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Conserved domains on  [gi|1972247512|ref|NP_001379869|]
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Methylmalonic aciduria type A homolog, mitochondrial [Caenorhabditis elegans]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
24-297 3.94e-138

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PRK09435:

Pssm-ID: 476819  Cd Length: 332  Bit Score: 393.42  E-value: 3.94e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  24 FRVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGGVTR 103
Cdd:PRK09435   57 LRIGITGVPGVGKSTFIEALGMHLIE-QGHKVAVLAVDPSSTRTGGSILGDKTRMERLSRHPNAFIRPSPSSGTLGGVAR 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 104 GIHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGIMEMSDLLVVTKDDGDLKAKAKMT 183
Cdd:PRK09435  136 KTRETMLLCEAAGYDVILVETVGVGQSETAVAGMVDFFLLLQLPGAGDELQGIKKGIMELADLIVINKADGDNKTAARRA 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 184 QAEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTIGESGDLERRRQDQMKKWMWNHVKDEIMSVFQKH 263
Cdd:PRK09435  216 AAEYRSALRLLRPKDPGWQPPVLTCSALEGEGIDEIWQAIEDHRAALTASGEFAARRREQQVDWMWEMVEEGLLDRLFAD 295
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1972247512 264 PKIAHLAPKLENEIRSGKITPGLAAETMIRTFFG 297
Cdd:PRK09435  296 PAVRARLPELEAAVAAGTLTPALAARQLLEAFGL 329
 
Name Accession Description Interval E-value
PRK09435 PRK09435
methylmalonyl Co-A mutase-associated GTPase MeaB;
24-297 3.94e-138

methylmalonyl Co-A mutase-associated GTPase MeaB;


Pssm-ID: 236515  Cd Length: 332  Bit Score: 393.42  E-value: 3.94e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  24 FRVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGGVTR 103
Cdd:PRK09435   57 LRIGITGVPGVGKSTFIEALGMHLIE-QGHKVAVLAVDPSSTRTGGSILGDKTRMERLSRHPNAFIRPSPSSGTLGGVAR 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 104 GIHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGIMEMSDLLVVTKDDGDLKAKAKMT 183
Cdd:PRK09435  136 KTRETMLLCEAAGYDVILVETVGVGQSETAVAGMVDFFLLLQLPGAGDELQGIKKGIMELADLIVINKADGDNKTAARRA 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 184 QAEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTIGESGDLERRRQDQMKKWMWNHVKDEIMSVFQKH 263
Cdd:PRK09435  216 AAEYRSALRLLRPKDPGWQPPVLTCSALEGEGIDEIWQAIEDHRAALTASGEFAARRREQQVDWMWEMVEEGLLDRLFAD 295
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1972247512 264 PKIAHLAPKLENEIRSGKITPGLAAETMIRTFFG 297
Cdd:PRK09435  296 PAVRARLPELEAAVAAGTLTPALAARQLLEAFGL 329
ArgK COG1703
GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, ...
24-296 1.68e-124

GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441309  Cd Length: 317  Bit Score: 358.23  E-value: 1.68e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  24 FRVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGGVTR 103
Cdd:COG1703    49 HRIGITGVPGAGKSTLIDALGLRLRE-RGKRVAVLAVDPSSPFTGGAILGDRTRMEELARDPGVFIRSSASRGSLGGLAR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 104 GIHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGIMEMSDLLVVTKDDGDlkaKAKMT 183
Cdd:COG1703   128 ATREAILLLEAAGFDVIIVETVGVGQSETDVAGMADTFLLLLLPGAGDELQGIKAGIMEIADIIVVNKADGD---GAERA 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 184 QAEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTIGESGDLERRRQDQMKKWMWNHVKDEIMSVFQKH 263
Cdd:COG1703   205 VRELRGALHLLRPAEPGWRPPVLTTSALTGEGIDELWEAIEEHRAYLKESGELEERRREQARRWLWELVRERLRERFREQ 284
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1972247512 264 PKIAHLAPKLENEIRSGKITPGLAAETMIRTFF 296
Cdd:COG1703   285 PEVRARLDELEEAVLAGELDPYAAADELLEALL 317
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
1-230 3.21e-119

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.


Pssm-ID: 349768  Cd Length: 252  Bit Score: 342.24  E-value: 3.21e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512   1 MLLKMVLDEerekykkfgrDSMIFRVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQE 80
Cdd:cd03114    34 ELLDALLPQ----------AGRAFRVGITGPPGAGKSTLIEALGRLLRE-QGHRVAVLAVDPSSPRSGGSILGDKTRMQR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  81 LSRNPKAYIRQSPTSGSLGGVTRGIHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGI 160
Cdd:cd03114   103 LARDPNAFIRPSPSRGTLGGVARATREAILLCEAAGYDVVLVETVGVGQSEVAVADMVDTFVLLLPPGGGDELQGIKAGI 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 161 MEMSDLLVVTKDDGDLKAKAKMTQAEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTI 230
Cdd:cd03114   183 MEIADLVVVNKADGDLKTGARRAQRELTSALKLLRPRSDGWRPPVLRTSALTGEGIDELWEAIEEHRAAL 252
MeaB pfam03308
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
25-264 1.96e-95

Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria.


Pssm-ID: 281323 [Multi-domain]  Cd Length: 272  Bit Score: 282.79  E-value: 1.96e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  25 RVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGGVTRG 104
Cdd:pfam03308  35 RVGVTGVPGAGKSTLIEALGMELRR-RGHRVAVLAVDPSSPRTGGSILGDKTRMDRLAVDPGAFIRPSPSRGALGGLSRK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 105 IHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGIMEMSDLLVVTKDDGDLKaKAKMTQ 184
Cdd:pfam03308 114 TREVVLLLEAAGFDVIIIETVGVGQSEVDVANMVDTFVLLTMPGGGDELQGIKAGIMEIADIYVVNKADGNLP-GAERAA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 185 AEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTIGESGDLERRRQDQMKKWMWNHVKDEIMSVFQKHP 264
Cdd:pfam03308 193 RELRAALHLLTPFEAGWRPPVLTTSAVRGEGIDELWDAIEEHREVLTATGLIEARRRAQVVRWLRELVEDDLLDRVKAAP 272
lao TIGR00750
LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of ...
25-293 5.33e-85

LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of two transporter system periplasmic binding proteins and consequently inhibits those transporters. This kinase is also found in Gram-positive bacteria, archaea, and the roundworm C. elegans. It may have a more general, but still unknown function. Mutations have also been found that do not phosphorylate the periplasmic binding proteins, yet still allow transport. The ATPase activity of this protein seems to be necessary, however. [Transport and binding proteins, Amino acids, peptides and amines, Regulatory functions, Protein interactions]


Pssm-ID: 129833 [Multi-domain]  Cd Length: 300  Bit Score: 257.01  E-value: 5.33e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  25 RVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGGVTRG 104
Cdd:TIGR00750  36 RVGITGTPGAGKSTLLEALGMELRR-RGLRVAVIAVDPSSPFTGGSILGDRTRMQRLATDPGAFIRSMPTRGHLGGLSQA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 105 IHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGIMEMSDLLVVTKDDGDLKAKAKMTQ 184
Cdd:TIGR00750 115 TRELVLLLDAAGYDVIIVETVGVGQSEVDIANMADTFVLVTIPGTGDDLQGIKAGVMEIADIYVVNKADGEGATNVRIAR 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 185 AEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTIGESGDLERRRQDQMKKWMWNHVKDEIMSVFQKHP 264
Cdd:TIGR00750 195 LMLSLALEEIRRREDGWRPPVLTTSAVEGRGIDELWDAIEEHKTFLTASGLLQERRRQRSVEWLKKLVEEEVLKKVFANE 274
                         250       260
                  ....*....|....*....|....*....
gi 1972247512 265 KIAHlapKLENEIRSGKITPGLAAETMIR 293
Cdd:TIGR00750 275 DVYR---DLLLAVLAGELDPYTAAEQILE 300
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
26-126 3.29e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 37.35  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512   26 VGISGSPGVGKSSFIEALGAELTENRGKkvaVLTIDptsamtggsvlGDLTRMQELSRNPKAYIRQSPTSGSLGGVTRGI 105
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPGGG---VIYID-----------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLA 70
                           90       100
                   ....*....|....*....|.
gi 1972247512  106 HEaviLCEGAGYDIVIIETVG 126
Cdd:smart00382  71 LA---LARKLKPDVLILDEIT 88
 
Name Accession Description Interval E-value
PRK09435 PRK09435
methylmalonyl Co-A mutase-associated GTPase MeaB;
24-297 3.94e-138

methylmalonyl Co-A mutase-associated GTPase MeaB;


Pssm-ID: 236515  Cd Length: 332  Bit Score: 393.42  E-value: 3.94e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  24 FRVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGGVTR 103
Cdd:PRK09435   57 LRIGITGVPGVGKSTFIEALGMHLIE-QGHKVAVLAVDPSSTRTGGSILGDKTRMERLSRHPNAFIRPSPSSGTLGGVAR 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 104 GIHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGIMEMSDLLVVTKDDGDLKAKAKMT 183
Cdd:PRK09435  136 KTRETMLLCEAAGYDVILVETVGVGQSETAVAGMVDFFLLLQLPGAGDELQGIKKGIMELADLIVINKADGDNKTAARRA 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 184 QAEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTIGESGDLERRRQDQMKKWMWNHVKDEIMSVFQKH 263
Cdd:PRK09435  216 AAEYRSALRLLRPKDPGWQPPVLTCSALEGEGIDEIWQAIEDHRAALTASGEFAARRREQQVDWMWEMVEEGLLDRLFAD 295
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1972247512 264 PKIAHLAPKLENEIRSGKITPGLAAETMIRTFFG 297
Cdd:PRK09435  296 PAVRARLPELEAAVAAGTLTPALAARQLLEAFGL 329
ArgK COG1703
GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, ...
24-296 1.68e-124

GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441309  Cd Length: 317  Bit Score: 358.23  E-value: 1.68e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  24 FRVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGGVTR 103
Cdd:COG1703    49 HRIGITGVPGAGKSTLIDALGLRLRE-RGKRVAVLAVDPSSPFTGGAILGDRTRMEELARDPGVFIRSSASRGSLGGLAR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 104 GIHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGIMEMSDLLVVTKDDGDlkaKAKMT 183
Cdd:COG1703   128 ATREAILLLEAAGFDVIIVETVGVGQSETDVAGMADTFLLLLLPGAGDELQGIKAGIMEIADIIVVNKADGD---GAERA 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 184 QAEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTIGESGDLERRRQDQMKKWMWNHVKDEIMSVFQKH 263
Cdd:COG1703   205 VRELRGALHLLRPAEPGWRPPVLTTSALTGEGIDELWEAIEEHRAYLKESGELEERRREQARRWLWELVRERLRERFREQ 284
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1972247512 264 PKIAHLAPKLENEIRSGKITPGLAAETMIRTFF 296
Cdd:COG1703   285 PEVRARLDELEEAVLAGELDPYAAADELLEALL 317
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
1-230 3.21e-119

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.


Pssm-ID: 349768  Cd Length: 252  Bit Score: 342.24  E-value: 3.21e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512   1 MLLKMVLDEerekykkfgrDSMIFRVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQE 80
Cdd:cd03114    34 ELLDALLPQ----------AGRAFRVGITGPPGAGKSTLIEALGRLLRE-QGHRVAVLAVDPSSPRSGGSILGDKTRMQR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  81 LSRNPKAYIRQSPTSGSLGGVTRGIHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGI 160
Cdd:cd03114   103 LARDPNAFIRPSPSRGTLGGVARATREAILLCEAAGYDVVLVETVGVGQSEVAVADMVDTFVLLLPPGGGDELQGIKAGI 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 161 MEMSDLLVVTKDDGDLKAKAKMTQAEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTI 230
Cdd:cd03114   183 MEIADLVVVNKADGDLKTGARRAQRELTSALKLLRPRSDGWRPPVLRTSALTGEGIDELWEAIEEHRAAL 252
MeaB pfam03308
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
25-264 1.96e-95

Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria.


Pssm-ID: 281323 [Multi-domain]  Cd Length: 272  Bit Score: 282.79  E-value: 1.96e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  25 RVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGGVTRG 104
Cdd:pfam03308  35 RVGVTGVPGAGKSTLIEALGMELRR-RGHRVAVLAVDPSSPRTGGSILGDKTRMDRLAVDPGAFIRPSPSRGALGGLSRK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 105 IHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGIMEMSDLLVVTKDDGDLKaKAKMTQ 184
Cdd:pfam03308 114 TREVVLLLEAAGFDVIIIETVGVGQSEVDVANMVDTFVLLTMPGGGDELQGIKAGIMEIADIYVVNKADGNLP-GAERAA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 185 AEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTIGESGDLERRRQDQMKKWMWNHVKDEIMSVFQKHP 264
Cdd:pfam03308 193 RELRAALHLLTPFEAGWRPPVLTTSAVRGEGIDELWDAIEEHREVLTATGLIEARRRAQVVRWLRELVEDDLLDRVKAAP 272
lao TIGR00750
LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of ...
25-293 5.33e-85

LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of two transporter system periplasmic binding proteins and consequently inhibits those transporters. This kinase is also found in Gram-positive bacteria, archaea, and the roundworm C. elegans. It may have a more general, but still unknown function. Mutations have also been found that do not phosphorylate the periplasmic binding proteins, yet still allow transport. The ATPase activity of this protein seems to be necessary, however. [Transport and binding proteins, Amino acids, peptides and amines, Regulatory functions, Protein interactions]


Pssm-ID: 129833 [Multi-domain]  Cd Length: 300  Bit Score: 257.01  E-value: 5.33e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  25 RVGISGSPGVGKSSFIEALGAELTEnRGKKVAVLTIDPTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGGVTRG 104
Cdd:TIGR00750  36 RVGITGTPGAGKSTLLEALGMELRR-RGLRVAVIAVDPSSPFTGGSILGDRTRMQRLATDPGAFIRSMPTRGHLGGLSQA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 105 IHEAVILCEGAGYDIVIIETVGVGQSETSVSDMCDMMCLLLSPAHGDELQGVKRGIMEMSDLLVVTKDDGDLKAKAKMTQ 184
Cdd:TIGR00750 115 TRELVLLLDAAGYDVIIVETVGVGQSEVDIANMADTFVLVTIPGTGDDLQGIKAGVMEIADIYVVNKADGEGATNVRIAR 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512 185 AEYISALKFMRPRLDVWRPKVMRSSIMDKESVSEVCSSLYEFWDTIGESGDLERRRQDQMKKWMWNHVKDEIMSVFQKHP 264
Cdd:TIGR00750 195 LMLSLALEEIRRREDGWRPPVLTTSAVEGRGIDELWDAIEEHKTFLTASGLLQERRRQRSVEWLKKLVEEEVLKKVFANE 274
                         250       260
                  ....*....|....*....|....*....
gi 1972247512 265 KIAHlapKLENEIRSGKITPGLAAETMIR 293
Cdd:TIGR00750 275 DVYR---DLLLAVLAGELDPYTAAEQILE 300
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
28-122 1.20e-04

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 40.49  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  28 ISGSPGVGKSSFIEALGAELtENRGKKVAVLTID-------PTSAMTGGSVLGDLTRMQELSRNPKAYIRQSPTSGSLGG 100
Cdd:cd01983     6 TGGKGGVGKTTLAAALAVAL-AAKGYKVLLIDLDdyvlidgGGGLETGLLLGTIVALLALKKADEVIVVVDPELGSLLEA 84
                          90       100
                  ....*....|....*....|..
gi 1972247512 101 VTRGIHEAvILCEGAGYDIVII 122
Cdd:cd01983    85 VKLLLALL-LLGIGIRPDGIVL 105
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
26-200 5.95e-04

CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.


Pssm-ID: 396860  Cd Length: 179  Bit Score: 39.93  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  26 VGISGSPGVGKSSFIEALgaeLTENR-GKKVAVLT-------IDPTSAMTGGSVLGDL-------TRMQELSRNPKAYIR 90
Cdd:pfam02492   3 TVITGFLGSGKTTLLNHL---LKQNRaGLRIAVIVnefgetgIDAELLSETGVLIVELsngciccTIREDLSMALEALLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512  91 QSPtsgslggvtrgiheavilcegaGYDIVIIETVGVGqSETSVSDMC-----------DMMCLLLSPAHGDELQGVKRG 159
Cdd:pfam02492  80 REG----------------------RLDVIFIETTGLA-EPAPVAQTFlspelrspvllDGVITVVDAANEADGEKIPRK 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1972247512 160 I---MEMSDLLVVTKDD--GDLKAKAKMtqAEYISAlkfMRPRLDV 200
Cdd:pfam02492 137 AgdqIAFADLIVLNKTDlaPEVALLEVL--EEDLRR---LNPGAPV 177
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
26-126 3.29e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 37.35  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972247512   26 VGISGSPGVGKSSFIEALGAELTENRGKkvaVLTIDptsamtggsvlGDLTRMQELSRNPKAYIRQSPTSGSLGGVTRGI 105
Cdd:smart00382   5 ILIVGPPGSGKTTLARALARELGPPGGG---VIYID-----------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLA 70
                           90       100
                   ....*....|....*....|.
gi 1972247512  106 HEaviLCEGAGYDIVIIETVG 126
Cdd:smart00382  71 LA---LARKLKPDVLILDEIT 88
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
11-68 3.96e-03

An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 37.30  E-value: 3.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972247512  11 REKYKKFGRDSMIFRVGISGSPGVGKSSFIEALgaeltenRGKKVAvltidPTSAMTG 68
Cdd:cd01859    87 RRTIKELAIDGKPVIVGVVGYPKVGKSSIINAL-------KGRHSA-----STSPIPG 132
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
5-56 4.41e-03

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 37.12  E-value: 4.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1972247512   5 MVLDEEREKYKKFGRDSMIFRVGISGSPGVGKSSFIEALgaeltenRGKKVA 56
Cdd:cd01856    97 KKLLKENEKLKAKGLLPRPLRAMVVGIPNVGKSTLINRL-------RGKKVA 141
 
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.
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