISCHGKGANYLAPEARGVIDIGGQDSKVIKIDDGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 491 LACRGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNCLYKVLKLHGNDNlgnrIVVQGGTMKNDSVVRA 570
Cdd:TIGR00241 147 LAEKADRKAKISSMCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAP----IVFTGGVSKNKGLVKA 222
|
250 260
....*....|....*....|....*
gi 433303179 571 FELLTGTEVARSNMPEMMGAYGCAL 595
Cdd:TIGR00241 223 LEKKLGMKVITPPEPQIVGAVGAAL 247
|
|
| CoA_E_activ |
TIGR00241 |
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ... |
5-256 |
4.17e-29 |
|
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely related proteins including the (R)-2-hydroxyglutaryl-CoA dehydratase activase of Acidaminococcus fermentans, in longer proteins from M. jannaschii and M. thermoautotrophicum that share an additional N-terminal domain, in a protein described as a subunit of the benzoyl-CoA reductase of Rhodopseudomonas palustris, and in two repeats of an uncharacterized protein of Aquifex aeolicus.This domain may be involved in generating or regenerating the active sites of enzymes related to (R)-2-hydroxyglutaryl-CoA dehydratase and benzoyl-CoA reductase.
Pssm-ID: 129344 Cd Length: 248 Bit Score: 117.59 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 5 YRVGLDVGSTTAKIAVLDhDDRLVYSRYERHNAKVNE---LVHNYLHEIRQQLGDVRlRLCVTG----SVGmsaaeqlGA 77
Cdd:TIGR00241 1 ISLGIDSGSTTTKMVLME-DGKVIGYKWLDTTPVIEEtarAILEALKEAGIGLEPID-KIVATGygrhKVG-------FA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 78 EFVQ-EVVAATVFARHRHPEAKALIDIGGEDAKVV-FFNGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQS 155
Cdd:TIGR00241 72 DKIVtEISCHGKGANYLAPEARGVIDIGGQDSKVIkIDDGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 156 THLYPMAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLSHgCDFTPPILLCGGpLTFLPSLRKAFADYLEL 235
Cdd:TIGR00241 152 DRKAKISSMCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQR-LKIEAPIVFTGG-VSKNKGLVKALEKKLGM 229
|
250 260
....*....|....*....|.
gi 433303179 236 sttDFIVVHEGNLIPAIGCAI 256
Cdd:TIGR00241 230 ---KVITPPEPQIVGAVGAAL 247
|
|
| ASKHA_NBD_YjiL-like |
cd24109 |
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ... |
6-256 |
4.81e-27 |
|
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YjiL, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.
Pssm-ID: 466959 [Multi-domain] Cd Length: 243 Bit Score: 111.52 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 6 RVGLDVGSTTAKIAVLDhDDRLVYSRYERHNAKVNELVHNYLHEIRQQLGDVRLRLCVTG----SVgmsaaeQLGAEFVQ 81
Cdd:cd24109 1 YIGIDIGSRATKIALFE-DDKILEKFVIPTGWFYKEYGRRIIKELLEDINYEDDKIVATGygrnNL------DFADKTIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 82 EVVAATVFARHRHPEAKALIDIGGEDAKVVFF-NGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQSTHLyP 160
Cdd:cd24109 74 EITAHAKGARYLTGKDFTVIDIGGQDTKVIKVeNGKVIDFIMNDKCAAGTGRFLENMANILGISLEEISKYAEDPEPL-S 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 161 MAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLS-HGCdftPPILLCGGpLTFLPSLRKAFADYLElstTD 239
Cdd:cd24109 153 ISSTCAVFAESEVISLIAEGVSRERIAAGVNYSIAKRVAPLLNrLKS---PPIVLTGG-VARNKAIIELLEKRLG---AE 225
|
250
....*....|....*..
gi 433303179 240 FIVVHEGNLIPAIGCAI 256
Cdd:cd24109 226 VIVPELPQFAGAIGAAL 242
|
|
| ASKHA_NBD_benz_CoA_BcrD_BadG |
cd24105 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ... |
335-595 |
7.08e-27 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar proteins; benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit D of benzoyl-CoA reductase.
Pssm-ID: 466955 Cd Length: 256 Bit Score: 111.14 E-value: 7.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 335 VVGIDSGSTTTKLVAVrargEQQGQLVfsDYSMN-LGNPIKAVAEGLrrLQTAADENGTDLRIVGSC-STGYGEELIkta 412
Cdd:cd24105 1 TAGIDVGSGYTKAVIM----DDGEKIL--AKRVErTRQRDEEVAREA--YNEALEEAGLKRDDIAYVaTTGEGRYVV--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 413 FGLDSGIIETMAHYRAAARLMPDVSFILDIGGQDMKAIFVD-GGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAGL 491
Cdd:cd24105 70 FFRDGHFTDLTTHARGAIFLFPGTRTVLDIGAQHTRAIRIDeKGKVLSFRMNDKCAAGSGQFLENIARYLGVALDEIGDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 492 ACRGTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNC--LYKVLKLHGNdnlgnrIVVQGGTMKNDSVVR 569
Cdd:cd24105 150 SLQADNPEPISGVCAVLAETEVINMVSRGIPVPDILRGIHLSLAGRSvqLLKRVGAEPE------VTLTGGLARNEGMVE 223
|
250 260
....*....|....*....|....*...
gi 433303179 570 AFELLTGT--EVARSNMPEMMGAYGCAL 595
Cdd:cd24105 224 ALEELLGAkvNVAEHDDSIYAGALGAAL 251
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
336-597 |
1.59e-26 |
|
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.
Pssm-ID: 396441 [Multi-domain] Cd Length: 271 Bit Score: 110.91 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 336 VGIDSGSTTTKLVAVRARGEQQGQLVF-SDYSMNLG--NPIKAVAEGLRRLQTAADENGTDLRIVGSCSTGYGEELIKTA 412
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGRAIAgSANFESVGveAAERNLKDAITEALEEAGLKLDDIEYMFLGLTGYGRAGVDGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 413 FGLDSGIIETMAHYRAAARLMPDVSF---ILDIGGQDMKAIFVDGGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFA 489
Cdd:pfam01869 81 FGKDIVREEITVHADGAVALAPGTRGedgVIDIGGTGSKVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARALGAVVRELD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 490 GLACRGT-HPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNcLYKVLKLHGNDnlGNRIVVQGGTMKNDSVV 568
Cdd:pfam01869 161 GLAPKTTlNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALR-VAALAKRLGFV--PDEVVLTGGVAKNAGLV 237
|
250 260 270
....*....|....*....|....*....|....
gi 433303179 569 RAFELLTGTEVAR-----SNMPEMMGAYGCALHA 597
Cdd:pfam01869 238 KALRDYLKENILGvkvnvHPDPQYAGAIGAALLA 271
|
|
| ASKHA_NBD_benz_CoA_BcrD_BadG |
cd24105 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ... |
7-260 |
4.85e-22 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar proteins; benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit D of benzoyl-CoA reductase.
Pssm-ID: 466955 Cd Length: 256 Bit Score: 97.27 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 7 VGLDVGSTTAKIAVLDHDDRLVYSRYERHNAKVNELVHNYLHEIRQQLG----DVRLrLCVTGSVGMSAAEQLGaeFVQE 82
Cdd:cd24105 2 AGIDVGSGYTKAVIMDDGEKILAKRVERTRQRDEEVAREAYNEALEEAGlkrdDIAY-VATTGEGRYVVFFRDG--HFTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 83 VVAATVFARHRHPEAKALIDIGGEDAKVVFF--NGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQSTHLYP 160
Cdd:cd24105 79 LTTHARGAIFLFPGTRTVLDIGAQHTRAIRIdeKGKVLSFRMNDKCAAGSGQFLENIARYLGVALDEIGDLSLQADNPEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 161 MAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLSH-GCDftPPILLCGGPLTFlPSLRKAFADYLElSTTD 239
Cdd:cd24105 159 ISGVCAVLAETEVINMVSRGIPVPDILRGIHLSLAGRSVQLLKRvGAE--PEVTLTGGLARN-EGMVEALEELLG-AKVN 234
|
250 260
....*....|....*....|.
gi 433303179 240 FIVVHEGNLIPAIGCAIRAGQ 260
Cdd:cd24105 235 VAEHDDSIYAGALGAALLGAF 255
|
|
| ASKHA_NBD_HgdC_HadI-like |
cd24103 |
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ... |
7-258 |
1.79e-21 |
|
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily includes a group of proteins such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). HgdC (EC 3.6.1.-), also called (R)-2-hydroxyglutaryl-CoA dehydratase activase, (R)-2-hydroxyglutaryl-CoA dehydratase (component A), ATP-coupled electron transfer protein HgdC, or activator of (R)-2-hydroxyglutaryl-CoA dehydratase, is involved in the fermentation of L-glutamate via the hydroxyglutarate pathway. HgdC (CompA) has a very low ATPase activity. Its role is to activate dehydratase HgdA-HgdB complex and then maintain an appropriate redox state via an ATP-dependent electron transfer. The dehydratase requires only catalytic amounts of ATP and substoichiometric amounts of HgdC (CompA) to be functional. HadI is involved in the reductive branch of L-leucine fermentation. It is required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. FldI (EC 3.6.1.-), also called initiator of phenyllactate dehydratase, is involved in the fermentation of L-phenylalanine via a Stickland reaction. It is required for the activation of the (R)-phenyllactate dehydratase complex FldABC. Only in the oxidized state, FldI exhibits significant ATPase activity, which appears to be essential for unidirectional electron transfer. LcdC, also called lactoyl-CoA dehydratase component E I, is required for the activation of lactoyl-CoA dehydratase. HadI, FldI and LcdC are extremely sensitive towards oxygen.
Pssm-ID: 466953 Cd Length: 255 Bit Score: 95.56 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 7 VGLDVGSTTAKIAVLDHDDRLV----------YSRYERHNAKVNELVHNYLHEIRqqlgdvrlRLCVTGsVGMSAAEQLG 76
Cdd:cd24103 2 MGIDIGSTASKCVILKDGKEIVaqsvisvgtgTSGPARALEEVLEKAGLAKEDIA--------YTVATG-YGRNSFEGAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 77 AEfVQEVVAATVFARHRHPEAKALIDIGGEDAKVVFFNGQSMELR--MNGNCAGGTGAFIDQMSVLMGCDNARLDELARQ 154
Cdd:cd24103 73 KQ-ISELSCHARGVNFLLPEVRTIIDIGGQDVKVLKLDDNGRLLNfvMNDKCAAGTGRFLDVMARVLEVKVSELGELDAQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 155 STHLYPMAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAvQTVTTLSHGCDFTPPILLCGGpLTFLPSLRKAFADYLE 234
Cdd:cd24103 152 STNPVSISSTCTVFAESEVISQLSEGAKIPDIIAGIHTSVA-SRVAGLAKRVGIEKDVVMTGG-VAQNSGVVRAMEEELG 229
|
250 260
....*....|....*....|....
gi 433303179 235 lstTDFIVVHEGNLIPAIGCAIRA 258
Cdd:cd24103 230 ---TEIIVSPNPQLTGALGAALYA 250
|
|
| ASKHA_NBD_benz_CoA_BzdQ |
cd24106 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and ... |
335-597 |
7.13e-21 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and similar proteins; bzd-type benzoyl-CoA reductase BzdQ is encoded by the gene bzdQ from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdQ may function the same as the A subunit of benzoyl-CoA reductase BcrA from Thauera aromatica and benzoyl-CoA reductase BadF from Rhodopseudomonas palustris.
Pssm-ID: 466956 Cd Length: 253 Bit Score: 93.82 E-value: 7.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 335 VVGIDSGSTTTKLVAVrargeQQGQLV-FSdySMNLGNPIKAVAEglRRLQTAADenGTDLR------IVGscsTGYGEE 407
Cdd:cd24106 1 TAGIDVGSVSSQAVIM-----VDGELYaYS--NMRTGSDSPESAQ--KALNAALE--KTGLKledihyIVG---TGYGRV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 408 LIKTAfglDSGIIETMAHYRAAARLMPD-VSFILDIGGQDMKAIFVD-GGAVVRMELNEACSSGCGTFIQTFATNLGYRV 485
Cdd:cd24106 67 NVPFA---NKAITEIACHARGANYMYGPsVRTVLDMGGQDCKAIRCDeKGKVTNFLMNDKCAAGTGRGMEVFADLLQVPI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 486 QDFAGLACR-GTHPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVrnclYKVLKLHGNDNLGNRIVVQGGTMKN 564
Cdd:cd24106 144 EEIGELSLEvDKEPPPVSSTCVVFAKSEALGLLREGWPKNDVLAAYCEAMA----HRVVTLLERVGVEKDFVITGGIAKN 219
|
250 260 270
....*....|....*....|....*....|....
gi 433303179 565 DSVVRAFELLTGTEVARSNM-PEMMGAYGCALHA 597
Cdd:cd24106 220 IGVVKRIEKELGIKALIPKEdPQIAGALGAALFA 253
|
|
| ASKHA_NBD_MJ0800-like |
cd24108 |
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar ... |
337-595 |
4.08e-17 |
|
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ0800, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.
Pssm-ID: 466958 Cd Length: 259 Bit Score: 82.89 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 337 GIDSGSTTTKLVAVrargeqQGQLVFSDYSMNLGNPIKAVAEGLRRLQTAADENGTDLRIVGscSTGYGEELIKTAFGLD 416
Cdd:cd24108 3 GIDSGSTTTKAVVM------KDNEIIGTGWMPTTDVIESAEKAFEEALEEAGIKLSDIEAIG--TTGYGRYTIGKHFNAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 417 SGIIETMAHYRAAARL---MPDVSFILDIGGQDMKAIFVDGGAVVRMELNEACSSGCGTFIQTFATNLGYRVQDFAGLAC 493
Cdd:cd24108 75 LVQEELTVNSKGAVYLadkQKGEATVIDIGGMDNKAITVNDGIPDNFTMGGICAGASGRFLEMTARRLGVDITELGELAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 494 RGT-HPCDLGTRCTVFMNSKVKQVMREGASVADIASGLSYSVVRNCLYKVLKlhgNDNLGNRIVVQGGTMKNDSVVRAFE 572
Cdd:cd24108 155 KGDwRKIRMNSYCIVFGIQDLVTSLAEGARAEDVAAAACHSVAEQVYEQQLQ---EIDVREPVIQVGGTSLIEGLVKALG 231
|
250 260
....*....|....*....|...
gi 433303179 573 LLTGTEVARSNMPEMMGAYGCAL 595
Cdd:cd24108 232 EVLGIEVIVPPYSQLIGAVGAAL 254
|
|
| ASKHA_NBD_MJ0800-like |
cd24108 |
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar ... |
8-258 |
5.75e-16 |
|
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ0800, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.
Pssm-ID: 466958 Cd Length: 259 Bit Score: 79.42 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 8 GLDVGSTTAKiAVLDHDDRLVYSRYERhNAKVNELVHNYLHEIRQQLGdVRLR----LCVTGSVGMSAAEQLGAEFVQEV 83
Cdd:cd24108 3 GIDSGSTTTK-AVVMKDNEIIGTGWMP-TTDVIESAEKAFEEALEEAG-IKLSdieaIGTTGYGRYTIGKHFNADLVQEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 84 V-----AATVFARHRHPEAkALIDIGGEDAKVV-FFNGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQST- 156
Cdd:cd24108 80 LtvnskGAVYLADKQKGEA-TVIDIGGMDNKAItVNDGIPDNFTMGGICAGASGRFLEMTARRLGVDITELGELALKGDw 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 157 HLYPMAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLSHGCDFTPPILLCGGPlTFLPSLRKAFADYLELs 236
Cdd:cd24108 159 RKIRMNSYCIVFGIQDLVTSLAEGARAEDVAAAACHSVAEQVYEQQLQEIDVREPVIQVGGT-SLIEGLVKALGEVLGI- 236
|
250 260
....*....|....*....|..
gi 433303179 237 ttDFIVVHEGNLIPAIGCAIRA 258
Cdd:cd24108 237 --EVIVPPYSQLIGAVGAALLA 256
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
7-234 |
2.28e-14 |
|
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.
Pssm-ID: 396441 [Multi-domain] Cd Length: 271 Bit Score: 75.08 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 7 VGLDVGSTTAKIAVLDHDDRLVY------SRYERHNAK-----VNELVHNYLHEIRQQLGDVRLRLCVTGSVGMSAAEQl 75
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGraiagsANFESVGVEaaernLKDAITEALEEAGLKLDDIEYMFLGLTGYGRAGVDG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 76 gaEFVQEVVAATVFARHR--------HPEAKALIDIGGEDAKVVFFNGQSME-LRMNGNCAGGTGAFIDQMSVLMGCDNA 146
Cdd:pfam01869 80 --HFGKDIVREEITVHADgavalapgTRGEDGVIDIGGTGSKVIGLDGGKVVrFGGNGQCAGGEGSFLEIAARALGAVVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 147 RLDELARQST-HLYPMAARCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLSHGCDFTPPILLCGGplTFLPS- 224
Cdd:pfam01869 158 ELDGLAPKTTlNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRLGFVPDEVVLTGG--VAKNAg 235
|
250
....*....|
gi 433303179 225 LRKAFADYLE 234
Cdd:pfam01869 236 LVKALRDYLK 245
|
|
| ASKHA_NBD_benz_CoA_BcrA_BadF |
cd24104 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ... |
7-203 |
1.60e-13 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar proteins; Benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit A of benzoyl-CoA reductase.
Pssm-ID: 466954 Cd Length: 253 Bit Score: 72.33 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 7 VGLDVGSTTAKIAVLDHDDRLVYSRYERHNAKVNELVHNYLHEIRQQLGDVRLRLC-VTGSVGMSAAEQLGAEFVQEVVA 85
Cdd:cd24104 2 AGVDVGSTQTKAVIIDEDGEIVGRGLTNTGANVVVAAERAFREAIEEAGIKEEEVEyVVGTGYGRYKVTFGNAQRTEISC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 86 ATVFARHRHPEAKALIDIGGEDAKV--VFFNGQSMELRMNGNCAGGTGAFIDQMSVLMGCDNARLDELARQSTHLYPMAA 163
Cdd:cd24104 82 HARGAHHMFPNTRTVLDIGGQDTKAirVDETGEVVDFVMNDKCAAGTGRFLGYAADALGIPLDELGPLALKSTKPVRISS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 433303179 164 RCGVFAKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTLS 203
Cdd:cd24104 162 TCTVFAESEIRSWLALGKKREDILGGVHRAIAARAVSLIR 201
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| ASKHA_NBD_benz_CoA_BzdQ |
cd24106 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and ... |
95-202 |
1.37e-09 |
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nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and similar proteins; bzd-type benzoyl-CoA reductase BzdQ is encoded by the gene bzdQ from a benzoate-inducible catabolic operon in Azoarcus sp. The bzd-type benzoyl-CoA reductase system catalyzes the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for several different aromatic compounds, such as phenol and toluene. BzdQ may function the same as the A subunit of benzoyl-CoA reductase BcrA from Thauera aromatica and benzoyl-CoA reductase BadF from Rhodopseudomonas palustris.
Pssm-ID: 466956 Cd Length: 253 Bit Score: 60.31 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 95 PEAKALIDIGGEDAKVVFFN--GQSMELRMNGNCAGGTGAFIDQMSVLMGcdnARLDELARQS----THLYPMAARCGVF 168
Cdd:cd24106 91 PSVRTVLDMGGQDCKAIRCDekGKVTNFLMNDKCAAGTGRGMEVFADLLQ---VPIEEIGELSlevdKEPPPVSSTCVVF 167
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90 100 110
....*....|....*....|....*....|....
gi 433303179 169 AKTDIQNLMSRNLPKSDIAASIFHSIAVQTVTTL 202
Cdd:cd24106 168 AKSEALGLLREGWPKNDVLAAYCEAMAHRVVTLL 201
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| ASKHA_NBD_PanK-II_bac |
cd24085 |
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ... |
7-256 |
4.21e-09 |
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nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins mainly from bacteria; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. The model corresponds to a group of PanK-II that is mainly from bacteria.
Pssm-ID: 466935 [Multi-domain] Cd Length: 262 Bit Score: 59.12 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 7 VGLDVGSTTAKIAVLDHDDRLVYSRYErhNAKVNELVHnylhEIRQQLGDVRLRLCVTGsvGMSA-----AEQLGAEFVQ 81
Cdd:cd24085 2 IGIDAGGTLTKIVLLENNGELKFKAFD--SLKIEALVK----FLNELGINDIEKIAVTG--GGASrlpenIDGIPIVKVD 73
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 82 EVVAATVFARH---RHPEAKALIDIGgedakvvffNGQSMeLRMNGNCA---GGT---GAFIDQMSVLMGC--DNARLDE 150
Cdd:cd24085 74 EFEAIGRGALYllgEILDDALVVSIG---------TGTSI-VLAKNGTIrhvGGTgvgGGTLLGLGKLLLGvtDYDEITE 143
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 433303179 151 LARQST---------HLYP----------MAARcgvFAKTDiqnlMSRNLPKSDIAASIFHSIAvQTVTTLS------HG 205
Cdd:cd24085 144 LARKGDrsnvdltvgDIYGggigplppdlTASN---FGKLA----DDNKASREDLAAALINLVG-ETIGTLAalaaraEG 215
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250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 433303179 206 CDftpPILLCGGPLTFlPSLRKAFADYLELSTTDFIVVHEGNLIPAIGCAI 256
Cdd:cd24085 216 VK---DIVLVGSTLRN-PLLKEVLERYTKLYGVKPIFPENGEFAGAIGALL 262
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