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Conserved domains on  [gi|1720426140|ref|XP_030099097|]
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methylmalonic aciduria type A homolog, mitochondrial isoform X2 [Mus musculus]

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 ...
1-252 8.70e-140

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: 395.34  E-value: 8.70e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   1 MLTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVG 80
Cdd:PRK09435   79 HLIEQGHKVAVLAVDPSSTRTGGSILGDKTRMERLSRHPNAFIRPSPSSGTLGGVARKTRETMLLCEAAGYDVILVETVG 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  81 VGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDLIVPARRIQAEYVSALKLLRRRSEVWRPKVI 160
Cdd:PRK09435  159 VGQSETAVAGMVDFFLLLQLPGAGDELQGIKKGIMELADLIVINKADGDNKTAARRAAAEYRSALRLLRPKDPGWQPPVL 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140 161 RISARSGEGITEMWDTMREFQHQMLASGELAAKRQTQHKVWMWNLIQENVLEHFKTHPSIREQIPLMERKVLSGALSPGR 240
Cdd:PRK09435  239 TCSALEGEGIDEIWQAIEDHRAALTASGEFAARRREQQVDWMWEMVEEGLLDRLFADPAVRARLPELEAAVAAGTLTPAL 318
                         250
                  ....*....|..
gi 1720426140 241 AADLLLKAFKSR 252
Cdd:PRK09435  319 AARQLLEAFGLQ 330
 
Name Accession Description Interval E-value
PRK09435 PRK09435
methylmalonyl Co-A mutase-associated GTPase MeaB;
1-252 8.70e-140

methylmalonyl Co-A mutase-associated GTPase MeaB;


Pssm-ID: 236515  Cd Length: 332  Bit Score: 395.34  E-value: 8.70e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   1 MLTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVG 80
Cdd:PRK09435   79 HLIEQGHKVAVLAVDPSSTRTGGSILGDKTRMERLSRHPNAFIRPSPSSGTLGGVARKTRETMLLCEAAGYDVILVETVG 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  81 VGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDLIVPARRIQAEYVSALKLLRRRSEVWRPKVI 160
Cdd:PRK09435  159 VGQSETAVAGMVDFFLLLQLPGAGDELQGIKKGIMELADLIVINKADGDNKTAARRAAAEYRSALRLLRPKDPGWQPPVL 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140 161 RISARSGEGITEMWDTMREFQHQMLASGELAAKRQTQHKVWMWNLIQENVLEHFKTHPSIREQIPLMERKVLSGALSPGR 240
Cdd:PRK09435  239 TCSALEGEGIDEIWQAIEDHRAALTASGEFAARRREQQVDWMWEMVEEGLLDRLFADPAVRARLPELEAAVAAGTLTPAL 318
                         250
                  ....*....|..
gi 1720426140 241 AADLLLKAFKSR 252
Cdd:PRK09435  319 AARQLLEAFGLQ 330
ArgK COG1703
GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, ...
1-250 1.73e-124

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


Pssm-ID: 441309  Cd Length: 317  Bit Score: 356.31  E-value: 1.73e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   1 MLTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVG 80
Cdd:COG1703    71 RLRERGKRVAVLAVDPSSPFTGGAILGDRTRMEELARDPGVFIRSSASRGSLGGLARATREAILLLEAAGFDVIIVETVG 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  81 VGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDlivPARRIQAEYVSALKLLRRRSEVWRPKVI 160
Cdd:COG1703   151 VGQSETDVAGMADTFLLLLLPGAGDELQGIKAGIMEIADIIVVNKADGD---GAERAVRELRGALHLLRPAEPGWRPPVL 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140 161 RISARSGEGITEMWDTMREFQHQMLASGELAAKRQTQHKVWMWNLIQENVLEHFKTHPSIREQIPLMERKVLSGALSPGR 240
Cdd:COG1703   228 TTSALTGEGIDELWEAIEEHRAYLKESGELEERRREQARRWLWELVRERLRERFREQPEVRARLDELEEAVLAGELDPYA 307
                         250
                  ....*....|
gi 1720426140 241 AADLLLKAFK 250
Cdd:COG1703   308 AADELLEALL 317
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
1-181 5.50e-114

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: 327.22  E-value: 5.50e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   1 MLTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVG 80
Cdd:cd03114    69 LLREQGHRVAVLAVDPSSPRSGGSILGDKTRMQRLARDPNAFIRPSPSRGTLGGVARATREAILLCEAAGYDVVLVETVG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  81 VGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDLIVPARRIQAEYVSALKLLRRRSEVWRPKVI 160
Cdd:cd03114   149 VGQSEVAVADMVDTFVLLLPPGGGDELQGIKAGIMEIADLVVVNKADGDLKTGARRAQRELTSALKLLRPRSDGWRPPVL 228
                         170       180
                  ....*....|....*....|.
gi 1720426140 161 RISARSGEGITEMWDTMREFQ 181
Cdd:cd03114   229 RTSALTGEGIDELWEAIEEHR 249
MeaB pfam03308
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
2-218 2.98e-93

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: 275.47  E-value: 2.98e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   2 LTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVGV 81
Cdd:pfam03308  57 LRRRGHRVAVLAVDPSSPRTGGSILGDKTRMDRLAVDPGAFIRPSPSRGALGGLSRKTREVVLLLEAAGFDVIIIETVGV 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  82 GQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDLiVPARRIQAEYVSALKLLRRRSEVWRPKVIR 161
Cdd:pfam03308 137 GQSEVDVANMVDTFVLLTMPGGGDELQGIKAGIMEIADIYVVNKADGNL-PGAERAARELRAALHLLTPFEAGWRPPVLT 215
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426140 162 ISARSGEGITEMWDTMREFQHQMLASGELAAKRQTQHKVWMWNLIQENVLEHFKTHP 218
Cdd:pfam03308 216 TSAVRGEGIDELWDAIEEHREVLTATGLIEARRRAQVVRWLRELVEDDLLDRVKAAP 272
lao TIGR00750
LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of ...
2-247 3.34e-90

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: 268.57  E-value: 3.34e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   2 LTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVGV 81
Cdd:TIGR00750  58 LRRRGLRVAVIAVDPSSPFTGGSILGDRTRMQRLATDPGAFIRSMPTRGHLGGLSQATRELVLLLDAAGYDVIIVETVGV 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  82 GQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDLIVPARRIQAEYVSALKLLRRRSEVWRPKVIR 161
Cdd:TIGR00750 138 GQSEVDIANMADTFVLVTIPGTGDDLQGIKAGVMEIADIYVVNKADGEGATNVRIARLMLSLALEEIRRREDGWRPPVLT 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140 162 ISARSGEGITEMWDTMREFQHQMLASGELAAKRQTQHKVWMWNLIQENVLEHFKTHPSIREQIplmERKVLSGALSPGRA 241
Cdd:TIGR00750 218 TSAVEGRGIDELWDAIEEHKTFLTASGLLQERRRQRSVEWLKKLVEEEVLKKVFANEDVYRDL---LLAVLAGELDPYTA 294

                  ....*.
gi 1720426140 242 ADLLLK 247
Cdd:TIGR00750 295 AEQILE 300
 
Name Accession Description Interval E-value
PRK09435 PRK09435
methylmalonyl Co-A mutase-associated GTPase MeaB;
1-252 8.70e-140

methylmalonyl Co-A mutase-associated GTPase MeaB;


Pssm-ID: 236515  Cd Length: 332  Bit Score: 395.34  E-value: 8.70e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   1 MLTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVG 80
Cdd:PRK09435   79 HLIEQGHKVAVLAVDPSSTRTGGSILGDKTRMERLSRHPNAFIRPSPSSGTLGGVARKTRETMLLCEAAGYDVILVETVG 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  81 VGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDLIVPARRIQAEYVSALKLLRRRSEVWRPKVI 160
Cdd:PRK09435  159 VGQSETAVAGMVDFFLLLQLPGAGDELQGIKKGIMELADLIVINKADGDNKTAARRAAAEYRSALRLLRPKDPGWQPPVL 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140 161 RISARSGEGITEMWDTMREFQHQMLASGELAAKRQTQHKVWMWNLIQENVLEHFKTHPSIREQIPLMERKVLSGALSPGR 240
Cdd:PRK09435  239 TCSALEGEGIDEIWQAIEDHRAALTASGEFAARRREQQVDWMWEMVEEGLLDRLFADPAVRARLPELEAAVAAGTLTPAL 318
                         250
                  ....*....|..
gi 1720426140 241 AADLLLKAFKSR 252
Cdd:PRK09435  319 AARQLLEAFGLQ 330
ArgK COG1703
GTPase of the G3E family (not a periplasmic protein kinase) [Posttranslational modification, ...
1-250 1.73e-124

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


Pssm-ID: 441309  Cd Length: 317  Bit Score: 356.31  E-value: 1.73e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   1 MLTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVG 80
Cdd:COG1703    71 RLRERGKRVAVLAVDPSSPFTGGAILGDRTRMEELARDPGVFIRSSASRGSLGGLARATREAILLLEAAGFDVIIVETVG 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  81 VGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDlivPARRIQAEYVSALKLLRRRSEVWRPKVI 160
Cdd:COG1703   151 VGQSETDVAGMADTFLLLLLPGAGDELQGIKAGIMEIADIIVVNKADGD---GAERAVRELRGALHLLRPAEPGWRPPVL 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140 161 RISARSGEGITEMWDTMREFQHQMLASGELAAKRQTQHKVWMWNLIQENVLEHFKTHPSIREQIPLMERKVLSGALSPGR 240
Cdd:COG1703   228 TTSALTGEGIDELWEAIEEHRAYLKESGELEERRREQARRWLWELVRERLRERFREQPEVRARLDELEEAVLAGELDPYA 307
                         250
                  ....*....|
gi 1720426140 241 AADLLLKAFK 250
Cdd:COG1703   308 AADELLEALL 317
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
1-181 5.50e-114

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: 327.22  E-value: 5.50e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   1 MLTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVG 80
Cdd:cd03114    69 LLREQGHRVAVLAVDPSSPRSGGSILGDKTRMQRLARDPNAFIRPSPSRGTLGGVARATREAILLCEAAGYDVVLVETVG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  81 VGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDLIVPARRIQAEYVSALKLLRRRSEVWRPKVI 160
Cdd:cd03114   149 VGQSEVAVADMVDTFVLLLPPGGGDELQGIKAGIMEIADLVVVNKADGDLKTGARRAQRELTSALKLLRPRSDGWRPPVL 228
                         170       180
                  ....*....|....*....|.
gi 1720426140 161 RISARSGEGITEMWDTMREFQ 181
Cdd:cd03114   229 RTSALTGEGIDELWEAIEEHR 249
MeaB pfam03308
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
2-218 2.98e-93

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: 275.47  E-value: 2.98e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   2 LTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVGV 81
Cdd:pfam03308  57 LRRRGHRVAVLAVDPSSPRTGGSILGDKTRMDRLAVDPGAFIRPSPSRGALGGLSRKTREVVLLLEAAGFDVIIIETVGV 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  82 GQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDLiVPARRIQAEYVSALKLLRRRSEVWRPKVIR 161
Cdd:pfam03308 137 GQSEVDVANMVDTFVLLTMPGGGDELQGIKAGIMEIADIYVVNKADGNL-PGAERAARELRAALHLLTPFEAGWRPPVLT 215
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426140 162 ISARSGEGITEMWDTMREFQHQMLASGELAAKRQTQHKVWMWNLIQENVLEHFKTHP 218
Cdd:pfam03308 216 TSAVRGEGIDELWDAIEEHREVLTATGLIEARRRAQVVRWLRELVEDDLLDRVKAAP 272
lao TIGR00750
LAO/AO transport system ATPase; In E. coli, mutation of this kinase blocks phosphorylation of ...
2-247 3.34e-90

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: 268.57  E-value: 3.34e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140   2 LTEQGHRLSVLAVDPSSCTSGGSLLGDKTRMIELSRDMNAYIRPSPTSGTLGGVTRTTNEAIVLCEGGGYDIILIETVGV 81
Cdd:TIGR00750  58 LRRRGLRVAVIAVDPSSPFTGGSILGDRTRMQRLATDPGAFIRSMPTRGHLGGLSQATRELVLLLDAAGYDVIIVETVGV 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  82 GQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVVITKSDGDLIVPARRIQAEYVSALKLLRRRSEVWRPKVIR 161
Cdd:TIGR00750 138 GQSEVDIANMADTFVLVTIPGTGDDLQGIKAGVMEIADIYVVNKADGEGATNVRIARLMLSLALEEIRRREDGWRPPVLT 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140 162 ISARSGEGITEMWDTMREFQHQMLASGELAAKRQTQHKVWMWNLIQENVLEHFKTHPSIREQIplmERKVLSGALSPGRA 241
Cdd:TIGR00750 218 TSAVEGRGIDELWDAIEEHKTFLTASGLLQERRRQRSVEWLKKLVEEEVLKKVFANEDVYRDL---LLAVLAGELDPYTA 294

                  ....*.
gi 1720426140 242 ADLLLK 247
Cdd:TIGR00750 295 AEQILE 300
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
70-172 2.78e-06

Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 46.59  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426140  70 GYDIILIETVG--VGQSEFAVAdmVDMFVLLLPPAGGDELQgIKRG-IIEMADLVVITKsdGDLivparriqAEYVSA-L 145
Cdd:COG0378    93 DLDLLFIENVGnlVCPAFFPLG--EDLKVVVLSVTEGDDKP-RKYPpMFTAADLLVINK--IDL--------APYVGFdL 159
                          90       100
                  ....*....|....*....|....*....
gi 1720426140 146 KLLRRRSEVWRP--KVIRISARSGEGITE 172
Cdd:COG0378   160 EVMEEDARRVNPgaPIFEVSAKTGEGLDE 188
 
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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