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Conserved domains on  [gi|499779743|ref|WP_011460477|]
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carbon monoxide dehydrogenase accessory protein CooC [Desulfitobacterium hafniense]

Protein Classification

similar to ATP-binding protein MJ0823( domain architecture ID 11466539)

protein similar to ATP-binding protein MJ0823

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-252 1.12e-126

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 359.48  E-value: 1.12e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIPEEnYRGITPFAKMKALAEERTGADGGygTFF 80
Cdd:COG3640    1 MKIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVE-ADLIKPLGEMRELIKERTGAPGG--GMF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  81 ILNPKVDDLPEQFCVEHEGIKLLLMGTVEQGGSGCVCPEHTLIKRLMQHLLVQRDEVVIMDMEAGIEHLGRGTAGAVDAL 160
Cdd:COG3640   78 KLNPKVDDIPEEYLVEGDGVDLLVMGTIEEGGSGCYCPENALLRALLNHLVLGNYEYVVVDMEAGIEHLGRGTAEGVDLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 161 IVVVEPGRRSVQTARQIQELAHDLGIQRVFMVASKVRSTEDLAFVgEALSDFPLLGHVTFSREIMDADLEGKALFDLGGE 240
Cdd:COG3640  158 LVVSEPSRRSIETARRIKELAEELGIKKIYLVGNKVREEEDEEFL-RELLGLELLGFIPYDEEVREADLEGKPLLDLPDS 236

                        250
                 ....*....|...
gi 499779743 241 P-VAEIRKIKENL 252
Cdd:COG3640  237 PaVAAVEEIAEKL 249
 
Name Accession Description Interval E-value
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-252 1.12e-126

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 359.48  E-value: 1.12e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIPEEnYRGITPFAKMKALAEERTGADGGygTFF 80
Cdd:COG3640    1 MKIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVE-ADLIKPLGEMRELIKERTGAPGG--GMF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  81 ILNPKVDDLPEQFCVEHEGIKLLLMGTVEQGGSGCVCPEHTLIKRLMQHLLVQRDEVVIMDMEAGIEHLGRGTAGAVDAL 160
Cdd:COG3640   78 KLNPKVDDIPEEYLVEGDGVDLLVMGTIEEGGSGCYCPENALLRALLNHLVLGNYEYVVVDMEAGIEHLGRGTAEGVDLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 161 IVVVEPGRRSVQTARQIQELAHDLGIQRVFMVASKVRSTEDLAFVgEALSDFPLLGHVTFSREIMDADLEGKALFDLGGE 240
Cdd:COG3640  158 LVVSEPSRRSIETARRIKELAEELGIKKIYLVGNKVREEEDEEFL-RELLGLELLGFIPYDEEVREADLEGKPLLDLPDS 236

                        250
                 ....*....|...
gi 499779743 241 P-VAEIRKIKENL 252
Cdd:COG3640  237 PaVAAVEEIAEKL 249
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-252 2.07e-110

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 318.49  E-value: 2.07e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIPEEnyrgITPFAKMKALAEERTGADGG-YGTF 79
Cdd:cd02034    1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVE----KLPLIKTIGDIRERTGAKKGePPEG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  80 FILNPKVDDLPEQFCVEHEGIKLLLMGTVEQGGSGCVCPEHTLIKRLMQHLLVQRDEVVIMDMEAGIEHLGRGTAGAVDA 159
Cdd:cd02034   77 MSLNPYVDDIIKEIIVEPDGIDLLVMGRPEGGGSGCYCPVNALLRELLRHLALKNYEYVVIDMEAGIEHLSRGTIRAVDL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 160 LIVVVEPGRRSVQTARQIQELAHDLGIQRVFMVASKVRSTEDLAFVGEALSDFPLLGHVTFSREIMDADLEGKALFDLGG 239
Cdd:cd02034  157 LIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRNEEEQELIEELLIKLKLIGVIPYDEEIMEADLKGKPLFDLDS 236

                        250
                 ....*....|...
gi 499779743 240 EPVAEIRKIKENL 252
Cdd:cd02034  237 AAVKAIEKIVEKL 249
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-232 1.64e-31

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: 115.91  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743    3 IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIpeENYRGITPfakmKALAEERTGadggygtFFI 81
Cdd:pfam01656   1 IAIAGtKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGL--EGDIAPAL----QALAEGLKG-------RVN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   82 LNPKVDDLPEQFCveheGIKLLLMGTVEQGGSGCVC--PEHTLIKRLMQHLLvQRDEVVIMDMEAGIEHLGRGTAGAVDA 159
Cdd:pfam01656  68 LDPILLKEKSDEG----GLDLIPGNIDLEKFEKELLgpRKEERLREALEALK-EDYDYVIIDGAPGLGELLRNALIAADY 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  160 LIVVVEPGRRSVQTARQIQELAHDLGIQ-------RVFMVASKVRS----TEDLAFVGEALSDFPLLGHVTFSREIMDAD 228
Cdd:pfam01656 143 VIIPLEPEVILVEDAKRLGGVIAALVGGyallglkIIGVVLNKVDGdnhgKLLKEALEELLRGLPVLGVIPRDEAVAEAP 222


                  ....
gi 499779743  229 LEGK 232
Cdd:pfam01656 223 ARGL 226
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-240 8.99e-13

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 67.39  E-value: 8.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   3 IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGI-PEENYRG-ITPFAKMKALAEERTGADGGYGTF 79
Cdd:PRK13869 124 IAVTNfKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVlPETDVGAnETLYAAIRYDDTRRPLRDVIRPTY 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  80 FI---LNPKVDDLPEqfcVEHEGIKLLLMGTVEQGgsgcvcpehTLIKRLMQHLLVQRD--EVVIMDMEAGIEHLGRGTA 154
Cdd:PRK13869 204 FDglhLVPGNLELME---FEHTTPKALSDKGTRDG---------LFFTRVAQAFDEVADdyDVVVIDCPPQLGFLTLSGL 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 155 GAVDALIVVVEPGRRSVQTARQIQELAHDL---------GIQRVFMVASKVR-------STEDLAFVGEALSDFPLLGHV 218
Cdd:PRK13869 272 CAATSMVITVHPQMLDIASMSQFLLMTRDLlgvvkeaggNLQYDFIRYLLTRyepqdapQTKVAALLRNMFEDHVLTNPM 351

                        250       260
                 ....*....|....*....|..
gi 499779743 219 TFSREIMDADLEGKALFDLGGE 240
Cdd:PRK13869 352 VKSAAVSDAGLTKQTLYEIGRE 373
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 3-55 1.97e-10

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 60.38  E-value: 1.97e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499779743    3 IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGI-PEENYRG 55
Cdd:TIGR03453 107 IAVTNfKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYqPEFDVGE 161
ParA_partition NF041546
ParA family partition ATPase;
3-38 1.98e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 56.02  E-value: 1.98e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 499779743   3 IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADP 38
Cdd:NF041546   2 IAVLNqKGGVGKTTLATHLAAALARRGYRVLLVDADP 38
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 6-49 3.33e-06

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 47.95  E-value: 3.33e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 499779743   6 TGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIP 49
Cdd:NF041417 339 TGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFGTE 382
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 6-47 1.63e-05

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 45.64  E-value: 1.63e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 499779743   6 TGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALG 47
Cdd:NF041417  18 SGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFG 59
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2-72 8.82e-04

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: 38.89  E-value: 8.82e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499779743     2 KIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIPEENYRGITPFAKMKALAEERTGA 72
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
 
Name Accession Description Interval E-value
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-252 1.12e-126

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 359.48  E-value: 1.12e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIPEEnYRGITPFAKMKALAEERTGADGGygTFF 80
Cdd:COG3640    1 MKIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVE-ADLIKPLGEMRELIKERTGAPGG--GMF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  81 ILNPKVDDLPEQFCVEHEGIKLLLMGTVEQGGSGCVCPEHTLIKRLMQHLLVQRDEVVIMDMEAGIEHLGRGTAGAVDAL 160
Cdd:COG3640   78 KLNPKVDDIPEEYLVEGDGVDLLVMGTIEEGGSGCYCPENALLRALLNHLVLGNYEYVVVDMEAGIEHLGRGTAEGVDLL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 161 IVVVEPGRRSVQTARQIQELAHDLGIQRVFMVASKVRSTEDLAFVgEALSDFPLLGHVTFSREIMDADLEGKALFDLGGE 240
Cdd:COG3640  158 LVVSEPSRRSIETARRIKELAEELGIKKIYLVGNKVREEEDEEFL-RELLGLELLGFIPYDEEVREADLEGKPLLDLPDS 236

                        250
                 ....*....|...
gi 499779743 241 P-VAEIRKIKENL 252
Cdd:COG3640  237 PaVAAVEEIAEKL 249
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-252 2.07e-110

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 318.49  E-value: 2.07e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIPEEnyrgITPFAKMKALAEERTGADGG-YGTF 79
Cdd:cd02034    1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVE----KLPLIKTIGDIRERTGAKKGePPEG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  80 FILNPKVDDLPEQFCVEHEGIKLLLMGTVEQGGSGCVCPEHTLIKRLMQHLLVQRDEVVIMDMEAGIEHLGRGTAGAVDA 159
Cdd:cd02034   77 MSLNPYVDDIIKEIIVEPDGIDLLVMGRPEGGGSGCYCPVNALLRELLRHLALKNYEYVVIDMEAGIEHLSRGTIRAVDL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 160 LIVVVEPGRRSVQTARQIQELAHDLGIQRVFMVASKVRSTEDLAFVGEALSDFPLLGHVTFSREIMDADLEGKALFDLGG 239
Cdd:cd02034  157 LIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRNEEEQELIEELLIKLKLIGVIPYDEEIMEADLKGKPLFDLDS 236

                        250
                 ....*....|...
gi 499779743 240 EPVAEIRKIKENL 252
Cdd:cd02034  237 AAVKAIEKIVEKL 249
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-232 1.64e-31

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: 115.91  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743    3 IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIpeENYRGITPfakmKALAEERTGadggygtFFI 81
Cdd:pfam01656   1 IAIAGtKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGL--EGDIAPAL----QALAEGLKG-------RVN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   82 LNPKVDDLPEQFCveheGIKLLLMGTVEQGGSGCVC--PEHTLIKRLMQHLLvQRDEVVIMDMEAGIEHLGRGTAGAVDA 159
Cdd:pfam01656  68 LDPILLKEKSDEG----GLDLIPGNIDLEKFEKELLgpRKEERLREALEALK-EDYDYVIIDGAPGLGELLRNALIAADY 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  160 LIVVVEPGRRSVQTARQIQELAHDLGIQ-------RVFMVASKVRS----TEDLAFVGEALSDFPLLGHVTFSREIMDAD 228
Cdd:pfam01656 143 VIIPLEPEVILVEDAKRLGGVIAALVGGyallglkIIGVVLNKVDGdnhgKLLKEALEELLRGLPVLGVIPRDEAVAEAP 222


                  ....
gi 499779743  229 LEGK 232
Cdd:pfam01656 223 ARGL 226
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-237 7.42e-17

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 77.59  E-value: 7.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   1 MK-IAVT-GKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIPEENyrgitpfakmkalaEERTGADggygt 78
Cdd:COG1192    1 MKvIAVAnQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDD--------------LDPTLYD----- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  79 FFILNPKVDDLPEQfcVEHEGIKLL-----LMGtVEQGGSGCVCPEHTLiKRLMQHLLVQRDeVVIMDMEAGIEHLGRGT 153
Cdd:COG1192   62 LLLDDAPLEDAIVP--TEIPGLDLIpanidLAG-AEIELVSRPGRELRL-KRALAPLADDYD-YILIDCPPSLGLLTLNA 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 154 AGAVDALIVVVEPGRRSVQTARQI--------QELAHDLGIQRVF--MVASKVRSTED-LAFVGEALSDFPLLGHVTFSR 222
Cdd:COG1192  137 LAAADSVLIPVQPEYLSLEGLAQLletieevrEDLNPKLEILGILltMVDPRTRLSREvLEELREEFGDKVLDTVIPRSV 216

                        250
                 ....*....|....*
gi 499779743 223 EIMDADLEGKALFDL 237
Cdd:COG1192  217 ALAEAPSAGKPVFEY 231
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 15-254 3.05e-14

MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440223 [Multi-domain]  Cd Length: 230  Bit Score: 69.92  E-value: 3.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  15 TLSGTLARLLAADGYRVLAVDADPD-ANLASALGIPEEnyrgitpfakmkalaeeRTGADggygtffILNPKVDdlPEQF 93
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLEPK-----------------ATLAD-------VLAGEAD--LEDA 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  94 CVEHE-GIKLLLMGTvEQGGSGCVCPEHTLIKRLmqHLLVQRDEVVIMDMEAGIEHLGRGTAGAVDALIVVVEPGRRSVQ 172
Cdd:COG0455   55 IVQGPgGLDVLPGGS-GPAELAELDPEERLIRVL--EELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSIT 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 173 -TARQIQELAHDLGIQRVFMVASKVRSTEDLAFVGEALS---------DFPLLGHVTFSREIMDADLEGKALFD--LGGE 240
Cdd:COG0455  132 dAYALLKLLRRRLGVRRAGVVVNRVRSEAEARDVFERLEqvaerflgvRLRVLGVIPEDPAVREAVRRGRPLVLaaPDSP 211

                        250
                 ....*....|....
gi 499779743 241 PVAEIRKIKENLIQ 254
Cdd:COG0455  212 AARAIRELAARLAG 225
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-46 8.34e-14

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 66.41  E-value: 8.34e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499779743   1 MKIAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASAL 46
Cdd:cd02042    1 KVIAVANqKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL 47
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-240 8.99e-13

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 67.39  E-value: 8.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   3 IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGI-PEENYRG-ITPFAKMKALAEERTGADGGYGTF 79
Cdd:PRK13869 124 IAVTNfKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVlPETDVGAnETLYAAIRYDDTRRPLRDVIRPTY 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  80 FI---LNPKVDDLPEqfcVEHEGIKLLLMGTVEQGgsgcvcpehTLIKRLMQHLLVQRD--EVVIMDMEAGIEHLGRGTA 154
Cdd:PRK13869 204 FDglhLVPGNLELME---FEHTTPKALSDKGTRDG---------LFFTRVAQAFDEVADdyDVVVIDCPPQLGFLTLSGL 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 155 GAVDALIVVVEPGRRSVQTARQIQELAHDL---------GIQRVFMVASKVR-------STEDLAFVGEALSDFPLLGHV 218
Cdd:PRK13869 272 CAATSMVITVHPQMLDIASMSQFLLMTRDLlgvvkeaggNLQYDFIRYLLTRyepqdapQTKVAALLRNMFEDHVLTNPM 351

                        250       260
                 ....*....|....*....|..
gi 499779743 219 TFSREIMDADLEGKALFDLGGE 240
Cdd:PRK13869 352 VKSAAVSDAGLTKQTLYEIGRE 373
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-48 3.05e-12

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 63.37  E-value: 3.05e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 499779743    1 MK-IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGI 48
Cdd:pfam13614   1 GKvIAIANqKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGI 50
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-206 4.37e-12

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 64.44  E-value: 4.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   3 IAVT-GKGGVGKTTLSGTLARLLAADGYRVLAVDADP-DANLASALGIpeENYRGITPFakmkaLAEERTGADggygtff 80
Cdd:COG0489   95 IAVTsGKGGEGKSTVAANLALALAQSGKRVLLIDADLrGPSLHRMLGL--ENRPGLSDV-----LAGEASLED------- 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  81 ILNPkvddlpeqfcVEHEGIKLLLMGTVEQGGSGCVcpEHTLIKRLMQHLLVQRDeVVIMDMEAGIEHL-GRGTAGAVDA 159
Cdd:COG0489  161 VIQP----------TEVEGLDVLPAGPLPPNPSELL--ASKRLKQLLEELRGRYD-YVIIDTPPGLGVAdATLLASLVDG 227

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 499779743 160 LIVVVEPGRRSVQTARQIQELAHDLGIQRVFMVASKVRSTEDLAFVG 206
Cdd:COG0489  228 VLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNMVCPKGERYYGG 274
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 3-49 2.00e-11

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 62.14  E-value: 2.00e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499779743   3 IAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIP 49
Cdd:cd02035    3 IFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQK 49
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
3-49 7.09e-11

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 60.99  E-value: 7.09e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499779743   3 IAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIP 49
Cdd:COG0003    6 IFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGTE 52
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 3-55 1.97e-10

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 60.38  E-value: 1.97e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499779743    3 IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGI-PEENYRG 55
Cdd:TIGR03453 107 IAVTNfKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQASLSALFGYqPEFDVGE 161
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-234 1.03e-09

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 57.21  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   3 IAVT-GKGGVGKTTLSGTLARLLAADGYRVLAVDADPD-ANLASALGIpeENyrgITPFAKMKALAEERTGADGGYGTFF 80
Cdd:cd02036    3 IVITsGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGlRNLDLILGL--EN---RIVYTLVDVLEGECRLEQALIKDKR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  81 ILNPKVddLPEQFCVEHEGIKlllmgtveqggsgcvcPEHtlIKRLMQhLLVQRDEVVIMDMEAGIEHLGRGTAGAVDAL 160
Cdd:cd02036   78 WENLYL--LPASQTRDKDALT----------------PEK--LEELVK-ELKDSFDFILIDSPAGIESGFINAIAPADEA 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 161 IVVVEPGRRSVQTARQIQELAHDLGIQRVFMVASKVR----------STEDLafvgEALSDFPLLGHVTFSREIMDADLE 230
Cdd:cd02036  137 IIVTNPEISSVRDADRVIGLLESKGIVNIGLIVNRYRpemvksgdmlSVEDI----QEILGIPLLGVIPEDPEVIVATNR 212


                 ....
gi 499779743 231 GKAL 234
Cdd:cd02036  213 GEPL 216
ParA_partition NF041546
ParA family partition ATPase;
3-38 1.98e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 56.02  E-value: 1.98e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 499779743   3 IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADP 38
Cdd:NF041546   2 IAVLNqKGGVGKTTLATHLAAALARRGYRVLLVDADP 38
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-201 1.36e-08

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 53.73  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   3 IAVT-GKGGVGKTTLSGTLARLLAADGYRVLAVDADPD-ANLASALGIPEEnyrgitpfakmKALaeertgadggyGTFF 80
Cdd:cd02038    3 IAVTsGKGGVGKTNVSANLALALSKLGKRVLLLDADLGlANLDILLGLAPK-----------KTL-----------GDVL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  81 ILNPKVDDLPeqfCVEHEGIKLLLmgtveqGGSGCV-----CPEH--TLIKRLMQhlLVQRDEVVIMDMEAGIEHLGRGT 153
Cdd:cd02038   61 KGRVSLEDII---VEGPEGLDIIP------GGSGMEelanlDPEQkaKLIEELSS--LESNYDYLLIDTGAGISRNVLDF 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 499779743 154 AGAVDALIVVVEPGRRSVQTA-RQIQELAHDLGIQRVFMVASKVRSTED 201
Cdd:cd02038  130 LLAADEVIVVTTPEPTSITDAyALIKVLSRRGGKKNFRLIVNMARSPKE 178
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-56 1.60e-08

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 53.89  E-value: 1.60e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499779743    1 MK-IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIPEENYRGI 56
Cdd:TIGR03371   1 MKvIAIVSvRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMDWSVRDGW 58
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 1-37 2.06e-08

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: 50.89  E-value: 2.06e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 499779743   1 MKIAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDAD 37
Cdd:cd01983    1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-37 9.93e-08

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 50.96  E-value: 9.93e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 499779743   2 KIAV-TGKGGVGKTTLSGTLARLLAADGYRVLAVDAD 37
Cdd:cd02037    2 IIAVlSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 3-227 1.74e-07

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 50.80  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743    3 IAVT-GKGGVGKTTLSGTLARLLAADGYRVLAVDADPD-ANLASALGIpeENyRGItpfakmkalaeertgadggYGTFF 80
Cdd:TIGR01968   4 IVITsGKGGVGKTTTTANLGTALARLGKKVVLIDADIGlRNLDLLLGL--EN-RIV-------------------YTLVD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   81 ILNPKVDdlPEQFCVEHEGIKLL-LMGTVEQGGSGCVCPEHtlIKRLMQHLLVQRDEVVImDMEAGIEHLGRGTAGAVDA 159
Cdd:TIGR01968  62 VVEGECR--LQQALIKDKRLKNLyLLPASQTRDKDAVTPEQ--MKKLVNELKEEFDYVII-DCPAGIESGFRNAVAPADE 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499779743  160 LIVVVEPGRRSVQTARQIQELAHDLGIQRVFMVASKVR----------STEDlafVGEALSdFPLLGHVTFSREIMDA 227
Cdd:TIGR01968 137 AIVVTTPEVSAVRDADRVIGLLEAKGIEKIHLIVNRLRpemvkkgdmlSVDD---VLEILS-IPLIGVIPEDEAIIVS 210
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 3-37 2.48e-07

Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 50.44  E-value: 2.48e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 499779743   3 IAVT-GKGGVGKTTLSGTLARLLAADGYRVLAVDAD 37
Cdd:COG2894    5 IVVTsGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-37 2.91e-07

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 50.14  E-value: 2.91e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 499779743    2 KIAVT-GKGGVGKTTLSGTLARLLAADGYRVLAVDAD 37
Cdd:pfam10609   5 VIAVAsGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 3-48 3.44e-07

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: 50.43  E-value: 3.44e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 499779743    3 IAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGI 48
Cdd:pfam02374   4 IFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQ 49
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 5-234 3.79e-07

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 49.73  E-value: 3.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743    5 VTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPD-ANLASALGIPEenyrgiTPFAKMKALAEERTGADGGYgtffiln 83
Cdd:TIGR01969   6 ASGKGGTGKTTITANLGVALAKLGKKVLALDADITmANLELILGMED------KPVTLHDVLAGEADIKDAIY------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   84 pkvddlpeqfcvEHEGIKLLLMGTVEQGGSGCVCPEhtLIKRLMQHlLVQRDEVVIMDMEAGIEHLGRGTAGAVDALIVV 163
Cdd:TIGR01969  73 ------------EGPFGVKVIPAGVSLEGLRKADPD--KLEDVLKE-IIDDTDFLLIDAPAGLERDAVTALAAADELLLV 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499779743  164 VEPGRRSVQTARQIQELAHDLGIQRVFMVASKVrsTEDLAFVG----EALSDFPLLGHVTFSREIMDADLEGKAL 234
Cdd:TIGR01969 138 VNPEISSITDALKTKIVAEKLGTAILGVVLNRV--TRDKTELGreeiETILEVPVLGVVPEDPEVRRAAAFGEPV 210
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 3-52 1.01e-06

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 47.95  E-value: 1.01e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499779743   3 IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADP-DANLASALGIPEEN 52
Cdd:cd05387   22 IAVTSaSPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPNEP 73
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 6-42 1.11e-06

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 49.32  E-value: 1.11e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 499779743    6 TGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANL 42
Cdd:TIGR04291   9 TGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNV 45
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
1-41 2.38e-06

4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;


Pssm-ID: 395090  Cd Length: 271  Bit Score: 47.44  E-value: 2.38e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 499779743    1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDAN 41
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKAD 41
PHA02518 PHA02518
ParA-like protein; Provisional
 1-45 2.40e-06

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 47.15  E-value: 2.40e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 499779743   1 MKIAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASA 45
Cdd:PHA02518   1 KIIAVLNqKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW 46
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 6-49 3.33e-06

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 47.95  E-value: 3.33e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 499779743   6 TGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIP 49
Cdd:NF041417 339 TGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFGTE 382
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 2-59 4.99e-06

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 46.61  E-value: 4.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499779743   2 KIAVT-GKGGVGKTTLSGTLARLLaadgYRVLAVDADPDA-NLASALGIP----EENYRGITPF 59
Cdd:cd03110    1 IIAVLsGKGGTGKTTITANLAVLL----YNVILVDCDVDApNLHLLLGPEpeeeEDFVGGKKAF 60
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 2-47 6.51e-06

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 46.30  E-value: 6.51e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 499779743   2 KIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALG 47
Cdd:PRK13230   3 KFCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLV 48
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 1-49 9.15e-06

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 45.58  E-value: 9.15e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDA----NLASALGIP 49
Cdd:cd02040    1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKAdstrLLLGGKAIP 53
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 1-38 1.37e-05

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 45.37  E-value: 1.37e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADP 38
Cdd:cd02032    1 LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDP 38
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 7-42 1.44e-05

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 45.85  E-value: 1.44e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 499779743    7 GKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANL 42
Cdd:TIGR04291 328 GKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHL 363
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 1-46 1.57e-05

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 45.05  E-value: 1.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASAL 46
Cdd:cd02117    1 ESIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLL 46
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 6-47 1.63e-05

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 45.64  E-value: 1.63e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 499779743   6 TGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALG 47
Cdd:NF041417  18 SGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFG 59
chlL CHL00072
photochlorophyllide reductase subunit L
 1-38 1.93e-05

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 45.11  E-value: 1.93e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADP 38
Cdd:CHL00072   1 MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDP 38
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 3-248 1.97e-05

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 45.11  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   3 IAVTG-KGGVGKTTLSGTLARLLAAD-GYRVLAVDAD-PDANLASALGIPEEnyRGITpfakmkALAEERTGADggyGTF 79
Cdd:COG4963  105 IAVVGaKGGVGATTLAVNLAWALAREsGRRVLLVDLDlQFGDVALYLDLEPR--RGLA------DALRNPDRLD---ETL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743  80 FilnpkvddlpEQFCVEHE-GIKLLLM-GTVEQGGSgcVCPEH--TLIKRLMQHLlvqrdEVVIMDMEAGIEHLGRGTAG 155
Cdd:COG4963  174 L----------DRALTRHSsGLSVLAApADLERAEE--VSPEAveRLLDLLRRHF-----DYVVVDLPRGLNPWTLAALE 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743 156 AVDALIVVVEPGRRSVQTARQIQELAHDLGI--QRVFMVASKV--RSTEDLAFVGEALsDFPLLGHVTFS-REIMDADLE 230
Cdd:COG4963  237 AADEVVLVTEPDLPSLRNAKRLLDLLRELGLpdDKVRLVLNRVpkRGEISAKDIEEAL-GLPVAAVLPNDpKAVAEAANQ 315

                        250       260
                 ....*....|....*....|
gi 499779743 231 GKALFDL--GGEPVAEIRKI 248
Cdd:COG4963  316 GRPLAEVapKSPLAKAIRKL 335
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 1-202 2.29e-05

Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 44.29  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743    1 MKI-AVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIPEENYRGITpfakmKALAEERTGADGGYGt 78
Cdd:pfam06564   1 MKIlALQGvRGGVGTTSILAALAWALQRLGERVLLIDLSPDNLLRLHFNVPFEHRQGWA-----RAELDGADWRDAALE- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   79 ffiLNPKVDDLP-EQFCVEhegiklllmgtvEQGGSGCVCPEHTLIKRLMQHLLVQRDEVVImDMEAGIEHLGRGTAGAV 157
Cdd:pfam06564  75 ---YTPGLDLLPfGRLSVE------------EQENLQQLQPDPGAWCRRLQQLKGRYDWVLF-DLPAGPSPLTRQLLSLA 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 499779743  158 DALIVVVEPGRRS-VQTARQIQELAHDLGIQRvFMVASKVRstEDL 202
Cdd:pfam06564 139 DLSLLVVNPDANChVLLHQQPLPDADHLLIND-FRPASQLQ--QDL 181
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
3-37 4.91e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 43.88  E-value: 4.91e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 499779743   3 IAVT-GKGGVGKTTLSGTLARLLAADGYRVLAVDAD 37
Cdd:PRK11670 110 IAVSsGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
PRK13695 PRK13695
NTPase;
1-31 6.41e-05

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 42.59  E-value: 6.41e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRV 31
Cdd:PRK13695   1 MKIGITGPPGVGKTTLVLKIAELLKEEGYKV 31
minD CHL00175
septum-site determining protein; Validated
 3-37 1.01e-04

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 42.84  E-value: 1.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 499779743   3 IAVT-GKGGVGKTTLSGTLARLLAADGYRVLAVDAD 37
Cdd:CHL00175  18 IVITsGKGGVGKTTTTANLGMSIARLGYRVALIDAD 53
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-38 1.10e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 42.64  E-value: 1.10e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADP 38
Cdd:PRK13185   3 LVLAVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDP 40
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
 1-66 1.41e-04

dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.


Pssm-ID: 349763 [Multi-domain]  Cd Length: 189  Bit Score: 41.79  E-value: 1.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499779743   1 MKIAVTGKG-GVGKTTLSGTLARLLAADGYRVLAV---------DADPDANLASALGIPEENYRGITPFAKMKALA 66
Cdd:cd03109    1 KTLFVTGTDtDVGKTVVSAGLARALRKKGIKVGYLkpvqtgcpgLEDSDAELLRKLAGLLLDLELINPYRFEAPLS 76
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
1-32 3.52e-04

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 40.18  E-value: 3.52e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLaadGYRVL 32
Cdd:COG1936    1 MRIAITGTPGTGKTTVAKLLAERL---GLEVI 29
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
1-31 4.45e-04

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 39.89  E-value: 4.45e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 499779743   1 MKIAVTGKGGVGKTTLSGTLARLLAADGYRV 31
Cdd:COG1618    1 MKIFITGRPGVGKTTLLLKVVEELRDEGLRV 31
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 3-35 7.50e-04

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: 39.86  E-value: 7.50e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 499779743   3 IAVTGKGGVGKTTLSGTLARLLAADGYRV--LAVD 35
Cdd:cd03114   49 VGITGPPGAGKSTLIEALGRLLREQGHRVavLAVD 83
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2-72 8.82e-04

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: 38.89  E-value: 8.82e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499779743     2 KIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADPDANLASALGIPEENYRGITPFAKMKALAEERTGA 72
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALA 74
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 6-56 8.88e-04

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 39.23  E-value: 8.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499779743   6 TGKGGVGKTTLSGTLARLLAADGYRVLAVDADP-DANLASALGIP----EENYRGI 56
Cdd:PRK00889  10 TGLSGAGKTTIARALAEKLREAGYPVEVLDGDAvRTNLSKGLGFSkedrDTNIRRI 65
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 6-112 1.05e-03

transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI superfamily which contains a ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. The specific function of TraL protein is unknown.


Pssm-ID: 349771  Cd Length: 155  Bit Score: 38.47  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779743   6 TGKGGVGKTTLSGTLARLLAADGYRVLAVDADPdaNLASALGIPEENYRG---ITPFAKM---------KALAEERTGA- 72
Cdd:cd05386    7 QGKGGVGKSVIASLLAQYLIDKGQPVSCIDTDP--VNKTFAGYKALNVQRiniIDNDEIIqskfdqlveQFLAEDGTVVi 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499779743  73 DGGYGTFFILNPKVD--DLPEQFcvEHEGIKlLLMGTVEQGG 112
Cdd:cd05386   85 DTGASTFLPLMNYLIdnDVPDLL--KDMGKE-VVIHTVINGG 123
RecA-like_Thep1 cd19482
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ...
 3-31 1.71e-03

RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the THEP1 family ATPase domain. It includes nucleoside-triphosphatase THEP 1 from Aquifex aeolicus (aaTHEP1) a nucleoside-phosphatase, with activity towards ATP, GTP, CTP, TTP and UTP; and which may hydrolyze nucleoside diphosphates with lower efficiency. The catalytic function of aaTHEP1 remains unclear, it may be a DNA/RNA modifying enzyme. Human THEP1 (hsTHEP1) may have a general function in many human tissues, as it is widely expressed in most examined tissues (such as in brain, heart, lymph node, skin, pancreas); it is especially highly expressed in embryonic and various tumor tissues. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410890 [Multi-domain]  Cd Length: 164  Bit Score: 37.97  E-value: 1.71e-03
                         10        20
                 ....*....|....*....|....*....
gi 499779743   3 IAVTGKGGVGKTTLSGTLARLLAADGYRV 31
Cdd:cd19482    1 IFITGPPGVGKTTLVLKVAELLKESGLKV 29
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
 2-31 2.14e-03

NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.


Pssm-ID: 460869  Cd Length: 168  Bit Score: 37.99  E-value: 2.14e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 499779743    2 KIAVTGKGGVGKTTLSGTLARLLAADGYRV 31
Cdd:pfam03266   1 RIFITGPPGVGKTTLVLKVAELLKSSGVKV 30
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 3-62 3.62e-03

adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 129547  Cd Length: 184  Bit Score: 37.45  E-value: 3.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499779743    3 IAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADP-DANLASALGIPE----ENYRGITPFAKM 62
Cdd:TIGR00455  21 IWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNvRHGLNKDLGFSEedrkENIRRIGEVAKL 85
mobB TIGR00176
molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor ...
 3-34 5.18e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobB; This molybdenum cofactor biosynthesis enzyme is similar to the urease accessory protein UreG and to the hydrogenase accessory protein HypB, both GTP hydrolases involved in loading nickel into the metallocenters of their respective target enzymes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 272943 [Multi-domain]  Cd Length: 155  Bit Score: 36.59  E-value: 5.18e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 499779743    3 IAVTGKGGVGKTTLSGTLARLLAADGYRVLAV 34
Cdd:TIGR00176   2 LQIVGPKNSGKTTLIERLVKALKARGYRVATI 33
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 3-37 6.50e-03

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 36.65  E-value: 6.50e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 499779743    3 IAVTG-KGGVGKTTLSGTLARLLAADGYRVLAVDAD 37
Cdd:TIGR01007  20 LLITSvKPGEGKSTTSANIAIAFAQAGYKTLLIDGD 55
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 3-37 7.30e-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: 36.37  E-value: 7.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 499779743    3 IAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDAD 37
Cdd:pfam00448   3 ILLVGLQGSGKTTTIAKLAAYLKKKGKKVLLVAAD 37
PRK13886 PRK13886
conjugal transfer protein TraL; Provisional
 1-38 7.32e-03

conjugal transfer protein TraL; Provisional


Pssm-ID: 184370  Cd Length: 241  Bit Score: 37.02  E-value: 7.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 499779743   1 MKIAVT--GKGGVGKTTLSGTLARLLAADGYRVLAVDADP 38
Cdd:PRK13886   2 AKIHMVlqGKGGVGKSFIAATIAQYKASKGQKPLCIDTDP 41
Grc3 COG1341
Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and ...
 2-38 8.40e-03

Polynucleotide 5'-kinase, involved in rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440952  Cd Length: 353  Bit Score: 36.92  E-value: 8.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 499779743   2 KIAVTGKGGVGKTTLSGTLARLLAADGYRVLAVDADP 38
Cdd:COG1341   37 RIMVLGPVDSGKSTLTTLLANKLLAEGLKVAIIDADV 73
 
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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