|
Name |
Accession |
Description |
Interval |
E-value |
| COG3581 |
COG3581 |
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function ... |
1019-1426 |
0e+00 |
|
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only];
Pssm-ID: 442800 Cd Length: 407 Bit Score: 566.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1019 PKRKLLVPQMSPIHFQFIEKAVNLSGWNVEVLQDTSREIIEEGLRYVNNDACYPAIIVIGQLISALKSGKYDLNNVSVGI 1098
Cdd:COG3581 2 KTMTILFPHMGPIHFRLLKAAFRGLGYEVEVLPPPDKETLELGLKYVNNDACYPLKIVLGQLIEALESGKYDPDATAIVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1099 TQTGGGCRATNYIGFLRKAMYESGFKDVPVVSLSAQGIEDN-GLKenVSLSLINRGFMAVVYGDLFMKVLYRTRPYEKVK 1177
Cdd:COG3581 82 TGTGGPCRAGNYIELLRKALKDAGYPDVPVISLNPQGLEFNpGFK--LTLKLLKRAWKAIVYGDLLEKLLYRTRPYEKNK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1178 GSANALYEKWVKICMDSLENAKLSTFSKNIKNIIRDFDNLEL-LDIKKPRVGLVGEILVKFHPTANNNIVDVLEREGAEA 1256
Cdd:COG3581 160 GSADRLYEKWLEKLEEALESGSLKELKKLLKEIVKEFDAIPLdEDEKKPRVGIVGEIYVKLEPFANNNIEKFLEEEGAEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1257 VMPEMANFFLYSAVNGIYKKDhKLEGTTKGKFMCKFFIGLVSFYQKTYVKELKNSKRFNAPEKIIELSKKTESLVSVGNQ 1336
Cdd:COG3581 240 VRPPLSDWILYNLYNRKFKAK-ELGGSKKSRLKKKLAIKVLEKYRKPIKKALRKSLRFEPPPDIKELAEAAKPYLSLGNI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1337 TGEGWLLPGEMIELIESGVENIVCMQPFGCLPNhIIGKGPIKELKARYPKANIIPIDYDPSASEVNQINRIKLMLSRAFK 1416
Cdd:COG3581 319 GGEGWLLIGEMVELIKEGYDGIICLQPFGCMPN-IVAKGILKKLRRDYPEIPILTLDYDEGASEVNQLTRLEAFLDLAKR 397
|
410
....*....|
gi 494496814 1417 NLHDDEDNTS 1426
Cdd:COG3581 398 RREKKEEEAL 407
|
|
| COG3580 |
COG3580 |
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function ... |
661-1006 |
1.45e-161 |
|
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only];
Pssm-ID: 442799 Cd Length: 343 Bit Score: 489.73 E-value: 1.45e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 661 LFKhYKPLKLEDAPRGEVGLPRALNMYEDYPFWFTLFTKLGFKVTLSGRSSKKLYERGMtSIASETVCYPGKMVHGHIQS 740
Cdd:COG3580 1 LFD-YKPLPPEKAMRGTIGIPRALNYYEYYPFWKTFFTELGFEVVLSPPTNKEIYEKGI-EIASDEACYPAKLAHGHVAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 741 LIDKGVKTIFYPAVTHEYREDKTSDNHYNCPVVISYSEIIKNNVpDLKKKNIKFINPFMTLNDKENLKDRLCQVFSyyfA 820
Cdd:COG3580 79 LLDKGVDYIFYPRIVSEPKEDEGADNHYNCPKVQGYPEVIKANI-DEEEKGIPFISPFLNLDDKELLAKRLYEELG---K 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 821 DLNISKSEIRDAVDAAKEEEFAFKADIRRAGEEAVEKIQKENLKGIVLAGRPYHL-DPEINHGMPELINSLDMAVLTEDS 899
Cdd:COG3580 155 GLGISKKEIKRAVEKAWEAQRAFRRDLRKKGEEILEELKENGEKGIVLLGRPYHIyDPEINHGIPELLRSLGVAVLTEDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 900 ICHLAQVQ--RPLRVVDQWVYHSRLYKAAEFVKKYDNIELVQLNSFGCGLDAVTTEQVQEILAEKSKIYTVIKIDEGNNL 977
Cdd:COG3580 235 LPHLGEDLsaRPLRKNLQWTYHSRLLGAAKFVARHPNLDGIQLTSFGCGPDSVTTDLVEEILERSGKPYLLLKIDEHSNE 314
|
330 340
....*....|....*....|....*....
gi 494496814 978 GAAKIRLRSLKAAMAEREANHISVKNIKE 1006
Cdd:COG3580 315 GGVKTRLEAFLDALKERKKKEAKALEFTK 343
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
316-583 |
1.05e-128 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 399.09 E-value: 1.05e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 316 KGNCFLGIDAGSTTTKAALIDENCNLVYTYYSSNEGSPLQTSINIVKDIYNKLP-KDVNIVSSCVTGYGEALLKKALkID 394
Cdd:COG1924 1 QGMIYLGIDIGSTTTKAVLLDEDGEILASAYLPTGGDPLEAAKEALKELLEEAGlKREDIAGVVATGYGRVLIGAAF-AD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 395 YGEIETMAHYKAAKYFDPEVDFILDIGGQDMKCLQIKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQ 474
Cdd:COG1924 80 KVVTEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLEDGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELALKAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 475 NPVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKNALFKVIKIrdlnELGKNIVVQGGTFYNDLVLRSFEKLIG 554
Cdd:COG1924 160 NPVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRV----GIGEPVVFQGGVAKNDGVVRALEKELG 235
|
250 260
....*....|....*....|....*....
gi 494496814 555 RNVTRPDISGIMGAFGAAIICKERYSEGH 583
Cdd:COG1924 236 KEVIVPPIPQLMGALGAALLAREKVKKGK 264
|
|
| ASKHA_NBD_O66634-like_rpt2 |
cd24035 |
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ... |
320-579 |
1.53e-125 |
|
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: 390.36 E-value: 1.53e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 320 FLGIDAGSTTTKAALIDENCNLVYTYYSSNEGSPLQTSINIVKDIYNKLPKDVNIVSSCVTGYGEALLKKALKIDYGEIE 399
Cdd:cd24035 1 YLGIDVGSTTTKAVLIDEDGEILASVYLRTKGNPIEAVKKGLKELREQLPEKVVIVGVGTTGSGRELLKDALGADVVKVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 400 TMAHYKAAKYFDPEVDFILDIGGQDMKCLQIKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQNPVDL 479
Cdd:cd24035 81 ITAHATAALHFDPDVDTIFEIGGQDSKYISLKNGVVKDFAMNEACSAGTGSFLEEQAKSLGIPIEEFAELALKAKNPPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 480 GSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKNALFKVIKIRDlneLGKNIVVQGGTFYNDLVLRSFEKLIGRNVTR 559
Cdd:cd24035 161 GSRCTVFMESDIKQAQQEGASKEDISAGLAYSVVKNYLNKVVGGRN---LGKKIVFQGGTFLNKAVLAAFEQVTGKEIIV 237
|
250 260
....*....|....*....|
gi 494496814 560 PDISGIMGAFGAAIICKERY 579
Cdd:cd24035 238 PPHPGLMGAYGAALLAKEEI 257
|
|
| ASKHA_NBD_O66634-like_rpt1 |
cd24034 |
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ... |
7-260 |
1.57e-103 |
|
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: 330.32 E-value: 1.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLD-KDKVIFKKYTRHFSDVKKAVKEVLTEVYEKLGDIRISTVVTGSGGIDISKYLGLKFVQEVISS 85
Cdd:cd24034 2 LGIDIGSTTVKAVVLDeKGNIVFSDYERHFGNPREALLELLEEIKERLGDEIARIAVTGSGGRGLAELLGLPFVQEVVAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 86 TKAIETFNPETDVVIELGGEDAKITYLSGG---IDQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIYPIASR 162
Cdd:cd24034 82 EAAVKHLHPDARTVIEIGGEDFKLIELDGDgklKDFRMNSKCAAGTGAFIDQQARRLGLSLEELAELALKAEPPAPIAGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 163 CGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLSCGRAIEGNVAFLGGPLYFLSELRTAFKNVLNlsDENIIFPQ 242
Cdd:cd24034 162 CSVFAKSDMIHLQNKGVPKEDIAAGLCRAVARNVIATLAKGREIEGPVILVGGVATNNAVLREAFEELLG--DEELIVPE 239
|
250
....*....|....*...
gi 494496814 243 DAQLYIAMGASILAKDEP 260
Cdd:cd24034 240 HAEYFEALGAALYALEEG 257
|
|
| DUF2229 |
pfam09989 |
CoA enzyme activase uncharacterized domain (DUF2229); Members of this family include various ... |
678-897 |
2.08e-101 |
|
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: 322.57 E-value: 2.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 678 VGLPRALNMYEDYPFWFTLFTKLGFKVTLSGRSSKKLYERGMTSIASETVCYPGKMVHGHIQSLIDKGVKTIFYPAVTHE 757
Cdd:pfam09989 1 IGIPRALNMYEYYPFWHTFFTELGFRVVLSPPSSKEIYEKGIETIPSETVCYPAKLAHGHVADLLKKGVDYIFYPCIVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 758 YREDKTSDNHYNCPVVISYSEIIKNNVpDLKKKNIKFINPFMTLNDKENLKDRLcqvfsyyFADLNISKSEIRDAVDAAK 837
Cdd:pfam09989 81 PREEDDADNHYNCPIVQGYPEVIKNNM-DEREEGIRFLSPFLDLDDGKLLAKQL-------FEELGISKKEIKRAVEKAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494496814 838 EEEFAFKADIRRAGEEAVEKIQKENLKGIVLAGRPYHL-DPEINHGMPELINSLDMAVLTE 897
Cdd:pfam09989 153 EAQEAFKEDLRKKGEEILEYLEENGKKGIVLAGRPYHIyDPEINHGIPELLASLGVAVLTE 213
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
1-259 |
5.25e-53 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 186.85 E-value: 5.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1 MKKIFnVGIDVGSTTVKIVVLDKD-KVIFKKYTRHFSDVKKAVKEVLTEVYEKLGDIRI---STVVTGSGGIDIskylGL 76
Cdd:COG1924 1 QGMIY-LGIDIGSTTTKAVLLDEDgEILASAYLPTGGDPLEAAKEALKELLEEAGLKREdiaGVVATGYGRVLI----GA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 77 KFVQEVISST----KAIETFNPETDVVIELGGEDAKITYLSGGI--DQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMA 150
Cdd:COG1924 76 AFADKVVTEItahaKGAHFLFPDVRTIIDIGGQDSKAIKLEDGVvvDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 151 KDYKVIYPIASRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLSCGRaIEGNVAFLGGPlyFLSE-LRTAFKN 229
Cdd:COG1924 156 LKAKNPVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVG-IGEPVVFQGGV--AKNDgVVRALEK 232
|
250 260 270
....*....|....*....|....*....|
gi 494496814 230 VLNlsdENIIFPQDAQLYIAMGASILAKDE 259
Cdd:COG1924 233 ELG---KEVIVPPIPQLMGALGAALLAREK 259
|
|
| CoA_E_activ |
TIGR00241 |
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ... |
321-574 |
7.03e-36 |
|
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: 137.23 E-value: 7.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 321 LGIDAGSTTTKAALIDENCNLVY--TYYSSNEGSPLQTSINIVKDIYNKLPKDVNIVsscVTGYGEALLKKALKIdygEI 398
Cdd:TIGR00241 3 LGIDSGSTTTKMVLMEDGKVIGYkwLDTTPVIEETARAILEALKEAGIGLEPIDKIV---ATGYGRHKVGFADKI---VT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 399 ETMAHYKAAKYFDPEVDFILDIGGQDMKCLQIKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQNPVD 478
Cdd:TIGR00241 77 EISCHGKGANYLAPEARGVIDIGGQDSKVIKIDDGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKADRKAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 479 LGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKN--ALFKVIKIRDlnelgkNIVVQGGTFYNDLVLRSFEKLIGRN 556
Cdd:TIGR00241 157 ISSMCTVFAESELISLLAAGVKKEDILAGVYESIAERvaEMLQRLKIEA------PIVFTGGVSKNKGLVKALEKKLGMK 230
|
250
....*....|....*...
gi 494496814 557 VTRPDISGIMGAFGAAII 574
Cdd:TIGR00241 231 VITPPEPQIVGAVGAALL 248
|
|
| CoA_E_activ |
TIGR00241 |
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ... |
7-255 |
2.50e-32 |
|
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: 126.83 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKDKVIFKKYTRhFSDVKKAVKEVLTEVYEKLGDIRIST---VVTGSGGIDISKylGLKFVQEVI 83
Cdd:TIGR00241 3 LGIDSGSTTTKMVLMEDGKVIGYKWLD-TTPVIEETARAILEALKEAGIGLEPIdkiVATGYGRHKVGF--ADKIVTEIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 84 SSTKAIETFNPETDVVIELGGEDAKITYLSGGI--DQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIYPIAS 161
Cdd:TIGR00241 80 CHGKGANYLAPEARGVIDIGGQDSKVIKIDDGKvdDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKADRKAKISS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 162 RCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLScGRAIEGNVAFLGGpLYFLSELRTAFKNVLNLsdeNIIFP 241
Cdd:TIGR00241 160 MCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQ-RLKIEAPIVFTGG-VSKNKGLVKALEKKLGM---KVITP 234
|
250
....*....|....
gi 494496814 242 QDAQLYIAMGASIL 255
Cdd:TIGR00241 235 PEPQIVGAVGAALL 248
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
321-574 |
5.07e-31 |
|
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: 123.62 E-value: 5.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 321 LGIDAGSTTTKAALIDENCNLVYTYYS---SNEGSPLQTSINIVKDIYNKL-------PKDVNIVSSCVTGYGEALLKKA 390
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGRAIAgsaNFESVGVEAAERNLKDAITEAleeaglkLDDIEYMFLGLTGYGRAGVDGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 391 LKIDYGEIETMAHYKAAKYFDPEV---DFILDIGGQDMKCLQIKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIE--- 464
Cdd:pfam01869 81 FGKDIVREEITVHADGAVALAPGTrgeDGVIDIGGTGSKVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARALGAVVReld 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 465 DFAKEGTFsqNPVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSViknALFKVIKIRDLNELGKNIVVQGGTFYNDL 544
Cdd:pfam01869 161 GLAPKTTL--NKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSI---ALRVAALAKRLGFVPDEVVLTGGVAKNAG 235
|
250 260 270
....*....|....*....|....*....|....*
gi 494496814 545 VLRSFEKLIGRNVTR-----PDISGIMGAFGAAII 574
Cdd:pfam01869 236 LVKALRDYLKENILGvkvnvHPDPQYAGAIGAALL 270
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
7-256 |
2.39e-17 |
|
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: 83.94 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKDKVIFKKY------------TRHFSDVKKAVKEVLTEVYEKLGDIR-ISTVVTGSGGIDISKY 73
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGRAiagsanfesvgvEAAERNLKDAITEALEEAGLKLDDIEyMFLGLTGYGRAGVDGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 74 LGLKFVQEVIS-STKAIETFNPET---DVVIELGGEDAKITYLSGGIDQR--MNGICAGGTGAFIDQMASLLKT---DAA 144
Cdd:pfam01869 81 FGKDIVREEITvHADGAVALAPGTrgeDGVIDIGGTGSKVIGLDGGKVVRfgGNGQCAGGEGSFLEIAARALGAvvrELD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 145 GLNEMAKDYKViyPIASRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLSCGRAIEGNVAFLGGpLYFLSELR 224
Cdd:pfam01869 161 GLAPKTTLNKG--AINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRLGFVPDEVVLTGG-VAKNAGLV 237
|
250 260 270
....*....|....*....|....*....|....
gi 494496814 225 TAFKNVL--NLSDENIIFPQDAQLYIAMGASILA 256
Cdd:pfam01869 238 KALRDYLkeNILGVKVNVHPDPQYAGAIGAALLA 271
|
|
| PRK13317 |
PRK13317 |
pantothenate kinase; Provisional |
1-257 |
2.53e-07 |
|
pantothenate kinase; Provisional
Pssm-ID: 237346 [Multi-domain] Cd Length: 277 Bit Score: 53.81 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1 MKKIfnVGIDVGSTTVKIVVLDKDKVIfkKYTRHFSDVKKAVKEVLTEVyEKLGDIRISTVvtGSGGIDISKYLGLK--F 78
Cdd:PRK13317 1 MEMK--IGIDAGGTLTKIVYLEEKKQR--TFKTEYSAEGKKVIDWLINL-QDIEKICLTGG--KAGYLQQLLNYGYPiaE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 79 VQEVISSTKAIETFNPET-----DVVIELGGEDAKITYLSGGIDQRMNGICAGGtgAFIDQMASLL--KTDAAGLNEMAK 151
Cdd:PRK13317 74 FVEFEATGLGVRYLLKEEghdlnDYIFTNIGTGTSIHYVDGNSQRRVGGTGIGG--GTIQGLSKLLtnISDYEQLIELAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 152 -------DYKV--IY-----PI-----ASRcgvFAKtdIQPLINDGARKSDIAMSIFNaVVVQTVSVLSCGRAIEGN--- 209
Cdd:PRK13317 152 hgdrnniDLKVgdIYkgplpPIpgdltASN---FGK--VLHHLDSEFTSSDILAGVIG-LVGEVITTLSIQAAREKNien 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 494496814 210 VAFLGGPLYFLSELRTAFKNVLNLSDENIIFPQDAQLYIAMGASILAK 257
Cdd:PRK13317 226 IVYIGSTLTNNPLLQEIIESYTKLRNCTPIFLENGGYSGAIGALLLAT 273
|
|
| PRK13317 |
PRK13317 |
pantothenate kinase; Provisional |
322-419 |
3.42e-04 |
|
pantothenate kinase; Provisional
Pssm-ID: 237346 [Multi-domain] Cd Length: 277 Bit Score: 44.18 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 322 GIDAGSTTTKAALIDENCNLVYTYYSSNEGsplqtsinivKDIYNKLPKDVNIVSSCVTGYGEALLKKALKIDYGEIET- 400
Cdd:PRK13317 6 GIDAGGTLTKIVYLEEKKQRTFKTEYSAEG----------KKVIDWLINLQDIEKICLTGGKAGYLQQLLNYGYPIAEFv 75
|
90 100
....*....|....*....|.
gi 494496814 401 --MAHYKAAKYFDPEVDFILD 419
Cdd:PRK13317 76 efEATGLGVRYLLKEEGHDLN 96
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG3581 |
COG3581 |
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function ... |
1019-1426 |
0e+00 |
|
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only];
Pssm-ID: 442800 Cd Length: 407 Bit Score: 566.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1019 PKRKLLVPQMSPIHFQFIEKAVNLSGWNVEVLQDTSREIIEEGLRYVNNDACYPAIIVIGQLISALKSGKYDLNNVSVGI 1098
Cdd:COG3581 2 KTMTILFPHMGPIHFRLLKAAFRGLGYEVEVLPPPDKETLELGLKYVNNDACYPLKIVLGQLIEALESGKYDPDATAIVM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1099 TQTGGGCRATNYIGFLRKAMYESGFKDVPVVSLSAQGIEDN-GLKenVSLSLINRGFMAVVYGDLFMKVLYRTRPYEKVK 1177
Cdd:COG3581 82 TGTGGPCRAGNYIELLRKALKDAGYPDVPVISLNPQGLEFNpGFK--LTLKLLKRAWKAIVYGDLLEKLLYRTRPYEKNK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1178 GSANALYEKWVKICMDSLENAKLSTFSKNIKNIIRDFDNLEL-LDIKKPRVGLVGEILVKFHPTANNNIVDVLEREGAEA 1256
Cdd:COG3581 160 GSADRLYEKWLEKLEEALESGSLKELKKLLKEIVKEFDAIPLdEDEKKPRVGIVGEIYVKLEPFANNNIEKFLEEEGAEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1257 VMPEMANFFLYSAVNGIYKKDhKLEGTTKGKFMCKFFIGLVSFYQKTYVKELKNSKRFNAPEKIIELSKKTESLVSVGNQ 1336
Cdd:COG3581 240 VRPPLSDWILYNLYNRKFKAK-ELGGSKKSRLKKKLAIKVLEKYRKPIKKALRKSLRFEPPPDIKELAEAAKPYLSLGNI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1337 TGEGWLLPGEMIELIESGVENIVCMQPFGCLPNhIIGKGPIKELKARYPKANIIPIDYDPSASEVNQINRIKLMLSRAFK 1416
Cdd:COG3581 319 GGEGWLLIGEMVELIKEGYDGIICLQPFGCMPN-IVAKGILKKLRRDYPEIPILTLDYDEGASEVNQLTRLEAFLDLAKR 397
|
410
....*....|
gi 494496814 1417 NLHDDEDNTS 1426
Cdd:COG3581 398 RREKKEEEAL 407
|
|
| COG3580 |
COG3580 |
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function ... |
661-1006 |
1.45e-161 |
|
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only];
Pssm-ID: 442799 Cd Length: 343 Bit Score: 489.73 E-value: 1.45e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 661 LFKhYKPLKLEDAPRGEVGLPRALNMYEDYPFWFTLFTKLGFKVTLSGRSSKKLYERGMtSIASETVCYPGKMVHGHIQS 740
Cdd:COG3580 1 LFD-YKPLPPEKAMRGTIGIPRALNYYEYYPFWKTFFTELGFEVVLSPPTNKEIYEKGI-EIASDEACYPAKLAHGHVAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 741 LIDKGVKTIFYPAVTHEYREDKTSDNHYNCPVVISYSEIIKNNVpDLKKKNIKFINPFMTLNDKENLKDRLCQVFSyyfA 820
Cdd:COG3580 79 LLDKGVDYIFYPRIVSEPKEDEGADNHYNCPKVQGYPEVIKANI-DEEEKGIPFISPFLNLDDKELLAKRLYEELG---K 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 821 DLNISKSEIRDAVDAAKEEEFAFKADIRRAGEEAVEKIQKENLKGIVLAGRPYHL-DPEINHGMPELINSLDMAVLTEDS 899
Cdd:COG3580 155 GLGISKKEIKRAVEKAWEAQRAFRRDLRKKGEEILEELKENGEKGIVLLGRPYHIyDPEINHGIPELLRSLGVAVLTEDS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 900 ICHLAQVQ--RPLRVVDQWVYHSRLYKAAEFVKKYDNIELVQLNSFGCGLDAVTTEQVQEILAEKSKIYTVIKIDEGNNL 977
Cdd:COG3580 235 LPHLGEDLsaRPLRKNLQWTYHSRLLGAAKFVARHPNLDGIQLTSFGCGPDSVTTDLVEEILERSGKPYLLLKIDEHSNE 314
|
330 340
....*....|....*....|....*....
gi 494496814 978 GAAKIRLRSLKAAMAEREANHISVKNIKE 1006
Cdd:COG3580 315 GGVKTRLEAFLDALKERKKKEAKALEFTK 343
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
316-583 |
1.05e-128 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 399.09 E-value: 1.05e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 316 KGNCFLGIDAGSTTTKAALIDENCNLVYTYYSSNEGSPLQTSINIVKDIYNKLP-KDVNIVSSCVTGYGEALLKKALkID 394
Cdd:COG1924 1 QGMIYLGIDIGSTTTKAVLLDEDGEILASAYLPTGGDPLEAAKEALKELLEEAGlKREDIAGVVATGYGRVLIGAAF-AD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 395 YGEIETMAHYKAAKYFDPEVDFILDIGGQDMKCLQIKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQ 474
Cdd:COG1924 80 KVVTEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLEDGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELALKAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 475 NPVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKNALFKVIKIrdlnELGKNIVVQGGTFYNDLVLRSFEKLIG 554
Cdd:COG1924 160 NPVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRV----GIGEPVVFQGGVAKNDGVVRALEKELG 235
|
250 260
....*....|....*....|....*....
gi 494496814 555 RNVTRPDISGIMGAFGAAIICKERYSEGH 583
Cdd:COG1924 236 KEVIVPPIPQLMGALGAALLAREKVKKGK 264
|
|
| ASKHA_NBD_O66634-like_rpt2 |
cd24035 |
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ... |
320-579 |
1.53e-125 |
|
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: 390.36 E-value: 1.53e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 320 FLGIDAGSTTTKAALIDENCNLVYTYYSSNEGSPLQTSINIVKDIYNKLPKDVNIVSSCVTGYGEALLKKALKIDYGEIE 399
Cdd:cd24035 1 YLGIDVGSTTTKAVLIDEDGEILASVYLRTKGNPIEAVKKGLKELREQLPEKVVIVGVGTTGSGRELLKDALGADVVKVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 400 TMAHYKAAKYFDPEVDFILDIGGQDMKCLQIKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQNPVDL 479
Cdd:cd24035 81 ITAHATAALHFDPDVDTIFEIGGQDSKYISLKNGVVKDFAMNEACSAGTGSFLEEQAKSLGIPIEEFAELALKAKNPPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 480 GSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKNALFKVIKIRDlneLGKNIVVQGGTFYNDLVLRSFEKLIGRNVTR 559
Cdd:cd24035 161 GSRCTVFMESDIKQAQQEGASKEDISAGLAYSVVKNYLNKVVGGRN---LGKKIVFQGGTFLNKAVLAAFEQVTGKEIIV 237
|
250 260
....*....|....*....|
gi 494496814 560 PDISGIMGAFGAAIICKERY 579
Cdd:cd24035 238 PPHPGLMGAYGAALLAKEEI 257
|
|
| ASKHA_NBD_O66634-like_rpt1 |
cd24034 |
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ... |
7-260 |
1.57e-103 |
|
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: 330.32 E-value: 1.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLD-KDKVIFKKYTRHFSDVKKAVKEVLTEVYEKLGDIRISTVVTGSGGIDISKYLGLKFVQEVISS 85
Cdd:cd24034 2 LGIDIGSTTVKAVVLDeKGNIVFSDYERHFGNPREALLELLEEIKERLGDEIARIAVTGSGGRGLAELLGLPFVQEVVAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 86 TKAIETFNPETDVVIELGGEDAKITYLSGG---IDQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIYPIASR 162
Cdd:cd24034 82 EAAVKHLHPDARTVIEIGGEDFKLIELDGDgklKDFRMNSKCAAGTGAFIDQQARRLGLSLEELAELALKAEPPAPIAGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 163 CGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLSCGRAIEGNVAFLGGPLYFLSELRTAFKNVLNlsDENIIFPQ 242
Cdd:cd24034 162 CSVFAKSDMIHLQNKGVPKEDIAAGLCRAVARNVIATLAKGREIEGPVILVGGVATNNAVLREAFEELLG--DEELIVPE 239
|
250
....*....|....*...
gi 494496814 243 DAQLYIAMGASILAKDEP 260
Cdd:cd24034 240 HAEYFEALGAALYALEEG 257
|
|
| DUF2229 |
pfam09989 |
CoA enzyme activase uncharacterized domain (DUF2229); Members of this family include various ... |
678-897 |
2.08e-101 |
|
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: 322.57 E-value: 2.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 678 VGLPRALNMYEDYPFWFTLFTKLGFKVTLSGRSSKKLYERGMTSIASETVCYPGKMVHGHIQSLIDKGVKTIFYPAVTHE 757
Cdd:pfam09989 1 IGIPRALNMYEYYPFWHTFFTELGFRVVLSPPSSKEIYEKGIETIPSETVCYPAKLAHGHVADLLKKGVDYIFYPCIVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 758 YREDKTSDNHYNCPVVISYSEIIKNNVpDLKKKNIKFINPFMTLNDKENLKDRLcqvfsyyFADLNISKSEIRDAVDAAK 837
Cdd:pfam09989 81 PREEDDADNHYNCPIVQGYPEVIKNNM-DEREEGIRFLSPFLDLDDGKLLAKQL-------FEELGISKKEIKRAVEKAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494496814 838 EEEFAFKADIRRAGEEAVEKIQKENLKGIVLAGRPYHL-DPEINHGMPELINSLDMAVLTE 897
Cdd:pfam09989 153 EAQEAFKEDLRKKGEEILEYLEENGKKGIVLAGRPYHIyDPEINHGIPELLASLGVAVLTE 213
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
1-259 |
5.25e-53 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 186.85 E-value: 5.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1 MKKIFnVGIDVGSTTVKIVVLDKD-KVIFKKYTRHFSDVKKAVKEVLTEVYEKLGDIRI---STVVTGSGGIDIskylGL 76
Cdd:COG1924 1 QGMIY-LGIDIGSTTTKAVLLDEDgEILASAYLPTGGDPLEAAKEALKELLEEAGLKREdiaGVVATGYGRVLI----GA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 77 KFVQEVISST----KAIETFNPETDVVIELGGEDAKITYLSGGI--DQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMA 150
Cdd:COG1924 76 AFADKVVTEItahaKGAHFLFPDVRTIIDIGGQDSKAIKLEDGVvvDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 151 KDYKVIYPIASRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLSCGRaIEGNVAFLGGPlyFLSE-LRTAFKN 229
Cdd:COG1924 156 LKAKNPVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVG-IGEPVVFQGGV--AKNDgVVRALEK 232
|
250 260 270
....*....|....*....|....*....|
gi 494496814 230 VLNlsdENIIFPQDAQLYIAMGASILAKDE 259
Cdd:COG1924 233 ELG---KEVIVPPIPQLMGALGAALLAREK 259
|
|
| ASKHA_NBD_O66634-like_rpt1 |
cd24034 |
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ... |
320-580 |
5.48e-53 |
|
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: 186.64 E-value: 5.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 320 FLGIDAGSTTTKAALIDENCNLVYTYYSSNEGSPLQTSINIVKDIYNKLPKDvnIVSSCVTGYGEALLKKALKIDYgEIE 399
Cdd:cd24034 1 YLGIDIGSTTVKAVVLDEKGNIVFSDYERHFGNPREALLELLEEIKERLGDE--IARIAVTGSGGRGLAELLGLPF-VQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 400 TMAHYKAAKYFDPEVDFILDIGGQDMKCLQIK-NGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQNPVD 478
Cdd:cd24034 78 VVAIEAAVKHLHPDARTVIEIGGEDFKLIELDgDGKLKDFRMNSKCAAGTGAFIDQQARRLGLSLEELAELALKAEPPAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 479 LGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKNALFKVIKIRDLNelgKNIVVQGGTFY-NDLVLRSFEKLIGR-N 556
Cdd:cd24034 158 IAGRCSVFAKSDMIHLQNKGVPKEDIAAGLCRAVARNVIATLAKGREIE---GPVILVGGVATnNAVLREAFEELLGDeE 234
|
250 260
....*....|....*....|....
gi 494496814 557 VTRPDISGIMGAFGAAIICKERYS 580
Cdd:cd24034 235 LIVPEHAEYFEALGAALYALEEGS 258
|
|
| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
320-574 |
1.81e-48 |
|
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: 173.49 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 320 FLGIDAGSTTTKAALIDENCNLVYTYYSSNEGSPLQTSINIVKDIYNKLPKDVNIVSSCV-TGYGEALLKKALKIDYgei 398
Cdd:cd24036 1 FAGIDVGSTTTKAVILDDKGKILGKAVIRTGTDPEKTAERALEEALEEAGLSREDIEYIVaTGYGRNSVPFADKTIT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 399 ETMAHYKAAKYFDPEVDFILDIGGQDMKCLQI-KNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQNPV 477
Cdd:cd24036 78 EITCHARGAHFLFPEARTVIDIGGQDSKVIRLdEDGKVLDFAMNDKCAAGTGRFLEVMARRLEVSLEELGELALKSTNPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 478 DLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKnalfKVIKIRDLNELGKNIVVQGGTFYNDLVLRSFEKLIGRNV 557
Cdd:cd24036 158 EISSTCTVFAESEVISLIAEGVPKEDIIAGIHNSIAK----RVAALAKRVGVEDPVVLTGGVAKNPGVVKALEEKLGVEV 233
|
250
....*....|....*..
gi 494496814 558 TRPDISGIMGAFGAAII 574
Cdd:cd24036 234 IVPPNPQLVGALGAALL 250
|
|
| ASKHA_NBD_BcrAD_BadFG-like |
cd24002 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ... |
7-255 |
9.35e-45 |
|
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: 162.99 E-value: 9.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKDK-VIFKKYTRH---FSDVKKAVKEVLTEVYEKLG--DIRISTVVTGSGGIDISKYLGLKFVQ 80
Cdd:cd24002 2 LGLDIGSTTSKAVLLDEGKnIVATEYERSgtgTSGPIEAVKKTLEKFLLEKGvkEEDIACTGVTGYGRVELFIDGDKQIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 81 EVISSTKAIETFNPETDVVIELGGEDAK-ITYLSGGI--DQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIY 157
Cdd:cd24002 82 EVSAHARGANHIYPDARTIIDVGGQDAKvIILDENGQmkNFKMNDKCAAGTGAFLDSMANKLNVKVEELADVKMNSKKEV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 158 PIASRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLSCGRAIEGNVAFLGGPLYFLSeLRTAFKNVLNlsdEN 237
Cdd:cd24002 162 SVSSTCAVFAETDINSFQSRGAPKEDIIAGLHKAVALRVMSLVGRLGVPKKDVVLQGGVARNSA-VVRALEEIIN---NE 237
|
250
....*....|....*...
gi 494496814 238 IIFPQDAQLYIAMGASIL 255
Cdd:cd24002 238 IIVPEIAQVMGALGAALL 255
|
|
| ASKHA_NBD_O66634-like_rpt2 |
cd24035 |
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ... |
7-259 |
3.68e-44 |
|
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: 161.16 E-value: 3.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKD-KVIFKKYTRHFSDVKKAVKEVLTEVYEKLGD--IRISTVVTGSGGIDISKYLGLKFVQ-EV 82
Cdd:cd24035 2 LGIDVGSTTTKAVLIDEDgEILASVYLRTKGNPIEAVKKGLKELREQLPEkvVIVGVGTTGSGRELLKDALGADVVKvEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 83 ISSTKAIETFNPETDVVIELGGEDAKITYLSGGI--DQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIYPIA 160
Cdd:cd24035 82 TAHATAALHFDPDVDTIFEIGGQDSKYISLKNGVvkDFAMNEACSAGTGSFLEEQAKSLGIPIEEFAELALKAKNPPDLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 161 SRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLSCGRAIEGNVAFLGGPLYFLSELRtAFKNVLNlsdENIIF 240
Cdd:cd24035 162 SRCTVFMESDIKQAQQEGASKEDISAGLAYSVVKNYLNKVVGGRNLGKKIVFQGGTFLNKAVLA-AFEQVTG---KEIIV 237
|
250
....*....|....*....
gi 494496814 241 PQDAQLYIAMGASILAKDE 259
Cdd:cd24035 238 PPHPGLMGAYGAALLAKEE 256
|
|
| ASKHA_NBD_BcrAD_BadFG-like |
cd24002 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ... |
320-574 |
1.93e-42 |
|
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: 156.44 E-value: 1.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 320 FLGIDAGSTTTKAALIDENCNLVYTYYSSNEG---SPLQTSINIVKDIYNKLP-KDVNIVSSCVTGYGEALLkkALKIDY 395
Cdd:cd24002 1 TLGLDIGSTTSKAVLLDEGKNIVATEYERSGTgtsGPIEAVKKTLEKFLLEKGvKEEDIACTGVTGYGRVEL--FIDGDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 396 GEIETMAHYKAAKYFDPEVDFILDIGGQDMKCLQ-IKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQ 474
Cdd:cd24002 79 QISEVSAHARGANHIYPDARTIIDVGGQDAKVIIlDENGQMKNFKMNDKCAAGTGAFLDSMANKLNVKVEELADVKMNSK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 475 NPVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKNALFKVikiRDLNELGKNIVVQGGTFYNDLVLRSFEKLIG 554
Cdd:cd24002 159 KEVSVSSTCAVFAETDINSFQSRGAPKEDIIAGLHKAVALRVMSLV---GRLGVPKKDVVLQGGVARNSAVVRALEEIIN 235
|
250 260
....*....|....*....|
gi 494496814 555 RNVTRPDISGIMGAFGAAII 574
Cdd:cd24002 236 NEIIVPEIAQVMGALGAALL 255
|
|
| ASKHA_NBD_YjiL-like |
cd24109 |
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ... |
320-574 |
5.91e-41 |
|
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: 151.58 E-value: 5.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 320 FLGIDAGSTTTKAALIDENCnLVYTYYSSNEGSPLQTSINIVKDIYNKL-PKDVNIVSscvTGYGEALLKKALKIdYGEI 398
Cdd:cd24109 1 YIGIDIGSRATKIALFEDDK-ILEKFVIPTGWFYKEYGRRIIKELLEDInYEDDKIVA---TGYGRNNLDFADKT-ITEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 399 EtmAHYKAAKYFDPEVDFILDIGGQDMKCLQIKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEgTFSQNPVD 478
Cdd:cd24109 76 T--AHAKGARYLTGKDFTVIDIGGQDTKVIKVENGKVIDFIMNDKCAAGTGRFLENMANILGISLEEISKY-AEDPEPLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 479 LGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKnalfKVIKIrdLNELGKN-IVVQGGTFYNDLVLRSFEKLIGRNV 557
Cdd:cd24109 153 ISSTCAVFAESEVISLIAEGVSRERIAAGVNYSIAK----RVAPL--LNRLKSPpIVLTGGVARNKAIIELLEKRLGAEV 226
|
250
....*....|....*..
gi 494496814 558 TRPDISGIMGAFGAAII 574
Cdd:cd24109 227 IVPELPQFAGAIGAALI 243
|
|
| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
7-255 |
5.31e-38 |
|
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: 143.06 E-value: 5.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLD-KDKVIFKKYTRHFSDVKKAVKEVLTEVYEKLGDIR--ISTVV-TGSGGIDISkylglkFVQEV 82
Cdd:cd24036 2 AGIDVGSTTTKAVILDdKGKILGKAVIRTGTDPEKTAERALEEALEEAGLSRedIEYIVaTGYGRNSVP------FADKT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 83 ISST----KAIETFNPETDVVIELGGEDAKITYLSGG---IDQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKV 155
Cdd:cd24036 76 ITEItchaRGAHFLFPEARTVIDIGGQDSKVIRLDEDgkvLDFAMNDKCAAGTGRFLEVMARRLEVSLEELGELALKSTN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 156 IYPIASRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQtVSVLSCGRAIEGNVAFLGGPLYFlSELRTAFKNVLNLsd 235
Cdd:cd24036 156 PVEISSTCTVFAESEVISLIAEGVPKEDIIAGIHNSIAKR-VAALAKRVGVEDPVVLTGGVAKN-PGVVKALEEKLGV-- 231
|
250 260
....*....|....*....|
gi 494496814 236 eNIIFPQDAQLYIAMGASIL 255
Cdd:cd24036 232 -EVIVPPNPQLVGALGAALL 250
|
|
| CoA_E_activ |
TIGR00241 |
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ... |
321-574 |
7.03e-36 |
|
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: 137.23 E-value: 7.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 321 LGIDAGSTTTKAALIDENCNLVY--TYYSSNEGSPLQTSINIVKDIYNKLPKDVNIVsscVTGYGEALLKKALKIdygEI 398
Cdd:TIGR00241 3 LGIDSGSTTTKMVLMEDGKVIGYkwLDTTPVIEETARAILEALKEAGIGLEPIDKIV---ATGYGRHKVGFADKI---VT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 399 ETMAHYKAAKYFDPEVDFILDIGGQDMKCLQIKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQNPVD 478
Cdd:TIGR00241 77 EISCHGKGANYLAPEARGVIDIGGQDSKVIKIDDGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKADRKAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 479 LGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKN--ALFKVIKIRDlnelgkNIVVQGGTFYNDLVLRSFEKLIGRN 556
Cdd:TIGR00241 157 ISSMCTVFAESELISLLAAGVKKEDILAGVYESIAERvaEMLQRLKIEA------PIVFTGGVSKNKGLVKALEKKLGMK 230
|
250
....*....|....*...
gi 494496814 557 VTRPDISGIMGAFGAAII 574
Cdd:TIGR00241 231 VITPPEPQIVGAVGAALL 248
|
|
| ASKHA_NBD_HgdC_HadI-like |
cd24103 |
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ... |
321-580 |
4.52e-35 |
|
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: 134.85 E-value: 4.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 321 LGIDAGSTTTKAALIDENCNLVYT-YYSSNEGSplQTSINIVKDIYNKL---PKDVNIVssCVTGYGEALLKKALKidyg 396
Cdd:cd24103 2 MGIDIGSTASKCVILKDGKEIVAQsVISVGTGT--SGPARALEEVLEKAglaKEDIAYT--VATGYGRNSFEGADK---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 397 EI-ETMAHYKAAKYFDPEVDFILDIGGQDMKCLQI-KNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQ 474
Cdd:cd24103 74 QIsELSCHARGVNFLLPEVRTIIDIGGQDVKVLKLdDNGRLLNFVMNDKCAAGTGRFLDVMARVLEVKVSELGELDAQST 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 475 NPVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKNA--LFKVIKIRdlnelgKNIVVQGGTFYNDLVLRSFEKL 552
Cdd:cd24103 154 NPVSISSTCTVFAESEVISQLSEGAKIPDIIAGIHTSVASRVagLAKRVGIE------KDVVMTGGVAQNSGVVRAMEEE 227
|
250 260
....*....|....*....|....*...
gi 494496814 553 IGRNVTRPDISGIMGAFGAAIICKERYS 580
Cdd:cd24103 228 LGTEIIVSPNPQLTGALGAALYAYEKAK 255
|
|
| ASKHA_NBD_benz_CoA_BzdP |
cd24107 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar ... |
7-256 |
8.22e-34 |
|
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: 131.13 E-value: 8.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKDKVIFKKYTRHFSDVKKAVKEVLTEVYEKLG----DIRiSTVVTGSGGIDISKylGLKFVQEV 82
Cdd:cd24107 2 AGIDVGSKFTKAVILEDGEILAKAIVPTGFDVAKAAERALDEALAAAGisrdDVK-KIVATGAGRKLVSF--ADDTVTEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 83 ISSTKAIETFNPETDVVIELGGEDAKITYLSGG---IDQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIYPI 159
Cdd:cd24107 79 VCAAKGAYFLFPSARTVIDVGAEEGRAIKLDENgkvVDFAQNDKCAAGAGAFLEAMSRALEVPLEELGELSLKSTKKIPM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 160 ASRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLScGRAIEGNVAFLGGPLYFLSeLRTAFKNVLNlsdENII 239
Cdd:cd24107 159 NAQCAVFAESEVVSLIHAGTPKEDIAAAVHDAIASRIASMVR-RVGIEDDVALIGGVAKNPG-FVESLKELLG---KEVL 233
|
250
....*....|....*..
gi 494496814 240 FPQDAQLYIAMGASILA 256
Cdd:cd24107 234 VPEDPEYVGALGAALIA 250
|
|
| ASKHA_NBD_benz_CoA_BcrA_BadF |
cd24104 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ... |
320-577 |
3.52e-33 |
|
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: 129.34 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 320 FLGIDAGSTTTKAALIDENCNLVytyyssneGSPL-QTSINIVK---DIYNKLPKDVNIVSSCV-----TGYGEAllkka 390
Cdd:cd24104 1 AAGVDVGSTQTKAVIIDEDGEIV--------GRGLtNTGANVVVaaeRAFREAIEEAGIKEEEVeyvvgTGYGRY----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 391 lKIDYGEI---ETMAHYKAAKYFDPEVDFILDIGGQDMKCLQI-KNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDF 466
Cdd:cd24104 68 -KVTFGNAqrtEISCHARGAHHMFPNTRTVLDIGGQDTKAIRVdETGEVVDFVMNDKCAAGTGRFLGYAADALGIPLDEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 467 AKEGTFSQNPVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKNALFKVIKIRDLNELgkniVVQGGTFYNDLVL 546
Cdd:cd24104 147 GPLALKSTKPVRISSTCTVFAESEIRSWLALGKKREDILGGVHRAIAARAVSLIRRVGIEPEF----TFTGGVARNEAMV 222
|
250 260 270
....*....|....*....|....*....|.
gi 494496814 547 RSFEKLIGRNVTRPDISGIMGAFGAAIICKE 577
Cdd:cd24104 223 KALEELLGVKINVSPDSHFMGALGAALFALE 253
|
|
| CoA_E_activ |
TIGR00241 |
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ... |
7-255 |
2.50e-32 |
|
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: 126.83 E-value: 2.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKDKVIFKKYTRhFSDVKKAVKEVLTEVYEKLGDIRIST---VVTGSGGIDISKylGLKFVQEVI 83
Cdd:TIGR00241 3 LGIDSGSTTTKMVLMEDGKVIGYKWLD-TTPVIEETARAILEALKEAGIGLEPIdkiVATGYGRHKVGF--ADKIVTEIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 84 SSTKAIETFNPETDVVIELGGEDAKITYLSGGI--DQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIYPIAS 161
Cdd:TIGR00241 80 CHGKGANYLAPEARGVIDIGGQDSKVIKIDDGKvdDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEKADRKAKISS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 162 RCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLScGRAIEGNVAFLGGpLYFLSELRTAFKNVLNLsdeNIIFP 241
Cdd:TIGR00241 160 MCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQ-RLKIEAPIVFTGG-VSKNKGLVKALEKKLGM---KVITP 234
|
250
....*....|....
gi 494496814 242 QDAQLYIAMGASIL 255
Cdd:TIGR00241 235 PEPQIVGAVGAALL 248
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
321-574 |
5.07e-31 |
|
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: 123.62 E-value: 5.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 321 LGIDAGSTTTKAALIDENCNLVYTYYS---SNEGSPLQTSINIVKDIYNKL-------PKDVNIVSSCVTGYGEALLKKA 390
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGRAIAgsaNFESVGVEAAERNLKDAITEAleeaglkLDDIEYMFLGLTGYGRAGVDGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 391 LKIDYGEIETMAHYKAAKYFDPEV---DFILDIGGQDMKCLQIKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIE--- 464
Cdd:pfam01869 81 FGKDIVREEITVHADGAVALAPGTrgeDGVIDIGGTGSKVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARALGAVVReld 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 465 DFAKEGTFsqNPVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSViknALFKVIKIRDLNELGKNIVVQGGTFYNDL 544
Cdd:pfam01869 161 GLAPKTTL--NKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSI---ALRVAALAKRLGFVPDEVVLTGGVAKNAG 235
|
250 260 270
....*....|....*....|....*....|....*
gi 494496814 545 VLRSFEKLIGRNVTR-----PDISGIMGAFGAAII 574
Cdd:pfam01869 236 LVKALRDYLKENILGvkvnvHPDPQYAGAIGAALL 270
|
|
| ASKHA_NBD_benz_CoA_BzdP |
cd24107 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar ... |
320-574 |
8.58e-29 |
|
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: 116.49 E-value: 8.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 320 FLGIDAGSTTTKAALIDENcnLVYTYYSSNEGSPLQTSINIVkdiYNKLPKDVNIVSS-----CVTGYGEALLKKAlkiD 394
Cdd:cd24107 1 TAGIDVGSKFTKAVILEDG--EILAKAIVPTGFDVAKAAERA---LDEALAAAGISRDdvkkiVATGAGRKLVSFA---D 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 395 YGEIETMAHYKAAKYFDPEVDFILDIGGQDMKCLQI-KNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFS 473
Cdd:cd24107 73 DTVTEVVCAAKGAYFLFPSARTVIDVGAEEGRAIKLdENGKVVDFAQNDKCAAGAGAFLEAMSRALEVPLEELGELSLKS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 474 QNPVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIK--NALFKVIKIRDlnelgkNIVVQGGTFYNDLVLRSFEK 551
Cdd:cd24107 153 TKKIPMNAQCAVFAESEVVSLIHAGTPKEDIAAAVHDAIASriASMVRRVGIED------DVALIGGVAKNPGFVESLKE 226
|
250 260
....*....|....*....|...
gi 494496814 552 LIGRNVTRPDISGIMGAFGAAII 574
Cdd:cd24107 227 LLGKEVLVPEDPEYVGALGAALI 249
|
|
| ASKHA_NBD_YjiL-like |
cd24109 |
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ... |
7-255 |
2.49e-28 |
|
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: 114.98 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKDKVIFKKYTRHFSDVKKAVKEVLTEVYEKLGDIRISTVVTGSGGIDISKylGLKFVQEVISST 86
Cdd:cd24109 2 IGIDIGSRATKIALFEDDKILEKFVIPTGWFYKEYGRRIIKELLEDINYEDDKIVATGYGRNNLDF--ADKTITEITAHA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 87 KAIETFNPETDVVIELGGEDAKITYLSGG--IDQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIyPIASRCG 164
Cdd:cd24109 80 KGARYLTGKDFTVIDIGGQDTKVIKVENGkvIDFIMNDKCAAGTGRFLENMANILGISLEEISKYAEDPEPL-SISSTCA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 165 VFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLScgrAIEGNVAFLGGPLYFLSELRTAFKNVLNLsdeNIIFPQDA 244
Cdd:cd24109 159 VFAESEVISLIAEGVSRERIAAGVNYSIAKRVAPLLN---RLKSPPIVLTGGVARNKAIIELLEKRLGA---EVIVPELP 232
|
250
....*....|.
gi 494496814 245 QLYIAMGASIL 255
Cdd:cd24109 233 QFAGAIGAALI 243
|
|
| ASKHA_NBD_HgdC_HadI-like |
cd24103 |
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ... |
7-259 |
3.22e-25 |
|
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: 106.34 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKDKVIFKKYTRHF----SDVKKAVKEVLTEVYEKLGDIRiSTVVTGSGGIDISKylGLKFVQEV 82
Cdd:cd24103 2 MGIDIGSTASKCVILKDGKEIVAQSVISVgtgtSGPARALEEVLEKAGLAKEDIA-YTVATGYGRNSFEG--ADKQISEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 83 ISSTKAIETFNPETDVVIELGGEDAKITYL--SGGIDQ-RMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIYPI 159
Cdd:cd24103 79 SCHARGVNFLLPEVRTIIDIGGQDVKVLKLddNGRLLNfVMNDKCAAGTGRFLDVMARVLEVKVSELGELDAQSTNPVSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 160 ASRCGVFAKTDIQPLINDGARKSDIAMSIFNAvVVQTVSVLSCGRAIEGNVAFLGGpLYFLSELRTAFKNVLNLSdenII 239
Cdd:cd24103 159 SSTCTVFAESEVISQLSEGAKIPDIIAGIHTS-VASRVAGLAKRVGIEKDVVMTGG-VAQNSGVVRAMEEELGTE---II 233
|
250 260
....*....|....*....|
gi 494496814 240 FPQDAQLYIAMGASILAKDE 259
Cdd:cd24103 234 VSPNPQLTGALGAALYAYEK 253
|
|
| ASKHA_NBD_benz_CoA_BcrD_BadG |
cd24105 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ... |
321-573 |
1.77e-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: 98.43 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 321 LGIDAGSTTTKAALIDENCNLVYTYYSSNEGSPLQTSINIVKDIYNKL---PKDVNIVSScvTGYGEALLKKAlkidYGE 397
Cdd:cd24105 2 AGIDVGSGYTKAVIMDDGEKILAKRVERTRQRDEEVAREAYNEALEEAglkRDDIAYVAT--TGEGRYVVFFR----DGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 398 IETM-AHYKAAKYFDPEVDFILDIGGQDMKCLQI-KNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAKEGTFSQN 475
Cdd:cd24105 76 FTDLtTHARGAIFLFPGTRTVLDIGAQHTRAIRIdEKGKVLSFRMNDKCAAGSGQFLENIARYLGVALDEIGDLSLQADN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 476 PVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKNA--LFKVIKIRDLnelgknIVVQGGTFYNDLVLRSFEKLI 553
Cdd:cd24105 156 PEPISGVCAVLAETEVINMVSRGIPVPDILRGIHLSLAGRSvqLLKRVGAEPE------VTLTGGLARNEGMVEALEELL 229
|
250 260
....*....|....*....|..
gi 494496814 554 GR--NVTRPDISGIMGAFGAAI 573
Cdd:cd24105 230 GAkvNVAEHDDSIYAGALGAAL 251
|
|
| ASKHA_NBD_MJ0800-like |
cd24108 |
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar ... |
8-256 |
5.39e-22 |
|
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: 97.14 E-value: 5.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 8 GIDVGSTTVKIVVLDKDKVIFKKY---TRHFSDVKKAVKEVLTEVYEKLGDIRiSTVVTGSGGIDISKYLGLKFVQEVIS 84
Cdd:cd24108 3 GIDSGSTTTKAVVMKDNEIIGTGWmptTDVIESAEKAFEEALEEAGIKLSDIE-AIGTTGYGRYTIGKHFNADLVQEELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 85 --STKAIETFNPETD--VVIELGGEDAKITYLSGGIDQR--MNGICAGGTGAFIDQMASLLKTDAAGLNEMA--KDYKVI 156
Cdd:cd24108 82 vnSKGAVYLADKQKGeaTVIDIGGMDNKAITVNDGIPDNftMGGICAGASGRFLEMTARRLGVDITELGELAlkGDWRKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 157 yPIASRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLSCGRAIEGNVAFLGGPlYFLSELRTAFKNVLNlsdE 236
Cdd:cd24108 162 -RMNSYCIVFGIQDLVTSLAEGARAEDVAAAACHSVAEQVYEQQLQEIDVREPVIQVGGT-SLIEGLVKALGEVLG---I 236
|
250 260
....*....|....*....|
gi 494496814 237 NIIFPQDAQLYIAMGASILA 256
Cdd:cd24108 237 EVIVPPYSQLIGAVGAALLA 256
|
|
| ASKHA_NBD_MJ0800-like |
cd24108 |
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar ... |
321-574 |
1.00e-21 |
|
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: 96.37 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 321 LGIDAGSTTTKAALIDENCNLvytyyssneGSPLQTSINIV---KDIYNKLPKDVNIVSS-----CVTGYGEALLKKALK 392
Cdd:cd24108 2 AGIDSGSTTTKAVVMKDNEII---------GTGWMPTTDVIesaEKAFEEALEEAGIKLSdieaiGTTGYGRYTIGKHFN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 393 IDYGEIETMAHYKAAKYFDPEVD---FILDIGGQDMKCLQIKNGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFAK- 468
Cdd:cd24108 73 ADLVQEELTVNSKGAVYLADKQKgeaTVIDIGGMDNKAITVNDGIPDNFTMGGICAGASGRFLEMTARRLGVDITELGEl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 469 --EGTfsQNPVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIKNAL---FKVIKIRDlnelgkNIVVQGGTFYND 543
Cdd:cd24108 153 alKGD--WRKIRMNSYCIVFGIQDLVTSLAEGARAEDVAAAACHSVAEQVYeqqLQEIDVRE------PVIQVGGTSLIE 224
|
250 260 270
....*....|....*....|....*....|.
gi 494496814 544 LVLRSFEKLIGRNVTRPDISGIMGAFGAAII 574
Cdd:cd24108 225 GLVKALGEVLGIEVIVPPYSQLIGAVGAALL 255
|
|
| ASKHA_NBD_benz_CoA_BcrA_BadF |
cd24104 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ... |
7-258 |
2.36e-20 |
|
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: 92.36 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKDKVIFKK---YTRhfSDVKKAVKEVLTEVYEKLGDIRIS---TVVTGSGGIDISkyLGLKFVQ 80
Cdd:cd24104 2 AGVDVGSTQTKAVIIDEDGEIVGRgltNTG--ANVVVAAERAFREAIEEAGIKEEEveyVVGTGYGRYKVT--FGNAQRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 81 EVISSTKAIETFNPETDVVIELGGEDAK-ITYLSGGI--DQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIY 157
Cdd:cd24104 78 EISCHARGAHHMFPNTRTVLDIGGQDTKaIRVDETGEvvDFVMNDKCAAGTGRFLGYAADALGIPLDELGPLALKSTKPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 158 PIASRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLScgRA-IEGNVAFLGG---PLYFLSELRTAFKNVLNL 233
Cdd:cd24104 158 RISSTCTVFAESEIRSWLALGKKREDILGGVHRAIAARAVSLIR--RVgIEPEFTFTGGvarNEAMVKALEELLGVKINV 235
|
250 260
....*....|....*....|....*.
gi 494496814 234 SDENIifpqdaqlYI-AMGASILAKD 258
Cdd:cd24104 236 SPDSH--------FMgALGAALFALE 253
|
|
| ASKHA_NBD_benz_CoA_BzdQ |
cd24106 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and ... |
322-574 |
9.48e-19 |
|
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: 87.66 E-value: 9.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 322 GIDAGSTTTKAALIDENCNLVYTYYSSNEGSPlQTSINIVKDIYNKLPKDVNIVSSCV-TGYGEALLKKALKIdygeI-E 399
Cdd:cd24106 3 GIDVGSVSSQAVIMVDGELYAYSNMRTGSDSP-ESAQKALNAALEKTGLKLEDIHYIVgTGYGRVNVPFANKA----ItE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 400 TMAHYKAAKY-FDPEVDFILDIGGQDMKCLQIK-NGVIDSIILNEACSSGCGSFLETFAKSLSMSIEDFakeGTFS---- 473
Cdd:cd24106 78 IACHARGANYmYGPSVRTVLDMGGQDCKAIRCDeKGKVTNFLMNDKCAAGTGRGMEVFADLLQVPIEEI---GELSlevd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 474 QNPVDLGSRCTVFMNSRVKQAQKEGATVADISAGLSYSVIK--NALFKVIKIRdlnelgKNIVVQGGTFYNDLVLRSFEK 551
Cdd:cd24106 155 KEPPPVSSTCVVFAKSEALGLLREGWPKNDVLAAYCEAMAHrvVTLLERVGVE------KDFVITGGIAKNIGVVKRIEK 228
|
250 260
....*....|....*....|....*
gi 494496814 552 LIGRN--VTRPDiSGIMGAFGAAII 574
Cdd:cd24106 229 ELGIKalIPKED-PQIAGALGAALF 252
|
|
| ASKHA_NBD_benz_CoA_BcrD_BadG |
cd24105 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ... |
7-256 |
1.38e-18 |
|
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: 87.26 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLD-KDKVIFKKYTRHFSDVKKAVKEVLTEVYEKLGDIR--ISTVVTGSGGIDISKYLGLKFVqEVI 83
Cdd:cd24105 2 AGIDVGSGYTKAVIMDdGEKILAKRVERTRQRDEEVAREAYNEALEEAGLKRddIAYVATTGEGRYVVFFRDGHFT-DLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 84 SSTKAIETFNPETDVVIELGGEDAK-ITYLSGG--IDQRMNGICAGGTGAFIDQMASLLKTDAAGLNEMAKDYKVIYPIA 160
Cdd:cd24105 81 THARGAIFLFPGTRTVLDIGAQHTRaIRIDEKGkvLSFRMNDKCAAGSGQFLENIARYLGVALDEIGDLSLQADNPEPIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 161 SRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLScgRA-IEGNVAFLGGPLY---FLSELRTAFKNVLNLSDE 236
Cdd:cd24105 161 GVCAVLAETEVINMVSRGIPVPDILRGIHLSLAGRSVQLLK--RVgAEPEVTLTGGLARnegMVEALEELLGAKVNVAEH 238
|
250 260
....*....|....*....|
gi 494496814 237 NiifpqDAQLYIAMGASILA 256
Cdd:cd24105 239 D-----DSIYAGALGAALLG 253
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
7-256 |
2.39e-17 |
|
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: 83.94 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKDKVIFKKY------------TRHFSDVKKAVKEVLTEVYEKLGDIR-ISTVVTGSGGIDISKY 73
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGRAiagsanfesvgvEAAERNLKDAITEALEEAGLKLDDIEyMFLGLTGYGRAGVDGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 74 LGLKFVQEVIS-STKAIETFNPET---DVVIELGGEDAKITYLSGGIDQR--MNGICAGGTGAFIDQMASLLKT---DAA 144
Cdd:pfam01869 81 FGKDIVREEITvHADGAVALAPGTrgeDGVIDIGGTGSKVIGLDGGKVVRfgGNGQCAGGEGSFLEIAARALGAvvrELD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 145 GLNEMAKDYKViyPIASRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLSCGRAIEGNVAFLGGpLYFLSELR 224
Cdd:pfam01869 161 GLAPKTTLNKG--AINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRLGFVPDEVVLTGG-VAKNAGLV 237
|
250 260 270
....*....|....*....|....*....|....
gi 494496814 225 TAFKNVL--NLSDENIIFPQDAQLYIAMGASILA 256
Cdd:pfam01869 238 KALRDYLkeNILGVKVNVHPDPQYAGAIGAALLA 271
|
|
| ASKHA_NBD_benz_CoA_BzdQ |
cd24106 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and ... |
8-256 |
1.92e-16 |
|
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: 80.73 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 8 GIDVGSTTVKIVVLDKDKVIFKKYTRHFSD----VKKAVKEVLTEVYEKLGDIRIsTVVTGSGGIDISkylglkFVQEVI 83
Cdd:cd24106 3 GIDVGSVSSQAVIMVDGELYAYSNMRTGSDspesAQKALNAALEKTGLKLEDIHY-IVGTGYGRVNVP------FANKAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 84 SSTK-----AIETFNPETDVVIELGGEDAKITYlsggIDQR-------MNGICAGGTGAFIDQMASLLKTDAAGLNEMA- 150
Cdd:cd24106 76 TEIAchargANYMYGPSVRTVLDMGGQDCKAIR----CDEKgkvtnflMNDKCAAGTGRGMEVFADLLQVPIEEIGELSl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 151 KDYKVIYPIASRCGVFAKTDIQPLINDGARKSDIAMSIFNAVVVQTVSVLscGRA-IEGNVAFLGGplyflselrtAFKN 229
Cdd:cd24106 152 EVDKEPPPVSSTCVVFAKSEALGLLREGWPKNDVLAAYCEAMAHRVVTLL--ERVgVEKDFVITGG----------IAKN 219
|
250 260 270
....*....|....*....|....*....|....*.
gi 494496814 230 V---------LNLsdENIIFPQDAQLYIAMGASILA 256
Cdd:cd24106 220 IgvvkriekeLGI--KALIPKEDPQIAGALGAALFA 253
|
|
| ASKHA_NBD_PanK-II_bac |
cd24085 |
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ... |
7-252 |
7.02e-13 |
|
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: 70.29 E-value: 7.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 7 VGIDVGSTTVKIVVLDKDKVI-FKKY-TRHFSDVKKAVKEvltevyekLGDIRISTV-VTGSGGIDI-SKYLGLK--FVQ 80
Cdd:cd24085 2 IGIDAGGTLTKIVLLENNGELkFKAFdSLKIEALVKFLNE--------LGINDIEKIaVTGGGASRLpENIDGIPivKVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 81 EV---ISSTKAIETFNPETDVVIELGGEDAkITYLSGGIDQRmngicAGGT---GAFIDQMASLL--KTDAAGLNEMAK- 151
Cdd:cd24085 74 EFeaiGRGALYLLGEILDDALVVSIGTGTS-IVLAKNGTIRH-----VGGTgvgGGTLLGLGKLLlgVTDYDEITELARk 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 152 ------DYKV--IYP----------IASRcgvFAKTDiqplINDGARKSDIAMSIFNAV--VVQTVSVLSCGRAIEGNVA 211
Cdd:cd24085 148 gdrsnvDLTVgdIYGggigplppdlTASN---FGKLA----DDNKASREDLAAALINLVgeTIGTLAALAARAEGVKDIV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 494496814 212 FLGGPLYFlSELRTAFKNVLNLSDENIIFPQDAQLYIAMGA 252
Cdd:cd24085 221 LVGSTLRN-PLLKEVLERYTKLYGVKPIFPENGEFAGAIGA 260
|
|
| PRK13317 |
PRK13317 |
pantothenate kinase; Provisional |
1-257 |
2.53e-07 |
|
pantothenate kinase; Provisional
Pssm-ID: 237346 [Multi-domain] Cd Length: 277 Bit Score: 53.81 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 1 MKKIfnVGIDVGSTTVKIVVLDKDKVIfkKYTRHFSDVKKAVKEVLTEVyEKLGDIRISTVvtGSGGIDISKYLGLK--F 78
Cdd:PRK13317 1 MEMK--IGIDAGGTLTKIVYLEEKKQR--TFKTEYSAEGKKVIDWLINL-QDIEKICLTGG--KAGYLQQLLNYGYPiaE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 79 VQEVISSTKAIETFNPET-----DVVIELGGEDAKITYLSGGIDQRMNGICAGGtgAFIDQMASLL--KTDAAGLNEMAK 151
Cdd:PRK13317 74 FVEFEATGLGVRYLLKEEghdlnDYIFTNIGTGTSIHYVDGNSQRRVGGTGIGG--GTIQGLSKLLtnISDYEQLIELAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 152 -------DYKV--IY-----PI-----ASRcgvFAKtdIQPLINDGARKSDIAMSIFNaVVVQTVSVLSCGRAIEGN--- 209
Cdd:PRK13317 152 hgdrnniDLKVgdIYkgplpPIpgdltASN---FGK--VLHHLDSEFTSSDILAGVIG-LVGEVITTLSIQAAREKNien 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 494496814 210 VAFLGGPLYFLSELRTAFKNVLNLSDENIIFPQDAQLYIAMGASILAK 257
Cdd:PRK13317 226 IVYIGSTLTNNPLLQEIIESYTKLRNCTPIFLENGGYSGAIGALLLAT 273
|
|
| ASKHA_NBD_PanK-II_bac |
cd24085 |
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ... |
320-391 |
8.40e-05 |
|
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: 46.02 E-value: 8.40e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494496814 320 FLGIDAGSTTTKAALIDENCNLVYTYYSSNEGSplqtsiNIVKDIYNKlpKDVNIVSSCVTGYGEALLKKAL 391
Cdd:cd24085 1 KIGIDAGGTLTKIVLLENNGELKFKAFDSLKIE------ALVKFLNEL--GINDIEKIAVTGGGASRLPENI 64
|
|
| COG3580 |
COG3580 |
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function ... |
1044-1087 |
2.25e-04 |
|
Predicted nucleotide-binding protein, sugar kinase/HSP70/actin superfamily [General function prediction only];
Pssm-ID: 442799 Cd Length: 343 Bit Score: 45.21 E-value: 2.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 494496814 1044 GWNVEVLQDTSREIIEEGLRYVNNDACYPAIIVIGQLISALKSG 1087
Cdd:COG3580 40 GFEVVLSPPTNKEIYEKGIEIASDEACYPAKLAHGHVADLLDKG 83
|
|
| PRK13317 |
PRK13317 |
pantothenate kinase; Provisional |
322-419 |
3.42e-04 |
|
pantothenate kinase; Provisional
Pssm-ID: 237346 [Multi-domain] Cd Length: 277 Bit Score: 44.18 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 322 GIDAGSTTTKAALIDENCNLVYTYYSSNEGsplqtsinivKDIYNKLPKDVNIVSSCVTGYGEALLKKALKIDYGEIET- 400
Cdd:PRK13317 6 GIDAGGTLTKIVYLEEKKQRTFKTEYSAEG----------KKVIDWLINLQDIEKICLTGGKAGYLQQLLNYGYPIAEFv 75
|
90 100
....*....|....*....|.
gi 494496814 401 --MAHYKAAKYFDPEVDFILD 419
Cdd:PRK13317 76 efEATGLGVRYLLKEEGHDLN 96
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
319-387 |
1.22e-03 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 42.96 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494496814 319 CFLGIDAGSTTTKAALIDENCNLV------YTYYSSNEGSP-------LQTSINIVKDIYNKLPKDvNIVSSCVTGYGEA 385
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILasasreTPLIHPGPGWAeldpeelWEAVKEAIREAAAQAGPD-PIAAISVSSQGES 79
|
..
gi 494496814 386 LL 387
Cdd:cd07773 80 GV 81
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
319-350 |
4.99e-03 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY 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: 466787 [Multi-domain] Cd Length: 392 Bit Score: 41.01 E-value: 4.99e-03
10 20 30
....*....|....*....|....*....|..
gi 494496814 319 CFLGIDAGSTTTKAALIDENCNLVYTYYSSNE 350
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYP 32
|
|
| |
