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Conserved domains on  [gi|505062422|ref|WP_015249524|]
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YcjF family protein [Singulisphaera acidiphila]

Protein Classification

YcjF family protein( domain architecture ID 10007594)

YcjF family protein is a DUF697 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3597 COG3597
Uncharacterized conserved protein, DUF697 family [Function unknown];
89-476 6.88e-44

Uncharacterized conserved protein, DUF697 family [Function unknown];


:

Pssm-ID: 442816 [Multi-domain]  Cd Length: 367  Bit Score: 158.31  E-value: 6.88e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  89 SRGKSSVLNALLGHEVFKVGTTHGTTVsrtsqrwehsatsEHPGLEGARLVLVDTPGIDEVGGEVRETLAREVARHADLI 168
Cdd:COG3597   14 SAGKTSLVGALLLTVGGLVGTGMGTTT-------------AAETYALKLVLLVLLLLLTDTGGILEAGAAGTLAELLALL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 169 LFVVSSDMQRCELEALSQLRQVQKPIILVFNQIDRYPETDRDQIYEKIKDERIRNLIRPEDVVMTAARPdPFKVKLQLPD 248
Cdd:COG3597   81 LAVEADLLLVVDDDDLRASELEILRALVLIGKKSLLLLVKLDLLEEALQEALLALLVLREVVEIAAAAV-AAAVAALQAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 249 GTTTVQWERPAPVIEPLKLRILDVLEREGKALVALNTLLLAGDLHEEIVA-HKLRIRDDAANRLIWNFALAkGAAVALNP 327
Cdd:COG3597  160 ALVAEELFEPEADIDLLLKRLAAALLAEGLLLLAAAILLAAQLLLEEAAAaAAGQRRRAAARRIILRYAIA-AAAVGAVP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 328 IPIADMAGGLAVDVGMIVALSKVYGIPLTRKTASSLVRDMMLALGALGAVEivtRLVAGGVKSslaglsilsgglaIPLt 407
Cdd:COG3597  239 IPFADLLALAALQAKMVAELAKIYGVELSRERAKELLASLGGGLGGLGLVR---QLLRSLLKL-------------IPG- 301
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505062422 408 aLGYGAIGLAQGGTASTTSYVLGHGAKHYLKQGCQWGPRGIKTVIHQILAEAKtdSVIDRLRDDLKRRV 476
Cdd:COG3597  302 -AGTVVGGAIQAATAAALTYALGRVAIEYFEKGGTFDPEGLKEVFKEAFQKAK--RFLKEFKQEAKARA 367
 
Name Accession Description Interval E-value
COG3597 COG3597
Uncharacterized conserved protein, DUF697 family [Function unknown];
89-476 6.88e-44

Uncharacterized conserved protein, DUF697 family [Function unknown];


Pssm-ID: 442816 [Multi-domain]  Cd Length: 367  Bit Score: 158.31  E-value: 6.88e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  89 SRGKSSVLNALLGHEVFKVGTTHGTTVsrtsqrwehsatsEHPGLEGARLVLVDTPGIDEVGGEVRETLAREVARHADLI 168
Cdd:COG3597   14 SAGKTSLVGALLLTVGGLVGTGMGTTT-------------AAETYALKLVLLVLLLLLTDTGGILEAGAAGTLAELLALL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 169 LFVVSSDMQRCELEALSQLRQVQKPIILVFNQIDRYPETDRDQIYEKIKDERIRNLIRPEDVVMTAARPdPFKVKLQLPD 248
Cdd:COG3597   81 LAVEADLLLVVDDDDLRASELEILRALVLIGKKSLLLLVKLDLLEEALQEALLALLVLREVVEIAAAAV-AAAVAALQAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 249 GTTTVQWERPAPVIEPLKLRILDVLEREGKALVALNTLLLAGDLHEEIVA-HKLRIRDDAANRLIWNFALAkGAAVALNP 327
Cdd:COG3597  160 ALVAEELFEPEADIDLLLKRLAAALLAEGLLLLAAAILLAAQLLLEEAAAaAAGQRRRAAARRIILRYAIA-AAAVGAVP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 328 IPIADMAGGLAVDVGMIVALSKVYGIPLTRKTASSLVRDMMLALGALGAVEivtRLVAGGVKSslaglsilsgglaIPLt 407
Cdd:COG3597  239 IPFADLLALAALQAKMVAELAKIYGVELSRERAKELLASLGGGLGGLGLVR---QLLRSLLKL-------------IPG- 301
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505062422 408 aLGYGAIGLAQGGTASTTSYVLGHGAKHYLKQGCQWGPRGIKTVIHQILAEAKtdSVIDRLRDDLKRRV 476
Cdd:COG3597  302 -AGTVVGGAIQAATAAALTYALGRVAIEYFEKGGTFDPEGLKEVFKEAFQKAK--RFLKEFKQEAKARA 367
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
83-237 7.08e-43

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 148.93  E-value: 7.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  83 AAFGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEHsatsehpgLEGARLVLVDTPGIDEVG--GEVRETLARE 160
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWEL--------LPLGPVVLIDTPGLDEEGglGRERVEEARQ 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505062422 161 VARHADLILFVVSSDMQRCELEA-LSQLRQVQKPIILVFNQIDRYPETDRdqiyEKIKDERIRNLIRPEDVVMTAARP 237
Cdd:cd00880   73 VADRADLVLLVVDSDLTPVEEEAkLGLLRERGKPVLLVLNKIDLVPESEE----EELLRERKLELLPDLPVIAVSALP 146
DUF697 pfam05128
Domain of unknown function (DUF697); Family of bacterial hypothetical proteins that is ...
287-460 2.54e-33

Domain of unknown function (DUF697); Family of bacterial hypothetical proteins that is sometimes associated with GTPase domains.


Pssm-ID: 368297  Cd Length: 162  Bit Score: 123.43  E-value: 2.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  287 LLAGDLHEEIVAHKLRIRDDAANRLIWNFALAKGAAVALNPIPIADMAGGLAVDVGMIVALSKVYGIPLTRKTASSLVRD 366
Cdd:pfam05128   1 LQAAELLELAERELLEQRDRQAKKLIERYAWIVAGVVAVSPLALVDLLAVAARNARMIRELARLYGIELGYEGAIRLARS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  367 MMLALGALGAVEIVTRLVAGGVKSSLAGlsILSGglaipltalgygaiGLAQGGTASTTSYVLGHGAKHYLKQGCQWGPR 446
Cdd:pfam05128  81 VLANLAGLGAVELGTDLLKQALGLNLAT--KLSG--------------RAGQGVVAGYLTARVGLSAIEYCRPLPDWGDG 144
                         170
                  ....*....|....*..
gi 505062422  447 G---IKTVIHQILAEAK 460
Cdd:pfam05128 145 GrpkLSEVVQRLLSQLK 161
era PRK00089
GTPase Era; Reviewed
91-235 2.13e-11

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 64.68  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVfkvgtthgTTVSRTSQrwehsaTSEHP--G---LEGARLVLVDTPGIDEVG---GEVRETLAREVA 162
Cdd:PRK00089  17 GKSTLLNALVGQKI--------SIVSPKPQ------TTRHRirGivtEDDAQIIFVDTPGIHKPKralNRAMNKAAWSSL 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505062422 163 RHADLILFVVSSDMQRCELEA--LSQLRQVQKPIILVFNQIDRypETDRDQIYEKIKDerIRNLIRPEDVVMTAA 235
Cdd:PRK00089  83 KDVDLVLFVVDADEKIGPGDEfiLEKLKKVKTPVILVLNKIDL--VKDKEELLPLLEE--LSELMDFAEIVPISA 153
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
14-202 1.72e-06

tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF (thiophene and furan oxidation protein), is a GTPase involved in tRNA modification to create 5-methylaminomethyl-2-thiouridine in the wobble position of some tRNAs. This protein and GidA form an alpha2/beta2 heterotetramer. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273083 [Multi-domain]  Cd Length: 442  Bit Score: 50.18  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422   14 LSPDDPELALILEELDdSKRDEIVDKARESLEETLQGMK--LTPAEELALGDELRQ-LRELGQKLEE-----------NT 79
Cdd:TIGR00450 125 LAPNNKVKDIALNKLA-GELDQKIEAIRKSLLQLLAQVEvnIDYEEDDDEQDSLNQlLLSIIAELKDilnsyklekldDG 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422   80 VEIAAFGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEhsatsehpgLEGARLVLVDTPGIDEVGGEVrETL-- 157
Cdd:TIGR00450 204 FKLAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFE---------LNGILIKLLDTAGIREHADFV-ERLgi 273
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 505062422  158 --AREVARHADLILFVV-SSDMQRCELEALSQLRQVQKPIILVFNQID 202
Cdd:TIGR00450 274 ekSFKAIKQADLVIYVLdASQPLTKDDFLIIDLNKSKKPFILVLNKID 321
 
Name Accession Description Interval E-value
COG3597 COG3597
Uncharacterized conserved protein, DUF697 family [Function unknown];
89-476 6.88e-44

Uncharacterized conserved protein, DUF697 family [Function unknown];


Pssm-ID: 442816 [Multi-domain]  Cd Length: 367  Bit Score: 158.31  E-value: 6.88e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  89 SRGKSSVLNALLGHEVFKVGTTHGTTVsrtsqrwehsatsEHPGLEGARLVLVDTPGIDEVGGEVRETLAREVARHADLI 168
Cdd:COG3597   14 SAGKTSLVGALLLTVGGLVGTGMGTTT-------------AAETYALKLVLLVLLLLLTDTGGILEAGAAGTLAELLALL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 169 LFVVSSDMQRCELEALSQLRQVQKPIILVFNQIDRYPETDRDQIYEKIKDERIRNLIRPEDVVMTAARPdPFKVKLQLPD 248
Cdd:COG3597   81 LAVEADLLLVVDDDDLRASELEILRALVLIGKKSLLLLVKLDLLEEALQEALLALLVLREVVEIAAAAV-AAAVAALQAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 249 GTTTVQWERPAPVIEPLKLRILDVLEREGKALVALNTLLLAGDLHEEIVA-HKLRIRDDAANRLIWNFALAkGAAVALNP 327
Cdd:COG3597  160 ALVAEELFEPEADIDLLLKRLAAALLAEGLLLLAAAILLAAQLLLEEAAAaAAGQRRRAAARRIILRYAIA-AAAVGAVP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 328 IPIADMAGGLAVDVGMIVALSKVYGIPLTRKTASSLVRDMMLALGALGAVEivtRLVAGGVKSslaglsilsgglaIPLt 407
Cdd:COG3597  239 IPFADLLALAALQAKMVAELAKIYGVELSRERAKELLASLGGGLGGLGLVR---QLLRSLLKL-------------IPG- 301
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505062422 408 aLGYGAIGLAQGGTASTTSYVLGHGAKHYLKQGCQWGPRGIKTVIHQILAEAKtdSVIDRLRDDLKRRV 476
Cdd:COG3597  302 -AGTVVGGAIQAATAAALTYALGRVAIEYFEKGGTFDPEGLKEVFKEAFQKAK--RFLKEFKQEAKARA 367
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
83-237 7.08e-43

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 148.93  E-value: 7.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  83 AAFGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEHsatsehpgLEGARLVLVDTPGIDEVG--GEVRETLARE 160
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWEL--------LPLGPVVLIDTPGLDEEGglGRERVEEARQ 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505062422 161 VARHADLILFVVSSDMQRCELEA-LSQLRQVQKPIILVFNQIDRYPETDRdqiyEKIKDERIRNLIRPEDVVMTAARP 237
Cdd:cd00880   73 VADRADLVLLVVDSDLTPVEEEAkLGLLRERGKPVLLVLNKIDLVPESEE----EELLRERKLELLPDLPVIAVSALP 146
DUF697 pfam05128
Domain of unknown function (DUF697); Family of bacterial hypothetical proteins that is ...
287-460 2.54e-33

Domain of unknown function (DUF697); Family of bacterial hypothetical proteins that is sometimes associated with GTPase domains.


Pssm-ID: 368297  Cd Length: 162  Bit Score: 123.43  E-value: 2.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  287 LLAGDLHEEIVAHKLRIRDDAANRLIWNFALAKGAAVALNPIPIADMAGGLAVDVGMIVALSKVYGIPLTRKTASSLVRD 366
Cdd:pfam05128   1 LQAAELLELAERELLEQRDRQAKKLIERYAWIVAGVVAVSPLALVDLLAVAARNARMIRELARLYGIELGYEGAIRLARS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  367 MMLALGALGAVEIVTRLVAGGVKSSLAGlsILSGglaipltalgygaiGLAQGGTASTTSYVLGHGAKHYLKQGCQWGPR 446
Cdd:pfam05128  81 VLANLAGLGAVELGTDLLKQALGLNLAT--KLSG--------------RAGQGVVAGYLTARVGLSAIEYCRPLPDWGDG 144
                         170
                  ....*....|....*..
gi 505062422  447 G---IKTVIHQILAEAK 460
Cdd:pfam05128 145 GrpkLSEVVQRLLSQLK 161
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
85-237 2.34e-32

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 121.02  E-value: 2.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  85 FGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEHSATSEhpglegaRLVLVDTPGIDEVGGEVRETLAREVARH 164
Cdd:cd00882    3 VGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDKGKV-------KLVLVDTPGLDEFGGLGREELARLLLRG 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505062422 165 ADLILFVVSSDMQRCELEA----LSQLRQVQKPIILVFNQIDRYPETDRDQIYEkikdERIRNLIRPEDVVMTAARP 237
Cdd:cd00882   76 ADLILLVVDSTDRESEEDAklliLRRLRKEGIPIILVGNKIDLLEEREVEELLR----LEELAKILGVPVFEVSAKT 148
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
82-281 3.30e-27

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 107.37  E-value: 3.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  82 IAAFGMVSRGKSSVLNALLGHEVF--KVGTTHGTTVSRTsqRWEHSATSehpglegARLVLVDTPGIDEVGgEVRETLAR 159
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFSleKYLSTNGVTIDKK--ELKLDGLD-------VDLVIWDTPGQDEFR-ETRQFYAR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 160 EVaRHADLILFVVSSDMQ---RCELEALSQLRQVQK--PIILVFNQIDRYPETDR---DQIYEKIKDERIrnlirpEDVV 231
Cdd:COG1100   76 QL-TGASLYLFVVDGTREetlQSLYELLESLRRLGKksPIILVLNKIDLYDEEEIedeERLKEALSEDNI------VEVV 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 505062422 232 MTAArpdpfkvklqlPDGtttvqwerpaPVIEPLKLRILDVLEREGKALV 281
Cdd:COG1100  149 ATSA-----------KTG----------EGVEELFAALAEILRGEGDSLD 177
YeeP COG3596
Predicted GTPase [General function prediction only];
41-364 1.55e-20

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 92.14  E-value: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  41 RESLEETLQGMKLTPAEelaLGDELRQLRElGQKLEENTVEIAAFGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSRTSQ 120
Cdd:COG3596    5 VSSLTERLEALKRLPQV---LRELLAEALE-RLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 121 RWEHSatsehpglEGARLVLVDTPGIDEVGG-EVRETLAREVARHADLILFVVSSDMQRC--ELEALSQLRQ--VQKPII 195
Cdd:COG3596   81 RLESD--------GLPGLVLLDTPGLGEVNErDREYRELRELLPEADLILWVVKADDRALatDEEFLQALRAqyPDPPVL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 196 LVFNQIDR-YPETDRDQIYEKIKDERIRNLIRpedvvMTAARPDPFKVKLQLPDGTTTvQWERPAPVIEPLKLRILDVLE 274
Cdd:COG3596  153 VVLTQVDRlEPEREWDPPYNWPSPPKEQNIRR-----ALEAIAEQLGVPIDRVIPVSA-AEDRTGYGLEELVDALAEALP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 275 REGKalvalntLLLAGDLHEEIVAH---KLRIRDDAANRLIWNFALAKGAAVALNPIPIADMAGGLAVDVGMIVALSKVY 351
Cdd:COG3596  227 EAKR-------SRLARLLRAKAIDRytlLAAAAALLAAALLALLALLLAALAAAPVALAGLGPAALKTALVASLAELALR 299
                        330
                 ....*....|...
gi 505062422 352 GIPLTRKTASSLV 364
Cdd:COG3596  300 AAAGAAAAAAELS 312
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
82-237 3.67e-19

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 84.91  E-value: 3.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  82 IAAFGMVSRGKSSVLNALLGHEVFKVGTTHgTTVSRTSQRWehsatsehpGLEGaRLVLVDTPGIDEVgGEVRETLAREV 161
Cdd:cd09912    3 LAVVGEFSAGKSTLLNALLGEEVLPTGVTP-TTAVITVLRY---------GLLK-GVVLVDTPGLNST-IEHHTEITESF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 162 ARHADLILFVVSSD--MQRCELEALSQLRQVQ-KPIILVFNQIDRY--PETDRDQIYEKIKDERIRNLIRPEDVVMTAAR 236
Cdd:cd09912   71 LPRADAVIFVLSADqpLTESEREFLKEILKWSgKKIFFVLNKIDLLseEELEEVLEYSREELGVLELGGGEPRIFPVSAK 150

                 .
gi 505062422 237 P 237
Cdd:cd09912  151 E 151
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
81-199 1.80e-17

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 78.04  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422   81 EIAAFGMVSRGKSSVLNALLGhEVFKVGTTHGTTVSRTSQRWEHsatsehpglEGARLVLVDTPGIDEvGGEVRETLARE 160
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTG-AKAIVSDYPGTTRDPNEGRLEL---------KGKQIILVDTPGLIE-GASEGEGLGRA 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 505062422  161 VARH--ADLILFVVSSDMQRCEL--EALSQLRQVQKPIILVFN 199
Cdd:pfam01926  70 FLAIieADLILFVVDSEEGITPLdeELLELLRENKKPIILVLN 112
Dynamin_N pfam00350
Dynamin family;
82-202 1.16e-14

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 71.49  E-value: 1.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422   82 IAAFGMVSRGKSSVLNALLGHEVFKVGTTHGT------TVSRTSQRWEHSATSEH------------------------- 130
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTrrptvlRLGESPGASEGAVKVEYkdgekkfedfselreeieketekia 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  131 ---------------PGLEGARLVLVDTPGIDEVggEVRET-LAREVARHADLILFVVS--SDMQRCELEALSQLRQVQK 192
Cdd:pfam00350  81 gtgkgissepivleiLSPLVPGLTLVDTPGLDSV--AVGDQeLTKEYIKPADIILAVTPanVDLSTSEALFLAREVDPNG 158
                         170
                  ....*....|
gi 505062422  193 PIILVFNQID 202
Cdd:pfam00350 159 KRTIGVLTKA 168
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
91-235 6.48e-14

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 69.41  E-value: 6.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVF----KVGTT----HG--TTvsrtsqrwehsatsehpglEGARLVLVDTPGI---DEVGGEVRETL 157
Cdd:cd04163   15 GKSTLLNALVGQKISivspKPQTTrnriRGiyTD-------------------DDAQIIFVDTPGIhkpKKKLGERMVKA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 158 AREVARHADLILFVVSSDMQRCELEA--LSQLRQVQKPIILVFNQIDRypETDRDQIYEKIkdERIRNLIRPEDVVMTAA 235
Cdd:cd04163   76 AWSALKDVDLVLFVVDASEWIGEGDEfiLELLKKSKTPVILVLNKIDL--VKDKEDLLPLL--EKLKELHPFAEIFPISA 151
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
91-203 1.16e-13

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 68.14  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWehsatsehpGLEGARLVLVDTPGIDEVGGEVRET--LAREVARHADLI 168
Cdd:cd11383    9 GKSSLCNALFGTEVAAVGDRRPTTRAAQAYVW---------QTGGDGLVLLDLPGVGERGRRDREYeeLYRRLLPEADLV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 505062422 169 LFVVSSDMQrceleALSQLRQVQ--------KPIILVFNQIDR 203
Cdd:cd11383   80 LWLLDADDR-----ALAADHDFYllplaghdAPLLFVLNQVDP 117
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
91-236 9.61e-12

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 65.40  E-value: 9.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVF----KVGTThgttvsRTSQRwehsatsehpG---LEGARLVLVDTPGIDEVGGEVRETL---ARE 160
Cdd:COG1159   15 GKSTLLNALVGQKVSivspKPQTT------RHRIR----------GivtREDAQIVFVDTPGIHKPKRKLGRRMnkaAWS 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505062422 161 VARHADLILFVVSSDMQRCELEA--LSQLRQVQKPIILVFNQIDRypeTDRDQIYEKIkdERIRNLIRPEDVVMTAAR 236
Cdd:COG1159   79 ALEDVDVILFVVDATEKIGEGDEfiLELLKKLKTPVILVINKIDL---VKKEELLPLL--AEYSELLDFAEIVPISAL 151
era PRK00089
GTPase Era; Reviewed
91-235 2.13e-11

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 64.68  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVfkvgtthgTTVSRTSQrwehsaTSEHP--G---LEGARLVLVDTPGIDEVG---GEVRETLAREVA 162
Cdd:PRK00089  17 GKSTLLNALVGQKI--------SIVSPKPQ------TTRHRirGivtEDDAQIIFVDTPGIHKPKralNRAMNKAAWSSL 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505062422 163 RHADLILFVVSSDMQRCELEA--LSQLRQVQKPIILVFNQIDRypETDRDQIYEKIKDerIRNLIRPEDVVMTAA 235
Cdd:PRK00089  83 KDVDLVLFVVDADEKIGPGDEfiLEKLKKVKTPVILVLNKIDL--VKDKEELLPLLEE--LSELMDFAEIVPISA 153
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
91-209 1.65e-10

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 59.43  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVFKVGTTHGTT---VSRTSQrwehsatsehpgLEGARLVLVDTPGIDEVGGEVrETL----AREVAR 163
Cdd:cd04164   15 GKSSLLNALAGRDRAIVSDIAGTTrdvIEEEID------------LGGIPVRLIDTAGLRETEDEI-EKIgierAREAIE 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 505062422 164 HADLILFVVSSDMQRCELEALSQLRQVQKPIILVFNQIDRYPETDR 209
Cdd:cd04164   82 EADLVLLVVDASEGLDEEDLEILELPAKKPVIVVLNKSDLLSDAEG 127
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
91-198 2.13e-08

AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).


Pssm-ID: 206651 [Multi-domain]  Cd Length: 201  Bit Score: 54.08  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVFKVGtTHGTTVSRTSQRweHSATsehpgLEGARLVLVDTPGIDEVGGEvRETLAREVAR------- 163
Cdd:cd01852   12 GKSATGNTILGRKVFESK-LSASGVTKTCQK--ESAV-----WDGRRVNVIDTPGLFDTSVS-PEQLSKEIIRclslsap 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 505062422 164 --HAdlILFVVS----SDMQRCELEALSQL--RQVQKPIILVF 198
Cdd:cd01852   83 gpHA--FLLVVPlgrfTEEEEQAVEELQELfgEKVLDHTIVLF 123
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
91-236 3.14e-08

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 55.84  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVfkvgtthgttvsrtsqrwehsA-TSEHPG-----------LEGARLVLVDTPGIDEVGGEVrETL- 157
Cdd:COG0486  225 GKSSLLNALLGEER---------------------AiVTDIAGttrdvieerinIGGIPVRLIDTAGLRETEDEV-EKIg 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 158 ---AREVARHADLILFVV--SSDMQRCELEALSQLRqvQKPIILVFNQIDRYPETDR---------------------DQ 211
Cdd:COG0486  283 ierAREAIEEADLVLLLLdaSEPLTEEDEEILEKLK--DKPVIVVLNKIDLPSEADGelkslpgepviaisaktgegiDE 360
                        170       180
                 ....*....|....*....|....*
gi 505062422 212 IYEKIKDERIRNLIRPEDVVMTAAR 236
Cdd:COG0486  361 LKEAILELVGEGALEGEGVLLTNAR 385
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
91-212 3.14e-08

tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 55.89  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVFKVGTTHGTT--VSRtsqrwehsatsEHPGLEGARLVLVDTPGIDEVGGEVrETL----AREVARH 164
Cdd:PRK05291 227 GKSSLLNALLGEERAIVTDIAGTTrdVIE-----------EHINLDGIPLRLIDTAGIRETDDEV-EKIgierSREAIEE 294
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 505062422 165 ADLILFVVSSDMQRCELEALSQLRQVQKPIILVFNQIDRYPETDRDQI 212
Cdd:PRK05291 295 ADLVLLVLDASEPLTEEDDEILEELKDKPVIVVLNKADLTGEIDLEEE 342
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
91-236 5.68e-08

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 54.41  E-value: 5.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422   91 GKSSVLNALLGHEVFKVGTTHGTT---VSRTSQrwehsatsehpgLEGARLVLVDTPGI----DEVGGE-VRetLAREVA 162
Cdd:pfam12631 106 GKSSLLNALLGEERAIVTDIPGTTrdvIEETIN------------IGGIPLRLIDTAGIretdDEVEKIgIE--RAREAI 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  163 RHADLILFVV-SSDMQRCELEALSQLRQVQKPIILVFNQIDRYPETDR--------------------DQIYEKIKDERI 221
Cdd:pfam12631 172 EEADLVLLVLdASRPLDEEDLEILELLKDKKPIIVVLNKSDLLGEIDEleelkgkpvlaisaktgeglDELEEAIKELFL 251
                         170
                  ....*....|....*
gi 505062422  222 RNLIRPEDVVMTAAR 236
Cdd:pfam12631 252 AGEIASDGPIITNAR 266
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
91-221 3.27e-07

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 50.92  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVF---KVGTTHGTTVSRtsqrwehsatSEHPGleGARLVLVDTPG-IDEVGGEV----RETLarEVA 162
Cdd:cd01878   53 GKSTLFNALTGADVLaedQLFATLDPTTRR----------IKLPG--GREVLLTDTVGfIRDLPHQLveafRSTL--EEV 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505062422 163 RHADLILFVV-SSDMQRCE-----LEALSQLRQVQKPIILVFNQIDRYPETDRDQIYEKIKDERI 221
Cdd:cd01878  119 AEADLLLHVVdASDPDREEqietvEEVLKELGADDIPIILVLNKIDLLDDEELEERLRAGRPDAV 183
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
91-202 5.86e-07

Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 48.99  E-value: 5.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVfKVGTTHGTTVSRTSQRWEHsatsehpglEGARLVLVDTPGI--------DEvggevretlarEVA 162
Cdd:cd01879    9 GKTTLFNALTGARQ-KVGNWPGVTVEKKEGEFKL---------GGKEIEIVDLPGTysltpyseDE-----------KVA 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 505062422 163 RH------ADLILFVV-SSDMQRCeLEALSQLRQVQKPIILVFNQID 202
Cdd:cd01879   68 RDfllgeePDLIVNVVdATNLERN-LYLTLQLLELGLPVVVALNMID 113
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
91-202 1.48e-06

Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 50.41  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVFKVGTTHGTTVSRtsqrweHSATSEhpgLEGARLVLVDTPGIDEVGGEVRETLAREVARHA----D 166
Cdd:COG1160   14 GKSTLFNRLTGRRDAIVDDTPGVTRDR------IYGEAE---WGGREFTLIDTGGIEPDDDDGLEAEIREQAELAieeaD 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 505062422 167 LILFVV-------SSDmqrcelEALSQ-LRQVQKPIILVFNQID 202
Cdd:COG1160   85 VILFVVdgragltPLD------EEIAKlLRRSGKPVILVVNKVD 122
mnmE_trmE_thdF TIGR00450
tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF ...
14-202 1.72e-06

tRNA modification GTPase TrmE; TrmE, also called MnmE and previously designated ThdF (thiophene and furan oxidation protein), is a GTPase involved in tRNA modification to create 5-methylaminomethyl-2-thiouridine in the wobble position of some tRNAs. This protein and GidA form an alpha2/beta2 heterotetramer. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273083 [Multi-domain]  Cd Length: 442  Bit Score: 50.18  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422   14 LSPDDPELALILEELDdSKRDEIVDKARESLEETLQGMK--LTPAEELALGDELRQ-LRELGQKLEE-----------NT 79
Cdd:TIGR00450 125 LAPNNKVKDIALNKLA-GELDQKIEAIRKSLLQLLAQVEvnIDYEEDDDEQDSLNQlLLSIIAELKDilnsyklekldDG 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422   80 VEIAAFGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEhsatsehpgLEGARLVLVDTPGIDEVGGEVrETL-- 157
Cdd:TIGR00450 204 FKLAIVGSPNVGKSSLLNALLKQDRAIVSDIKGTTRDVVEGDFE---------LNGILIKLLDTAGIREHADFV-ERLgi 273
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 505062422  158 --AREVARHADLILFVV-SSDMQRCELEALSQLRQVQKPIILVFNQID 202
Cdd:TIGR00450 274 ekSFKAIKQADLVIYVLdASQPLTKDDFLIIDLNKSKKPFILVLNKID 321
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
91-202 1.74e-06

Fe2+ transporter FeoB [Inorganic ion transport and metabolism];


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 50.50  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLG-HEvfKVGTTHGTTVSRTSQRWEHsatsehpglEGARLVLVDTPGI--------DEVggEVRETLAREv 161
Cdd:COG0370   15 GKTTLFNALTGsRQ--KVGNWPGVTVEKKEGKFKL---------KGKEIELVDLPGTyslsayspDEK--VARDFLLEE- 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 505062422 162 arHADLILFVV-SSDMQRcELEALSQLRQVQKPIILVFNQID 202
Cdd:COG0370   81 --KPDVVVNVVdATNLER-NLYLTLQLLELGIPVVLALNMMD 119
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
91-202 2.04e-06

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 47.43  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVFKVGTTHGTTVSRtsqrweHSATSEhpgLEGARLVLVDTPGIDEVG----GEVRETlAREVARHAD 166
Cdd:cd01894    9 GKSTLFNRLTGRRDAIVSDTPGVTRDR------KYGEAE---WGGREFILIDTGGIEPDDegisKEIREQ-AEIAIEEAD 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 505062422 167 LILFVVSSdmqRCELEAL-----SQLRQVQKPIILVFNQID 202
Cdd:cd01894   79 VILFVVDG---REGLTPAdeeiaKYLRKSKKPVILVVNKID 116
CrfC COG0699
Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, ...
61-203 2.68e-06

Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, recombination and repair];


Pssm-ID: 440463 [Multi-domain]  Cd Length: 582  Bit Score: 50.02  E-value: 2.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  61 LGDELRQLRELGQKLEENTVEIAAFGMVSRGKSSVLNALLGHEVFKVGTTHGT--------------------------- 113
Cdd:COG0699   14 RADLRRRLDQARLDLADPSLRIVMAGTTSQGKSQLVNALLGRRLLPSGAGETTgvpteikhaegssarllptagsvadtk 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 114 ---------------TVSRTSQR---------WEHSATS-EHPGLEGArLVLVDTPGIDEVGGEVRE-TLAREVARHADL 167
Cdd:COG0699   94 rwpgldteeiynpihQVSQTKKRrargsngpeVLRALVGlPHPLLRQG-LVIVDTPGLGALVGSEAElTLAKLPDADAVL 172
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 505062422 168 ILFVVSSDMQRCELEALSQLRQVQKP---IILVFNQIDR 203
Cdd:COG0699  173 VVLDADAEVTASEMELLRRVIQNLRIcpsVFVVLNKIDR 211
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
91-218 2.79e-06

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 48.74  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLghevFKVGTTH-------GTTVSRTS---QRWEHS--ATSEHPGLEGARLVLVDTPGIDEVGGEVRETLa 158
Cdd:cd04170   11 GKTTLAEALL----YATGAIDrlgrvedGNTVSDYDpeeKKRKMSieTSVAPLEWNGHKINLIDTPGYADFVGETLSAL- 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505062422 159 revaRHADLILFVVSSDMQR---CELeALSQLRQVQKPIILVFNQIDRyPETDRDQIYEKIKD 218
Cdd:cd04170   86 ----RAVDAALIVVEAQSGVevgTEK-VWEFLDDAKLPRIIFINKMDR-ARADFDKTLAALRE 142
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
91-214 3.01e-06

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 49.28  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEhsatsehpgLEGARLVLVDTPGI----DEVGGEVREtLAREVARHAD 166
Cdd:PRK00093  13 GKSTLFNRLTGKRDAIVADTPGVTRDRIYGEAE---------WLGREFILIDTGGIepddDGFEKQIRE-QAELAIEEAD 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505062422 167 LILFVVSSdmqRCEL----EALSQ-LRQVQKPIILVFNQIDRypETDRDQIYE 214
Cdd:PRK00093  83 VILFVVDG---RAGLtpadEEIAKiLRKSNKPVILVVNKVDG--PDEEADAYE 130
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
91-202 3.15e-06

Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 47.06  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422   91 GKSSVLNALLGHEVfKVGTTHGTTVSRTSQRWEHsatsehpglEGARLVLVDTPGI--------DEVggEVRETLAREva 162
Cdd:pfam02421  12 GKTTLFNALTGANQ-HVGNWPGVTVEKKEGKFKY---------KGYEIEIVDLPGIyslspyseEER--VARDYLLNE-- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 505062422  163 rHADLILFVV-SSDMQRCeLEALSQLRQVQKPIILVFNQID 202
Cdd:pfam02421  78 -KPDVIVNVVdATNLERN-LYLTLQLLELGLPVVLALNMMD 116
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
79-202 1.31e-05

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 45.44  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422   79 TVEIAAFGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSrtsqrweHSATSEHPGLEGARLVLVDTPGIDEVG----GEVR 154
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRN-------YVTTVIEEDGKTYKFNLLDTAGQEDYDairrLYYP 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 505062422  155 ETLAreVARHADLILFVVS-SDMQRCELEALSQLRQVQKPIILVFNQID 202
Cdd:TIGR00231  74 QVER--SLRVFDIVILVLDvEEILEKQTKEIIHHADSGVPIILVGNKID 120
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
86-219 1.36e-05

Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.


Pssm-ID: 206668 [Multi-domain]  Cd Length: 167  Bit Score: 45.46  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  86 GMVSRGKSSVLNALLGHEVfKVGTTHGTTVSrtsqrwEHSATSEHPglEGARLVLVDTPGI----DEVGGEVRETLAreV 161
Cdd:cd01881    4 GLPNVGKSTLLSALTSAKV-EIASYPFTTLE------PNVGVFEFG--DGVDIQIIDLPGLldgaSEGRGLGEQILA--H 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 162 ARHADLILFVVSSDMQ------------RCELeALSQLRQVQKPIILVFNQIDrypETDRDQIYEKIKDE 219
Cdd:cd01881   73 LYRSDLILHVIDASEDcvgdpledqktlNEEV-SGSFLFLKNKPEMIVANKID---MASENNLKRLKLDK 138
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
91-218 1.96e-05

50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 46.62  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  91 GKSSVLNALLGHEVF---KVGTTHGTTVSRTsqrwehsatsEHPGleGARLVLVDTpgideVGGeVRE-----------T 156
Cdd:COG2262  211 GKSTLFNRLTGADVLaedKLFATLDPTTRRL----------ELPD--GRPVLLTDT-----VGF-IRKlphqlveafrsT 272
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505062422 157 LarEVARHADLILFVV-SSDMQRceleaLSQLRQVQ----------KPIILVFNQIDRYPETDRDQIYEKIKD 218
Cdd:COG2262  273 L--EEVREADLLLHVVdASDPDF-----EEQIETVNevleelgaddKPIILVFNKIDLLDDEELERLRAGYPD 338
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
91-235 2.60e-05

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 44.91  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422   91 GKSSVLNALLGHEVFKVGtTHGTTVSRTSQRweHSATsehpgLEGARLVLVDTPGIDEvGGEVRETLAREVAR------- 163
Cdd:pfam04548  12 GKSATGNSILGRKAFESK-LRAQGVTKTCQL--VSRT-----WDGRIINVIDTPGLFD-LSVSNDFISKEIIRclllaep 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  164 --HAdlILFVVS-SDMQRCELEALSQLR-----QVQKPIILVFNQIDRYPETDRDQIYEKIKDERIRNLIRPEDVVMTAA 235
Cdd:pfam04548  83 gpHA--VLLVLSlGRFTEEEEQALRTLQelfgsKILDYMIVVFTRKDDLEDDSLDDYLSDGCPEFLKEVLRTADGEEKEE 160
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
11-202 3.66e-05

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 46.33  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  11 DSPLSPDDPELALILEELD-DSKRDEIVDKARESLEETLQGMKLTPAEELALGDELRQL---RELGQKLEENTVE----I 82
Cdd:PRK09518 199 TSFLSAADGVTTLDNSDLDfDETLDLLIGLVEDAIEEQEYDQYAANLEGYELDEGDEDLlegSGFVAGDEKAGPKavgvV 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  83 AAFGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEHSatsehpgleGARLVLVDTPGIDEVGGEVRETLAR--E 160
Cdd:PRK09518 279 AIVGRPNVGKSTLVNRILGRREAVVEDTPGVTRDRVSYDAEWA---------GTDFKLVDTGGWEADVEGIDSAIASqaQ 349
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 505062422 161 VA-RHADLILFVVSSDMQRCELEAL--SQLRQVQKPIILVFNQID 202
Cdd:PRK09518 350 IAvSLADAVVFVVDGQVGLTSTDERivRMLRRAGKPVVLAVNKID 394
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
81-222 8.23e-04

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206738  Cd Length: 278  Bit Score: 41.08  E-value: 8.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  81 EIAAFGMVSRGKSSVLNALLGHEVFKVGT--------------THGTTVSRTSQRW---------EHSATSEHPG-LEGA 136
Cdd:cd08771    5 QIVVVGDQSSGKSSVLEALVGRDFLPRGSgictrrplelqlrrSPSESDEDEKEEWgeflhlkskEFTDFEELREeIEKE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 137 --------------------------RLVLVDTPGIDEVGGEVR--------ETLAREVARHAD-LILFVVSSDMQRCEL 181
Cdd:cd08771   85 tdrvagenkgispepirleiespdvpNLTLVDLPGLIKVPVGDQpedieeqiRSMVKSYISNPRsIILAVVPANVDLANS 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 505062422 182 EALSQLRQV---QKPIILVFNQID-RYPETDRDQIYEKIKDERIR 222
Cdd:cd08771  165 EALKLAREVdpeGERTIGVLTKLDlMDPGTDAEDILLLLQGKVIP 209
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
137-231 1.26e-03

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 39.82  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  137 RLVLVDTPG----IDEVggevrETlareVARHADLILFVVSSDMQRCE--LEALSQLRQVQKPIILVFNQIDRYPETDRD 210
Cdd:pfam00009  70 LINLIDTPGhvdfVKEV-----IR----GLAQADGAILVVDAVEGVMPqtREHLRLARQLGVPIIVFINKMDRVDGAELE 140
                          90       100
                  ....*....|....*....|.
gi 505062422  211 QIYEKIKDERIRNLIRPEDVV 231
Cdd:pfam00009 141 EVVEEVSRELLEKYGEDGEFV 161
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
81-219 1.27e-03

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 39.42  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  81 EIAAFGmvsR---GKSSVLNALLG-HEVFKVGTTHGTTvsRTSQ--RWehsatsehpgleGARLVLVDTPG--------- 145
Cdd:cd01876    1 EVAFAG---RsnvGKSSLINALTNrKKLARTSKTPGRT--QLINffNV------------GDKFRLVDLPGygyakvske 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 146 -IDEVGGEV------RETLAREV----ARHADLILfvvssdmqrcELEALSQLRQVQKPIILVFNQIDRYPETDRDQIYE 214
Cdd:cd01876   64 vREKWGKLIeeylenRENLKGVVllidARHGPTPI----------DLEMLEFLEELGIPFLIVLTKADKLKKSELAKVLK 133

                 ....*
gi 505062422 215 KIKDE 219
Cdd:cd01876  134 KIKEE 138
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
137-229 1.97e-03

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 38.99  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 137 RLVLVDTPGiDEVGGEVRetlAReVARHADLILFVVSSD---MQRCElEALSQLRQVQKPIILVFNQIDRYPETDRDQiy 213
Cdd:cd01887   50 GITFIDTPG-HEAFTNMR---AR-GASVTDIAILVVAADdgvMPQTI-EAINHAKAANVPIIVAINKIDKPYGTEADP-- 121
                         90
                 ....*....|....*.
gi 505062422 214 EKIKDERIRNLIRPED 229
Cdd:cd01887  122 ERVKNELSELGLVGEE 137
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
91-146 2.19e-03

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 39.05  E-value: 2.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505062422  91 GKSSVLNALLGHEVFKVGTTHGTTvsrTSQRWEHSAtsehPGLEgarlvLVDTPGI 146
Cdd:cd01856  127 GKSTLINRLRGKKVAKVGNKPGVT---RGQQWIRIG----PNIE-----LLDTPGI 170
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
82-175 2.77e-03

Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 39.45  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  82 IAAFGMVSRGKSSVLNALLGHEVfKVGTTHGTTVsrtsqrwehsaTSeHPGL---EGARLVLVDTPGIDEvG-----GEV 153
Cdd:cd01896    3 VALVGFPSVGKSTLLSKLTNTKS-EVAAYEFTTL-----------TC-VPGVmeyKGAKIQLLDLPGIIE-GasdgkGRG 68
                         90       100
                 ....*....|....*....|..
gi 505062422 154 RETLAreVARHADLILFVVSSD 175
Cdd:cd01896   69 RQVIA--VARTADLILIVLDAT 88
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
91-150 3.72e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 38.53  E-value: 3.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505062422  91 GKSSVLNALLGHEVFKVGtthgtTVSRTSQRWEHSAT-SE-HPGLEGArlVLVDTPGIDEVG 150
Cdd:cd01854   97 GKSTLLNALLPELVLATG-----EISEKLGRGRHTTThRElFPLPGGG--LIIDTPGFRELG 151
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
57-202 4.42e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 39.57  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  57 EELALGDElrQLRELGQKLEENTVEIAAFGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEHSatsehpgleGA 136
Cdd:PRK03003  18 SDWELDDE--DLAELEAAEGGPLPVVAVVGRPNVGKSTLVNRILGRREAVVEDVPGVTRDRVSYDAEWN---------GR 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505062422 137 RLVLVDTPGIDEVGGEVRETLAR--EVA-RHADLILFVVSSDMQRCEL-EALSQ-LRQVQKPIILVFNQID 202
Cdd:PRK03003  87 RFTVVDTGGWEPDAKGLQASVAEqaEVAmRTADAVLFVVDATVGATATdEAVARvLRRSGKPVILAANKVD 157
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
73-147 4.47e-03

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 38.46  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  73 QKLEENTVEIAAFGMVSRGKSSVLNALLG-HEVFKVGTTHGTTvsrTSQRW------EHSATSEHPglegarLVLVDTPG 145
Cdd:cd01851    1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGtSDGFDVMDTSQQT---TKGIWmwsdpfKDTDGKKHA------VLLLDTEG 71

                 ..
gi 505062422 146 ID 147
Cdd:cd01851   72 TD 73
YcjF COG3768
Uncharacterized membrane protein YcjF, UPF0283 family [Function unknown];
301-403 5.80e-03

Uncharacterized membrane protein YcjF, UPF0283 family [Function unknown];


Pssm-ID: 442982  Cd Length: 339  Bit Score: 38.68  E-value: 5.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 301 LRIRDDAANRLIWNFALAKGAAVALNPIPIADMAGGLAVDVGMIVALSKVYGIPLTrkTASS--LVRDMMLALGALGAVE 378
Cdd:COG3768  189 LAPLDAQARREISRAAREVAVVTAVSPLALVDMAFVLWRNLRMIRRIAELYGGRPG--YLGRlrLFRAVLAHLAVTGASA 266
                         90       100
                 ....*....|....*....|....*
gi 505062422 379 IVTRLvaggvksslaGLSILSGGLA 403
Cdd:COG3768  267 VGDDL----------GQQVLGHGLA 281
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
82-229 5.85e-03

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 37.66  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  82 IAAFGMVSRGKSSVLNALLG--HEVFKVGTTHGTTVSRTSQRWE-----HSATSEHPgLEGARLVLVDTPG-IDEVggev 153
Cdd:cd00881    2 VGVIGHVDHGKTTLTGSLLYqtGAIDRRGTRKETFLDTLKEERErgitiKTGVVEFE-WPKRRINFIDTPGhEDFS---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422 154 RETLAreVARHADLILFVVSSD----MQrcELEALSQLRQVQKPIILVFNQIDRYPETDRDQIYEKIKdERIRNLIRPED 229
Cdd:cd00881   77 KETVR--GLAQADGALLVVDANegvePQ--TREHLNIALAGGLPIIVAVNKIDRVGEEDFDEVLREIK-ELLKLIGFTFL 151
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
57-146 7.17e-03

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 36.98  E-value: 7.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  57 EELALGDELRQLRELGQKLEENTVEIaaFGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEHsatsehpglega 136
Cdd:cd01849   71 GILKLKAEITKQKLKLKYKKGIRVGV--VGLPNVGKSSFINALLNKFKLKVGSIPGTTKLQQDVKLDK------------ 136
                         90
                 ....*....|
gi 505062422 137 RLVLVDTPGI 146
Cdd:cd01849  137 EIYLYDTPGI 146
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
91-146 7.58e-03

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. Since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 37.41  E-value: 7.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505062422  91 GKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEHsatsehpglEGARLVLVDTPGI 146
Cdd:cd01895   14 GKSSLLNALLGEERVIVSDIAGTTRDSIDVPFEY---------DGQKYTLIDTAGI 60
PRK13351 PRK13351
elongation factor G-like protein;
82-203 7.60e-03

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 38.78  E-value: 7.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  82 IAAFGMVSRGKSSVLNALL--GHEVFKVGTTH-GTTVSR-TSQRWEH----SATSEHPGLEGARLVLVDTPGIDEVGGEV 153
Cdd:PRK13351  11 IGILAHIDAGKTTLTERILfyTGKIHKMGEVEdGTTVTDwMPQEQERgitiESAATSCDWDNHRINLIDTPGHIDFTGEV 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 505062422 154 RETLarevaRHADLILFVVSSDM--QRCELEALSQLRQVQKPIILVFNQIDR 203
Cdd:PRK13351  91 ERSL-----RVLDGAVVVFDAVTgvQPQTETVWRQADRYGIPRLIFINKMDR 137
PRK01889 PRK01889
GTPase RsgA; Reviewed
91-150 8.10e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 38.38  E-value: 8.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505062422  91 GKSSVLNALLGHEVFKVGTT--------HgTTVSRtsqrwehsatSEHPGLEGArlVLVDTPGIDEVG 150
Cdd:PRK01889 207 GKSTLVNALLGEEVQKTGAVreddskgrH-TTTHR----------ELHPLPSGG--LLIDTPGMRELQ 261
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
69-219 8.41e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 38.62  E-value: 8.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505062422  69 RELGQKLEENTVEIAAFGMVSRGKSSVLNALLGHEVFKVGTTHGTTVSRTSQRWEhsatsehpgLEGARLVLVDTPGIDE 148
Cdd:PRK09518 440 KTSGFLTPSGLRRVALVGRPNVGKSSLLNQLTHEERAVVNDLAGTTRDPVDEIVE---------IDGEDWLFIDTAGIKR 510
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505062422 149 -----VGGEVRETL-AREVARHADLILFVV--SSDMQRCELEALSQLRQVQKPIILVFNQIDRYPETDRDQIYEKIKDE 219
Cdd:PRK09518 511 rqhklTGAEYYSSLrTQAAIERSELALFLFdaSQPISEQDLKVMSMAVDAGRALVLVFNKWDLMDEFRRQRLERLWKTE 589
 
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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