NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|737122455|ref|WP_035110143|]
View 

ferrous iron transport protein B [Clostridium tetani]

Protein Classification

ferrous iron transporter B( domain architecture ID 11417566)

ferrous iron transporter B is part of an Fe(2+) uptake system that is probably driven by GTP hydrolysis

CATH:  1.10.287.1770
Gene Symbol:  feoB
Gene Ontology:  GO:0015093|GO:0005525|GO:0006826
PubMed:  12446835
SCOP:  4004042
TCDB:  9.A.8

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-587 0e+00

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


:

Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 851.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   1 MITVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENI 77
Cdd:COG0370    3 MITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFklkGKEIELVDLPGTYSLSAYSPDEKVARDFLLEEKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  78 DVILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETL--- 154
Cdd:COG0370   83 DVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAIiea 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 155 ---KVSNFSDINIDNEF---------------------------------------------QFRSE------------- 173
Cdd:COG0370  163 aegKKPRPLRIDYPEEIeeaieeleelleedgpypsrwlaikllegdeevlellsellelleEIREEleeelgedlesii 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 174 -EETYSLIEKVLEKTVVYSNSNKSSITDKIDNLLLNRFLAYPIFLGILYFIFQFTFSWvGQPLSDLLDEGLnDSLIPYLN 252
Cdd:COG0370  243 aDARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTV-GAPLMDLIDGGF-GWLGDWVA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 253 DSLSSlsPWFKSLLVDGIVGGIGSVIVFLPIILALFLGISFLEDSGYMSRAAFIMDKLMRRMGLSGKAFIPLIIGFGCSV 332
Cdd:COG0370  321 ALLPP--GWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 333 PGIMASRTLESEKDRKLTALLVPLMSCNARLPVYALFASVFFPGNETLIVFSLYLLGILIAFLIGLLFKNTIFKKDEEPF 412
Cdd:COG0370  399 PAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPSPF 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 413 IIELSQYKMPGFKSLTKLTWEKGKGFLKKAGTIIFAASVVIWFLSNFNFTGMVE-MNDSLLASIGKFIAPIFKPLGFgSW 491
Cdd:COG0370  479 VMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGESEdLENSYLGRIGKALEPVFAPLGF-DW 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 492 ENSVAILTGITAKEIILSSMGVIYG--------GNLREVLPNHFTILSSYSFLVFVLLYTPCVSVVAAMKKEYGN-KMMF 562
Cdd:COG0370  558 QIGVALITGFAAKEVVVGTLGTLYGvgedaeesASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGSwKWTL 637
                        650       660
                 ....*....|....*....|....*
gi 737122455 563 LSVFYQLVLAWIVSFIAYNIGLLLI 587
Cdd:COG0370  638 FAVGYMTVLAYLVAFLVYQIGRLLG 662
 
Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-587 0e+00

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 851.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   1 MITVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENI 77
Cdd:COG0370    3 MITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFklkGKEIELVDLPGTYSLSAYSPDEKVARDFLLEEKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  78 DVILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETL--- 154
Cdd:COG0370   83 DVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAIiea 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 155 ---KVSNFSDINIDNEF---------------------------------------------QFRSE------------- 173
Cdd:COG0370  163 aegKKPRPLRIDYPEEIeeaieeleelleedgpypsrwlaikllegdeevlellsellelleEIREEleeelgedlesii 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 174 -EETYSLIEKVLEKTVVYSNSNKSSITDKIDNLLLNRFLAYPIFLGILYFIFQFTFSWvGQPLSDLLDEGLnDSLIPYLN 252
Cdd:COG0370  243 aDARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTV-GAPLMDLIDGGF-GWLGDWVA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 253 DSLSSlsPWFKSLLVDGIVGGIGSVIVFLPIILALFLGISFLEDSGYMSRAAFIMDKLMRRMGLSGKAFIPLIIGFGCSV 332
Cdd:COG0370  321 ALLPP--GWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 333 PGIMASRTLESEKDRKLTALLVPLMSCNARLPVYALFASVFFPGNETLIVFSLYLLGILIAFLIGLLFKNTIFKKDEEPF 412
Cdd:COG0370  399 PAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPSPF 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 413 IIELSQYKMPGFKSLTKLTWEKGKGFLKKAGTIIFAASVVIWFLSNFNFTGMVE-MNDSLLASIGKFIAPIFKPLGFgSW 491
Cdd:COG0370  479 VMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGESEdLENSYLGRIGKALEPVFAPLGF-DW 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 492 ENSVAILTGITAKEIILSSMGVIYG--------GNLREVLPNHFTILSSYSFLVFVLLYTPCVSVVAAMKKEYGN-KMMF 562
Cdd:COG0370  558 QIGVALITGFAAKEVVVGTLGTLYGvgedaeesASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGSwKWTL 637
                        650       660
                 ....*....|....*....|....*
gi 737122455 563 LSVFYQLVLAWIVSFIAYNIGLLLI 587
Cdd:COG0370  638 FAVGYMTVLAYLVAFLVYQIGRLLG 662
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
8-555 0e+00

ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 538.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455    8 GNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENIDVILNIA 84
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLgfqGEDIEIVDLPGIYSLTTFSLEEEVARDYLLNEKPDLVVNVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   85 DASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETLKVSN------ 158
Cdd:TIGR00437  81 DASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGRGIERLKDAIRKAIglkelk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  159 -----------------FSDINIDNEFQFRSEEE----------TYSLIEKVLEKTVVYSNSNKSSITD----------- 200
Cdd:TIGR00437 161 kraieivpeayqvvevvEGLIEIIYSISKRGLEIllglledlslEIEKIERNLAEVVIKESPSNLSPTEiadedrvlvek 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  201 KIDNLLLNRFLAYPIFLGILYFIFQFTFSwVGQPLSDLLdEGLNDSLIPYLNDSLSSlsPWFKSLLVDGIVGGIGSVIVF 280
Cdd:TIGR00437 241 SIGRKILDRFLGLPIFLFVMFILFLLTFL-VGQPLVDLI-ETGFSFLSEAVKSFIGN--YWLASLLGDGLIGGVGAVLSF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  281 LPIILALFLGISFLEDSGYMSRAAFIMDKLMRRMGLSGKAFIPLIIGFGCSVPGIMASRTLESEKDRKLTALLVPLMSCN 360
Cdd:TIGR00437 317 VPLIAILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPAIMATRTLETRRERLLTALVIPFMSCS 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  361 ARLPVY-ALFASVFFPGNETLIVFSLYLLGILIAFLIGLLFKNTIFKKDEEPFIIELSQYKMPGFKSLTKLTWEKGKGFL 439
Cdd:TIGR00437 397 ARLPVIvLLFAAAFPGKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFIMELPPYRLPRFRVVFIQTWTRLRSFI 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  440 KKAGTIIFAASVVIWFLSNFnftGMVEMNDSLLASIGKFIAPIFKPLGFG-SWENSVAILTGITAKEIILSSMGVIYG-G 517
Cdd:TIGR00437 477 KKAGTIIVIGSVLIWFLSSF---PGGKILESWLAAIGSIMAPLFVPLGKIlDWFASVALIFGFVAKEVVVATLGVLYGlG 553
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 737122455  518 NLREVLPNHFTILSSYSFLVFVLLYTPCVSVVAAMKKE 555
Cdd:TIGR00437 554 NILSSIGHAMVPVEALSYMLFVLLYVPCLATLAAIARE 591
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
2-582 9.61e-168

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 496.16  E-value: 9.61e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   2 ITVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNE----EKVSKNYLST 74
Cdd:PRK09554   4 LTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFsttDHQVTLVDLPGTYSLTTISSQtsldEQIACHYILS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  75 ENIDVILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETL 154
Cdd:PRK09554  84 GDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEALKLAI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 155 --------------------KVSNFSDINIDN--------------------------------EFQFRSEEET------ 176
Cdd:PRK09554 164 drhqanenvelvhypqpllnEADSLAKVMPSDiplqqrrwlglqmlegdiysrayageasqhldAALARLRNEMddpalh 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 177 -----YSLIEKVLEKTVVYSNSNKSSITDKIDNLLLNRFLAYPIFLGILYFIFQFTFSWVG--QPLSDLLDEGLNDSLIP 249
Cdd:PRK09554 244 iadarYQCIAAICDAVSNTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIGGalQPLFDVGSVAIFIHGIQ 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 250 YLNDSLSsLSPWFKSLLVDGIVGGIGSVIVFLPIILALFLGISFLEDSGYMSRAAFIMDKLMRRMGLSGKAFIPLIIGFG 329
Cdd:PRK09554 324 WLGYTLH-FPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 330 CSVPGIMASRTLESEKDRKLTALLVPLMSCNARLPVYALFASVFFPGNETLIVFSLYLLGILIAFLIGLLFKNTIFKKDE 409
Cdd:PRK09554 403 CNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLGIVMAILTGLMLKYTIMRGEA 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 410 EPFIIELSQYKMPGFKSLTKLTWEKGKGFLKKAGTIIFAASVVIWFLSNFNFTGMV--EMNDSLLASIGKFIAPIFKPLG 487
Cdd:PRK09554 483 SPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIvdNINDSALASVSRVITPVLKPIG 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 488 FGS--WENSVAILTGITAKEIILSSMGVIYGG---NLREVLPNHFTIL-------------------------------- 530
Cdd:PRK09554 563 VHEdnWQATVGLFTGAMAKEVVVGTLNTLYTAeniQDEEFNPAEFNLGdelfgavdetwqslkdtfslsvlanpieaskg 642
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737122455 531 --------------------SSYSFLVFVLLYTPCVSVVAAMKKEYGNKMMFLSVFYQLVLAWIVSFIAYNI 582
Cdd:PRK09554 643 dgemgtgamgvmsqkfgsaaAAYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQV 714
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
5-155 5.25e-85

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: 261.62  E-value: 5.25e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   5 ALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENIDVIL 81
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFklgGKEIEIVDLPGTYSLTPYSEDEKVARDFLLGEEPDLIV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737122455  82 NIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETLK 155
Cdd:cd01879   81 NVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDELLDAIA 154
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
2-154 7.92e-84

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: 258.53  E-value: 7.92e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455    2 ITVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEG---YIDNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENID 78
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGkfkYKGYEIEIVDLPGIYSLSPYSEEERVARDYLLNEKPD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737122455   79 VILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETL 154
Cdd:pfam02421  81 VIVNVVDATNLERNLYLTLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSARKGEGIDELLDAI 156
 
Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-587 0e+00

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 851.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   1 MITVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENI 77
Cdd:COG0370    3 MITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFklkGKEIELVDLPGTYSLSAYSPDEKVARDFLLEEKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  78 DVILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETL--- 154
Cdd:COG0370   83 DVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAIiea 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 155 ---KVSNFSDINIDNEF---------------------------------------------QFRSE------------- 173
Cdd:COG0370  163 aegKKPRPLRIDYPEEIeeaieeleelleedgpypsrwlaikllegdeevlellsellelleEIREEleeelgedlesii 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 174 -EETYSLIEKVLEKTVVYSNSNKSSITDKIDNLLLNRFLAYPIFLGILYFIFQFTFSWvGQPLSDLLDEGLnDSLIPYLN 252
Cdd:COG0370  243 aDARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTV-GAPLMDLIDGGF-GWLGDWVA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 253 DSLSSlsPWFKSLLVDGIVGGIGSVIVFLPIILALFLGISFLEDSGYMSRAAFIMDKLMRRMGLSGKAFIPLIIGFGCSV 332
Cdd:COG0370  321 ALLPP--GWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 333 PGIMASRTLESEKDRKLTALLVPLMSCNARLPVYALFASVFFPGNETLIVFSLYLLGILIAFLIGLLFKNTIFKKDEEPF 412
Cdd:COG0370  399 PAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPSPF 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 413 IIELSQYKMPGFKSLTKLTWEKGKGFLKKAGTIIFAASVVIWFLSNFNFTGMVE-MNDSLLASIGKFIAPIFKPLGFgSW 491
Cdd:COG0370  479 VMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGESEdLENSYLGRIGKALEPVFAPLGF-DW 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 492 ENSVAILTGITAKEIILSSMGVIYG--------GNLREVLPNHFTILSSYSFLVFVLLYTPCVSVVAAMKKEYGN-KMMF 562
Cdd:COG0370  558 QIGVALITGFAAKEVVVGTLGTLYGvgedaeesASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGSwKWTL 637
                        650       660
                 ....*....|....*....|....*
gi 737122455 563 LSVFYQLVLAWIVSFIAYNIGLLLI 587
Cdd:COG0370  638 FAVGYMTVLAYLVAFLVYQIGRLLG 662
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
8-555 0e+00

ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane protein required for iron(II) update, is encoded in an operon with FeoA (75 amino acids), which is also required, and is regulated by Fur. There appear to be two copies in Archaeoglobus fulgidus and Clostridium acetobutylicum. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273077 [Multi-domain]  Cd Length: 591  Bit Score: 538.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455    8 GNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENIDVILNIA 84
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLgfqGEDIEIVDLPGIYSLTTFSLEEEVARDYLLNEKPDLVVNVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   85 DASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETLKVSN------ 158
Cdd:TIGR00437  81 DASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGRGIERLKDAIRKAIglkelk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  159 -----------------FSDINIDNEFQFRSEEE----------TYSLIEKVLEKTVVYSNSNKSSITD----------- 200
Cdd:TIGR00437 161 kraieivpeayqvvevvEGLIEIIYSISKRGLEIllglledlslEIEKIERNLAEVVIKESPSNLSPTEiadedrvlvek 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  201 KIDNLLLNRFLAYPIFLGILYFIFQFTFSwVGQPLSDLLdEGLNDSLIPYLNDSLSSlsPWFKSLLVDGIVGGIGSVIVF 280
Cdd:TIGR00437 241 SIGRKILDRFLGLPIFLFVMFILFLLTFL-VGQPLVDLI-ETGFSFLSEAVKSFIGN--YWLASLLGDGLIGGVGAVLSF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  281 LPIILALFLGISFLEDSGYMSRAAFIMDKLMRRMGLSGKAFIPLIIGFGCSVPGIMASRTLESEKDRKLTALLVPLMSCN 360
Cdd:TIGR00437 317 VPLIAILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPAIMATRTLETRRERLLTALVIPFMSCS 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  361 ARLPVY-ALFASVFFPGNETLIVFSLYLLGILIAFLIGLLFKNTIFKKDEEPFIIELSQYKMPGFKSLTKLTWEKGKGFL 439
Cdd:TIGR00437 397 ARLPVIvLLFAAAFPGKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFIMELPPYRLPRFRVVFIQTWTRLRSFI 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  440 KKAGTIIFAASVVIWFLSNFnftGMVEMNDSLLASIGKFIAPIFKPLGFG-SWENSVAILTGITAKEIILSSMGVIYG-G 517
Cdd:TIGR00437 477 KKAGTIIVIGSVLIWFLSSF---PGGKILESWLAAIGSIMAPLFVPLGKIlDWFASVALIFGFVAKEVVVATLGVLYGlG 553
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 737122455  518 NLREVLPNHFTILSSYSFLVFVLLYTPCVSVVAAMKKE 555
Cdd:TIGR00437 554 NILSSIGHAMVPVEALSYMLFVLLYVPCLATLAAIARE 591
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
2-582 9.61e-168

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 496.16  E-value: 9.61e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   2 ITVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNE----EKVSKNYLST 74
Cdd:PRK09554   4 LTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFsttDHQVTLVDLPGTYSLTTISSQtsldEQIACHYILS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  75 ENIDVILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETL 154
Cdd:PRK09554  84 GDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEALKLAI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 155 --------------------KVSNFSDINIDN--------------------------------EFQFRSEEET------ 176
Cdd:PRK09554 164 drhqanenvelvhypqpllnEADSLAKVMPSDiplqqrrwlglqmlegdiysrayageasqhldAALARLRNEMddpalh 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 177 -----YSLIEKVLEKTVVYSNSNKSSITDKIDNLLLNRFLAYPIFLGILYFIFQFTFSWVG--QPLSDLLDEGLNDSLIP 249
Cdd:PRK09554 244 iadarYQCIAAICDAVSNTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIGGalQPLFDVGSVAIFIHGIQ 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 250 YLNDSLSsLSPWFKSLLVDGIVGGIGSVIVFLPIILALFLGISFLEDSGYMSRAAFIMDKLMRRMGLSGKAFIPLIIGFG 329
Cdd:PRK09554 324 WLGYTLH-FPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 330 CSVPGIMASRTLESEKDRKLTALLVPLMSCNARLPVYALFASVFFPGNETLIVFSLYLLGILIAFLIGLLFKNTIFKKDE 409
Cdd:PRK09554 403 CNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLGIVMAILTGLMLKYTIMRGEA 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 410 EPFIIELSQYKMPGFKSLTKLTWEKGKGFLKKAGTIIFAASVVIWFLSNFNFTGMV--EMNDSLLASIGKFIAPIFKPLG 487
Cdd:PRK09554 483 SPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIvdNINDSALASVSRVITPVLKPIG 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 488 FGS--WENSVAILTGITAKEIILSSMGVIYGG---NLREVLPNHFTIL-------------------------------- 530
Cdd:PRK09554 563 VHEdnWQATVGLFTGAMAKEVVVGTLNTLYTAeniQDEEFNPAEFNLGdelfgavdetwqslkdtfslsvlanpieaskg 642
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737122455 531 --------------------SSYSFLVFVLLYTPCVSVVAAMKKEYGNKMMFLSVFYQLVLAWIVSFIAYNI 582
Cdd:PRK09554 643 dgemgtgamgvmsqkfgsaaAAYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQV 714
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
5-155 5.25e-85

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: 261.62  E-value: 5.25e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   5 ALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENIDVIL 81
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFklgGKEIEIVDLPGTYSLTPYSEDEKVARDFLLGEEPDLIV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737122455  82 NIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETLK 155
Cdd:cd01879   81 NVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDELLDAIA 154
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
2-154 7.92e-84

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: 258.53  E-value: 7.92e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455    2 ITVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEG---YIDNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENID 78
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGkfkYKGYEIEIVDLPGIYSLSPYSEEERVARDYLLNEKPD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737122455   79 VILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETL 154
Cdd:pfam02421  81 VIVNVVDATNLERNLYLTLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSARKGEGIDELLDAI 156
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
5-154 4.58e-28

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: 110.03  E-value: 4.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   5 ALVGNPNVGKTSLFNALTGSNQ-YVGNWAGVT--VEKKEGYIDNL--VKIVDLPGIYAMDTYSnEEKVSKNYLSTENIDV 79
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVgIVSPIPGTTrdPVRKEWELLPLgpVVLIDTPGLDEEGGLG-RERVEEARQVADRADL 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737122455  80 ILNIADASNLERNLYLTYQ-LKEFKKPIILLLNMMDIVEEK--NIKIDLELLSRELNVKVIPISASKNMGIDKLKETL 154
Cdd:cd00880   80 VLLVVDSDLTPVEEEAKLGlLRERGKPVLLVLNKIDLVPESeeEELLRERKLELLPDLPVIAVSALPGEGIDELRKKI 157
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
3-112 3.03e-24

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: 97.69  E-value: 3.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455    3 TVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYamDTYSNEEKVSKNYLSTENIDV 79
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLelkGKQIILVDTPGLI--EGASEGEGLGRAFLAIIEADL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 737122455   80 ILNIADASNL--ERNLYLTYQLKEFKKPIILLLNM 112
Cdd:pfam01926  79 ILFVVDSEEGitPLDEELLELLRENKKPIILVLNK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
5-154 1.51e-20

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: 88.67  E-value: 1.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   5 ALVGNPNVGKTSLFNALTGSNQY-VGNWAGVTVE-----KKEGYIDNLVKIVDLPGIYAMDtYSNEEKVSKNYLSTenID 78
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGeVSDVPGTTRDpdvyvKELDKGKVKLVLVDTPGLDEFG-GLGREELARLLLRG--AD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  79 VILNIADASNLE----RNLYLTYQLKEFKKPIILLLNMMDIVEEKNIK--IDLELLSRELNVKVIPISASKNMGIDKLKE 152
Cdd:cd00882   78 LILLVVDSTDREseedAKLLILRRLRKEGIPIILVGNKIDLLEEREVEelLRLEELAKILGVPVFEVSAKTGEGVDELFE 157

                 ..
gi 737122455 153 TL 154
Cdd:cd00882  158 KL 159
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
277-370 1.74e-15

Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for determining nucleoside specificity in the human CNT1 and CNT2 proteins. In the FeoB proteins, which are believed to be Fe2+ transporters, it includes the membrane pore region, so the function of this region is likely to be more general than just nucleoside specificity. This family may represent the pore and gate, with a wide potential range of specificity. Hence its name 'Gate'.


Pssm-ID: 429586 [Multi-domain]  Cd Length: 101  Bit Score: 72.29  E-value: 1.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  277 VIVFLPIILALFLGISFLEDSGYMSRAAFIMDKLMRRMG---LSGKAFIPLIIGFGC---SVPGIMASRTLESEKDRKLT 350
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYSGLLDRIGKLLGPLMRPLGlfpLPGKAAIALLLGFGAkevGVPLLATPYGIDTPRERLAA 80
                          90       100
                  ....*....|....*....|.
gi 737122455  351 ALLVPLMS-CNARLPVYALFA 370
Cdd:pfam07670  81 LLFTSFSTpCGATLPVYAGEL 101
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
5-153 4.69e-15

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: 73.20  E-value: 4.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   5 ALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYIDNL----VKIVDLPGIYAmDTYSNEEKVSKNYLSTENIDVI 80
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGdgvdIQIIDLPGLLD-GASEGRGLGEQILAHLYRSDLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  81 LNIADASN------LERNLYLTYQLKEFK-----KPIILLLNMMDIVEEKNIKIDLELLSRElNVKVIPISASKNMGIDK 149
Cdd:cd01881   80 LHVIDASEdcvgdpLEDQKTLNEEVSGSFlflknKPEMIVANKIDMASENNLKRLKLDKLKR-GIPVVPTSALTRLGLDR 158

                 ....
gi 737122455 150 LKET 153
Cdd:cd01881  159 VIRT 162
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
3-155 5.00e-15

Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in eukaryotes ranging from trypanosomes to humans. NOG1 is functionally linked to ribosome biogenesis and found in association with the nuclear pore complexes and identified in many preribosomal complexes. Thus, defects in NOG1 can lead to defects in 60S biogenesis. The S. cerevisiae NOG1 gene is essential for cell viability, and mutations in the predicted G motifs abrogate function. It is a member of the ODN family of GTP-binding proteins that also includes the bacterial Obg and DRG proteins.


Pssm-ID: 206684 [Multi-domain]  Cd Length: 167  Bit Score: 72.98  E-value: 5.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   3 TVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYID---NLVKIVDLPGI--YAMDTYSNEEKVSKNYLstENI 77
Cdd:cd01897    2 TLVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDykyLRWQVIDTPGIldRPLEERNTIEMQAITAL--AHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  78 -DVILNIADASN-----LERNLYLTYQLKE-FKKPIILLLNMMDIVEEKNIKIDLELLSRElNVKVIPISASKNMGIDKL 150
Cdd:cd01897   80 rAAVLFFIDPSEtcgysIEEQLSLFKEIKPlFNKPVIVVLNKIDLLTEEDLSEIEKELEKE-GEEVIKISTLTEEGVDEL 158

                 ....*
gi 737122455 151 KETLK 155
Cdd:cd01897  159 KNKAC 163
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
2-154 9.73e-15

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 72.32  E-value: 9.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   2 ITVALVGNPNVGKTSLFNALTGsnQYVGNWA-----GVTVEKKEGYIDNL---VKIVDLPGIyamDTYsneEKVSKNYLS 73
Cdd:COG1100    4 KKIVVVGTGGVGKTSLVNRLVG--DIFSLEKylstnGVTIDKKELKLDGLdvdLVIWDTPGQ---DEF---RETRQFYAR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  74 T-ENIDVILNIADAS---NLERNLYLTYQLKEFKK--PIILLLNMMDIVEEKNIKIDLEL---LSRELNVKVIPISASKN 144
Cdd:COG1100   76 QlTGASLYLFVVDGTreeTLQSLYELLESLRRLGKksPIILVLNKIDLYDEEEIEDEERLkeaLSEDNIVEVVATSAKTG 155
                        170
                 ....*....|
gi 737122455 145 MGIDKLKETL 154
Cdd:COG1100  156 EGVEELFAAL 165
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
5-150 1.12e-14

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: 71.70  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   5 ALVGNPNVGKTSLFNALTGSNQ-YVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENIDVI 80
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRDaIVSDTPGVTRDRKYGEAewgGREFILIDTGGIEPDDEGISKEIREQAEIAIEEADVI 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737122455  81 LNIADASN--LERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRElnvKVIPISASKNMGIDKL 150
Cdd:cd01894   81 LFVVDGREglTPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAEFYSLGFG---EPIPISAEHGRGIGDL 149
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
2-155 4.88e-14

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: 69.83  E-value: 4.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   2 ITVALVGNPNVGKTSLFNALTG------SNQyvgnwAGVTVEKKEGYID---NLVKIVDLPGIyaMDTYSNEEK--VSKN 70
Cdd:cd04164    4 IKVVIAGKPNVGKSSLLNALAGrdraivSDI-----AGTTRDVIEEEIDlggIPVRLIDTAGL--RETEDEIEKigIERA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  71 YLSTENIDVILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLsrelnvKVIPISASKNMGIDKL 150
Cdd:cd04164   77 REAIEEADLVLLVVDASEGLDEEDLEILELPAKKPVIVVLNKSDLLSDAEGISELNGK------PIIAISAKTGEGIDEL 150

                 ....*
gi 737122455 151 KETLK 155
Cdd:cd04164  151 KEALL 155
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
2-155 8.32e-14

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: 69.77  E-value: 8.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   2 ITVALVGNPNVGKTSLFNALTGSNQ-YVGNWAGVT-------VEKKegyiDNLVKIVDLPGI-------YAMDTYSneek 66
Cdd:cd01895    3 IKIAIIGRPNVGKSSLLNALLGEERvIVSDIAGTTrdsidvpFEYD----GQKYTLIDTAGIrkkgkvtEGIEKYS---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  67 VSKNYLSTENIDVILNIADASN--LERNLYLTYQLKEFKKPIILLLNMMDIVEE-----KNIKIDLEllsRELN----VK 135
Cdd:cd01895   75 VLRTLKAIERADVVLLVLDASEgiTEQDLRIAGLILEEGKALIIVVNKWDLVEKdektmKEFEKELR---RKLPfldyAP 151
                        170       180
                 ....*....|....*....|
gi 737122455 136 VIPISASKNMGIDKLKETLK 155
Cdd:cd01895  152 IVFISALTGQGVDKLFDAIK 171
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
4-155 8.89e-14

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 71.94  E-value: 8.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNAL------------------------TGSNQYVgnwagvtvekkegyidnlvkIVDLPGI---- 55
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALvgqkvsivspkpqttrhrirgivtREDAQIV--------------------FVDTPGIhkpk 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  56 YAMDTYSNEEKVSknylSTENIDVILNIADASNL--ERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELN 133
Cdd:COG1159   66 RKLGRRMNKAAWS----ALEDVDVILFVVDATEKigEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLD 141
                        170       180
                 ....*....|....*....|...
gi 737122455 134 -VKVIPISASKNMGIDKLKETLK 155
Cdd:COG1159  142 fAEIVPISALKGDNVDELLDEIA 164
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
2-168 2.73e-13

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: 70.97  E-value: 2.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455    2 ITVALVGNPNVGKTSLFNALTGSNQyvgnwAGVT---------VEkkeGYIdNL----VKIVDLPGIyaMDTysnEEKV- 67
Cdd:pfam12631  95 IKVVIVGKPNVGKSSLLNALLGEER-----AIVTdipgttrdvIE---ETI-NIggipLRLIDTAGI--RET---DDEVe 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   68 ------SKNYLstENIDVILNIADASN-LERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLEllsrelNVKVIPIS 140
Cdd:pfam12631 161 kigierAREAI--EEADLVLLVLDASRpLDEEDLEILELLKDKKPIIVVLNKSDLLGEIDELEELK------GKPVLAIS 232
                         170       180
                  ....*....|....*....|....*....
gi 737122455  141 ASKNMGIDKLKETLK-VSNFSDINIDNEF 168
Cdd:pfam12631 233 AKTGEGLDELEEAIKeLFLAGEIASDGPI 261
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
4-155 3.49e-13

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: 67.87  E-value: 3.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTGS-------------NQYVGnwagVTVEKKEGYIdnlvkIVDLPGIYAMDTYSNEEKVsKN 70
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQkisivspkpqttrNRIRG----IYTDDDAQII-----FVDTPGIHKPKKKLGERMV-KA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  71 YLST-ENIDVILNIADASNL--ERNLYLTYQLKEFKKPIILLLNMMDIVEEKNI--KIDLELLSRELNVKVIPISASKNM 145
Cdd:cd04163   76 AWSAlKDVDLVLFVVDASEWigEGDEFILELLKKSKTPVILVLNKIDLVKDKEDllPLLEKLKELHPFAEIFPISALKGE 155
                        170
                 ....*....|
gi 737122455 146 GIDKLKETLK 155
Cdd:cd04163  156 NVDELLEYIV 165
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
3-154 4.45e-13

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: 68.25  E-value: 4.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   3 TVALVGNPNVGKTSLFNALTGSNQYVGN--------------WAGV-------TVekkeGYIDNLVK-IVD-----Lpgi 55
Cdd:cd01878   43 TVALVGYTNAGKSTLFNALTGADVLAEDqlfatldpttrrikLPGGrevlltdTV----GFIRDLPHqLVEafrstL--- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  56 yamdtysnEEkvsknylsTENIDVILNIADAS--NLERNLYLTYQ-LKEFK---KPIILLLNMMDIVEEknikIDLELLS 129
Cdd:cd01878  116 --------EE--------VAEADLLLHVVDASdpDREEQIETVEEvLKELGaddIPIILVLNKIDLLDD----EELEERL 175
                        170       180
                 ....*....|....*....|....*
gi 737122455 130 RELNVKVIPISASKNMGIDKLKETL 154
Cdd:cd01878  176 RAGRPDAVFISAKTGEGLDLLKEAI 200
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
4-211 5.53e-13

ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase with a duplication of its GTP-binding domain. It is broadly to universally distributed among bacteria. It appears to function in ribosome biogenesis or stability. [Protein synthesis, Other]


Pssm-ID: 274667 [Multi-domain]  Cd Length: 428  Bit Score: 70.94  E-value: 5.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455    4 VALVGNPNVGKTSLFNALTGSNQ-YVGNWAGVTVEKKEGYI---DNLVKIVDLPGIYAMDTYSNEEKVSKNYLSTENIDV 79
Cdd:TIGR03594   1 VAIVGRPNVGKSTLFNRLTGKRDaIVDDTPGVTRDRIYGDAewgGREFILIDTGGIEEDDDGIDAQIREQAEIAIEEADV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   80 ILNIADASN--LERNLYLTYQLKEFKKPIILLLNMMDiveekNIKIDLELLS-RELNV-KVIPISASKNMGIDKLKETLk 155
Cdd:TIGR03594  81 ILFVVDGREglTPEDEEIAKWLRKSGKPVILVANKID-----GPKEDADAAEfYSLGFgEPIPISAEHGRGIGDLLDAI- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  156 VSNFsdinidNEFQFRSEEETY----SLIEKVlektvvysNSNKSSitdkidnlLLNRFL 211
Cdd:TIGR03594 155 LELL------PEEEEEEEEEEDpikiAIIGRP--------NVGKST--------LVNALL 192
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
439-555 9.89e-13

Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for determining nucleoside specificity in the human CNT1 and CNT2 proteins. In the FeoB proteins, which are believed to be Fe2+ transporters, it includes the membrane pore region, so the function of this region is likely to be more general than just nucleoside specificity. This family may represent the pore and gate, with a wide potential range of specificity. Hence its name 'Gate'.


Pssm-ID: 429586 [Multi-domain]  Cd Length: 101  Bit Score: 64.58  E-value: 9.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  439 LKKAGTIIFAASVVIWFLSNFnftgmvemndSLLASIGKFIAPIFKPLGFG--SWENSVAILTGITAKEIILSSMGVIYG 516
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYS----------GLLDRIGKLLGPLMRPLGLFplPGKAAIALLLGFGAKEVGVPLLATPYG 70
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 737122455  517 gnlrevlpnHFTILSSYSFLVFVLLYTPCVSVVAAMKKE 555
Cdd:pfam07670  71 ---------IDTPRERLAALLFTSFSTPCGATLPVYAGE 100
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
4-154 1.06e-12

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: 66.38  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTGSNQ--YVGNWAGVTveKKEGY--IDNLVKIVDLPG-IYAmdtysneeKVSK--------- 69
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTNRKKlaRTSKTPGRT--QLINFfnVGDKFRLVDLPGyGYA--------KVSKevrekwgkl 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  70 --NYLST-ENIDVILNIADASN--LERNLYLTYQLKEFKKPIILLLNMMD-----IVEEKNIKIDLELLSRELNVKVIPI 139
Cdd:cd01876   72 ieEYLENrENLKGVVLLIDARHgpTPIDLEMLEFLEELGIPFLIVLTKADklkksELAKVLKKIKEELNLFNILPPVILF 151
                        170
                 ....*....|....*
gi 737122455 140 SASKNMGIDKLKETL 154
Cdd:cd01876  152 SSKKGTGIDELRALI 166
era PRK00089
GTPase Era; Reviewed
4-155 2.97e-12

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 67.38  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTG------SNQyvgnwAGVTVEKKEG-YIDNLVKI--VDLPGI----YAMDTYSNEEKVSkn 70
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGqkisivSPK-----PQTTRHRIRGiVTEDDAQIifVDTPGIhkpkRALNRAMNKAAWS-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  71 ylSTENIDVILNIADASNL--ERNLYLTYQLKEFKKPIILLLNMMDIVEEKNI--KIDLELLSRELNVKVIPISASKNMG 146
Cdd:PRK00089  81 --SLKDVDLVLFVVDADEKigPGDEFILEKLKKVKTPVILVLNKIDLVKDKEEllPLLEELSELMDFAEIVPISALKGDN 158

                 ....*....
gi 737122455 147 IDKLKETLK 155
Cdd:PRK00089 159 VDELLDVIA 167
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
2-155 5.77e-12

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: 67.78  E-value: 5.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   2 ITVALVGNPNVGKTSLFNALTG------SNQyvgnwAGVTVEKKEGYID---NLVKIVDLPGIyaMDTySNE-EK--VSK 69
Cdd:COG0486  214 IKVVIVGRPNVGKSSLLNALLGeeraivTDI-----AGTTRDVIEERINiggIPVRLIDTAGL--RET-EDEvEKigIER 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  70 NYLSTENIDVILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIdlellSRELNVKVIPISASKNMGIDK 149
Cdd:COG0486  286 AREAIEEADLVLLLLDASEPLTEEDEEILEKLKDKPVIVVLNKIDLPSEADGEL-----KSLPGEPVIAISAKTGEGIDE 360

                 ....*.
gi 737122455 150 LKETLK 155
Cdd:COG0486  361 LKEAIL 366
Rbg1 COG1163
Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];
3-154 6.02e-12

Ribosome-interacting GTPase RBG1 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440777 [Multi-domain]  Cd Length: 368  Bit Score: 67.52  E-value: 6.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   3 TVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEG---YIDNLVKIVDLPGIY---AMDTYSNEEKVSknylSTEN 76
Cdd:COG1163   65 TVVLVGFPSVGKSTLLNKLTNAKSEVGAYEFTTLDVVPGmleYKGAKIQILDVPGLIegaASGKGRGKEVLS----VVRN 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  77 IDVILNIADASNLE------RNLY------------------------------LTYQ-------LKEFK---------- 103
Cdd:COG1163  141 ADLILIVLDVFELEqydvlkEELYdagirlnkpppdvtiekkgkggirvnstgkLDLDeedikkiLREYGivnadvlire 220
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737122455 104 -----------------KPIILLLNMMDIVEEKNIKIDLELLSRElnVKVIPISASKNMGIDKLKETL 154
Cdd:COG1163  221 dvtlddlidalmgnrvyKPAIVVVNKIDLADEEYVEELKSKLPDG--VPVIFISAEKGIGLEELKEEI 286
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
4-154 6.27e-12

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 63.98  E-value: 6.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTGSNQYVGNWA--------GVtVEKKEGyiDNLVkIVDLPGIYamdtysneEKVSKN----- 70
Cdd:cd01898    3 VGLVGLPNAGKSTLLSAISNAKPKIADYPfttlvpnlGV-VRVDDG--RSFV-IADIPGLI--------EGASEGkglgh 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  71 -YL-STENIDVILNIADASNLErNLYLTYQL--KE--------FKKPIILLLNMMDIVEEKNIKIDL-ELLSRELNVKVI 137
Cdd:cd01898   71 rFLrHIERTRVLLHVIDLSGED-DPVEDYETirNEleaynpglAEKPRIVVLNKIDLLDAEERFEKLkELLKELKGKKVF 149
                        170
                 ....*....|....*..
gi 737122455 138 PISASKNMGIDKLKETL 154
Cdd:cd01898  150 PISALTGEGLDELLKKL 166
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
3-213 1.67e-11

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 66.26  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   3 TVALVGNPNVGKTSLFNALTGsnqyvgnwAGVTVEkkegyiDNL-------VKIVDLPGIYAM---DTysneekV---SK 69
Cdd:COG2262  201 TVALVGYTNAGKSTLFNRLTG--------ADVLAE------DKLfatldptTRRLELPDGRPVlltDT------VgfiRK 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  70 nyLSTENI-------------DVILNIADAS--NLERNLYLTYQ-LKEFK---KPIILLLNMMDIVEEKNIKIDlellsR 130
Cdd:COG2262  261 --LPHQLVeafrstleevreaDLLLHVVDASdpDFEEQIETVNEvLEELGaddKPIILVFNKIDLLDDEELERL-----R 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455 131 ELNVKVIPISASKNMGIDKLKETLkVSNFSDINIdnEFQFRSEEETYSLIEKVLEKTVVYS---NSNKSSITDKIDNLLL 207
Cdd:COG2262  334 AGYPDAVFISAKTGEGIDELLEAI-EERLPEDRV--EVELLLPYSDGDLVAWLHEHGEVLSeeyDEDGTLLTVRLPPEDL 410

                 ....*.
gi 737122455 208 NRFLAY 213
Cdd:COG2262  411 ARLEAY 416
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
2-153 2.54e-11

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 65.84  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   2 ITVALVGNPNVGKTSLFNALTGSNQY-VGNWAGVT-------VEKKegyiDNLVKIVDLPGI-------YAMDTYSneek 66
Cdd:PRK00093 174 IKIAIIGRPNVGKSSLINALLGEERViVSDIAGTTrdsidtpFERD----GQKYTLIDTAGIrrkgkvtEGVEKYS---- 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  67 VSKNYLSTENIDVILNIADASNLernlyLTYQ-LK------EFKKPIILLLNMMDIVEEKNIKIDLELLSRELN----VK 135
Cdd:PRK00093 246 VIRTLKAIERADVVLLVIDATEG-----ITEQdLRiaglalEAGRALVIVVNKWDLVDEKTMEEFKKELRRRLPfldyAP 320
                        170
                 ....*....|....*...
gi 737122455 136 VIPISASKNMGIDKLKET 153
Cdd:PRK00093 321 IVFISALTGQGVDKLLEA 338
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
2-185 3.41e-11

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 65.52  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   2 ITVALVGNPNVGKTSLFNALTGSNQ-YVGNWAGVTVEKKEGYID---NLVKIVDLPGIyaMDTySNE-EK--VSKNYLST 74
Cdd:PRK05291 216 LKVVIAGRPNVGKSSLLNALLGEERaIVTDIAGTTRDVIEEHINldgIPLRLIDTAGI--RET-DDEvEKigIERSREAI 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  75 ENIDVILNIADASNLERNLYLTYQLKEFKKPIILLLNmmdiveekniKIDL---ELLSRELNVKVIPISASKNMGIDKLK 151
Cdd:PRK05291 293 EEADLVLLVLDASEPLTEEDDEILEELKDKPVIVVLN----------KADLtgeIDLEEENGKPVIRISAKTGEGIDELR 362
                        170       180       190
                 ....*....|....*....|....*....|....
gi 737122455 152 ETLKVSNFSDINIDNEFQFRSEEETYSLIEKVLE 185
Cdd:PRK05291 363 EAIKELAFGGFGGNQEGVFLTNARHLEALERALE 396
FeoB_C pfam07664
Ferrous iron transport protein B C terminus; Escherichia coli has an iron(II) transport system ...
382-431 9.80e-11

Ferrous iron transport protein B C terminus; 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 has been previously erroneously described as being ATP-binding. Recent work shows that it is similar to eukaryotic G-proteins and that it is a GTPase.


Pssm-ID: 462224 [Multi-domain]  Cd Length: 51  Bit Score: 57.03  E-value: 9.80e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 737122455  382 VFSLYLLGILIAFLIGLLFKN-TIFKKDEEPFIIELSQYKMPGFKSLTKLT 431
Cdd:pfam07664   1 LFSLYLLGILVALLVALLLKKtTLLKGEPSPFVMELPPYRLPTLKNVLRKT 51
PRK04213 PRK04213
GTP-binding protein EngB;
1-169 2.62e-10

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 60.32  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   1 MITVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEGYIDNLVkIVDLPGIYAMDTYSNE--EKVSKN---YLST- 74
Cdd:PRK04213   9 KPEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRKPNHYDWGDFI-LTDLPGFGFMSGVPKEvqEKIKDEivrYIEDn 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  75 -ENIDVILNIADASNL----ER---------NLYLTYQLKEFKKPIILLLNMMDIVEEKNIKID-----LELLS--RELN 133
Cdd:PRK04213  88 aDRILAAVLVVDGKSFieiiERwegrgeipiDVEMFDFLRELGIPPIVAVNKMDKIKNRDEVLDeiaerLGLYPpwRQWQ 167
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 737122455 134 VKVIPISASKNmGIDKLKETLKvSNFSDINIDNEFQ 169
Cdd:PRK04213 168 DIIAPISAKKG-GIEELKEAIR-KRLHEAKRDDLFK 201
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
2-155 3.14e-10

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 62.35  E-value: 3.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   2 ITVALVGNPNVGKTSLFNALTGSNQY-VGNWAGVT-------VEKKegyiDNLVKIVDLPGI-------YAMDTYSneek 66
Cdd:COG1160  176 IKIAIVGRPNVGKSSLINALLGEERViVSDIAGTTrdsidtpFERD----GKKYTLIDTAGIrrkgkvdEGIEKYS---- 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  67 VSKNYLSTENIDVILNIADASN--LERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKID--LELLSRELN----VKVIP 138
Cdd:COG1160  248 VLRTLRAIERADVVLLVIDATEgiTEQDLKIAGLALEAGKALVIVVNKWDLVEKDRKTREelEKEIRRRLPfldyAPIVF 327
                        170
                 ....*....|....*..
gi 737122455 139 ISASKNMGIDKLKETLK 155
Cdd:COG1160  328 ISALTGQGVDKLLEAVD 344
obgE PRK12297
GTPase CgtA; Reviewed
4-191 1.09e-09

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 60.89  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTGSNQYVGNWA--------GVtVEKKEGYidNLVkIVDLPGIYamdtysneEKVSK------ 69
Cdd:PRK12297 161 VGLVGFPNVGKSTLLSVVSNAKPKIANYHfttlvpnlGV-VETDDGR--SFV-MADIPGLI--------EGASEgvglgh 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  70 NYLS-TENIDVILNIADASNLE-RNLYLTYQ-----LKEF-----KKPIILLLNMMDIVE-EKNikidLELLSRELNVKV 136
Cdd:PRK12297 229 QFLRhIERTRVIVHVIDMSGSEgRDPIEDYEkinkeLKLYnprllERPQIVVANKMDLPEaEEN----LEEFKEKLGPKV 304
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737122455 137 IPISASKNMGIDKLKETL--KVSNFSDINIDNEFQ-------FRSEEETYSL--------------IEKVLEKTVVYS 191
Cdd:PRK12297 305 FPISALTGQGLDELLYAVaeLLEETPEFPLEEEEVeeevyykFEEEEKDFTItrdedgvfvvsgekIERLFKMTNFNR 382
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
3-167 1.21e-09

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 60.42  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   3 TVALVGNPNVGKTSLFNALTGSNQ-YVGNWAGVTVEKKEGYI---DNLVKIVDLPGIyamdtysneEKVSKNYLSTEnI- 77
Cdd:COG1160    4 VVAIVGRPNVGKSTLFNRLTGRRDaIVDDTPGVTRDRIYGEAewgGREFTLIDTGGI---------EPDDDDGLEAE-Ir 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  78 ----------DVILNIADASN--LERNLYLTYQLKEFKKPIILLLNmmdiveekniKIDLEllSRELNV---------KV 136
Cdd:COG1160   74 eqaelaieeaDVILFVVDGRAglTPLDEEIAKLLRRSGKPVILVVN----------KVDGP--KREADAaefyslglgEP 141
                        170       180       190
                 ....*....|....*....|....*....|.
gi 737122455 137 IPISASKNMGIDKLKETLkVSNFSDINIDNE 167
Cdd:COG1160  142 IPISAEHGRGVGDLLDAV-LELLPEEEEEEE 171
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
1-167 1.54e-09

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 60.45  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   1 MITVALVGNPNVGKTSLFNALTGSNQ-YVGNWAGVTVEKKEGYI---DNLVKIVDLPGIyamdtYSNEEKVSKN-----Y 71
Cdd:PRK00093   1 KPVVAIVGRPNVGKSTLFNRLTGKRDaIVADTPGVTRDRIYGEAewlGREFILIDTGGI-----EPDDDGFEKQireqaE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  72 LSTENIDVILNIADASNLernlyLTYQLKEF-------KKPIILLLNMMDiveekNIKIDLELLS-RELNV-KVIPISAS 142
Cdd:PRK00093  76 LAIEEADVILFVVDGRAG-----LTPADEEIakilrksNKPVILVVNKVD-----GPDEEADAYEfYSLGLgEPYPISAE 145
                        170       180
                 ....*....|....*....|....*
gi 737122455 143 KNMGIDKLKETLkVSNFSDINIDNE 167
Cdd:PRK00093 146 HGRGIGDLLDAI-LEELPEEEEEDE 169
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
1-55 1.71e-09

A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein that functions as a regulator of cell growth and proliferation in stem cells and in several types of cancer cells, but is not expressed in the differentiated cells of most mammalian adult tissues. NS shuttles between the nucleolus and nucleoplasm bidirectionally at a rate that is fast and independent of cell type. Lowering GTP levels decreases the nucleolar retention of NS, and expression of NS is abruptly down-regulated during differentiation prior to terminal cell division. Found only in eukaryotes, NS consists of an N-terminal basic domain, a coiled-coil domain, a GTP-binding domain, an intermediate domain, and a C-terminal acidic domain. Experimental evidence indicates that NS uses its GTP-binding property as a molecular switch to control the transition between the nucleolus and nucleoplasm, and this process involves interaction between the basic, GTP-binding, and intermediate domains of the protein.


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 57.20  E-value: 1.71e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 737122455   1 MITVALVGNPNVGKTSLFNALTGSN-QYVGNWAGVTVEKKEGYIDNLVKIVDLPGI 55
Cdd:cd04178  116 SITVGVVGYPNVGKSSVINSLKRSRaCNVGATPGVTKSMQEVHLDKHVKLLDSPGV 171
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
4-154 2.06e-08

GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 439988 [Multi-domain]  Cd Length: 194  Bit Score: 54.31  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTGSNQ--YVGNWAGVTVE----KkegyIDNLVKIVDLPGI-YAmdtysneeKVSK------- 69
Cdd:COG0218   26 IAFAGRSNVGKSSLINALTNRKKlaRTSKTPGKTQLinffL----INDKFYLVDLPGYgYA--------KVSKaekekwq 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  70 ----NYLST-ENIDVILNIADA----SNLERNLYltYQLKEFKKPIILLLNMMDIV----EEKNIK-IDLELLSRELNVK 135
Cdd:COG0218   94 klieDYLEGrENLKGVVLLIDIrhppKELDLEML--EWLDEAGIPFLIVLTKADKLkkseLAKQLKaIKKALGKDPAAPE 171
                        170
                 ....*....|....*....
gi 737122455 136 VIPISASKNMGIDKLKETL 154
Cdd:COG0218  172 VILFSSLKKEGIDELRAAI 190
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
2-155 2.65e-08

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: 53.53  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455    2 ITVALVGNPNVGKTSLFNALTGSNQYVGN---------WAGVTVEKKEGYidnLVKIVDLPGI--YAMDTYSNEEKVSKn 70
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEyypgttrnyVTTVIEEDGKTY---KFNLLDTAGQedYDAIRRLYYPQVER- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   71 YLSTENIdVILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKL 150
Cdd:TIGR00231  78 SLRVFDI-VILVLDVEEILEKQTKEIIHHADSGVPIILVGNKIDLKDADLKTHVASEFAKLNGEPIIPLSAETGKNIDSA 156

                  ....*
gi 737122455  151 KETLK 155
Cdd:TIGR00231 157 FKIVE 161
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
2-154 1.48e-07

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: 52.55  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   2 ITVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVEKKEG---YIDNLVKIVDLPGIY--AMDTYSNEEKVsknyLST-E 75
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGvmeYKGAKIQLLDLPGIIegASDGKGRGRQV----IAVaR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  76 NIDVILNIADASN-------LERNLY---------------------------------LTYQ-----LKEFK------- 103
Cdd:cd01896   77 TADLILIVLDATKpegqreiLERELEgvgirlnkkppnvtikkkkkgginitstvpltkLDEKtvkaiLREYKihnadvl 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737122455 104 --------------------KPIILLLNMMDIVEEKnikiDLELLSRELNvkVIPISASKNMGIDKLKETL 154
Cdd:cd01896  157 ireditvddlidviegnrvyIPCLYVYNKIDLISIE----ELDRLARIPN--SVVISAEKDLNLDELLERI 221
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
4-150 2.45e-07

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 53.64  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTGSNQ-YVGNWAGVTVEKkegyIDNLVKIVDLPGIYaMDTYSNEEKVSK-------NYLST- 74
Cdd:PRK09518 453 VALVGRPNVGKSSLLNQLTHEERaVVNDLAGTTRDP----VDEIVEIDGEDWLF-IDTAGIKRRQHKltgaeyySSLRTq 527
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  75 ---ENIDVILNIADASN--LERNLYLTYQLKEFKKPIILLLNMMDIVEEKnikiDLELLSRELNVKV--------IPISA 141
Cdd:PRK09518 528 aaiERSELALFLFDASQpiSEQDLKVMSMAVDAGRALVLVFNKWDLMDEF----RRQRLERLWKTEFdrvtwarrVNLSA 603

                 ....*....
gi 737122455 142 SKNMGIDKL 150
Cdd:PRK09518 604 KTGWHTNRL 612
YeeP COG3596
Predicted GTPase [General function prediction only];
3-154 2.90e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 52.46  E-value: 2.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   3 TVALVGNPNVGKTSLFNALTGSNQY-VGNWAGVT-----VEKKEGYIDNLVkIVDLPGIYAMDTYSNEEKVSKNYLstEN 76
Cdd:COG3596   41 VIALVGKTGAGKSSLINALFGAEVAeVGVGRPCTreiqrYRLESDGLPGLV-LLDTPGLGEVNERDREYRELRELL--PE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  77 IDVILNIADASN----LERNLYLTYQLKEFKKPIILLLNMMDIVE----------------EKNIKIDLELLSRELNV-- 134
Cdd:COG3596  118 ADLILWVVKADDralaTDEEFLQALRAQYPDPPVLVVLTQVDRLEperewdppynwpsppkEQNIRRALEAIAEQLGVpi 197
                        170       180
                 ....*....|....*....|....
gi 737122455 135 -KVIPISASKNM---GIDKLKETL 154
Cdd:COG3596  198 dRVIPVSAAEDRtgyGLEELVDAL 221
obgE PRK12299
GTPase CgtA; Reviewed
4-154 3.47e-07

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 52.38  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTGSNQYVGNWA--------GVtVEKKEGyiDNLVkIVDLPGIyamdtysneekvsknylste 75
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAAKPKIADYPfttlhpnlGV-VRVDDY--KSFV-IADIPGL-------------------- 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  76 nidvilnIADASN-----------LERN---LYL----------TYQ-----LKEF-----KKPIILLLNMMDIVEEKNI 121
Cdd:PRK12299 217 -------IEGASEgaglghrflkhIERTrllLHLvdieavdpveDYKtirneLEKYspelaDKPRILVLNKIDLLDEEEE 289
                        170       180       190
                 ....*....|....*....|....*....|....
gi 737122455 122 -KIDLELLSRELNVKVIPISASKNMGIDKLKETL 154
Cdd:PRK12299 290 rEKRAALELAALGGPVFLISAVTGEGLDELLRAL 323
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
4-55 3.39e-06

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 49.97  E-value: 3.39e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTGSNQ-YVGNWAGVTVEKkegyIDNLV-------KIVDLPGI 55
Cdd:PRK03003 214 VALVGKPNVGKSSLLNKLAGEERsVVDDVAGTTVDP----VDSLIelggktwRFVDTAGL 269
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
2-55 7.44e-06

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: 45.84  E-value: 7.44e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 737122455   2 ITVALVGNPNVGKTSLFNAL-TGSNQYVGNWAGVTVEKKEGYIDNLVKIVDLPGI 55
Cdd:cd01849   92 IRVGVVGLPNVGKSSFINALlNKFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPGI 146
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
6-155 1.05e-05

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 45.79  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   6 LVGNPNVGKTSLFNALTGS--NQYVGNWAGVTVEKKEGYIDNLVKIVdlpgIYAMDTYSNEEKVSKN--YLSTENID-VI 80
Cdd:cd09914    6 LVGQGGVGKTSLCKQLIGEkfDGDESSTHGINVQDWKIPAPERKKIR----LNVWDFGGQEIYHATHqfFLTSRSLYlLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  81 LNIADASNLERNLYLTYQLKEF--KKPIILLLNMMDivEEKNIKIDLELLSRELNVKV---IPISASKNMGIDKLKETLK 155
Cdd:cd09914   82 FDLRTGDEVSRVPYWLRQIKAFggVSPVILVGTHID--ESCDEDILKKALNKKFPAIIndiHFVSCKNGKGIAELKKAIA 159
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
4-152 1.54e-05

Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, Gem/Kir) subfamily of Ras GTPases are expressed in a tissue-specific manner and are dynamically regulated by transcriptional and posttranscriptional mechanisms in response to environmental cues. RGK proteins bind to the beta subunit of L-type calcium channels, causing functional down-regulation of these voltage-dependent calcium channels, and either termination of calcium-dependent secretion or modulation of electrical conduction and contractile function. Inhibition of L-type calcium channels by Rem2 may provide a mechanism for modulating calcium-triggered exocytosis in hormone-secreting cells, and has been proposed to influence the secretion of insulin in pancreatic beta cells. RGK proteins also interact with and inhibit the Rho/Rho kinase pathway to modulate remodeling of the cytoskeleton. Two characteristics of RGK proteins cited in the literature are N-terminal and C-terminal extensions beyond the GTPase domain typical of Ras superfamily members. The N-terminal extension is not conserved among family members; the C-terminal extension is reported to be conserved among the family and lack the CaaX prenylation motif typical of membrane-associated Ras proteins. However, a putative CaaX motif has been identified in the alignment of the C-terminal residues of this CD.


Pssm-ID: 206715 [Multi-domain]  Cd Length: 219  Bit Score: 46.24  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTGSnqyVGNWAGVTVEKKEGYIDNLVKIVDLPGIYAMDTYSNEEKVS-KNYLSTeNID---V 79
Cdd:cd04148    3 VVLLGDSGVGKSSLANIFTAG---VYEDSAYEASGDDTYERTVSVDGEEATLVVYDHWEQEDGMWlEDSCMQ-VGDayvI 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 737122455  80 ILNIADASNLERNLYLTYQLKEFK----KPIILLLNMMDIVEEKNIKIDL-ELLSRELNVKVIPISASKNMGIDKLKE 152
Cdd:cd04148   79 VYSVTDRSSFEKASELRIQLRRARqaedIPIILVGNKSDLVRSREVSVQEgRACAVVFDCKFIETSAALQHNVDELFE 156
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
78-198 4.08e-05

An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 44.23  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  78 DVILNIADASN--LERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRElNVKVIPISASKNMGIDKLKETLK 155
Cdd:cd01859   13 DVVLEVVDARDpeLTRSRKLERMALELGKKLIIVLNKADLVPREVLEKWKEVFESE-GLPVVYVSARERLGTRILRRTIK 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 737122455 156 vsnfsdinidnefqfRSEEETysliEKVLEKTVVYSNSNKSSI 198
Cdd:cd01859   92 ---------------ELAIDG----KPVIVGVVGYPKVGKSSI 115
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
97-154 4.75e-05

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: 44.44  E-value: 4.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 737122455   97 YQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSREL---------NVKVIPISASKNMGIDKLKETL 154
Cdd:pfam00009 115 RLARQLGVPIIVFINKMDRVDGAELEEVVEEVSRELlekygedgeFVPVVPGSALKGEGVQTLLDAL 181
PRK09602 PRK09602
translation-associated GTPase; Reviewed
1-37 6.18e-05

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 45.57  E-value: 6.18e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 737122455   1 MITVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVE 37
Cdd:PRK09602   1 MITIGLVGKPNVGKSTFFNAATLADVEIANYPFTTID 37
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
2-55 7.00e-05

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: 43.67  E-value: 7.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 737122455   2 ITVALVGNPNVGKTSLFNALTGSNQY-VGNWAGVTVEKKEGYIDNLVKIVDLPGI 55
Cdd:cd01856  116 LRAMVVGIPNVGKSTLINRLRGKKVAkVGNKPGVTRGQQWIRIGPNIELLDTPGI 170
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
3-37 1.39e-04

Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 44.24  E-value: 1.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 737122455   3 TVALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVE 37
Cdd:COG0012    2 KCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIE 36
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
3-152 2.76e-04

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: 42.28  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   3 TVALVGNPNVGKTSLFNALTGSN------QYVGNWA----------GVTVE---KKEGYIDNLVKIVDLPGiyamdtysn 63
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLYQTgaidrrGTRKETFldtlkeererGITIKtgvVEFEWPKRRINFIDTPG--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  64 EEKVSKN-YLSTENIDVILNIADAS-----NLERNLYLtyqLKEFKKPIILLLNMMDiveeKNIKIDLELLSREL----- 132
Cdd:cd00881   72 HEDFSKEtVRGLAQADGALLVVDANegvepQTREHLNI---ALAGGLPIIVAVNKID----RVGEEDFDEVLREIkellk 144
                        170       180       190
                 ....*....|....*....|....*....|
gi 737122455 133 ----------NVKVIPISASKNMGIDKLKE 152
Cdd:cd00881  145 ligftflkgkDVPIIPISALTGEGIEELLD 174
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
99-154 3.48e-04

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: 41.69  E-value: 3.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737122455  99 LKEFKKPIILLLNMMD---IVEE-----KNIKIDLELLSREL--NVKVIPISASKNMGIDKLKETL 154
Cdd:cd01887   97 AKAANVPIIVAINKIDkpyGTEAdpervKNELSELGLVGEEWggDVSIVPISAKTGEGIDDLLEAI 162
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
105-155 4.49e-04

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: 42.00  E-value: 4.49e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 737122455 105 PIILLLNMMDIVEEKNIKIDLELLsRELNVKVIPISASKNMGIDKLKETLK 155
Cdd:cd01854   35 EPVIVLNKADLVDDEELEELLEIY-EKLGYPVLAVSAKTGEGLDELRELLK 84
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
2-55 6.39e-04

An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 40.76  E-value: 6.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 737122455   2 ITVALVGNPNVGKTSLFNALTG----SNQYVGNWAGVTVEKKEGYIDNLVKIVDLPGI 55
Cdd:cd01859  100 VIVGVVGYPKVGKSSIINALKGrhsaSTSPIPGSPGYTKGIQLVRIDSKIYLIDTPGV 157
HSR1_MMR1 cd01857
A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC ...
3-24 8.55e-04

A circularly permuted subfamily of the Ras GTPases; Human HSR1 is localized to the human MHC class I region and is highly homologous to a putative GTP-binding protein, MMR1 from mouse. These proteins represent a new subfamily of GTP-binding proteins that has only eukaryote members. This subfamily shows a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with sequence NKXD) are relocated to the N-terminus.


Pssm-ID: 206750 [Multi-domain]  Cd Length: 140  Bit Score: 39.91  E-value: 8.55e-04
                         10        20
                 ....*....|....*....|..
gi 737122455   3 TVALVGNPNVGKTSLFNALTGS 24
Cdd:cd01857   84 TIGLVGYPNVGKSSLINALVGS 105
infB CHL00189
translation initiation factor 2; Provisional
4-187 1.19e-03

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 41.74  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   4 VALVGNPNVGKTSLFNALTGSNQYVGNWAGVT-----VEKKEGYIDNLVKIV--DLPGiyaMDTYSNEEKVSknyLSTEN 76
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIRKTQIAQKEAGGITqkigaYEVEFEYKDENQKIVflDTPG---HEAFSSMRSRG---ANVTD 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  77 IDVILNIADASNLERNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSREL-------NVKVIPISASKNMGIDK 149
Cdd:CHL00189 321 IAILIIAADDGVKPQTIEAINYIQAANVPIIVAINKIDKANANTERIKQQLAKYNLipekwggDTPMIPISASQGTNIDK 400
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 737122455 150 LKET-LKVSNFSDINIDNEfqfrsEEETYSLIEKVLEKT 187
Cdd:CHL00189 401 LLETiLLLAEIEDLKADPT-----QLAQGIILEAHLDKT 434
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
7-25 1.84e-03

YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of GTPases: Obg, DRG, Ygr210, and NOG1. Obg is an essential gene that is involved in DNA replication in C. crescentus and Streptomyces griseus and is associated with the ribosome. Several members of the family, including YchF, possess the TGS domain related to the RNA-binding proteins. Experimental data and genomic analysis suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translational factor.


Pssm-ID: 206687 [Multi-domain]  Cd Length: 274  Bit Score: 40.52  E-value: 1.84e-03
                         10
                 ....*....|....*....
gi 737122455   7 VGNPNVGKTSLFNALTGSN 25
Cdd:cd01900    4 VGLPNVGKSTLFNALTKSN 22
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
78-157 1.88e-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: 38.90  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  78 DVILNIADASNLE--RNLYLTYQLKEFKKPIILLLNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETLK 155
Cdd:cd01849    1 DVVVEVVDARDPLssRNPDIEVLINEKNKKLIMVLNKADLVPKEVLRKWVAELSELYGTKTFFISATNGQGILKLKAEIT 80

                 ..
gi 737122455 156 VS 157
Cdd:cd01849   81 KQ 82
PRK00098 PRK00098
GTPase RsgA; Reviewed
104-160 2.50e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 40.19  E-value: 2.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 737122455 104 KPIILLlNMMDIVEEKNIKIDLELLSRELNVKVIPISASKNMGIDKLKETL--KVSNFS 160
Cdd:PRK00098 113 KPIIVL-NKIDLLDDLEEARELLALYRAIGYDVLELSAKEGEGLDELKPLLagKVTVLA 170
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
4-154 2.73e-03

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 38.65  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455    4 VALVGNPNVGKTSLFNALTgSNQYVgnwagvtvekkEGYI-----DNLVKIVDLPGIYAM----DTYSNEEKVSKNYLST 74
Cdd:pfam00071   2 LVLVGDGGVGKSSLLIRFT-QNKFP-----------EEYIptigvDFYTKTIEVDGKTVKlqiwDTAGQERFRALRPLYY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   75 ENIDVIL---NIADASNLE--RNLYltYQLKEFKK---PIILLLNMMDIVEEKNIKIDL-ELLSRELNVKVIPISASKNM 145
Cdd:pfam00071  70 RGADGFLlvyDITSRDSFEnvKKWV--EEILRHADenvPIVLVGNKCDLEDQRVVSTEEgEALAKELGLPFMETSAKTNE 147

                  ....*....
gi 737122455  146 GIDKLKETL 154
Cdd:pfam00071 148 NVEEAFEEL 156
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
5-154 2.85e-03

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: 38.48  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   5 ALVGNPNVGKTSLFNALTGSN-QYVGNWAGVTVEKKE---GYIDNLVKIVDLPGI-YAMDTYSNEEKVSKNYLstENIDV 79
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEvAAVGDRRPTTRAAQAyvwQTGGDGLVLLDLPGVgERGRRDREYEELYRRLL--PEADL 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 737122455  80 ILNIADASN----LERNLYLTYqLKEFKKPIILLLNMMDiveeknikidlellsrelnvKVIPISASKNMGIDKLKETL 154
Cdd:cd11383   79 VLWLLDADDralaADHDFYLLP-LAGHDAPLLFVLNQVD--------------------PVLAVSARTGWGLDELAEAL 136
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
4-37 3.25e-03

Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They are characterized by a distinct glycine-rich motif immediately following the Walker B motif. The Ygr210 and YyaF/YchF subfamilies appear to form one major branch of the Obg-like family. Among eukaryotes, the Ygr210 subfamily is represented only in fungi. These fungal proteins form a tight cluster with their archaeal orthologs, which suggests the possibility of horizontal transfer from archaea to fungi.


Pssm-ID: 206686 [Multi-domain]  Cd Length: 318  Bit Score: 39.90  E-value: 3.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 737122455   4 VALVGNPNVGKTSLFNALTGSNQYVGNWAGVTVE 37
Cdd:cd01899    1 IGLVGKPNVGKSTFFNAATLADVEIANYPFTTID 34
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
6-55 4.38e-03

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH 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.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 38.78  E-value: 4.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737122455   6 LVGNPNVGKTSLFNALTGSNQY------------VGNWAGVTVEKKEGYIDNLVKIVDLPGI 55
Cdd:cd01855  130 VVGATNVGKSTLINALLKSNGGkvqaqalvqrltVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
3-154 5.26e-03

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 37.89  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455   3 TVALVGNPNVGKTSLfnaltgSNQYVgnwAGVTVEKKEGYIDNL-VKIVDLPGIYAM----DTYSNEEKVSKNYLSTENI 77
Cdd:cd00876    1 KLVVLGAGGVGKSAL------TIRFV---SGEFVEEYDPTIEDSyRKQIVVDGETYTldilDTAGQEEFSAMRDQYIRNG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455  78 DVIL---NIADASNLErnlyltyQLKEFKK-----------PIILLLNMMDIVEEKNI-KIDLELLSRELNVKVIPISAS 142
Cdd:cd00876   72 DGFIlvySITSRESFE-------EIKNIREqilrvkdkedvPIVLVGNKCDLENERQVsTEEGEALAEEWGCPFLETSAK 144
                        170
                 ....*....|..
gi 737122455 143 KNMGIDKLKETL 154
Cdd:cd00876  145 TNINIDELFNTL 156
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
1-150 6.62e-03

Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.


Pssm-ID: 402341 [Multi-domain]  Cd Length: 137  Bit Score: 37.26  E-value: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737122455    1 MITVALVGNPNVGKTSLFNALTGSN-QYvgnwagvtveKKEGYIDNLVKIVDLPGIYAMDtysneekvsKNYLSTENI-- 77
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEElKY----------KKTQAIEFYDNAIDTPGEYLEN---------RRYYSALIVts 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 737122455   78 ---DVILNIADASNlERNLYLTYQLKEFKKPIILLLNMMDIVE-EKNIKIDLELLSRELNVKVIPISASKNMGIDKL 150
Cdd:pfam10662  62 adaDVIALVQDATE-PESTFPPGFASMFNKPVIGIITKIDLAKdEANIEIAEEWLSLAGAQKIFRISAVEKIGIEEL 137
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH