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Conserved domains on  [gi|6226573|sp|P31897|]
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RecName: Full=Carbon monoxide dehydrogenase accessory protein CooC

Protein Classification

carbon monoxide dehydrogenase accessory protein CooC( domain architecture ID 10114056)

carbon monoxide dehydrogenase accessory protein CooC, 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)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-252 1.72e-124

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: 353.92  E-value: 1.72e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVPAERLsallPISKMTGLARERTGASETT-GTH 79
Cdd:cd02034   1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKL----PLIKTIGDIRERTGAKKGEpPEG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   80 FILNPRVDDIPEQFCVDHAGIKLLLMGTVNHAGSGCVCPEHALVRTLLRHILTKRKECVLIDMEAGIEHFGRGTIEAVDL 159
Cdd:cd02034  77 MSLNPYVDDIIKEIIVEPDGIDLLVMGRPEGGGSGCYCPVNALLRELLRHLALKNYEYVVIDMEAGIEHLSRGTIRAVDL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  160 LVIVIEPGSRSLQTAAQIEGLARDLGIKTICHIANKLASPVDVGFILDRADQFDLLGSIPFDSAIQAADQAGLSCYDLSP 239
Cdd:cd02034 157 LIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRNEEEQELIEELLIKLKLIGVIPYDEEIMEADLKGKPLFDLDS 236

                       250
                ....*....|...
gi 6226573  240 ACRDKAHALMAAL 252
Cdd:cd02034 237 AAVKAIEKIVEKL 249
 
Name Accession Description Interval E-value
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-252 1.72e-124

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: 353.92  E-value: 1.72e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVPAERLsallPISKMTGLARERTGASETT-GTH 79
Cdd:cd02034   1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKL----PLIKTIGDIRERTGAKKGEpPEG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   80 FILNPRVDDIPEQFCVDHAGIKLLLMGTVNHAGSGCVCPEHALVRTLLRHILTKRKECVLIDMEAGIEHFGRGTIEAVDL 159
Cdd:cd02034  77 MSLNPYVDDIIKEIIVEPDGIDLLVMGRPEGGGSGCYCPVNALLRELLRHLALKNYEYVVIDMEAGIEHLSRGTIRAVDL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  160 LVIVIEPGSRSLQTAAQIEGLARDLGIKTICHIANKLASPVDVGFILDRADQFDLLGSIPFDSAIQAADQAGLSCYDLSP 239
Cdd:cd02034 157 LIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRNEEEQELIEELLIKLKLIGVIPYDEEIMEADLKGKPLFDLDS 236

                       250
                ....*....|...
gi 6226573  240 ACRDKAHALMAAL 252
Cdd:cd02034 237 AAVKAIEKIVEKL 249
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-252 2.50e-108

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 313.26  E-value: 2.50e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVPAErLSALLPISKMTGLARERTGASEttGTHF 80
Cdd:COG3640   1 MKIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVE-ADLIKPLGEMRELIKERTGAPG--GGMF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   81 ILNPRVDDIPEQFCVDHAGIKLLLMGTVNHAGSGCVCPEHALVRTLLRHILTKRKECVLIDMEAGIEHFGRGTIEAVDLL 160
Cdd:COG3640  78 KLNPKVDDIPEEYLVEGDGVDLLVMGTIEEGGSGCYCPENALLRALLNHLVLGNYEYVVVDMEAGIEHLGRGTAEGVDLL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  161 VIVIEPGSRSLQTAAQIEGLARDLGIKTICHIANKLASPVDVGFILDRADqFDLLGSIPFDSAIQAADQAGLSCYDL-SP 239
Cdd:COG3640 158 LVVSEPSRRSIETARRIKELAEELGIKKIYLVGNKVREEEDEEFLRELLG-LELLGFIPYDEEVREADLEGKPLLDLpDS 236

                       250
                ....*....|...
gi 6226573  240 ACRDKAHALMAAL 252
Cdd:COG3640 237 PAVAAVEEIAEKL 249
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-233 7.92e-26

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: 101.27  E-value: 7.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573      3 IAVTG-KGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVPAERLSALLPISkmTGLARERTgasettgthfi 81
Cdd:pfam01656   1 IAIAGtKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALA--EGLKGRVN----------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573     82 LNPRVDDIPEQFCvdhaGIKLLLMGTVNHAGSGCVC---PEHALVRTLlrHILTKRKECVLIDMEAGIEHFGRGTIEAVD 158
Cdd:pfam01656  68 LDPILLKEKSDEG----GLDLIPGNIDLEKFEKELLgprKEERLREAL--EALKEDYDYVIIDGAPGLGELLRNALIAAD 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    159 LLVIVIEPGSRSLQTAAQIEGLARDLGIKTICH-------IANKLASPVDVGFILDRADQ----FDLLGSIPFDSAIQAA 227
Cdd:pfam01656 142 YVIIPLEPEVILVEDAKRLGGVIAALVGGYALLglkiigvVLNKVDGDNHGKLLKEALEEllrgLPVLGVIPRDEAVAEA 221


                  ....*.
gi 6226573    228 DQAGLS 233
Cdd:pfam01656 222 PARGLP 227
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 2-47 5.54e-08

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 52.47  E-value: 5.54e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 6226573     2 KIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIG 47
Cdd:PRK13230   3 KFCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLV 48
ParA_partition NF041546
ParA family partition ATPase;
8-58 5.65e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 48.70  E-value: 5.65e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6226573     8 KGGVGKSTIVGMLARALSDEGWRVMAIDADP------------DANLASAIGVPAERLSALLP 58
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPqgsaldwaaareDERPFPVVGLARPTLHRELP 70
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 5-239 6.95e-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: 48.96  E-value: 6.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573      5 VTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPD-ANLASAIGVPAerlsalLPISKMTGLARERtgasettgthfiln 83
Cdd:TIGR01969   6 ASGKGGTGKTTITANLGVALAKLGKKVLALDADITmANLELILGMED------KPVTLHDVLAGEA-------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573     84 prvdDIPEQFCVDHAGIKLLLMGtVNHAGSGCVCPEhaLVRTLLRHILtKRKECVLIDMEAGIEHFGRGTIEAVDLLVIV 163
Cdd:TIGR01969  66 ----DIKDAIYEGPFGVKVIPAG-VSLEGLRKADPD--KLEDVLKEII-DDTDFLLIDAPAGLERDAVTALAAADELLLV 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    164 IEPGSRSLQTAAQIEGLARDLGIKTICHIANKLA------SPVDVGFILDradqFDLLGSIPFDSAIQAADQAGLSCYDL 237
Cdd:TIGR01969 138 VNPEISSITDALKTKIVAEKLGTAILGVVLNRVTrdktelGREEIETILE----VPVLGVVPEDPEVRRAAAFGEPVVIY 213


                  ..
gi 6226573    238 SP 239
Cdd:TIGR01969 214 NP 215
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 6-49 1.27e-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: 46.03  E-value: 1.27e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 6226573     6 TGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVP 49
Cdd:NF041417 339 TGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFGTE 382
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 6-47 3.86e-04

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: 41.40  E-value: 3.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 6226573     6 TGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIG 47
Cdd:NF041417  18 SGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFG 59
 
Name Accession Description Interval E-value
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 1-252 1.72e-124

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: 353.92  E-value: 1.72e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVPAERLsallPISKMTGLARERTGASETT-GTH 79
Cdd:cd02034   1 MKIAVAGKGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKL----PLIKTIGDIRERTGAKKGEpPEG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   80 FILNPRVDDIPEQFCVDHAGIKLLLMGTVNHAGSGCVCPEHALVRTLLRHILTKRKECVLIDMEAGIEHFGRGTIEAVDL 159
Cdd:cd02034  77 MSLNPYVDDIIKEIIVEPDGIDLLVMGRPEGGGSGCYCPVNALLRELLRHLALKNYEYVVIDMEAGIEHLSRGTIRAVDL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  160 LVIVIEPGSRSLQTAAQIEGLARDLGIKTICHIANKLASPVDVGFILDRADQFDLLGSIPFDSAIQAADQAGLSCYDLSP 239
Cdd:cd02034 157 LIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKVRNEEEQELIEELLIKLKLIGVIPYDEEIMEADLKGKPLFDLDS 236

                       250
                ....*....|...
gi 6226573  240 ACRDKAHALMAAL 252
Cdd:cd02034 237 AAVKAIEKIVEKL 249
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-252 2.50e-108

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 313.26  E-value: 2.50e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVPAErLSALLPISKMTGLARERTGASEttGTHF 80
Cdd:COG3640   1 MKIAVAGKGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVE-ADLIKPLGEMRELIKERTGAPG--GGMF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   81 ILNPRVDDIPEQFCVDHAGIKLLLMGTVNHAGSGCVCPEHALVRTLLRHILTKRKECVLIDMEAGIEHFGRGTIEAVDLL 160
Cdd:COG3640  78 KLNPKVDDIPEEYLVEGDGVDLLVMGTIEEGGSGCYCPENALLRALLNHLVLGNYEYVVVDMEAGIEHLGRGTAEGVDLL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  161 VIVIEPGSRSLQTAAQIEGLARDLGIKTICHIANKLASPVDVGFILDRADqFDLLGSIPFDSAIQAADQAGLSCYDL-SP 239
Cdd:COG3640 158 LVVSEPSRRSIETARRIKELAEELGIKKIYLVGNKVREEEDEEFLRELLG-LELLGFIPYDEEVREADLEGKPLLDLpDS 236

                       250
                ....*....|...
gi 6226573  240 ACRDKAHALMAAL 252
Cdd:COG3640 237 PAVAAVEEIAEKL 249
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 3-233 7.92e-26

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: 101.27  E-value: 7.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573      3 IAVTG-KGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVPAERLSALLPISkmTGLARERTgasettgthfi 81
Cdd:pfam01656   1 IAIAGtKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALA--EGLKGRVN----------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573     82 LNPRVDDIPEQFCvdhaGIKLLLMGTVNHAGSGCVC---PEHALVRTLlrHILTKRKECVLIDMEAGIEHFGRGTIEAVD 158
Cdd:pfam01656  68 LDPILLKEKSDEG----GLDLIPGNIDLEKFEKELLgprKEERLREAL--EALKEDYDYVIIDGAPGLGELLRNALIAAD 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    159 LLVIVIEPGSRSLQTAAQIEGLARDLGIKTICH-------IANKLASPVDVGFILDRADQ----FDLLGSIPFDSAIQAA 227
Cdd:pfam01656 142 YVIIPLEPEVILVEDAKRLGGVIAALVGGYALLglkiigvVLNKVDGDNHGKLLKEALEEllrgLPVLGVIPRDEAVAEA 221


                  ....*.
gi 6226573    228 DQAGLS 233
Cdd:pfam01656 222 PARGLP 227
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 1-257 4.32e-13

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: 67.19  E-value: 4.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    1 MK-IAVT-GKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVPAERlsalLPISKMTGLARERTGASETTGT 78
Cdd:COG1192   1 MKvIAVAnQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDD----LDPTLYDLLLDDAPLEDAIVPT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   79 HFilnPRVDDIPEqfCVDHAGIKLLLMGTVNhagsgcvcPEHALvRTLLRHILtKRKECVLIDMEAGIEHFGRGTIEAVD 158
Cdd:COG1192  77 EI---PGLDLIPA--NIDLAGAEIELVSRPG--------RELRL-KRALAPLA-DDYDYILIDCPPSLGLLTLNALAAAD 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  159 LLVIVIEPGSRSLQTAAQIeglardlgIKTICHIANKLASPVDV-GFILDRAD---------------QFD---LLGSIP 219
Cdd:COG1192 142 SVLIPVQPEYLSLEGLAQL--------LETIEEVREDLNPKLEIlGILLTMVDprtrlsrevleelreEFGdkvLDTVIP 213

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 6226573  220 FDSAIQAADQAGLSCYDLSPACRDKA--HALMAALLERVG 257
Cdd:COG1192 214 RSVALAEAPSAGKPVFEYDPKSKGAKayRALAEELLERLE 253
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 15-258 2.39e-11

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: 61.83  E-value: 2.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   15 TIVGMLARALSDEGWRVMAIDADPD-ANLASAIGVPAER-LSALLpiskmtglARERTgasettgthfilnprvddiPEQ 92
Cdd:COG0455   1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLEPKAtLADVL--------AGEAD-------------------LED 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   93 FCVDH-AGIKLLLMGTvNHAGSGCVCPEHALVRTLlrHILTKRKECVLIDMEAGIEHFGRGTIEAVDLLVIVIEPGSRSL 171
Cdd:COG0455  54 AIVQGpGGLDVLPGGS-GPAELAELDPEERLIRVL--EELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSI 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  172 Q-TAAQIEGLARDLGIKTICHIANKLASPVDVGFILDR----ADQF-----DLLGSIPFDSAIQAADQAGLSCYDLSPAC 241
Cdd:COG0455 131 TdAYALLKLLRRRLGVRRAGVVVNRVRSEAEARDVFERleqvAERFlgvrlRVLGVIPEDPAVREAVRRGRPLVLAAPDS 210

                       250
                ....*....|....*....
gi 6226573  242 --RDKAHALMAALLERVGP 258
Cdd:COG0455 211 paARAIRELAARLAGWPVP 229
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-44 8.27e-11

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: 58.32  E-value: 8.27e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6226573    1 MKIAVTG-KGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLAS 44
Cdd:cd02042   1 KVIAVANqKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTS 45
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 3-227 3.49e-10

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: 58.35  E-value: 3.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    3 IAVT-GKGGVGKSTIVGMLARALSDEGWRVMAIDADPD-ANLASAIGVPAER-LSALLpiskmTGLARERTGASETTGth 79
Cdd:cd02038   3 IAVTsGKGGVGKTNVSANLALALSKLGKRVLLLDADLGlANLDILLGLAPKKtLGDVL-----KGRVSLEDIIVEGPE-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   80 filnprvddipeqfcvdhaGIKLLLmgtvnhAGSGCV-----CPEH-ALVRTLLRHILtKRKECVLIDMEAGIEHFGRGT 153
Cdd:cd02038  76 -------------------GLDIIP------GGSGMEelanlDPEQkAKLIEELSSLE-SNYDYLLIDTGAGISRNVLDF 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  154 IEAVDLLVIVIEPGSRSLQTA-AQIEGLARDLGIKTICHIANKLASPVDVGFILDR----ADQF-----DLLGSIPFDSA 223
Cdd:cd02038 130 LLAADEVIVVTTPEPTSITDAyALIKVLSRRGGKKNFRLIVNMARSPKEGRATFERlkkvAKRFldinlDFVGFIPYDQS 209


                ....
gi 6226573  224 IQAA 227
Cdd:cd02038 210 VRRA 213
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 1-48 4.26e-09

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: 54.51  E-value: 4.26e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 6226573      1 MK-IAVTG-KGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGV 48
Cdd:pfam13614   1 GKvIAIANqKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGI 50
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 2-47 5.54e-08

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 52.47  E-value: 5.54e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 6226573     2 KIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIG 47
Cdd:PRK13230   3 KFCFYGKGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLV 48
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-37 1.01e-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: 51.30  E-value: 1.01e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 6226573      2 KIAVT-GKGGVGKSTIVGMLARALSDEGWRVMAIDAD 37
Cdd:pfam10609   5 VIAVAsGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 1-40 1.66e-07

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: 50.97  E-value: 1.66e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 6226573    1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDA 40
Cdd:cd02040   1 RQIAIYGKGGIGKSTTASNLSAALAEMGKKVLHVGCDPKA 40
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 3-51 2.47e-07

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 51.21  E-value: 2.47e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 6226573     3 IAVTG-KGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVPAE 51
Cdd:PRK13869 124 IAVTNfKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALLGVLPE 173
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 1-37 5.13e-07

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: 47.04  E-value: 5.13e-07
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 6226573    1 MKIAVTG-KGGVGKSTIVGMLARALSDEGWRVMAIDAD 37
Cdd:cd01983   1 RVIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ParA_partition NF041546
ParA family partition ATPase;
8-58 5.65e-07

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 48.70  E-value: 5.65e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6226573     8 KGGVGKSTIVGMLARALSDEGWRVMAIDADP------------DANLASAIGVPAERLSALLP 58
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPqgsaldwaaareDERPFPVVGLARPTLHRELP 70
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-37 6.76e-07

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: 48.65  E-value: 6.76e-07
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6226573    2 KIAV-TGKGGVGKSTIVGMLARALSDEGWRVMAIDAD 37
Cdd:cd02037   2 IIAVlSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 5-239 6.95e-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: 48.96  E-value: 6.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573      5 VTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPD-ANLASAIGVPAerlsalLPISKMTGLARERtgasettgthfiln 83
Cdd:TIGR01969   6 ASGKGGTGKTTITANLGVALAKLGKKVLALDADITmANLELILGMED------KPVTLHDVLAGEA-------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573     84 prvdDIPEQFCVDHAGIKLLLMGtVNHAGSGCVCPEhaLVRTLLRHILtKRKECVLIDMEAGIEHFGRGTIEAVDLLVIV 163
Cdd:TIGR01969  66 ----DIKDAIYEGPFGVKVIPAG-VSLEGLRKADPD--KLEDVLKEII-DDTDFLLIDAPAGLERDAVTALAAADELLLV 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    164 IEPGSRSLQTAAQIEGLARDLGIKTICHIANKLA------SPVDVGFILDradqFDLLGSIPFDSAIQAADQAGLSCYDL 237
Cdd:TIGR01969 138 VNPEISSITDALKTKIVAEKLGTAILGVVLNRVTrdktelGREEIETILE----VPVLGVVPEDPEVRRAAAFGEPVVIY 213


                  ..
gi 6226573    238 SP 239
Cdd:TIGR01969 214 NP 215
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 3-195 7.06e-07

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: 49.41  E-value: 7.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    3 IAVT-GKGGVGKSTIVGMLARALSDEGWRVMAIDAD---PdanlasaigvpaeRLSALLPISKMTGLARERTGASETTGt 78
Cdd:COG0489  95 IAVTsGKGGEGKSTVAANLALALAQSGKRVLLIDADlrgP-------------SLHRMLGLENRPGLSDVLAGEASLED- 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   79 hfILNPrvddipeqfcVDHAGIKLLLMGTVNHAGSGCVcpEHALVRTLLRHiLTKRKECVLIDMEAGIehfgrGTIEA-- 156
Cdd:COG0489 161 --VIQP----------TEVEGLDVLPAGPLPPNPSELL--ASKRLKQLLEE-LRGRYDYVIIDTPPGL-----GVADAtl 220

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 6226573  157 ----VDLLVIVIEPGSRSLQTAAQIEGLARDLGIKTICHIANK 195
Cdd:COG0489 221 laslVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM 263
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 3-231 9.84e-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: 48.87  E-value: 9.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573      3 IAVT-GKGGVGKSTIVGMLARALSDEGWRVMAIDADpdanlasaIGVpaERLSALLpiskmtGLARErtgasettgthfI 81
Cdd:TIGR01968   4 IVITsGKGGVGKTTTTANLGTALARLGKKVVLIDAD--------IGL--RNLDLLL------GLENR------------I 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573     82 LNPRVDDIPEQFCVDHAGIK------LLLMGTVNHAGSGCVCPEH--ALVRTLLRHIltkrkECVLIDMEAGIEHFGRGT 153
Cdd:TIGR01968  56 VYTLVDVVEGECRLQQALIKdkrlknLYLLPASQTRDKDAVTPEQmkKLVNELKEEF-----DYVIIDCPAGIESGFRNA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    154 IEAVDLLVIVIEPGSRSLQTAAQIEGLARDLGIKTICHIANKLASP-VDVGFILDRADQFD-----LLGSIPFDSAIQAA 227
Cdd:TIGR01968 131 VAPADEAIVVTTPEVSAVRDADRVIGLLEAKGIEKIHLIVNRLRPEmVKKGDMLSVDDVLEilsipLIGVIPEDEAIIVS 210


                  ....
gi 6226573    228 DQAG 231
Cdd:TIGR01968 211 TNKG 214
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 1-38 1.01e-06

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: 48.83  E-value: 1.01e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 6226573    1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADP 38
Cdd:cd02032   1 LVIAVYGKGGIGKSTTSSNLSAAFAKRGKKVLQIGCDP 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 3-56 1.18e-06

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: 48.27  E-value: 1.18e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6226573    3 IAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVP---------AERLSAL 56
Cdd:cd02035   3 IFFGGKGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGQKlggetpvkgAPNLWAM 65
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
3-56 3.33e-06

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 47.12  E-value: 3.33e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6226573    3 IAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIG---------VPAERLSAL 56
Cdd:COG0003   6 IFFTGKGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGtelgnepteVAVPNLYAL 68
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
1-41 3.57e-06

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 47.05  E-value: 3.57e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 6226573      1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDAN 41
Cdd:pfam00142   1 RQIAIYGKGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKAD 41
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 3-240 4.06e-06

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: 46.81  E-value: 4.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    3 IAVT-GKGGVGKSTIVGMLARALSDEGWRVMAIDADPD-ANLASAIGVpaERLSALLPISKMTGLARertgasetTGTHF 80
Cdd:cd02036   3 IVITsGKGGVGKTTTTANLGVALAKLGKKVLLIDADIGlRNLDLILGL--ENRIVYTLVDVLEGECR--------LEQAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   81 ILNPRVDdipeqfcvdhaGIKLLLMG-TVNHAGsgcVCPEHalVRTLLRHILTKrKECVLIDMEAGIEhfgRGTIEAV-- 157
Cdd:cd02036  73 IKDKRWE-----------NLYLLPASqTRDKDA---LTPEK--LEELVKELKDS-FDFILIDSPAGIE---SGFINAIap 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  158 -DLLVIVIEPGSRSLQTAAQIEGLARDLGIKTICHIANKL-ASPVDVGFILDRAD-----QFDLLGSIPFDSAIQAADQA 230
Cdd:cd02036 133 aDEAIIVTNPEISSVRDADRVIGLLESKGIVNIGLIVNRYrPEMVKSGDMLSVEDiqeilGIPLLGVIPEDPEVIVATNR 212

                       250
                ....*....|...
gi 6226573  231 G---LSCYDLSPA 240
Cdd:cd02036 213 GeplVLYKPNSLA 225
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 1-240 4.62e-06

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: 46.57  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573      1 MK-IAVTG-KGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLasaigvpaeRLSALLPISKMTGLAR-ERTGASETTG 77
Cdd:TIGR03371   1 MKvIAIVSvRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLL---------RLHFGMDWSVRDGWARaLLNGADWAAA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573     78 THFILNprvddipeqfcvdhaGIKLLLMGTVNHAG--SGCVCPEHALVRtLLRHILTKRKECVLIDMEAGIEHFGRGTIE 155
Cdd:TIGR03371  72 AYRSPD---------------GVLFLPYGDLSADEreAYQAHDAGWLAR-LLQQLDLAARDWVLIDLPRGPSPITRQALA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    156 AVDLLVIVIEPGSRSLQTAAQ-IEGLARDLGIKTICHIA-NKL--ASPVDVGF---ILDRADQFDLLGSIPFDSAIQAAD 228
Cdd:TIGR03371 136 AADLVLVVVNADAACYATLHQlALALFAGSGPRDGPRFLiNQFdpARQLSRDVravLRQTLGSRLLPFVIHRDEAVSEAL 215

                         250
                  ....*....|..
gi 6226573    229 QAGLSCYDLSPA 240
Cdd:TIGR03371 216 ARGTPVLNYAPH 227
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 1-166 5.82e-06

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: 46.22  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573      1 MKI-AVTG-KGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLasaigvpaeRLSALLPISKMTGLAR-ERTGASETTG 77
Cdd:pfam06564   1 MKIlALQGvRGGVGTTSILAALAWALQRLGERVLLIDLSPDNLL---------RLHFNVPFEHRQGWARaELDGADWRDA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573     78 ThFILNPRVDDIPeqFCVDHAGIKLLLMGTVNHAGSGCvcpeHALVRtllrhiLTKRKECVLIDMEAGIEHFGRGTIEAV 157
Cdd:pfam06564  72 A-LEYTPGLDLLP--FGRLSVEEQENLQQLQPDPGAWC----RRLQQ------LKGRYDWVLFDLPAGPSPLTRQLLSLA 138


                  ....*....
gi 6226573    158 DLLVIVIEP 166
Cdd:pfam06564 139 DLSLLVVNP 147
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 3-260 7.73e-06

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: 46.26  E-value: 7.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    3 IAVTG-KGGVGKSTIVGMLARALSDE-GWRVMAIDAD-PDANLASAIGVPAER--LSALLPISKMTGLARERTGASETTG 77
Cdd:COG4963 105 IAVVGaKGGVGATTLAVNLAWALAREsGRRVLLVDLDlQFGDVALYLDLEPRRglADALRNPDRLDETLLDRALTRHSSG 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   78 THFILNPRVDDIPEQFcvdhagiklllmgtvnhagsgcvcpEHALVRTLLRhILTKRKECVLIDMEAGIEHFGRGTIEAV 157
Cdd:COG4963 185 LSVLAAPADLERAEEV-------------------------SPEAVERLLD-LLRRHFDYVVVDLPRGLNPWTLAALEAA 238

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  158 DLLVIVIEPGSRSLQTAAQIEGLARDLGIKT--ICHIANKLASPVDvgfiLDRAD-----QFDLLGSIPFD--SAIQAAD 228
Cdd:COG4963 239 DEVVLVTEPDLPSLRNAKRLLDLLRELGLPDdkVRLVLNRVPKRGE----ISAKDieealGLPVAAVLPNDpkAVAEAAN 314

                       250       260       270
                ....*....|....*....|....*....|..
gi 6226573  229 QaGLSCYDLSPacRDKAHALMAALLERVGPTQ 260
Cdd:COG4963 315 Q-GRPLAEVAP--KSPLAKAIRKLAARLTGRP 343
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
3-37 1.22e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 45.80  E-value: 1.22e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 6226573     3 IAVT-GKGGVGKSTIVGMLARALSDEGWRVMAIDAD 37
Cdd:PRK11670 110 IAVSsGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 6-49 1.27e-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: 46.03  E-value: 1.27e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 6226573     6 TGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVP 49
Cdd:NF041417 339 TGKGGVGKSTIASTTATYLAEEGYETLIVTTDPASHLQDIFGTE 382
chlL CHL00072
photochlorophyllide reductase subunit L
 1-38 1.52e-05

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 45.11  E-value: 1.52e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 6226573     1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADP 38
Cdd:CHL00072   1 MKLAVYGKGGIGKSTTSCNISIALARRGKKVLQIGCDP 38
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 3-48 1.80e-05

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: 45.03  E-value: 1.80e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 6226573      3 IAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGV 48
Cdd:pfam02374   4 IFFGGKGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQ 49
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 6-42 1.92e-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: 45.46  E-value: 1.92e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 6226573      6 TGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANL 42
Cdd:TIGR04291   9 TGKGGVGKTSIACATAINLADQGKRVLLVSTDPASNV 45
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 1-38 2.20e-05

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 44.57  E-value: 2.20e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 6226573     1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADP 38
Cdd:PRK13185   3 LVLAVYGKGGIGKSTTSSNLSAAFAKLGKKVLQIGCDP 40
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 1-46 2.51e-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: 44.66  E-value: 2.51e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 6226573    1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAI 46
Cdd:cd02117   1 ESIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLL 46
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 2-41 3.95e-05

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 44.02  E-value: 3.95e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 6226573     2 KIAVTGKGGVGKSTIVGMLARALSDEGwRVMAIDADPDAN 41
Cdd:PRK13231   4 KIAIYGKGGIGKSTTVSNMAAAYSNDH-RVLVIGCDPKAD 42
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 3-37 7.58e-05

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 43.12  E-value: 7.58e-05
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 6226573    3 IAVT-GKGGVGKSTIVGMLARALSDEGWRVMAIDAD 37
Cdd:COG2894   5 IVVTsGKGGVGKTTTTANLGTALALLGKKVVLIDAD 40
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
 2-31 1.15e-04

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: 41.46  E-value: 1.15e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 6226573      2 KIAVTGKGGVGKSTIVGMLARALSDEGWRV 31
Cdd:pfam03266   1 RIFITGPPGVGKTTLVLKVAELLKSSGVKV 30
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 2-219 1.21e-04

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: 42.37  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    2 KIAVT-GKGGVGKSTIVGMLARALSDegwrVMAIDADPDA-NLASAIGVPAERLSALLPISKMT---------GLARE-- 68
Cdd:cd03110   1 IIAVLsGKGGTGKTTITANLAVLLYN----VILVDCDVDApNLHLLLGPEPEEEEDFVGGKKAFidqekcircGNCERvc 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573   69 RTGASETTGTHFILNPR--------VDDIPE-----------QFCVDHAGIKLLLMGTVN--HAGSGcvcpehALVRTLL 127
Cdd:cd03110  77 KFGAILEFFQKLIVDESlcegcgacVIICPRgaiylkdrdtgKIFISSSDGGPLVHGRLNigEENSG------KLVTELR 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573  128 RHILTKRKEC--VLIDMEAGIEHFGRGTIEAVDLLVIVIEPGSRSLQTAAQIEGLARDLGIKTICHIANKLASPVDVGFI 205
Cdd:cd03110 151 KKALERSKECdlAIIDGPPGTGCPVVASITGADAVLLVTEPTPSGLHDLKRAIELAKHFGIPTGIVINRYDINDEISEEI 230

                       250
                ....*....|....*.
gi 6226573  206 LDRADQF--DLLGSIP 219
Cdd:cd03110 231 EDFADEEgiPLLGKIP 246
PRK13695 PRK13695
NTPase;
1-31 2.33e-04

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 40.67  E-value: 2.33e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 6226573     1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRV 31
Cdd:PRK13695   1 MKIGITGPPGVGKTTLVLKIAELLKEEGYKV 31
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 6-47 3.86e-04

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: 41.40  E-value: 3.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 6226573     6 TGKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIG 47
Cdd:NF041417  18 SGKGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFG 59
PHA02518 PHA02518
ParA-like protein; Provisional
 1-64 6.21e-04

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 39.83  E-value: 6.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6226573     1 MKIAVTG-KGGVGKSTIVGMLARALSDEGWRVMAIDADPDANLASAIGVpAERLSALLPISKMTG 64
Cdd:PHA02518   1 KIIAVLNqKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEA-REEGEPLIPVVRMGK 64
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
1-31 7.49e-04

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 39.50  E-value: 7.49e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 6226573    1 MKIAVTGKGGVGKSTIVGMLARALSDEGWRV 31
Cdd:COG1618   1 MKIFITGRPGVGKTTLLLKVVEELRDEGLRV 31
TraL cd05386
transfer origin protein TraL; The transfer origin protein TraL is member of the SIMIBI ...
 6-38 8.55e-04

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: 38.86  E-value: 8.55e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 6226573    6 TGKGGVGKSTIVGMLARALSDEGWRVMAIDADP 38
Cdd:cd05386   7 QGKGGVGKSVIASLLAQYLIDKGQPVSCIDTDP 39
RecA-like_Thep1 cd19482
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ...
 3-31 1.50e-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: 38.35  E-value: 1.50e-03
                        10        20
                ....*....|....*....|....*....
gi 6226573    3 IAVTGKGGVGKSTIVGMLARALSDEGWRV 31
Cdd:cd19482   1 IFITGPPGVGKTTLVLKVAELLKESGLKV 29
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 7-42 1.68e-03

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: 39.30  E-value: 1.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6226573      7 GKGGVGKSTIVGMLARALSDEGWRVMAIDADPDANL 42
Cdd:TIGR04291 328 GKGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHL 363
minD CHL00175
septum-site determining protein; Validated
 3-221 1.83e-03

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 38.98  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573     3 IAVT-GKGGVGKSTIVGMLARALSDEGWRVMAIDADpdanlasaIGVpaERLSALLpiskmtGLARErtgasettgthfI 81
Cdd:CHL00175  18 IVITsGKGGVGKTTTTANLGMSIARLGYRVALIDAD--------IGL--RNLDLLL------GLENR------------V 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226573    82 LNPRVDDIPEQFCVDHAGIK------LLLMGTVNHAGSGCVCPEHalVRTLLRHILTKRKECVLIDMEAGIEHFGRGTIE 155
Cdd:CHL00175  70 LYTAMDVLEGECRLDQALIRdkrwknLSLLAISKNRQRYNVTRKN--MNMLVDSLKNRGYDYILIDCPAGIDVGFINAIA 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6226573   156 AVDLLVIVIEPGSRSLQTAAQIEGLARDLGIKTICHIANKL----------ASPVDVGFILDradqFDLLGSIPFD 221
Cdd:CHL00175 148 PAQEAIVVTTPEITAIRDADRVAGLLEANGIYNVKLLVNRVrpdmiqandmMSVRDVQEMLG----IPLLGAIPED 219
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
1-24 2.94e-03

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


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 37.49  E-value: 2.94e-03
                        10        20
                ....*....|....*....|....
gi 6226573    1 MKIAVTGKGGVGKSTIVGMLARAL 24
Cdd:COG1936   1 MRIAITGTPGTGKTTVAKLLAERL 24
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 8-37 3.44e-03

ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 37.82  E-value: 3.44e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 6226573      8 KGGVGKSTIVGMLARALSDEGWRVMAIDAD 37
Cdd:pfam09140   9 KGGSGKSTTAVHVAVALLYKGARVAAIDLD 38
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 3-52 4.80e-03

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: 37.16  E-value: 4.80e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6226573    3 IAVTG-KGGVGKSTIVGMLARALSDEGWRVMAIDADP-DANLASAIGVPAER 52
Cdd:cd05387  22 IAVTSaSPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPNEP 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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