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Conserved domains on  [gi|2753981738|dbj|GAB0312060|]
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urease accessory protein UreG [Staphylococcus pseudintermedius]

Protein Classification

urease accessory protein UreG( domain architecture ID 12943093)

urease accessory protein UreG facilitates the functional incorporation of the urease nickel metallocenter

CATH:  3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924|GO:0016151|GO:0043419
SCOP:  4003988

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UreG cd05540
urease accessory protein UreG; UreG is one of the four accessory proteins of urease. Urease is ...
 4-194 1.52e-123

urease accessory protein UreG; UreG is one of the four accessory proteins of urease. Urease is an enzyme which catalyzes the decomposition of urea to form ammonia and carbon dioxide. Bacterial urease is a trimer of three subunits which are encoded by genes ureA, ureB, and ureC. Up to four accessory proteins (ureD, ureE, ureF, and ureG) are required for urease catalytical function. UreG may play an important role in nickel incorporation of the urease metallocenter. UreG is a member of the Fer4_NifH superfamily which contains an ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


:

Pssm-ID: 349776  Cd Length: 191  Bit Score: 346.94  E-value: 1.52e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   4 IKIGVGGPVGAGKTQLIEKLVKRLSEEKSIGVITNDIYTKEDQKILVNSGVLPEDRIIGVETGGCPHTAIREDASMNFAA 83
Cdd:cd05540     1 LTVGIGGPVGSGKTALVEALCRALRDKYSIAVVTNDIYTKEDAEFLIRNGALPEERIRGVETGGCPHTAIREDASMNLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  84 IDELMERHSDIELIFIESGGDNLAATFSPELVDFSIYIIDVAQGEKIPRKGGQGMIKSDYFVINKTDLAQYVGASLERMA 163
Cdd:cd05540    81 IEELTAKFPDLDLLLVESGGDNLAATFSPELADYIIYVIDVAGGDKIPRKGGPGITQSDLLVINKTDLAPYVGADLDVME 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2753981738 164 EDTEKFRKNRPFAFTNLKTDEGLDDVLNWIK 194
Cdd:cd05540   161 RDAKKMRGGGPFVFTNLKTDVGLDEVIDWIL 191
 
Name Accession Description Interval E-value
UreG cd05540
urease accessory protein UreG; UreG is one of the four accessory proteins of urease. Urease is ...
 4-194 1.52e-123

urease accessory protein UreG; UreG is one of the four accessory proteins of urease. Urease is an enzyme which catalyzes the decomposition of urea to form ammonia and carbon dioxide. Bacterial urease is a trimer of three subunits which are encoded by genes ureA, ureB, and ureC. Up to four accessory proteins (ureD, ureE, ureF, and ureG) are required for urease catalytical function. UreG may play an important role in nickel incorporation of the urease metallocenter. UreG is a member of the Fer4_NifH superfamily which contains an ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349776  Cd Length: 191  Bit Score: 346.94  E-value: 1.52e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   4 IKIGVGGPVGAGKTQLIEKLVKRLSEEKSIGVITNDIYTKEDQKILVNSGVLPEDRIIGVETGGCPHTAIREDASMNFAA 83
Cdd:cd05540     1 LTVGIGGPVGSGKTALVEALCRALRDKYSIAVVTNDIYTKEDAEFLIRNGALPEERIRGVETGGCPHTAIREDASMNLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  84 IDELMERHSDIELIFIESGGDNLAATFSPELVDFSIYIIDVAQGEKIPRKGGQGMIKSDYFVINKTDLAQYVGASLERMA 163
Cdd:cd05540    81 IEELTAKFPDLDLLLVESGGDNLAATFSPELADYIIYVIDVAGGDKIPRKGGPGITQSDLLVINKTDLAPYVGADLDVME 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2753981738 164 EDTEKFRKNRPFAFTNLKTDEGLDDVLNWIK 194
Cdd:cd05540   161 RDAKKMRGGGPFVFTNLKTDVGLDEVIDWIL 191
ureG TIGR00101
urease accessory protein UreG; This model represents UreG, a GTP hydrolase that acts in the ...
 3-200 4.08e-99

urease accessory protein UreG; This model represents UreG, a GTP hydrolase that acts in the assembly of the nickel metallocenter of urease. It is found only in urease-positive species, although some urease-positive species (e.g. Bacillus subtilis) lack this protein. A similar protein, hypB, is an accessory protein for expression of hydrogenase, which also uses nickel. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 129208  Cd Length: 199  Bit Score: 285.61  E-value: 4.08e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   3 PIKIGVGGPVGAGKTQLIEKLVKRLSEEKSIGVITNDIYTKEDQKILVNSGVLPEDRIIGVETGGCPHTAIREDASMNFA 82
Cdd:TIGR00101   1 MVKIGVAGPVGSGKTALIEALTRHMSKKYDMAVITNDIYTQEDAEFLCKNSVLPPERIIGVETGGCPHTAIREDASMNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  83 AIDELMERHSDIELIFIESGGDNLAATFSPELVDFSIYIIDVAQGEKIPRKGGQGMIKSDYFVINKTDLAQYVGASLERM 162
Cdd:TIGR00101  81 AVEEMHGRFPNLELVFIESGGDNLSATFSPELADFTIFVIDVAEGDKIPRKGGPGITRSDLLVINKIDLAPYVGADLKVM 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2753981738 163 AEDTEKFRKNRPFAFTNLKTDEGLDDVLNWIKKDIFFE 200
Cdd:TIGR00101 161 ERDAKKMRGEKPFIFTNLRAKEGLDDVIAWIERYALLK 198
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 1-195 3.84e-86

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


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 252.67  E-value: 3.84e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   1 MKPIKIGVGGPVGAGKTQLIEKLVKRLSEEKSIGVITNDIYTKEDQKILVNSGVlpedRIIGVETGGCPHTaireDASMN 80
Cdd:COG0378    11 KGVLAVNLMGSPGSGKTTLLEKTIRALKDRLRIAVIEGDIYTTEDAERLRAAGV----PVVQINTGGCCHL----DASMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  81 FAAIDELmeRHSDIELIFIESGGDNLAATFSPELVDFSIYIIDVAQGEKIPRKGGQGMIKSDYFVINKTDLAQYVGASLE 160
Cdd:COG0378    83 LEALEEL--DLPDLDLLFIENVGNLVCPAFFPLGEDLKVVVLSVTEGDDKPRKYPPMFTAADLLVINKIDLAPYVGFDLE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2753981738 161 RMAEDTEKFRKNRPFAFTNLKTDEGLDDVLNWIKK 195
Cdd:COG0378   161 VMEEDARRVNPGAPIFEVSAKTGEGLDEWADWLRE 195
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
 6-177 4.93e-52

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


Pssm-ID: 396860  Cd Length: 179  Bit Score: 165.12  E-value: 4.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   6 IGVGGPVGAGKTQLIEKLVKRLSEEKSIGVITNDIY-TKEDQKILVNSGVLpedrIIGVETGGCPHTaIREDASMNFAAi 84
Cdd:pfam02492   3 TVITGFLGSGKTTLLNHLLKQNRAGLRIAVIVNEFGeTGIDAELLSETGVL----IVELSNGCICCT-IREDLSMALEA- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  85 deLMERHSDIELIFIESGGdNLAATFS-----------PELVDFSIYIIDV---AQGEKIPRKGGQGMIKSDYFVINKTD 150
Cdd:pfam02492  77 --LLEREGRLDVIFIETTG-LAEPAPVaqtflspelrsPVLLDGVITVVDAaneADGEKIPRKAGDQIAFADLIVLNKTD 153

                         170       180
                  ....*....|....*....|....*..
gi 2753981738 151 LAQYVgASLERMAEDTEKFRKNRPFAF 177
Cdd:pfam02492 154 LAPEV-ALLEVLEEDLRRLNPGAPVVP 179
PRK10463 PRK10463
hydrogenase nickel incorporation protein HypB; Provisional
 13-193 2.61e-08

hydrogenase nickel incorporation protein HypB; Provisional


Pssm-ID: 182479  Cd Length: 290  Bit Score: 52.50  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  13 GAGKTQLIEKLVKRLSEEKSIGVITNDIYTKEDQKILVNSGVlpedRIIGVETG-GCpHTaireDASMNFAAIDEL-MER 90
Cdd:PRK10463  114 GSGKTTLLTETLMRLKDSVPCAVIEGDQQTVNDAARIRATGT----PAIQVNTGkGC-HL----DAQMIADAAPRLpLDD 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  91 HSdieLIFIESGGdNLAATFSPELVDFS-IYIIDVAQGEKIPRKGGQGMIKSDYFVINKTDLAQYVGASLERMAEDTEKF 169
Cdd:PRK10463  185 NG---ILFIENVG-NLVCPASFDLGEKHkVAVLSVTEGEDKPLKYPHMFAAASLMLLNKVDLLPYLNFDVEKCIACAREV 260

                         170       180
                  ....*....|....*....|....
gi 2753981738 170 RKNRPFAFTNLKTDEGLDDVLNWI 193
Cdd:PRK10463  261 NPEIEIILISATSGEGMDQWLNWL 284
 
Name Accession Description Interval E-value
UreG cd05540
urease accessory protein UreG; UreG is one of the four accessory proteins of urease. Urease is ...
 4-194 1.52e-123

urease accessory protein UreG; UreG is one of the four accessory proteins of urease. Urease is an enzyme which catalyzes the decomposition of urea to form ammonia and carbon dioxide. Bacterial urease is a trimer of three subunits which are encoded by genes ureA, ureB, and ureC. Up to four accessory proteins (ureD, ureE, ureF, and ureG) are required for urease catalytical function. UreG may play an important role in nickel incorporation of the urease metallocenter. UreG is a member of the Fer4_NifH superfamily which contains an ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349776  Cd Length: 191  Bit Score: 346.94  E-value: 1.52e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   4 IKIGVGGPVGAGKTQLIEKLVKRLSEEKSIGVITNDIYTKEDQKILVNSGVLPEDRIIGVETGGCPHTAIREDASMNFAA 83
Cdd:cd05540     1 LTVGIGGPVGSGKTALVEALCRALRDKYSIAVVTNDIYTKEDAEFLIRNGALPEERIRGVETGGCPHTAIREDASMNLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  84 IDELMERHSDIELIFIESGGDNLAATFSPELVDFSIYIIDVAQGEKIPRKGGQGMIKSDYFVINKTDLAQYVGASLERMA 163
Cdd:cd05540    81 IEELTAKFPDLDLLLVESGGDNLAATFSPELADYIIYVIDVAGGDKIPRKGGPGITQSDLLVINKTDLAPYVGADLDVME 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2753981738 164 EDTEKFRKNRPFAFTNLKTDEGLDDVLNWIK 194
Cdd:cd05540   161 RDAKKMRGGGPFVFTNLKTDVGLDEVIDWIL 191
ureG TIGR00101
urease accessory protein UreG; This model represents UreG, a GTP hydrolase that acts in the ...
 3-200 4.08e-99

urease accessory protein UreG; This model represents UreG, a GTP hydrolase that acts in the assembly of the nickel metallocenter of urease. It is found only in urease-positive species, although some urease-positive species (e.g. Bacillus subtilis) lack this protein. A similar protein, hypB, is an accessory protein for expression of hydrogenase, which also uses nickel. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 129208  Cd Length: 199  Bit Score: 285.61  E-value: 4.08e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   3 PIKIGVGGPVGAGKTQLIEKLVKRLSEEKSIGVITNDIYTKEDQKILVNSGVLPEDRIIGVETGGCPHTAIREDASMNFA 82
Cdd:TIGR00101   1 MVKIGVAGPVGSGKTALIEALTRHMSKKYDMAVITNDIYTQEDAEFLCKNSVLPPERIIGVETGGCPHTAIREDASMNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  83 AIDELMERHSDIELIFIESGGDNLAATFSPELVDFSIYIIDVAQGEKIPRKGGQGMIKSDYFVINKTDLAQYVGASLERM 162
Cdd:TIGR00101  81 AVEEMHGRFPNLELVFIESGGDNLSATFSPELADFTIFVIDVAEGDKIPRKGGPGITRSDLLVINKIDLAPYVGADLKVM 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2753981738 163 AEDTEKFRKNRPFAFTNLKTDEGLDDVLNWIKKDIFFE 200
Cdd:TIGR00101 161 ERDAKKMRGEKPFIFTNLRAKEGLDDVIAWIERYALLK 198
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 1-195 3.84e-86

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


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 252.67  E-value: 3.84e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   1 MKPIKIGVGGPVGAGKTQLIEKLVKRLSEEKSIGVITNDIYTKEDQKILVNSGVlpedRIIGVETGGCPHTaireDASMN 80
Cdd:COG0378    11 KGVLAVNLMGSPGSGKTTLLEKTIRALKDRLRIAVIEGDIYTTEDAERLRAAGV----PVVQINTGGCCHL----DASMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  81 FAAIDELmeRHSDIELIFIESGGDNLAATFSPELVDFSIYIIDVAQGEKIPRKGGQGMIKSDYFVINKTDLAQYVGASLE 160
Cdd:COG0378    83 LEALEEL--DLPDLDLLFIENVGNLVCPAFFPLGEDLKVVVLSVTEGDDKPRKYPPMFTAADLLVINKIDLAPYVGFDLE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2753981738 161 RMAEDTEKFRKNRPFAFTNLKTDEGLDDVLNWIKK 195
Cdd:COG0378   161 VMEEDARRVNPGAPIFEVSAKTGEGLDEWADWLRE 195
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
 6-177 4.93e-52

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


Pssm-ID: 396860  Cd Length: 179  Bit Score: 165.12  E-value: 4.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   6 IGVGGPVGAGKTQLIEKLVKRLSEEKSIGVITNDIY-TKEDQKILVNSGVLpedrIIGVETGGCPHTaIREDASMNFAAi 84
Cdd:pfam02492   3 TVITGFLGSGKTTLLNHLLKQNRAGLRIAVIVNEFGeTGIDAELLSETGVL----IVELSNGCICCT-IREDLSMALEA- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  85 deLMERHSDIELIFIESGGdNLAATFS-----------PELVDFSIYIIDV---AQGEKIPRKGGQGMIKSDYFVINKTD 150
Cdd:pfam02492  77 --LLEREGRLDVIFIETTG-LAEPAPVaqtflspelrsPVLLDGVITVVDAaneADGEKIPRKAGDQIAFADLIVLNKTD 153

                         170       180
                  ....*....|....*....|....*..
gi 2753981738 151 LAQYVgASLERMAEDTEKFRKNRPFAF 177
Cdd:pfam02492 154 LAPEV-ALLEVLEEDLRRLNPGAPVVP 179
HypB cd05390
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ...
 13-195 1.79e-22

nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the maturation of nickel-dependent hydrogenases, like carbon monoxide dehydrogenase or urease. HypB is a GTP-binding protein and has GTP hyrolase activity. It forms homodimer and is capable of binding two nickel ions and two zinc ions. The active site is located on the dimer interface. Energy from hydrolysis of GTP is used to insert nickels into hydrogenases.


Pssm-ID: 349775  Cd Length: 203  Bit Score: 89.96  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  13 GAGKTQLIEKLVKRLSEEKSIGVITNDIYTKEDQKILVNSGVlpedRIIGVETGGCPHTaireDASMNFAAIDELMErhS 92
Cdd:cd05390    31 GSGKTTLLERTIDALKDELKIAVIEGDLETDNDAERIRATGV----PAIQINTGGACHL----DADMVARALHDLDL--D 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  93 DIELIFIESGGdNLAATFSPEL-VDFSIYIIDVAQGEKIPRKGGQGMIKSDYFVINKTDLAQYVGASLERMAEDTEKFRK 171
Cdd:cd05390   101 ELDLLFIENVG-NLVCPAEFDLgEHKNVVLLSVTEGDDKPLKYPLMFQVADVVLINKIDLLPYFDFDVEKAKEDIKKLNP 179

                         170       180
                  ....*....|....*....|....
gi 2753981738 172 NRPFAFTNLKTDEGLDDVLNWIKK 195
Cdd:cd05390   180 NAPIIEVSAKTGEGMEAWIDWLRE 203
PRK10463 PRK10463
hydrogenase nickel incorporation protein HypB; Provisional
 13-193 2.61e-08

hydrogenase nickel incorporation protein HypB; Provisional


Pssm-ID: 182479  Cd Length: 290  Bit Score: 52.50  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  13 GAGKTQLIEKLVKRLSEEKSIGVITNDIYTKEDQKILVNSGVlpedRIIGVETG-GCpHTaireDASMNFAAIDEL-MER 90
Cdd:PRK10463  114 GSGKTTLLTETLMRLKDSVPCAVIEGDQQTVNDAARIRATGT----PAIQVNTGkGC-HL----DAQMIADAAPRLpLDD 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  91 HSdieLIFIESGGdNLAATFSPELVDFS-IYIIDVAQGEKIPRKGGQGMIKSDYFVINKTDLAQYVGASLERMAEDTEKF 169
Cdd:PRK10463  185 NG---ILFIENVG-NLVCPASFDLGEKHkVAVLSVTEGEDKPLKYPHMFAAASLMLLNKVDLLPYLNFDVEKCIACAREV 260

                         170       180
                  ....*....|....*....|....
gi 2753981738 170 RKNRPFAFTNLKTDEGLDDVLNWI 193
Cdd:PRK10463  261 NPEIEIILISATSGEGMDQWLNWL 284
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
 13-152 8.67e-08

cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.


Pssm-ID: 349766  Cd Length: 198  Bit Score: 50.21  E-value: 8.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  13 GAGKTQLIEKLVKRLSEEKsIGVITNDI-YTKEDQKILVNSGvlPEDRIIGVeTGGCPHTAIREDAsmnFAAIDELMERH 91
Cdd:cd03112    10 GAGKTTLLNHILSEQHGKR-IAVIVNEFgEVGIDAALLADSG--GGEEVVEL-SNGCICCTLKGDL---VKALEQLLERR 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753981738  92 SDIELIFIESGG--D--NLAATF-SPELVDFSIYI------IDVAQGEKI--PRKGGQGMIK----SDYFVINKTDLA 152
Cdd:cd03112    83 GKFDYILIETTGlaDpgPIAQTLwSDEELESRLRLdgvvtvVDAKNFLKQldEEDVSDLAVDqiafADVIVLNKTDLV 160
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
6-103 2.49e-04

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 41.13  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   6 IGVGGPVGAGKTQLIEKLVKRLSEE---KSIGVITNDIYTKEDQKILVNSGvlpedRIIGVetggcphtAIREDASMnfA 82
Cdd:PRK12727  353 IALVGPTGAGKTTTIAKLAQRFAAQhapRDVALVTTDTQRVGGREQLHSYG-----RQLGI--------AVHEADSA--E 417

                          90       100
                  ....*....|....*....|.
gi 2753981738  83 AIDELMERHSDIELIFIESGG 103
Cdd:PRK12727  418 SLLDLLERLRDYKLVLIDTAG 438
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 6-189 3.10e-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: 40.25  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738   6 IGVGGPVGAGKTQLIEKLVKRLSEE-KSIGVITND---IYTKedqkilvnsGVLPEDRIIGVETGGCPHTAIREDASMNF 81
Cdd:cd03114    49 VGITGPPGAGKSTLIEALGRLLREQgHRVAVLAVDpssPRSG---------GSILGDKTRMQRLARDPNAFIRPSPSRGT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753981738  82 -----AAIDELME--RHSDIELIFIESGGDNLAATFSPELVDFSIYII-----DVAQGEKIprkggqGMIK-SDYFVINK 148
Cdd:cd03114   120 lggvaRATREAILlcEAAGYDVVLVETVGVGQSEVAVADMVDTFVLLLppgggDELQGIKA------GIMEiADLVVVNK 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2753981738 149 TDLAQYVGA-SLERMAEDTEKFRKNRPFAF------TNLKTDEGLDDV 189
Cdd:cd03114   194 ADGDLKTGArRAQRELTSALKLLRPRSDGWrppvlrTSALTGEGIDEL 241
PRK14490 PRK14490
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ...
 3-34 3.83e-04

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; Provisional


Pssm-ID: 237728 [Multi-domain]  Cd Length: 369  Bit Score: 40.42  E-value: 3.83e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2753981738   3 PIKIGVGGPVGAGKTQLIEKLVKRLSEEKSIG 34
Cdd:PRK14490    5 PFEIAFCGYSGSGKTTLITALVRRLSERFSVG 36
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 1-46 4.32e-03

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 36.68  E-value: 4.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2753981738   1 MKPIKIGVGGPVGAGKTQLIEKLVKRLSEEkSIGVITNDIYTKeDQ 46
Cdd:PRK05480    4 KKPIIIGIAGGSGSGKTTVASTIYEELGDE-SIAVIPQDSYYK-DQ 47
PRK13695 PRK13695
NTPase;
4-40 4.80e-03

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 36.43  E-value: 4.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2753981738   4 IKIGVGGPVGAGKTQLIEKLVKRLSEE--KSIGVITNDI 40
Cdd:PRK13695    1 MKIGITGPPGVGKTTLVLKIAELLKEEgyKVGGFYTEEV 39
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 6-36 6.41e-03

Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 441369 [Multi-domain]  Cd Length: 162  Bit Score: 35.93  E-value: 6.41e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2753981738   6 IGVGGPVGAGKTQLIEKLVKRLSEE-KSIGVI 36
Cdd:COG1763     4 LGIVGYSGSGKTTLLEKLIPELKARgLRVGTI 35
PRK07429 PRK07429
phosphoribulokinase; Provisional
 2-58 8.41e-03

phosphoribulokinase; Provisional


Pssm-ID: 180975  Cd Length: 327  Bit Score: 36.14  E-value: 8.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2753981738   2 KPIKIGVGGPVGAGKTQLIEKLVKRLSEEKsIGVITNDIYTKEDQKILVNSGVLPED 58
Cdd:PRK07429    7 RPVLLGVAGDSGCGKTTFLRGLADLLGEEL-VTVICTDDYHSYDRKQRKELGITALD 62
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 10-38 8.64e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 35.92  E-value: 8.64e-03
                          10        20
                  ....*....|....*....|....*....
gi 2753981738  10 GPVGAGKTQLIEKLVKRLSEEKSIGVITN 38
Cdd:COG3267    50 GEVGTGKTTLLRRLLERLPDDVKVAYIPN 78
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
 5-44 9.20e-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: 35.29  E-value: 9.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2753981738   5 KIGVGGPVGAGKTQLIEKLVKRLSEEksiGVITNDIYTKE 44
Cdd:pfam03266   1 RIFITGPPGVGKTTLVLKVAELLKSS---GVKVGGFYTPE 37
 
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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