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Conserved domains on  [gi|2378373656|dbj|BDU52750|]
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ATPase/protein kinase [Limnohabitans sp. INBF002]

Protein Classification

ArgK/MeaB family GTPase( domain architecture ID 10013236)

ArgK/MeaB family GTPase such as human mitochondrial methylmalonic aciduria type A protein, mycobacterial methylmalonyl Co-A mutase-associated GTPase MeaB, and Escherichia coli GTPase ArgK

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09435 PRK09435
methylmalonyl Co-A mutase-associated GTPase MeaB;
1-334 0e+00

methylmalonyl Co-A mutase-associated GTPase MeaB;


:

Pssm-ID: 236515  Cd Length: 332  Bit Score: 556.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656   1 MTPEQLLDGLLRGNAAVQRRAMAKAITLLESTRTDHRALADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIA 80
Cdd:PRK09435    3 MRRELDVDELVEGVLAGDRAALARAITLVESTRPDHRALAQELLDALLPHTGNALRIGITGVPGVGKSTFIEALGMHLIE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  81 QGHRVAVLTIDPSSTVSGGSILGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQS 160
Cdd:PRK09435   83 QGHKVAVLAVDPSSTRTGGSILGDKTRMERLSRHPNAFIRPSPSSGTLGGVARKTRETMLLCEAAGYDVILVETVGVGQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 161 ETAVANMTDMFVLLQLPNAGDDLQAIKKGVMEIADLVVINKAD-IDATAATRAQLQITSALQLLGMHggaghahrnTEVW 239
Cdd:PRK09435  163 ETAVAGMVDFFLLLQLPGAGDELQGIKKGIMELADLIVINKADgDNKTAARRAAAEYRSALRLLRPK---------DPGW 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 240 HPKVVQLSALLNQGVDAFWAAVCEFKALQTQNGRFAERRQHQALSWMWERIDAGLKQAFRAQPRVQTLLPQLSQHVASGQ 319
Cdd:PRK09435  234 QPPVLTCSALEGEGIDEIWQAIEDHRAALTASGEFAARRREQQVDWMWEMVEEGLLDRLFADPAVRARLPELEAAVAAGT 313

                         330
                  ....*....|....*
gi 2378373656 320 LAASTAARQLLSAYQ 334
Cdd:PRK09435  314 LTPALAARQLLEAFG 328
 
Name Accession Description Interval E-value
PRK09435 PRK09435
methylmalonyl Co-A mutase-associated GTPase MeaB;
1-334 0e+00

methylmalonyl Co-A mutase-associated GTPase MeaB;


Pssm-ID: 236515  Cd Length: 332  Bit Score: 556.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656   1 MTPEQLLDGLLRGNAAVQRRAMAKAITLLESTRTDHRALADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIA 80
Cdd:PRK09435    3 MRRELDVDELVEGVLAGDRAALARAITLVESTRPDHRALAQELLDALLPHTGNALRIGITGVPGVGKSTFIEALGMHLIE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  81 QGHRVAVLTIDPSSTVSGGSILGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQS 160
Cdd:PRK09435   83 QGHKVAVLAVDPSSTRTGGSILGDKTRMERLSRHPNAFIRPSPSSGTLGGVARKTRETMLLCEAAGYDVILVETVGVGQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 161 ETAVANMTDMFVLLQLPNAGDDLQAIKKGVMEIADLVVINKAD-IDATAATRAQLQITSALQLLGMHggaghahrnTEVW 239
Cdd:PRK09435  163 ETAVAGMVDFFLLLQLPGAGDELQGIKKGIMELADLIVINKADgDNKTAARRAAAEYRSALRLLRPK---------DPGW 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 240 HPKVVQLSALLNQGVDAFWAAVCEFKALQTQNGRFAERRQHQALSWMWERIDAGLKQAFRAQPRVQTLLPQLSQHVASGQ 319
Cdd:PRK09435  234 QPPVLTCSALEGEGIDEIWQAIEDHRAALTASGEFAARRREQQVDWMWEMVEEGLLDRLFADPAVRARLPELEAAVAAGT 313

                         330
                  ....*....|....*
gi 2378373656 320 LAASTAARQLLSAYQ 334
Cdd:PRK09435  314 LTPALAARQLLEAFG 328
ArgK COG1703
GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, ...
 1-333 4.45e-175

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


Pssm-ID: 441309  Cd Length: 317  Bit Score: 488.04  E-value: 4.45e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656   1 MTPEQLLDGLLRGNaavqRRAMAKAITLLESTRTDHraLADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIA 80
Cdd:COG1703     1 LDVEELVEGLLAGD----RRALARAITLVESRRPEH--LARELLKALLPHTGKAHRIGITGVPGAGKSTLIDALGLRLRE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  81 QGHRVAVLTIDPSSTVSGGSILGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQS 160
Cdd:COG1703    75 RGKRVAVLAVDPSSPFTGGAILGDRTRMEELARDPGVFIRSSASRGSLGGLARATREAILLLEAAGFDVIIVETVGVGQS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 161 ETAVANMTDMFVLLQLPNAGDDLQAIKKGVMEIADLVVINKADIDatAATRAQLQITSALQLLgmhggaghaHRNTEVWH 240
Cdd:COG1703   155 ETDVAGMADTFLLLLLPGAGDELQGIKAGIMEIADIIVVNKADGD--GAERAVRELRGALHLL---------RPAEPGWR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 241 PKVVQLSALLNQGVDAFWAAVCEFKALQTQNGRFAERRQHQALSWMWERIDAGLKQAFRAQPRVQTLLPQLSQHVASGQL 320
Cdd:COG1703   224 PPVLTTSALTGEGIDELWEAIEEHRAYLKESGELEERRREQARRWLWELVRERLRERFREQPEVRARLDELEEAVLAGEL 303

                         330
                  ....*....|...
gi 2378373656 321 AASTAARQLLSAY 333
Cdd:COG1703   304 DPYAAADELLEAL 316
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 6-266 1.68e-124

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: 357.27  E-value: 1.68e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656   6 LLDGLLRGnaavQRRAMAKAITLLESTRTDHRALADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIAQGHRV 85
Cdd:cd03114     2 LIAGLRSG----DRRALARAITLVESGRPDHRELAQELLDALLPQAGRAFRVGITGPPGAGKSTLIEALGRLLREQGHRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  86 AVLTIDPSSTVSGGSILGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQSETAVA 165
Cdd:cd03114    78 AVLAVDPSSPRSGGSILGDKTRMQRLARDPNAFIRPSPSRGTLGGVARATREAILLCEAAGYDVVLVETVGVGQSEVAVA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 166 NMTDMFVLLQLPNAGDDLQAIKKGVMEIADLVVINKADID-ATAATRAQLQITSALQLLgmhggaghaHRNTEVWHPKVV 244
Cdd:cd03114   158 DMVDTFVLLLPPGGGDELQGIKAGIMEIADLVVVNKADGDlKTGARRAQRELTSALKLL---------RPRSDGWRPPVL 228

                         250       260
                  ....*....|....*....|..
gi 2378373656 245 QLSALLNQGVDAFWAAVCEFKA 266
Cdd:cd03114   229 RTSALTGEGIDELWEAIEEHRA 250
MeaB pfam03308
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
 22-302 8.76e-120

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: 345.96  E-value: 8.76e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  22 MAKAITLLESTRTDHRALADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIAQGHRVAVLTIDPSSTVSGGSI 101
Cdd:pfam03308   1 LARAITLVESRRPDHQAEARELLRRLMPRAGRAHRVGVTGVPGAGKSTLIEALGMELRRRGHRVAVLAVDPSSPRTGGSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 102 LGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQSETAVANMTDMFVLLQLPNAGD 181
Cdd:pfam03308  81 LGDKTRMDRLAVDPGAFIRPSPSRGALGGLSRKTREVVLLLEAAGFDVIIIETVGVGQSEVDVANMVDTFVLLTMPGGGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 182 DLQAIKKGVMEIADLVVINKADIDATAATRAQLQITSALQLLgMHGGAGhahrntevWHPKVVQLSALLNQGVDAFWAAV 261
Cdd:pfam03308 161 ELQGIKAGIMEIADIYVVNKADGNLPGAERAARELRAALHLL-TPFEAG--------WRPPVLTTSAVRGEGIDELWDAI 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2378373656 262 CEFKALQTQNGRFAERRQHQALSWMWERIDAGLKQAFRAQP 302
Cdd:pfam03308 232 EEHREVLTATGLIEARRRAQVVRWLRELVEDDLLDRVKAAP 272
lao TIGR00750
LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of ...
 19-330 1.56e-110

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: 323.65  E-value: 1.56e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  19 RRAMAKAITLLESTRTDhralADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIAQGHRVAVLTIDPSSTVSG 98
Cdd:TIGR00750   3 RRALARAITLVENRHPE----AKELLDRIMPYTGNAHRVGITGTPGAGKSTLLEALGMELRRRGLRVAVIAVDPSSPFTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  99 GSILGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQSETAVANMTDMFVLLQLPN 178
Cdd:TIGR00750  79 GSILGDRTRMQRLATDPGAFIRSMPTRGHLGGLSQATRELVLLLDAAGYDVIIVETVGVGQSEVDIANMADTFVLVTIPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 179 AGDDLQAIKKGVMEIADLVVINKADID-ATAATRAQLQITSALQLLGmhggaghahRNTEVWHPKVVQLSALLNQGVDAF 257
Cdd:TIGR00750 159 TGDDLQGIKAGVMEIADIYVVNKADGEgATNVRIARLMLSLALEEIR---------RREDGWRPPVLTTSAVEGRGIDEL 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2378373656 258 WAAVCEFKALQTQNGRFAERRQHQALSWMWERIDAGLKQAFRAQPRVQTllpQLSQHVASGQLAASTAARQLL 330
Cdd:TIGR00750 230 WDAIEEHKTFLTASGLLQERRRQRSVEWLKKLVEEEVLKKVFANEDVYR---DLLLAVLAGELDPYTAAEQIL 299
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 53-120 1.83e-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: 38.12  E-value: 1.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2378373656   53 KSFRLGISGVPGVGKSTFIEALGLYLIAQGHRVAVLTIDPSSTVSGGSILGDKTRMEFLSVHAQAYIR 120
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLR 68
 
Name Accession Description Interval E-value
PRK09435 PRK09435
methylmalonyl Co-A mutase-associated GTPase MeaB;
1-334 0e+00

methylmalonyl Co-A mutase-associated GTPase MeaB;


Pssm-ID: 236515  Cd Length: 332  Bit Score: 556.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656   1 MTPEQLLDGLLRGNAAVQRRAMAKAITLLESTRTDHRALADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIA 80
Cdd:PRK09435    3 MRRELDVDELVEGVLAGDRAALARAITLVESTRPDHRALAQELLDALLPHTGNALRIGITGVPGVGKSTFIEALGMHLIE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  81 QGHRVAVLTIDPSSTVSGGSILGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQS 160
Cdd:PRK09435   83 QGHKVAVLAVDPSSTRTGGSILGDKTRMERLSRHPNAFIRPSPSSGTLGGVARKTRETMLLCEAAGYDVILVETVGVGQS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 161 ETAVANMTDMFVLLQLPNAGDDLQAIKKGVMEIADLVVINKAD-IDATAATRAQLQITSALQLLGMHggaghahrnTEVW 239
Cdd:PRK09435  163 ETAVAGMVDFFLLLQLPGAGDELQGIKKGIMELADLIVINKADgDNKTAARRAAAEYRSALRLLRPK---------DPGW 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 240 HPKVVQLSALLNQGVDAFWAAVCEFKALQTQNGRFAERRQHQALSWMWERIDAGLKQAFRAQPRVQTLLPQLSQHVASGQ 319
Cdd:PRK09435  234 QPPVLTCSALEGEGIDEIWQAIEDHRAALTASGEFAARRREQQVDWMWEMVEEGLLDRLFADPAVRARLPELEAAVAAGT 313

                         330
                  ....*....|....*
gi 2378373656 320 LAASTAARQLLSAYQ 334
Cdd:PRK09435  314 LTPALAARQLLEAFG 328
ArgK COG1703
GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, ...
 1-333 4.45e-175

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


Pssm-ID: 441309  Cd Length: 317  Bit Score: 488.04  E-value: 4.45e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656   1 MTPEQLLDGLLRGNaavqRRAMAKAITLLESTRTDHraLADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIA 80
Cdd:COG1703     1 LDVEELVEGLLAGD----RRALARAITLVESRRPEH--LARELLKALLPHTGKAHRIGITGVPGAGKSTLIDALGLRLRE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  81 QGHRVAVLTIDPSSTVSGGSILGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQS 160
Cdd:COG1703    75 RGKRVAVLAVDPSSPFTGGAILGDRTRMEELARDPGVFIRSSASRGSLGGLARATREAILLLEAAGFDVIIVETVGVGQS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 161 ETAVANMTDMFVLLQLPNAGDDLQAIKKGVMEIADLVVINKADIDatAATRAQLQITSALQLLgmhggaghaHRNTEVWH 240
Cdd:COG1703   155 ETDVAGMADTFLLLLLPGAGDELQGIKAGIMEIADIIVVNKADGD--GAERAVRELRGALHLL---------RPAEPGWR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 241 PKVVQLSALLNQGVDAFWAAVCEFKALQTQNGRFAERRQHQALSWMWERIDAGLKQAFRAQPRVQTLLPQLSQHVASGQL 320
Cdd:COG1703   224 PPVLTTSALTGEGIDELWEAIEEHRAYLKESGELEERRREQARRWLWELVRERLRERFREQPEVRARLDELEEAVLAGEL 303

                         330
                  ....*....|...
gi 2378373656 321 AASTAARQLLSAY 333
Cdd:COG1703   304 DPYAAADELLEAL 316
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 6-266 1.68e-124

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: 357.27  E-value: 1.68e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656   6 LLDGLLRGnaavQRRAMAKAITLLESTRTDHRALADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIAQGHRV 85
Cdd:cd03114     2 LIAGLRSG----DRRALARAITLVESGRPDHRELAQELLDALLPQAGRAFRVGITGPPGAGKSTLIEALGRLLREQGHRV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  86 AVLTIDPSSTVSGGSILGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQSETAVA 165
Cdd:cd03114    78 AVLAVDPSSPRSGGSILGDKTRMQRLARDPNAFIRPSPSRGTLGGVARATREAILLCEAAGYDVVLVETVGVGQSEVAVA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 166 NMTDMFVLLQLPNAGDDLQAIKKGVMEIADLVVINKADID-ATAATRAQLQITSALQLLgmhggaghaHRNTEVWHPKVV 244
Cdd:cd03114   158 DMVDTFVLLLPPGGGDELQGIKAGIMEIADLVVVNKADGDlKTGARRAQRELTSALKLL---------RPRSDGWRPPVL 228

                         250       260
                  ....*....|....*....|..
gi 2378373656 245 QLSALLNQGVDAFWAAVCEFKA 266
Cdd:cd03114   229 RTSALTGEGIDELWEAIEEHRA 250
MeaB pfam03308
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
 22-302 8.76e-120

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: 345.96  E-value: 8.76e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  22 MAKAITLLESTRTDHRALADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIAQGHRVAVLTIDPSSTVSGGSI 101
Cdd:pfam03308   1 LARAITLVESRRPDHQAEARELLRRLMPRAGRAHRVGVTGVPGAGKSTLIEALGMELRRRGHRVAVLAVDPSSPRTGGSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 102 LGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQSETAVANMTDMFVLLQLPNAGD 181
Cdd:pfam03308  81 LGDKTRMDRLAVDPGAFIRPSPSRGALGGLSRKTREVVLLLEAAGFDVIIIETVGVGQSEVDVANMVDTFVLLTMPGGGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 182 DLQAIKKGVMEIADLVVINKADIDATAATRAQLQITSALQLLgMHGGAGhahrntevWHPKVVQLSALLNQGVDAFWAAV 261
Cdd:pfam03308 161 ELQGIKAGIMEIADIYVVNKADGNLPGAERAARELRAALHLL-TPFEAG--------WRPPVLTTSAVRGEGIDELWDAI 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2378373656 262 CEFKALQTQNGRFAERRQHQALSWMWERIDAGLKQAFRAQP 302
Cdd:pfam03308 232 EEHREVLTATGLIEARRRAQVVRWLRELVEDDLLDRVKAAP 272
lao TIGR00750
LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of ...
 19-330 1.56e-110

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: 323.65  E-value: 1.56e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  19 RRAMAKAITLLESTRTDhralADDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIAQGHRVAVLTIDPSSTVSG 98
Cdd:TIGR00750   3 RRALARAITLVENRHPE----AKELLDRIMPYTGNAHRVGITGTPGAGKSTLLEALGMELRRRGLRVAVIAVDPSSPFTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  99 GSILGDKTRMEFLSVHAQAYIRPSPSSGTLGGVAEKTRESMLVCEAAGYDVVIVETVGVGQSETAVANMTDMFVLLQLPN 178
Cdd:TIGR00750  79 GSILGDRTRMQRLATDPGAFIRSMPTRGHLGGLSQATRELVLLLDAAGYDVIIVETVGVGQSEVDIANMADTFVLVTIPG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 179 AGDDLQAIKKGVMEIADLVVINKADID-ATAATRAQLQITSALQLLGmhggaghahRNTEVWHPKVVQLSALLNQGVDAF 257
Cdd:TIGR00750 159 TGDDLQGIKAGVMEIADIYVVNKADGEgATNVRIARLMLSLALEEIR---------RREDGWRPPVLTTSAVEGRGIDEL 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2378373656 258 WAAVCEFKALQTQNGRFAERRQHQALSWMWERIDAGLKQAFRAQPRVQTllpQLSQHVASGQLAASTAARQLL 330
Cdd:TIGR00750 230 WDAIEEHKTFLTASGLLQERRRQRSVEWLKKLVEEEVLKKVFANEDVYR---DLLLAVLAGELDPYTAAEQIL 299
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 59-201 5.28e-05

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: 41.65  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  59 ISGVPGVGKSTFIEALGLYLIAQGHRVAVLTIDpsstvsggsilgdktrmeflsvhaqayirpspssgtlggvaektres 138
Cdd:cd01983     6 TGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD----------------------------------------------- 38

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2378373656 139 mlvceaagyDVVIVETVGVGQSETA--------VANMTDMFVLLQLPNAGDDLQAIKKGVMEIA-------DLVVINK 201
Cdd:cd01983    39 ---------DYVLIDGGGGLETGLLlgtivallALKKADEVIVVVDPELGSLLEAVKLLLALLLlgigirpDGIVLNK 107
TMPK cd01672
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ...
 59-118 6.51e-05

Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).


Pssm-ID: 238835  Cd Length: 200  Bit Score: 43.41  E-value: 6.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  59 ISGVPGVGKSTFIEALGLYLIAQGHRVaVLTIDPsstvsGGSILGDKTRMEFLSVHAQAY 118
Cdd:cd01672     5 FEGIDGAGKTTLIELLAERLEARGYEV-VLTREP-----GGTPIGEAIRELLLDPEDEKM 58
Thymidylate_kin pfam02223
Thymidylate kinase;
59-118 2.78e-04

Thymidylate kinase;


Pssm-ID: 396690  Cd Length: 184  Bit Score: 41.13  E-value: 2.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  59 ISGVPGVGKSTFIEALGLYLIAQGHRVaVLTIDPSSTVSGGSILGDKTRMEFLSVHAQAY 118
Cdd:pfam02223   1 IEGLDGAGKTTQAELLKERLKEQGIKV-VFTREPGGTPIGEKIRELLLRNEELSPLTEAL 59
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 64-209 6.80e-04

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 40.41  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  64 GVGKSTFIEALGLYLIAQGHRVAVLTIDPSSTVS---------------------GGSILGDKTRMEFLSVHAQAYIRPS 122
Cdd:pfam01656   9 GVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsveglegdiapalqalaeglkGRVNLDPILLKEKSDEGGLDLIPGN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656 123 PSSGTLGGVAEKTRESMLVCEA-----AGYDVVIVETV-GVG-QSETAVANMTDMFVLLQLP--------NAGDDLQAIK 187
Cdd:pfam01656  89 IDLEKFEKELLGPRKEERLREAlealkEDYDYVIIDGApGLGeLLRNALIAADYVIIPLEPEvilvedakRLGGVIAALV 168

                         170       180
                  ....*....|....*....|....*
gi 2378373656 188 KGVMEIADL---VVINKADIDATAA 209
Cdd:pfam01656 169 GGYALLGLKiigVVLNKVDGDNHGK 193
PRK07667 PRK07667
uridine kinase; Provisional
 41-91 7.21e-04

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 40.10  E-value: 7.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2378373656  41 DDLLTAMLPHTGKSFRLGISGVPGVGKSTFIEALGLYLIAQGHRVAVLTID 91
Cdd:PRK07667    4 NELINIMKKHKENRFILGIDGLSRSGKTTFVANLKENMKQEGIPFHIFHID 54
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 61-156 7.82e-04

GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 40.05  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  61 GVPGVGKSTFIEALGLYLIAQGHRVAVLTIDpssTVSGGSIlgdktrmEFLSVHAQAYIRPSPSSGTLGGVAEKTRESML 140
Cdd:cd03115     7 GLQGSGKTTTLAKLARYYQEKGKKVLLIAAD---TFRAAAV-------EQLKTLAEKLGVPVFESYTGTDPASIAQEAVE 76

                          90
                  ....*....|....*.
gi 2378373656 141 VCEAAGYDVVIVETVG 156
Cdd:cd03115    77 KAKLEGYDVLLVDTAG 92
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 53-120 1.83e-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: 38.12  E-value: 1.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2378373656   53 KSFRLGISGVPGVGKSTFIEALGLYLIAQGHRVAVLTIDPSSTVSGGSILGDKTRMEFLSVHAQAYIR 120
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLR 68
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
 61-156 2.05e-03

GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349786  Cd Length: 193  Bit Score: 38.73  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  61 GVPGVGKSTFIEALGLYLIAQGHRVAVLTID---PSStVSGGSILGDKTRMEFLSVHAQAyirpspssgtlgGVAEKTRE 137
Cdd:cd18539     7 GLQGSGKTTTAAKLALYLKKKGKKVLLVAADvyrPAA-IEQLQTLGEQVGVPVFESGDGQ------------SPVDIAKR 73

                          90
                  ....*....|....*....
gi 2378373656 138 SMLVCEAAGYDVVIVETVG 156
Cdd:cd18539    74 ALEKAKEEGFDVVIVDTAG 92
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
64-97 3.68e-03

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 38.65  E-value: 3.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2378373656  64 GVGKSTFIEALGLYLIAQGHRVAVLTIDPSSTVS 97
Cdd:COG0003    13 GVGKTTVAAATALALAERGKRTLLVSTDPAHSLG 46
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 59-97 5.11e-03

Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.


Pssm-ID: 396792  Cd Length: 302  Bit Score: 38.10  E-value: 5.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2378373656  59 ISGVPGVGKSTFIEALGLYLIAQGHRVAVLTIDPSSTVS 97
Cdd:pfam02374   6 FGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLS 44
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 61-163 6.19e-03

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 37.14  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2378373656  61 GVPGVGKSTFIEALGLYLIAQGHRVAVLTIDpssTVSGGSIlgdktrmEFLSVHAQAYIRPSPSSGTLGGVAEKTRESML 140
Cdd:pfam00448   7 GLQGSGKTTTIAKLAAYLKKKGKKVLLVAAD---TFRAAAI-------EQLKQLAEKLGVPVFGSKTGADPAAVAFDAVE 76

                          90       100
                  ....*....|....*....|...
gi 2378373656 141 VCEAAGYDVVIVETVGVGQSETA 163
Cdd:pfam00448  77 KAKAENYDVVLVDTAGRLQNDKN 99
PRK13768 PRK13768
GTPase; Provisional
 59-92 7.10e-03

GTPase; Provisional


Pssm-ID: 237498 [Multi-domain]  Cd Length: 253  Bit Score: 37.54  E-value: 7.10e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2378373656  59 ISGVPGVGKSTFIEALGLYLIAQGHRVAVLTIDP 92
Cdd:PRK13768    7 FLGTAGSGKTTLTKALSDWLEEQGYDVAIVNLDP 40
GPN2 cd17871
GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization ...
 61-92 7.17e-03

GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). It forms heterodimers with GPN1 or GPN3.


Pssm-ID: 349780  Cd Length: 196  Bit Score: 37.13  E-value: 7.17e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2378373656  61 GVPGVGKSTFIEALGLYLIAQGHRVAVLTIDP 92
Cdd:cd17871     7 GPPGSGKTTYCKGMQQFLSALGRKVAVVNLDP 38
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 49-91 9.08e-03

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 36.74  E-value: 9.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2378373656  49 PHTGKSFRLGISGVPGVGKSTFIEALGLYLiaQGHRVAVLTID 91
Cdd:COG0572     2 ARSGKPRIIGIAGPSGSGKTTFARRLAEQL--GADKVVVISLD 42
Tmk COG0125
Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the ...
 59-107 9.10e-03

Thymidylate kinase [Nucleotide transport and metabolism]; Thymidylate kinase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 439895 [Multi-domain]  Cd Length: 206  Bit Score: 37.06  E-value: 9.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2378373656  59 ISGVPGVGKSTFIEALGLYLIAQGHRVaVLTIDPsstvsGGSILGDKTR 107
Cdd:COG0125     8 FEGIDGSGKSTQIKLLAEYLEARGYDV-VLTREP-----GGTPLGEAIR 50
 
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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