NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490309354|ref|WP_004204155|]
View 

MULTISPECIES: putative 2-hydroxyacyl-CoA dehydratase activator YjiL [Klebsiella]

Protein Classification

acetate and sugar kinases/Hsc70/actin family protein( domain architecture ID 99298)

acetate and sugar kinases/Hsc70/actin (ASKHA) family protein catalyzes phosphoryl transfer from ATP to their respective substrates

CATH:  3.30.420.40
Gene Ontology:  GO:0000166
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 3-247 3.30e-116

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member TIGR00241:

Pssm-ID: 483947  Cd Length: 248  Bit Score: 332.91  E-value: 3.30e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354    3 YTVGIDSGSTATKGILLADG-VVTRRFLCPTPFRPAD--AIHEAWETLRAGLAETPFLTLTGYGRQLVDFANKQVTEISC 79
Cdd:TIGR00241   1 ISLGIDSGSTTTKMVLMEDGkVIGYKWLDTTPVIEETarAILEALKEAGIGLEPIDKIVATGYGRHKVGFADKIVTEISC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   80 HGLGARLLAPDTRTVIDIGGQDSKVIQLDaGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAITD-GVEPHAITS 158
Cdd:TIGR00241  81 HGKGANYLAPEARGVIDIGGQDSKVIKID-DGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEkADRKAKISS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGMAVTTHPDAQF 238
Cdd:TIGR00241 160 MCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFTGGVSKNKGLVKALEKKLGMKVITPPEPQI 239


                  ....*....
gi 490309354  239 AGAIGAALI 247
Cdd:TIGR00241 240 VGAVGAALL 248
 
Name Accession Description Interval E-value
CoA_E_activ TIGR00241
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
 3-247 3.30e-116

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: 332.91  E-value: 3.30e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354    3 YTVGIDSGSTATKGILLADG-VVTRRFLCPTPFRPAD--AIHEAWETLRAGLAETPFLTLTGYGRQLVDFANKQVTEISC 79
Cdd:TIGR00241   1 ISLGIDSGSTTTKMVLMEDGkVIGYKWLDTTPVIEETarAILEALKEAGIGLEPIDKIVATGYGRHKVGFADKIVTEISC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   80 HGLGARLLAPDTRTVIDIGGQDSKVIQLDaGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAITD-GVEPHAITS 158
Cdd:TIGR00241  81 HGKGANYLAPEARGVIDIGGQDSKVIKID-DGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEkADRKAKISS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGMAVTTHPDAQF 238
Cdd:TIGR00241 160 MCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFTGGVSKNKGLVKALEKKLGMKVITPPEPQI 239


                  ....*....
gi 490309354  239 AGAIGAALI 247
Cdd:TIGR00241 240 VGAVGAALL 248
ASKHA_NBD_YjiL-like cd24109
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ...
 5-247 4.68e-114

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: 327.23  E-value: 4.68e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   5 VGIDSGSTATKGILLADGVVTRRFLCPTPFRPADAIHEAWETLRAGLA-ETPFLTLTGYGRQLVDFANKQVTEISCHGLG 83
Cdd:cd24109    2 IGIDIGSRATKIALFEDDKILEKFVIPTGWFYKEYGRRIIKELLEDINyEDDKIVATGYGRNNLDFADKTITEITAHAKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  84 ARLLAPDTRTVIDIGGQDSKVIQLDaGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAITDGVEPHAITSMCTVF 163
Cdd:cd24109   82 ARYLTGKDFTVIDIGGQDTKVIKVE-NGKVIDFIMNDKCAAGTGRFLENMANILGISLEEISKYAEDPEPLSISSTCAVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 164 AESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQgPLLFTGGVSRCAAFARMLESHVGMAVTTHPDAQFAGAIG 243
Cdd:cd24109  161 AESEVISLIAEGVSRERIAAGVNYSIAKRVAPLLNRLKSP-PIVLTGGVARNKAIIELLEKRLGAEVIVPELPQFAGAIG 239


                 ....
gi 490309354 244 AALI 247
Cdd:cd24109  240 AALI 243
YjiL COG1924
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ...
 1-255 1.44e-106

Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];


Pssm-ID: 441527 [Multi-domain]  Cd Length: 264  Bit Score: 308.96  E-value: 1.44e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   1 MIYTVGIDSGSTATKGILL-ADGVVTRRFLCPTPFRPADAIHEAWETL--RAGLAETP--FLTLTGYGRQLVD--FANKQ 73
Cdd:COG1924    2 GMIYLGIDIGSTTTKAVLLdEDGEILASAYLPTGGDPLEAAKEALKELleEAGLKREDiaGVVATGYGRVLIGaaFADKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  74 VTEISCHGLGARLLAPDTRTVIDIGGQDSKVIQLDaGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAIT-DGVE 152
Cdd:COG1924   82 VTEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLE-DGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELAlKAKN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 153 PHAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGMAVTT 232
Cdd:COG1924  161 PVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVGIGEPVVFQGGVAKNDGVVRALEKELGKEVIV 240

                        250       260
                 ....*....|....*....|...
gi 490309354 233 HPDAQFAGAIGAALIGQRQRRRG 255
Cdd:COG1924  241 PPIPQLMGALGAALLAREKVKKG 263
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
 5-248 2.74e-70

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: 216.84  E-value: 2.74e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354    5 VGIDSGSTATKGILLADG--VVTRRFLCPTPFRPA----------DAIHEAWETLRAGLA--ETPFLTLTGYGRQLVD-- 68
Cdd:pfam01869   1 LGIDGGSTKTKAVLMDDDgeVLGRAIAGSANFESVgveaaernlkDAITEALEEAGLKLDdiEYMFLGLTGYGRAGVDgh 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   69 FANKQVT-EISCHGLGARLLAPDTR---TVIDIGGQDSKVIQLDaGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQL 144
Cdd:pfam01869  81 FGKDIVReEITVHADGAVALAPGTRgedGVIDIGGTGSKVIGLD-GGKVVRFGGNGQCAGGEGSFLEIAARALGAVVREL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  145 DAITDGV--EPHAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGP-LLFTGGVSRCAAFARM 221
Cdd:pfam01869 160 DGLAPKTtlNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRLGFVPDeVVLTGGVAKNAGLVKA 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 490309354  222 L-----ESHVGMAVTTHPDAQFAGAIGAALIG 248
Cdd:pfam01869 240 LrdylkENILGVKVNVHPDPQYAGAIGAALLA 271
 
Name Accession Description Interval E-value
CoA_E_activ TIGR00241
CoA-substrate-specific enzyme activase, putative; This domain is found in a set of closely ...
 3-247 3.30e-116

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: 332.91  E-value: 3.30e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354    3 YTVGIDSGSTATKGILLADG-VVTRRFLCPTPFRPAD--AIHEAWETLRAGLAETPFLTLTGYGRQLVDFANKQVTEISC 79
Cdd:TIGR00241   1 ISLGIDSGSTTTKMVLMEDGkVIGYKWLDTTPVIEETarAILEALKEAGIGLEPIDKIVATGYGRHKVGFADKIVTEISC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   80 HGLGARLLAPDTRTVIDIGGQDSKVIQLDaGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAITD-GVEPHAITS 158
Cdd:TIGR00241  81 HGKGANYLAPEARGVIDIGGQDSKVIKID-DGKVDDFTMNDKCAAGTGRFLEVTARRLGVSVEELGSLAEkADRKAKISS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGMAVTTHPDAQF 238
Cdd:TIGR00241 160 MCTVFAESELISLLAAGVKKEDILAGVYESIAERVAEMLQRLKIEAPIVFTGGVSKNKGLVKALEKKLGMKVITPPEPQI 239


                  ....*....
gi 490309354  239 AGAIGAALI 247
Cdd:TIGR00241 240 VGAVGAALL 248
ASKHA_NBD_YjiL-like cd24109
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ...
 5-247 4.68e-114

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: 327.23  E-value: 4.68e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   5 VGIDSGSTATKGILLADGVVTRRFLCPTPFRPADAIHEAWETLRAGLA-ETPFLTLTGYGRQLVDFANKQVTEISCHGLG 83
Cdd:cd24109    2 IGIDIGSRATKIALFEDDKILEKFVIPTGWFYKEYGRRIIKELLEDINyEDDKIVATGYGRNNLDFADKTITEITAHAKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  84 ARLLAPDTRTVIDIGGQDSKVIQLDaGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAITDGVEPHAITSMCTVF 163
Cdd:cd24109   82 ARYLTGKDFTVIDIGGQDTKVIKVE-NGKVIDFIMNDKCAAGTGRFLENMANILGISLEEISKYAEDPEPLSISSTCAVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 164 AESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQgPLLFTGGVSRCAAFARMLESHVGMAVTTHPDAQFAGAIG 243
Cdd:cd24109  161 AESEVISLIAEGVSRERIAAGVNYSIAKRVAPLLNRLKSP-PIVLTGGVARNKAIIELLEKRLGAEVIVPELPQFAGAIG 239


                 ....
gi 490309354 244 AALI 247
Cdd:cd24109  240 AALI 243
ASKHA_NBD_BcrAD_BadFG_HgdC_HadI cd24036
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ...
 4-247 2.24e-108

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: 312.94  E-value: 2.24e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   4 TVGIDSGSTATKGILLAD-GVVTRRFLCPTPFRP----ADAIHEAWETLRAGLAETPFLTLTGYGRQLVDFANKQVTEIS 78
Cdd:cd24036    1 FAGIDVGSTTTKAVILDDkGKILGKAVIRTGTDPektaERALEEALEEAGLSREDIEYIVATGYGRNSVPFADKTITEIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  79 CHGLGARLLAPDTRTVIDIGGQDSKVIQLDAGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAI-TDGVEPHAIT 157
Cdd:cd24036   81 CHARGAHFLFPEARTVIDIGGQDSKVIRLDEDGKVLDFAMNDKCAAGTGRFLEVMARRLEVSLEELGELaLKSTNPVEIS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 158 SMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGMAVTTHPDAQ 237
Cdd:cd24036  161 STCTVFAESEVISLIAEGVPKEDIIAGIHNSIAKRVAALAKRVGVEDPVVLTGGVAKNPGVVKALEEKLGVEVIVPPNPQ 240

                        250
                 ....*....|
gi 490309354 238 FAGAIGAALI 247
Cdd:cd24036  241 LVGALGAALL 250
YjiL COG1924
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ...
 1-255 1.44e-106

Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];


Pssm-ID: 441527 [Multi-domain]  Cd Length: 264  Bit Score: 308.96  E-value: 1.44e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   1 MIYTVGIDSGSTATKGILL-ADGVVTRRFLCPTPFRPADAIHEAWETL--RAGLAETP--FLTLTGYGRQLVD--FANKQ 73
Cdd:COG1924    2 GMIYLGIDIGSTTTKAVLLdEDGEILASAYLPTGGDPLEAAKEALKELleEAGLKREDiaGVVATGYGRVLIGaaFADKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  74 VTEISCHGLGARLLAPDTRTVIDIGGQDSKVIQLDaGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAIT-DGVE 152
Cdd:COG1924   82 VTEITAHAKGAHFLFPDVRTIIDIGGQDSKAIKLE-DGVVVDFAMNDKCAAGTGRFLEVMARRLGIPIEEFGELAlKAKN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 153 PHAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGMAVTT 232
Cdd:COG1924  161 PVDISSRCTVFAESEVISLLAEGAPKEDIAAGLCYSVAKRVLNLVKRVGIGEPVVFQGGVAKNDGVVRALEKELGKEVIV 240

                        250       260
                 ....*....|....*....|...
gi 490309354 233 HPDAQFAGAIGAALIGQRQRRRG 255
Cdd:COG1924  241 PPIPQLMGALGAALLAREKVKKG 263
ASKHA_NBD_HgdC_HadI-like cd24103
nucleotide-binding domain (NBD) of the HgdC/HadI-like subfamily; The HgdC/HadI-like subfamily ...
 4-246 4.28e-78

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: 236.15  E-value: 4.28e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   4 TVGIDSGSTATKGILLADG-VVTRRFLCPT---PFRPADAIHEAWETLRAGLAETPFLTLTGYGRQLVDFANKQVTEISC 79
Cdd:cd24103    1 TMGIDIGSTASKCVILKDGkEIVAQSVISVgtgTSGPARALEEVLEKAGLAKEDIAYTVATGYGRNSFEGADKQISELSC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  80 HGLGARLLAPDTRTVIDIGGQDSKVIQLDAGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAIT-DGVEPHAITS 158
Cdd:cd24103   81 HARGVNFLLPEVRTIIDIGGQDVKVLKLDDNGRLLNFVMNDKCAAGTGRFLDVMARVLEVKVSELGELDaQSTNPVSISS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGMAVTTHPDAQF 238
Cdd:cd24103  161 TCTVFAESEVISQLSEGAKIPDIIAGIHTSVASRVAGLAKRVGIEKDVVMTGGVAQNSGVVRAMEEELGTEIIVSPNPQL 240


                 ....*...
gi 490309354 239 AGAIGAAL 246
Cdd:cd24103  241 TGALGAAL 248
ASKHA_NBD_benz_CoA_BzdP cd24107
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, BzdP subunit and similar ...
 4-247 1.50e-74

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: 227.04  E-value: 1.50e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   4 TVGIDSGSTATKGILLADGVVTRRFLCPTPFRPADAIHEAWETL--RAGLA--ETPFLTLTGYGRQLVDFANKQVTEISC 79
Cdd:cd24107    1 TAGIDVGSKFTKAVILEDGEILAKAIVPTGFDVAKAAERALDEAlaAAGISrdDVKKIVATGAGRKLVSFADDTVTEVVC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  80 HGLGARLLAPDTRTVIDIGGQDSKVIQLDAGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAI-TDGVEPHAITS 158
Cdd:cd24107   81 AAKGAYFLFPSARTVIDVGAEEGRAIKLDENGKVVDFAQNDKCAAGAGAFLEAMSRALEVPLEELGELsLKSTKKIPMNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGMAVTTHPDAQF 238
Cdd:cd24107  161 QCAVFAESEVVSLIHAGTPKEDIAAAVHDAIASRIASMVRRVGIEDDVALIGGVAKNPGFVESLKELLGKEVLVPEDPEY 240


                 ....*....
gi 490309354 239 AGAIGAALI 247
Cdd:cd24107  241 VGALGAALI 249
ASKHA_NBD_benz_CoA_BcrA_BadF cd24104
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ...
 5-250 3.15e-74

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: 226.41  E-value: 3.15e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   5 VGIDSGSTATKGILL-ADGVVTRRFLCPTPFR----PADAIHEAWETLRAGLAETPFLTLTGYGRQLVDFANKQVTEISC 79
Cdd:cd24104    2 AGVDVGSTQTKAVIIdEDGEIVGRGLTNTGANvvvaAERAFREAIEEAGIKEEEVEYVVGTGYGRYKVTFGNAQRTEISC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  80 HGLGARLLAPDTRTVIDIGGQDSKVIQLDAGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAIT-DGVEPHAITS 158
Cdd:cd24104   82 HARGAHHMFPNTRTVLDIGGQDTKAIRVDETGEVVDFVMNDKCAAGTGRFLGYAADALGIPLDELGPLAlKSTKPVRISS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGMAVTTHPDAQF 238
Cdd:cd24104  162 TCTVFAESEIRSWLALGKKREDILGGVHRAIAARAVSLIRRVGIEPEFTFTGGVARNEAMVKALEELLGVKINVSPDSHF 241

                        250
                 ....*....|..
gi 490309354 239 AGAIGAALIGQR 250
Cdd:cd24104  242 MGALGAALFALE 253
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
 5-248 2.74e-70

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: 216.84  E-value: 2.74e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354    5 VGIDSGSTATKGILLADG--VVTRRFLCPTPFRPA----------DAIHEAWETLRAGLA--ETPFLTLTGYGRQLVD-- 68
Cdd:pfam01869   1 LGIDGGSTKTKAVLMDDDgeVLGRAIAGSANFESVgveaaernlkDAITEALEEAGLKLDdiEYMFLGLTGYGRAGVDgh 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   69 FANKQVT-EISCHGLGARLLAPDTR---TVIDIGGQDSKVIQLDaGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQL 144
Cdd:pfam01869  81 FGKDIVReEITVHADGAVALAPGTRgedGVIDIGGTGSKVIGLD-GGKVVRFGGNGQCAGGEGSFLEIAARALGAVVREL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  145 DAITDGV--EPHAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGP-LLFTGGVSRCAAFARM 221
Cdd:pfam01869 160 DGLAPKTtlNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRLGFVPDeVVLTGGVAKNAGLVKA 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 490309354  222 L-----ESHVGMAVTTHPDAQFAGAIGAALIG 248
Cdd:pfam01869 240 LrdylkENILGVKVNVHPDPQYAGAIGAALLA 271
ASKHA_NBD_benz_CoA_BcrD_BadG cd24105
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit D (BcrD/BadG) and similar ...
 4-251 3.74e-70

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: 215.91  E-value: 3.74e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   4 TVGIDSGSTATKGILLADG--VVTRRFLcPTPFRPADAIHEAWETL--RAGLAET--PFLTLTGYGRQLVDFANKQVTEI 77
Cdd:cd24105    1 TAGIDVGSGYTKAVIMDDGekILAKRVE-RTRQRDEEVAREAYNEAleEAGLKRDdiAYVATTGEGRYVVFFRDGHFTDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  78 SCHGLGARLLAPDTRTVIDIGGQDSKVIQLDAGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAI-TDGVEPHAI 156
Cdd:cd24105   80 TTHARGAIFLFPGTRTVLDIGAQHTRAIRIDEKGKVLSFRMNDKCAAGSGQFLENIARYLGVALDEIGDLsLQADNPEPI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 157 TSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGMAVTT--HP 234
Cdd:cd24105  160 SGVCAVLAETEVINMVSRGIPVPDILRGIHLSLAGRSVQLLKRVGAEPEVTLTGGLARNEGMVEALEELLGAKVNVaeHD 239

                        250
                 ....*....|....*..
gi 490309354 235 DAQFAGAIGAALIGQRQ 251
Cdd:cd24105  240 DSIYAGALGAALLGAFR 256
ASKHA_NBD_benz_CoA_BzdQ cd24106
nucleotide-binding domain (NBD) of benzoyl-CoA reductase, bzd-type, Q subunit (BzdQ) and ...
 4-248 4.72e-70

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: 215.55  E-value: 4.72e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   4 TVGIDSGSTATKGILLADGVVTRRFLCPTPfrpADAIHEAWETLRAGLAETPfLTL--------TGYGRQLVDFANKQVT 75
Cdd:cd24106    1 TAGIDVGSVSSQAVIMVDGELYAYSNMRTG---SDSPESAQKALNAALEKTG-LKLedihyivgTGYGRVNVPFANKAIT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  76 EISCHGLGARLLAPDT-RTVIDIGGQDSKVIQLDAGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLD--AITDGVE 152
Cdd:cd24106   77 EIACHARGANYMYGPSvRTVLDMGGQDCKAIRCDEKGKVTNFLMNDKCAAGTGRGMEVFADLLQVPIEEIGelSLEVDKE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 153 PHAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQGPLLFTGGVSRCAAFARMLESHVGM-AVT 231
Cdd:cd24106  157 PPPVSSTCVVFAKSEALGLLREGWPKNDVLAAYCEAMAHRVVTLLERVGVEKDFVITGGIAKNIGVVKRIEKELGIkALI 236

                        250
                 ....*....|....*..
gi 490309354 232 THPDAQFAGAIGAALIG 248
Cdd:cd24106  237 PKEDPQIAGALGAALFA 253
ASKHA_NBD_BcrAD_BadFG-like cd24002
nucleotide-binding domain (NBD) of the BcrAD/BadFG-like ATPase family; The BcrAD/BadFG-like ...
 4-247 4.58e-64

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: 200.35  E-value: 4.58e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   4 TVGIDSGSTATKGILLADG--VVTRRFLC--PTPFRPADAIHEAWETLRAGLAETPFLTL----TGYGRQLVDF-ANKQV 74
Cdd:cd24002    1 TLGLDIGSTTSKAVLLDEGknIVATEYERsgTGTSGPIEAVKKTLEKFLLEKGVKEEDIActgvTGYGRVELFIdGDKQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  75 TEISCHGLGARLLAPDTRTVIDIGGQDSKVIQLDAGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAIT-DGVEP 153
Cdd:cd24002   81 SEVSAHARGANHIYPDARTIIDVGGQDAKVIILDENGQMKNFKMNDKCAAGTGAFLDSMANKLNVKVEELADVKmNSKKE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 154 HAITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRL-SAQGPLLFTGGVSRCAAFARMLESHVGMAVTT 232
Cdd:cd24002  161 VSVSSTCAVFAETDINSFQSRGAPKEDIIAGLHKAVALRVMSLVGRLgVPKKDVVLQGGVARNSAVVRALEEIINNEIIV 240

                        250
                 ....*....|....*
gi 490309354 233 HPDAQFAGAIGAALI 247
Cdd:cd24002  241 PEIAQVMGALGAALL 255
ASKHA_NBD_O66634-like_rpt1 cd24034
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ...
 4-251 4.68e-57

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: 182.79  E-value: 4.68e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   4 TVGIDSGSTATKGILL-ADGVVTRRFLCPTPFRPADAIHEAWETLRAGLAETPF-LTLTG-YGRQLVDFAN-KQVTEISC 79
Cdd:cd24034    1 YLGIDIGSTTVKAVVLdEKGNIVFSDYERHFGNPREALLELLEEIKERLGDEIArIAVTGsGGRGLAELLGlPFVQEVVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  80 HGLGARLLAPDTRTVIDIGGQDSKVIQLDAGGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAITDGVEPHA-ITS 158
Cdd:cd24034   81 IEAAVKHLHPDARTVIEIGGEDFKLIELDGDGKLKDFRMNSKCAAGTGAFIDQQARRLGLSLEELAELALKAEPPApIAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 159 MCTVFAESEVISLRSAGVAPEAILAGVINAMARrsaNFIGRLS----AQGPLLFTGGVS-RCAAFARMLESHVGMA-VTT 232
Cdd:cd24034  161 RCSVFAKSDMIHLQNKGVPKEDIAAGLCRAVAR---NVIATLAkgreIEGPVILVGGVAtNNAVLREAFEELLGDEeLIV 237

                        250
                 ....*....|....*....
gi 490309354 233 HPDAQFAGAIGAALIGQRQ 251
Cdd:cd24034  238 PEHAEYFEALGAALYALEE 256
ASKHA_NBD_O66634-like_rpt2 cd24035
nucleotide-binding domain (NBD) of the second repeat of Aquifex aeolicus hypothetical protein ...
 5-253 2.07e-52

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: 170.79  E-value: 2.07e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   5 VGIDSGSTATKGILL-ADG-VVTRRFLcPTPFRPADAIHEAWETLRAGLAETPFLT---LTGYGRQLV-DF--ANKQVTE 76
Cdd:cd24035    2 LGIDVGSTTTKAVLIdEDGeILASVYL-RTKGNPIEAVKKGLKELREQLPEKVVIVgvgTTGSGRELLkDAlgADVVKVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  77 ISCHGLGARLLAPDTRTVIDIGGQDSKVIQLDAgGNLSDFLMNDKCAAGTGRFLEVISRTLGASVEQLDAIT-DGVEPHA 155
Cdd:cd24035   81 ITAHATAALHFDPDVDTIFEIGGQDSKYISLKN-GVVKDFAMNEACSAGTGSFLEEQAKSLGIPIEEFAELAlKAKNPPD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 156 ITSMCTVFAESEVISLRSAGVAPEAILAGVINAMARRSANFIGRLSAQG-PLLFTGGVSRCAAFARMLESHVGMAVTTHP 234
Cdd:cd24035  160 LGSRCTVFMESDIKQAQQEGASKEDISAGLAYSVVKNYLNKVVGGRNLGkKIVFQGGTFLNKAVLAAFEQVTGKEIIVPP 239

                        250
                 ....*....|....*....
gi 490309354 235 DAQFAGAIGAALIGQRQRR 253
Cdd:cd24035  240 HPGLMGAYGAALLAKEEIK 258
ASKHA_NBD_MJ0800-like cd24108
nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ0800 and similar ...
 4-247 2.68e-29

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: 111.01  E-value: 2.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354   4 TVGIDSGSTATKGILLADGVVTRRFLCPTpfrpADAIHEAWETLRAGLAETPF-------LTLTGYGRQLV-DFANKQVT 75
Cdd:cd24108    1 TAGIDSGSTTTKAVVMKDNEIIGTGWMPT----TDVIESAEKAFEEALEEAGIklsdieaIGTTGYGRYTIgKHFNADLV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354  76 --EISCHGLGARLLAPDTR---TVIDIGGQDSKVIQLDAG--GNlsdFLMNDKCAAGTGRFLEVISRTLGASVEQLDAIT 148
Cdd:cd24108   77 qeELTVNSKGAVYLADKQKgeaTVIDIGGMDNKAITVNDGipDN---FTMGGICAGASGRFLEMTARRLGVDITELGELA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490309354 149 DGVEPHAIT--SMCTVFAESEVISLRSAGVAPEAILAGVINAMARRS-ANFIGRLSAQGPLLFTGGVSRCAAFARMLESH 225
Cdd:cd24108  154 LKGDWRKIRmnSYCIVFGIQDLVTSLAEGARAEDVAAAACHSVAEQVyEQQLQEIDVREPVIQVGGTSLIEGLVKALGEV 233

                        250       260
                 ....*....|....*....|..
gi 490309354 226 VGMAVTTHPDAQFAGAIGAALI 247
Cdd:cd24108  234 LGIEVIVPPYSQLIGAVGAALL 255
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH