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Conserved domains on  [gi|500754663|ref|WP_011987982|]
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ferrous iron transport protein B [Clostridium botulinum]

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

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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 500754663   1 MITTALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFV---NDSIKIVDLPGIYAMDTFSNEEKVSKNFLINGNV 77
Cdd:COG0370    3 MITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFklkGKEIELVDLPGTYSLSAYSPDEKVARDFLLEEKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  78 DVIIDIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIGIDKLIETLEN- 156
Cdd:COG0370   83 DVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAIIEa 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 157 ------------------------KTFLSYKDNNDYNFES----ERDA-------------------------------- 176
Cdd:COG0370  163 aegkkprplridypeeieeaieelEELLEEDGPYPSRWLAikllEGDEevlellsellelleeireeleeelgedlesii 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 177 ----YKFIGNIFEKAVTLEYKKTISNTDKIDKIVLNPVLAYPLFLGILYIIFKFTFNWvGTPLADYIDALLnDSLIPYLG 252
Cdd:COG0370  243 adarYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTV-GAPLMDLIDGGF-GWLGDWVA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 253 TLLesTAPWFKSLLLDGIVAGVGSVIVFLPVILTLFLGISFLEDSGYMARAAFIMDKLMRKMGLSGKAFIPMVVGFGCSV 332
Cdd:COG0370  321 ALL--PPGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 333 PGIMSARTLESERDRKLTALLVPLMSCNARLPVYALFASVFFSGHETSIVFSLYILGILLAFIIGLLFKNTLFKKDEEPF 412
Cdd:COG0370  399 PAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPSPF 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 413 IIELPEYKMPEFKNLMLHTWDKGKGFLKKAGTIIFSISVIVWLLSNFNFSG-MVDINESFLASLGRVLSPIFKPLGFSgW 491
Cdd:COG0370  479 VMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGeSEDLENSYLGRIGKALEPVFAPLGFD-W 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 492 QTSVSLLTGLMAKEVIVGTMGVIYG--------GDLKVTLLNHFTPLSAYSFLVFVLLYTPCVSVVATMRKEYGS-RMAL 562
Cdd:COG0370  558 QIGVALITGFAAKEVVVGTLGTLYGvgedaeesASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGSwKWTL 637
                        650       660
                 ....*....|....*....|....*
gi 500754663 563 FSVTYQIILAWIISFLIYNVGALII 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 500754663   1 MITTALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFV---NDSIKIVDLPGIYAMDTFSNEEKVSKNFLINGNV 77
Cdd:COG0370    3 MITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFklkGKEIELVDLPGTYSLSAYSPDEKVARDFLLEEKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  78 DVIIDIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIGIDKLIETLEN- 156
Cdd:COG0370   83 DVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAIIEa 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 157 ------------------------KTFLSYKDNNDYNFES----ERDA-------------------------------- 176
Cdd:COG0370  163 aegkkprplridypeeieeaieelEELLEEDGPYPSRWLAikllEGDEevlellsellelleeireeleeelgedlesii 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 177 ----YKFIGNIFEKAVTLEYKKTISNTDKIDKIVLNPVLAYPLFLGILYIIFKFTFNWvGTPLADYIDALLnDSLIPYLG 252
Cdd:COG0370  243 adarYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTV-GAPLMDLIDGGF-GWLGDWVA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 253 TLLesTAPWFKSLLLDGIVAGVGSVIVFLPVILTLFLGISFLEDSGYMARAAFIMDKLMRKMGLSGKAFIPMVVGFGCSV 332
Cdd:COG0370  321 ALL--PPGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 333 PGIMSARTLESERDRKLTALLVPLMSCNARLPVYALFASVFFSGHETSIVFSLYILGILLAFIIGLLFKNTLFKKDEEPF 412
Cdd:COG0370  399 PAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPSPF 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 413 IIELPEYKMPEFKNLMLHTWDKGKGFLKKAGTIIFSISVIVWLLSNFNFSG-MVDINESFLASLGRVLSPIFKPLGFSgW 491
Cdd:COG0370  479 VMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGeSEDLENSYLGRIGKALEPVFAPLGFD-W 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 492 QTSVSLLTGLMAKEVIVGTMGVIYG--------GDLKVTLLNHFTPLSAYSFLVFVLLYTPCVSVVATMRKEYGS-RMAL 562
Cdd:COG0370  558 QIGVALITGFAAKEVVVGTLGTLYGvgedaeesASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGSwKWTL 637
                        650       660
                 ....*....|....*....|....*
gi 500754663 563 FSVTYQIILAWIISFLIYNVGALII 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: 541.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663    8 GNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFVN---DSIKIVDLPGIYAMDTFSNEEKVSKNFLINGNVDVIIDIV 84
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGfqgEDIEIVDLPGIYSLTTFSLEEEVARDYLLNEKPDLVVNVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   85 DASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIG-------IDKLIETLENK 157
Cdd:TIGR00437  81 DASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGRGierlkdaIRKAIGLKELK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  158 TFL------SYKDNN-------DYNFESERDAYKFIGNIFEKAVTLE---------------YKKTISNTDKIDKI---- 205
Cdd:TIGR00437 161 KRAieivpeAYQVVEvveglieIIYSISKRGLEILLGLLEDLSLEIEkiernlaevvikespSNLSPTEIADEDRVlvek 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  206 -----VLNPVLAYPLFLGILYIIFKFTFNwVGTPLADYIDAL---LNDSLIPYLGTllestaPWFKSLLLDGIVAGVGSV 277
Cdd:TIGR00437 241 sigrkILDRFLGLPIFLFVMFILFLLTFL-VGQPLVDLIETGfsfLSEAVKSFIGN------YWLASLLGDGLIGGVGAV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  278 IVFLPVILTLFLGISFLEDSGYMARAAFIMDKLMRKMGLSGKAFIPMVVGFGCSVPGIMSARTLESERDRKLTALLVPLM 357
Cdd:TIGR00437 314 LSFVPLIAILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPAIMATRTLETRRERLLTALVIPFM 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  358 SCNARLPVY-ALFASVFFSGHETSIVFSLYILGILLAFIIGLLFKNTLFKKDEEPFIIELPEYKMPEFKNLMLHTWDKGK 436
Cdd:TIGR00437 394 SCSARLPVIvLLFAAAFPGKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFIMELPPYRLPRFRVVFIQTWTRLR 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  437 GFLKKAGTIIFSISVIVWLLSNFnfsGMVDINESFLASLGRVLSPIFKPLGFSG-WQTSVSLLTGLMAKEVIVGTMGVIY 515
Cdd:TIGR00437 474 SFIKKAGTIIVIGSVLIWFLSSF---PGGKILESWLAAIGSIMAPLFVPLGKILdWFASVALIFGFVAKEVVVATLGVLY 550
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 500754663  516 G-GDLKVTLLNHFTPLSAYSFLVFVLLYTPCVSVVATMRKE 555
Cdd:TIGR00437 551 GlGNILSSIGHAMVPVEALSYMLFVLLYVPCLATLAAIARE 591
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
2-582 7.38e-173

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 509.26  E-value: 7.38e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   2 ITTALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFVNDS---IKIVDLPGIYAMDTFSNE----EKVSKNFLIN 74
Cdd:PRK09554   4 LTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTdhqVTLVDLPGTYSLTTISSQtsldEQIACHYILS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  75 GNVDVIIDIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIGIDKLIETL 154
Cdd:PRK09554  84 GDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEALKLAI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 155 ------ENKTFLSYKD-------------NNDYNFESER----------------------------------------- 174
Cdd:PRK09554 164 drhqanENVELVHYPQpllneadslakvmPSDIPLQQRRwlglqmlegdiysrayageasqhldaalarlrnemddpalh 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 175 --DA-YKFIGNIFEKAVTLEYKKTISNTDKIDKIVLNPVLAYPLFLGILYIIFKFTFNWVG--TPLADYIDALLNDSLIP 249
Cdd:PRK09554 244 iaDArYQCIAAICDAVSNTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIGGalQPLFDVGSVAIFIHGIQ 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 250 YLGTLLeSTAPWFKSLLLDGIVAGVGSVIVFLPVILTLFLGISFLEDSGYMARAAFIMDKLMRKMGLSGKAFIPMVVGFG 329
Cdd:PRK09554 324 WLGYTL-HFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 330 CSVPGIMSARTLESERDRKLTALLVPLMSCNARLPVYALFASVFFSGHETSIVFSLYILGILLAFIIGLLFKNTLFKKDE 409
Cdd:PRK09554 403 CNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLGIVMAILTGLMLKYTIMRGEA 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 410 EPFIIELPEYKMPEFKNLMLHTWDKGKGFLKKAGTIIFSISVIVWLLSNFNFSGMV--DINESFLASLGRVLSPIFKPLG 487
Cdd:PRK09554 483 SPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIvdNINDSALASVSRVITPVLKPIG 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 488 F--SGWQTSVSLLTGLMAKEVIVGTMGVIY-----------------GGDLK-------VTLLNHFT------------- 528
Cdd:PRK09554 563 VheDNWQATVGLFTGAMAKEVVVGTLNTLYtaeniqdeefnpaefnlGDELFgavdetwQSLKDTFSlsvlanpieaskg 642
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500754663 529 ------------------PLSAYSFLVFVLLYTPCVSVVATMRKEYGSRMALFSVTYQIILAWIISFLIYNV 582
Cdd:PRK09554 643 dgemgtgamgvmsqkfgsAAAAYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQV 714
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
5-154 4.64e-84

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: 259.31  E-value: 4.64e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFV---NDSIKIVDLPGIYAMDTFSNEEKVSKNFLINGNVDVII 81
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFklgGKEIEIVDLPGTYSLTPYSEDEKVARDFLLGEEPDLIV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500754663  82 DIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIGIDKLIETL 154
Cdd:cd01879   81 NVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDELLDAI 153
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
2-154 1.06e-81

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: 252.76  E-value: 1.06e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663    2 ITTALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFV---NDSIKIVDLPGIYAMDTFSNEEKVSKNFLINGNVD 78
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFkykGYEIEIVDLPGIYSLSPYSEEERVARDYLLNEKPD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500754663   79 VIIDIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIGIDKLIETL 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 500754663   1 MITTALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFV---NDSIKIVDLPGIYAMDTFSNEEKVSKNFLINGNV 77
Cdd:COG0370    3 MITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFklkGKEIELVDLPGTYSLSAYSPDEKVARDFLLEEKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  78 DVIIDIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIGIDKLIETLEN- 156
Cdd:COG0370   83 DVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAIIEa 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 157 ------------------------KTFLSYKDNNDYNFES----ERDA-------------------------------- 176
Cdd:COG0370  163 aegkkprplridypeeieeaieelEELLEEDGPYPSRWLAikllEGDEevlellsellelleeireeleeelgedlesii 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 177 ----YKFIGNIFEKAVTLEYKKTISNTDKIDKIVLNPVLAYPLFLGILYIIFKFTFNWvGTPLADYIDALLnDSLIPYLG 252
Cdd:COG0370  243 adarYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTV-GAPLMDLIDGGF-GWLGDWVA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 253 TLLesTAPWFKSLLLDGIVAGVGSVIVFLPVILTLFLGISFLEDSGYMARAAFIMDKLMRKMGLSGKAFIPMVVGFGCSV 332
Cdd:COG0370  321 ALL--PPGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 333 PGIMSARTLESERDRKLTALLVPLMSCNARLPVYALFASVFFSGHETSIVFSLYILGILLAFIIGLLFKNTLFKKDEEPF 412
Cdd:COG0370  399 PAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPSPF 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 413 IIELPEYKMPEFKNLMLHTWDKGKGFLKKAGTIIFSISVIVWLLSNFNFSG-MVDINESFLASLGRVLSPIFKPLGFSgW 491
Cdd:COG0370  479 VMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGeSEDLENSYLGRIGKALEPVFAPLGFD-W 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 492 QTSVSLLTGLMAKEVIVGTMGVIYG--------GDLKVTLLNHFTPLSAYSFLVFVLLYTPCVSVVATMRKEYGS-RMAL 562
Cdd:COG0370  558 QIGVALITGFAAKEVVVGTLGTLYGvgedaeesASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGSwKWTL 637
                        650       660
                 ....*....|....*....|....*
gi 500754663 563 FSVTYQIILAWIISFLIYNVGALII 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: 541.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663    8 GNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFVN---DSIKIVDLPGIYAMDTFSNEEKVSKNFLINGNVDVIIDIV 84
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGfqgEDIEIVDLPGIYSLTTFSLEEEVARDYLLNEKPDLVVNVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   85 DASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIG-------IDKLIETLENK 157
Cdd:TIGR00437  81 DASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGRGierlkdaIRKAIGLKELK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  158 TFL------SYKDNN-------DYNFESERDAYKFIGNIFEKAVTLE---------------YKKTISNTDKIDKI---- 205
Cdd:TIGR00437 161 KRAieivpeAYQVVEvveglieIIYSISKRGLEILLGLLEDLSLEIEkiernlaevvikespSNLSPTEIADEDRVlvek 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  206 -----VLNPVLAYPLFLGILYIIFKFTFNwVGTPLADYIDAL---LNDSLIPYLGTllestaPWFKSLLLDGIVAGVGSV 277
Cdd:TIGR00437 241 sigrkILDRFLGLPIFLFVMFILFLLTFL-VGQPLVDLIETGfsfLSEAVKSFIGN------YWLASLLGDGLIGGVGAV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  278 IVFLPVILTLFLGISFLEDSGYMARAAFIMDKLMRKMGLSGKAFIPMVVGFGCSVPGIMSARTLESERDRKLTALLVPLM 357
Cdd:TIGR00437 314 LSFVPLIAILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPAIMATRTLETRRERLLTALVIPFM 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  358 SCNARLPVY-ALFASVFFSGHETSIVFSLYILGILLAFIIGLLFKNTLFKKDEEPFIIELPEYKMPEFKNLMLHTWDKGK 436
Cdd:TIGR00437 394 SCSARLPVIvLLFAAAFPGKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFIMELPPYRLPRFRVVFIQTWTRLR 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  437 GFLKKAGTIIFSISVIVWLLSNFnfsGMVDINESFLASLGRVLSPIFKPLGFSG-WQTSVSLLTGLMAKEVIVGTMGVIY 515
Cdd:TIGR00437 474 SFIKKAGTIIVIGSVLIWFLSSF---PGGKILESWLAAIGSIMAPLFVPLGKILdWFASVALIFGFVAKEVVVATLGVLY 550
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 500754663  516 G-GDLKVTLLNHFTPLSAYSFLVFVLLYTPCVSVVATMRKE 555
Cdd:TIGR00437 551 GlGNILSSIGHAMVPVEALSYMLFVLLYVPCLATLAAIARE 591
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
2-582 7.38e-173

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 509.26  E-value: 7.38e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   2 ITTALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFVNDS---IKIVDLPGIYAMDTFSNE----EKVSKNFLIN 74
Cdd:PRK09554   4 LTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTdhqVTLVDLPGTYSLTTISSQtsldEQIACHYILS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  75 GNVDVIIDIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIGIDKLIETL 154
Cdd:PRK09554  84 GDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEALKLAI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 155 ------ENKTFLSYKD-------------NNDYNFESER----------------------------------------- 174
Cdd:PRK09554 164 drhqanENVELVHYPQpllneadslakvmPSDIPLQQRRwlglqmlegdiysrayageasqhldaalarlrnemddpalh 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 175 --DA-YKFIGNIFEKAVTLEYKKTISNTDKIDKIVLNPVLAYPLFLGILYIIFKFTFNWVG--TPLADYIDALLNDSLIP 249
Cdd:PRK09554 244 iaDArYQCIAAICDAVSNTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIGGalQPLFDVGSVAIFIHGIQ 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 250 YLGTLLeSTAPWFKSLLLDGIVAGVGSVIVFLPVILTLFLGISFLEDSGYMARAAFIMDKLMRKMGLSGKAFIPMVVGFG 329
Cdd:PRK09554 324 WLGYTL-HFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 330 CSVPGIMSARTLESERDRKLTALLVPLMSCNARLPVYALFASVFFSGHETSIVFSLYILGILLAFIIGLLFKNTLFKKDE 409
Cdd:PRK09554 403 CNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLGIVMAILTGLMLKYTIMRGEA 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 410 EPFIIELPEYKMPEFKNLMLHTWDKGKGFLKKAGTIIFSISVIVWLLSNFNFSGMV--DINESFLASLGRVLSPIFKPLG 487
Cdd:PRK09554 483 SPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIvdNINDSALASVSRVITPVLKPIG 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663 488 F--SGWQTSVSLLTGLMAKEVIVGTMGVIY-----------------GGDLK-------VTLLNHFT------------- 528
Cdd:PRK09554 563 VheDNWQATVGLFTGAMAKEVVVGTLNTLYtaeniqdeefnpaefnlGDELFgavdetwQSLKDTFSlsvlanpieaskg 642
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500754663 529 ------------------PLSAYSFLVFVLLYTPCVSVVATMRKEYGSRMALFSVTYQIILAWIISFLIYNV 582
Cdd:PRK09554 643 dgemgtgamgvmsqkfgsAAAAYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQV 714
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
5-154 4.64e-84

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: 259.31  E-value: 4.64e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFV---NDSIKIVDLPGIYAMDTFSNEEKVSKNFLINGNVDVII 81
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFklgGKEIEIVDLPGTYSLTPYSEDEKVARDFLLGEEPDLIV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500754663  82 DIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIGIDKLIETL 154
Cdd:cd01879   81 NVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDELLDAI 153
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
2-154 1.06e-81

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: 252.76  E-value: 1.06e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663    2 ITTALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFV---NDSIKIVDLPGIYAMDTFSNEEKVSKNFLINGNVD 78
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFkykGYEIEIVDLPGIYSLSPYSEEERVARDYLLNEKPD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500754663   79 VIIDIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVKVIPIIASKGIGIDKLIETL 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 ...
5-156 3.15e-25

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: 101.94  E-value: 3.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQ-YVGNWAGVTVEKKEGFV----NDSIKIVDLPGIYAMDTFSnEEKVSKNFLINGNVDV 79
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVgIVSPIPGTTRDPVRKEWellpLGPVVLIDTPGLDEEGGLG-RERVEEARQVADRADL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  80 IIDIVDASNLDRNLYLTTQ-LKQFNKPIILVLNMIDVAENKGIKINYDILSKELN--VKVIPIIASKGIGIDKLIETLEN 156
Cdd:cd00880   80 VLLVVDSDLTPVEEEAKLGlLRERGKPVLLVLNKIDLVPESEEEELLRERKLELLpdLPVIAVSALPGEGIDELRKKIAE 159
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
5-112 9.14e-23

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: 93.45  E-value: 9.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663    5 ALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFVN---DSIKIVDLPGIYamDTFSNEEKVSKNFLINGNVDVII 81
Cdd:pfam01926   3 ALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLElkgKQIILVDTPGLI--EGASEGEGLGRAFLAIIEADLIL 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 500754663   82 DIVDASNL--DRNLYLTTQLKQFNKPIILVLNM 112
Cdd:pfam01926  81 FVVDSEEGitPLDEELLELLRENKKPIILVLNK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
5-154 4.34e-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: 87.51  E-value: 4.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQY-VGNWAGVTVE-----KKEGFVNDSIKIVDLPGIYAMDTFSNEEKVSKnfLINGnVD 78
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGeVSDVPGTTRDpdvyvKELDKGKVKLVLVDTPGLDEFGGLGREELARL--LLRG-AD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  79 VIIDIVDASNL----DRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYD--ILSKELNVKVIPIIASKGIGIDKLIE 152
Cdd:cd00882   78 LILLVVDSTDReseeDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRleELAKILGVPVFEVSAKTGEGVDELFE 157

                 ..
gi 500754663 153 TL 154
Cdd:cd00882  158 KL 159
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
277-370 2.69e-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: 71.90  E-value: 2.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  277 VIVFLPVILTLFLGISFLEDSGYMARAAFIMDKLMRKMG---LSGKAFIPMVVGFGC---SVPGIMSARTLESERDRKLT 350
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYSGLLDRIGKLLGPLMRPLGlfpLPGKAAIALLLGFGAkevGVPLLATPYGIDTPRERLAA 80
                          90       100
                  ....*....|....*....|.
gi 500754663  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 1.91e-14

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: 71.27  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFVND----SIKIVDLPGIYAmDTFSNE---EKVSKNFLINgnv 77
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFgdgvDIQIIDLPGLLD-GASEGRglgEQILAHLYRS--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  78 DVIIDIVDASNLDRNLYLTTQLKQF-----------NKPIILVLNMIDVAENKGIKINYDILSKElNVKVIPIIASKGIG 146
Cdd:cd01881   77 DLILHVIDASEDCVGDPLEDQKTLNeevsgsflflkNKPEMIVANKIDMASENNLKRLKLDKLKR-GIPVVPTSALTRLG 155

                 ....*..
gi 500754663 147 IDKLIET 153
Cdd:cd01881  156 LDRVIRT 162
FeoB_C pfam07664
Ferrous iron transport protein B C terminus; Escherichia coli has an iron(II) transport system ...
382-431 9.71e-14

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: 65.51  E-value: 9.71e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 500754663  382 VFSLYILGILLAFIIGLLFKN-TLFKKDEEPFIIELPEYKMPEFKNLMLHT 431
Cdd:pfam07664   1 LFSLYLLGILVALLVALLLKKtTLLKGEPSPFVMELPPYRLPTLKNVLRKT 51
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
5-155 2.67e-13

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: 67.85  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQ-YVGNWAGVTVEKKEGFV---NDSIKIVDLPGIyamdtfsneEKVSKNF--LINGNV- 77
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRDaIVSDTPGVTRDRKYGEAewgGREFILIDTGGI---------EPDDEGIskEIREQAe 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  78 ------DVIIDIVDASN--LDRNLYLTTQLKQFNKPIILVLNMIDvaeNKGIKIN-YDILSkeLNV-KVIPIIASKGIGI 147
Cdd:cd01894   72 iaieeaDVILFVVDGREglTPADEEIAKYLRKSKKPVILVVNKID---NIKEEEEaAEFYS--LGFgEPIPISAEHGRGI 146

                 ....*...
gi 500754663 148 DKLIETLE 155
Cdd:cd01894  147 GDLLDAIL 154
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
5-157 6.89e-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: 66.72  E-value: 6.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTG------SNQyvgnwAGVTVEKKEGFVNDS---IKIVDLPGIYAmdtfsnEEKVSKNFLIN- 74
Cdd:cd04163    7 AIIGRPNVGKSTLLNALVGqkisivSPK-----PQTTRNRIRGIYTDDdaqIIFVDTPGIHK------PKKKLGERMVKa 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  75 -----GNVDVIIDIVDASN----LDRnlYLTTQLKQFNKPIILVLNMIDVAENKGI--KINYDILSKELNVKVIPIIASK 143
Cdd:cd04163   76 awsalKDVDLVLFVVDASEwigeGDE--FILELLKKSKTPVILVLNKIDLVKDKEDllPLLEKLKELHPFAEIFPISALK 153
                        170
                 ....*....|....
gi 500754663 144 GIGIDKLIETLENK 157
Cdd:cd04163  154 GENVDELLEYIVEY 167
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
439-555 6.90e-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: 64.97  E-value: 6.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  439 LKKAGTIIFSISVIVWLLSNFnfsgmvdineSFLASLGRVLSPIFKPLGFSG--WQTSVSLLTGLMAKEVIVGTMGVIYG 516
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYS----------GLLDRIGKLLGPLMRPLGLFPlpGKAAIALLLGFGAKEVGVPLLATPYG 70
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 500754663  517 gdlkvtllnHFTPLSAYSFLVFVLLYTPCVSVVATMRKE 555
Cdd:pfam07670  71 ---------IDTPRERLAALLFTSFSTPCGATLPVYAGE 100
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
5-154 1.11e-12

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 66.54  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGsnQYVGNWA-----GVTVEKKE---GFVNDSIKIVDLPGIYAMDTFSneEKVSKNFLingN 76
Cdd:COG1100    7 VVVGTGGVGKTSLVNRLVG--DIFSLEKylstnGVTIDKKElklDGLDVDLVIWDTPGQDEFRETR--QFYARQLT---G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  77 VDVIIDIVDAS---NLDRNLYLTTQLKQFNK--PIILVLNMIDVAENKGIKIN---YDILSKELNVKVIPIIASKGIGID 148
Cdd:COG1100   80 ASLYLFVVDGTreeTLQSLYELLESLRRLGKksPIILVLNKIDLYDEEEIEDEerlKEALSEDNIVEVVATSAKTGEGVE 159

                 ....*.
gi 500754663 149 KLIETL 154
Cdd:COG1100  160 ELFAAL 165
GTPase_EngA TIGR03594
ribosome-associated GTPase EngA; EngA (YfgK, Der) is a ribosome-associated essential GTPase ...
5-154 7.91e-12

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: 67.47  E-value: 7.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663    5 ALLGNPNVGKTSLFNQLTGSNQ-YVGNWAGVTVEKKEGFV---NDSIKIVDLPGIYAmdtfsNEEKVSKnfLINGNV--- 77
Cdd:TIGR03594   2 AIVGRPNVGKSTLFNRLTGKRDaIVDDTPGVTRDRIYGDAewgGREFILIDTGGIEE-----DDDGIDA--QIREQAeia 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   78 ----DVIIDIVDA----SNLDRnlYLTTQLKQFNKPIILVLNMIDvaenkGIKINYDILS-KELNV-KVIPIIASKGIGI 147
Cdd:TIGR03594  75 ieeaDVILFVVDGreglTPEDE--EIAKWLRKSGKPVILVANKID-----GPKEDADAAEfYSLGFgEPIPISAEHGRGI 147

                  ....*..
gi 500754663  148 DKLIETL 154
Cdd:TIGR03594 148 GDLLDAI 154
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
5-154 5.75e-11

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 63.47  E-value: 5.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGsnqyvgnwagvtvEK------K--------EGFVNDS---IKIVDLPGI----YAMDTFSN 63
Cdd:COG1159    7 AIVGRPNVGKSTLLNALVG-------------QKvsivspKpqttrhriRGIVTREdaqIVFVDTPGIhkpkRKLGRRMN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  64 eeKVSKNFLinGNVDVIIDIVDASNL--DRNLYLTTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELN-VKVIPII 140
Cdd:COG1159   74 --KAAWSAL--EDVDVILFVVDATEKigEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLDfAEIVPIS 149
                        170
                 ....*....|....
gi 500754663 141 ASKGIGIDKLIETL 154
Cdd:COG1159  150 ALKGDNVDELLDEI 163
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
2-157 7.73e-11

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: 60.59  E-value: 7.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   2 ITTALLGNPNVGKTSLFNQLTG------SNQyvgnwAGVT---VEkkEGFVND--SIKIVDLPGIyaMDTfsnEEKV--- 67
Cdd:cd04164    4 IKVVIAGKPNVGKSSLLNALAGrdraivSDI-----AGTTrdvIE--EEIDLGgiPVRLIDTAGL--RET---EDEIeki 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  68 ----SKNFLinGNVDVIIDIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENKgikinyDILSKELNVKVIPIIASK 143
Cdd:cd04164   72 gierAREAI--EEADLVLLVVDASEGLDEEDLEILELPAKKPVIVVLNKSDLLSDA------EGISELNGKPIIAISAKT 143
                        170
                 ....*....|....
gi 500754663 144 GIGIDKLIETLENK 157
Cdd:cd04164  144 GEGIDELKEALLEL 157
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
8-157 9.32e-11

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: 60.65  E-value: 9.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   8 GNPNVGKTSLFNQLTGSNQYVGNWAGVTvekKEGFVN------DSIKIVDLPGI--YAMDTFSNEEKVSKNFLINGNvDV 79
Cdd:cd01897    7 GYPNVGKSSLVNKLTRAKPEVAPYPFTT---KSLFVGhfdykyLRWQVIDTPGIldRPLEERNTIEMQAITALAHLR-AA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  80 IIDIVDASN-----LDRNLYLTTQLKQ-FNKPIILVLNMIDVAENKGIKINYDILSKElNVKVIPIIASKGIGIDKLIET 153
Cdd:cd01897   83 VLFFIDPSEtcgysIEEQLSLFKEIKPlFNKPVIVVLNKIDLLTEEDLSEIEKELEKE-GEEVIKISTLTEEGVDELKNK 161

                 ....
gi 500754663 154 LENK 157
Cdd:cd01897  162 ACEL 165
era PRK00089
GTPase Era; Reviewed
5-154 1.94e-10

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 61.99  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTG------SNQyvgnwAGVTVEKKEGFVNDS---IKIVDLPGI----YAMDTFSNeeKVSKNF 71
Cdd:PRK00089   9 AIVGRPNVGKSTLLNALVGqkisivSPK-----PQTTRHRIRGIVTEDdaqIIFVDTPGIhkpkRALNRAMN--KAAWSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  72 LinGNVDVIIDIVDASNL--DRNLYLTTQLKQFNKPIILVLNMIDVAENKGI---KINYdiLSKELN-VKVIPIIASKGI 145
Cdd:PRK00089  82 L--KDVDLVLFVVDADEKigPGDEFILEKLKKVKTPVILVLNKIDLVKDKEEllpLLEE--LSELMDfAEIVPISALKGD 157

                 ....*....
gi 500754663 146 GIDKLIETL 154
Cdd:PRK00089 158 NVDELLDVI 166
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
5-158 2.69e-10

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: 59.45  E-value: 2.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQ--YVGNWAGVTveKKEGF--VNDSIKIVDLPG-IYAmdtfsneeKVSK---------- 69
Cdd:cd01876    3 AFAGRSNVGKSSLINALTNRKKlaRTSKTPGRT--QLINFfnVGDKFRLVDLPGyGYA--------KVSKevrekwgkli 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  70 -NFLIN-GNVDVIIDIVDAS----NLDRNLYltTQLKQFNKPIILVLNMIDVAENKGIKINYDILSKELNVK-----VIP 138
Cdd:cd01876   73 eEYLENrENLKGVVLLIDARhgptPIDLEML--EFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFnilppVIL 150
                        170       180
                 ....*....|....*....|
gi 500754663 139 IIASKGIGIDKLIETLENKT 158
Cdd:cd01876  151 FSSKKGTGIDELRALIAEWL 170
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
2-167 4.69e-10

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: 61.34  E-value: 4.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663    2 ITTALLGNPNVGKTSLFNQLTGSN----------------QYVgNWAGVTVekkegfvndsiKIVDLPGIyaMDTfsnEE 65
Cdd:pfam12631  95 IKVVIVGKPNVGKSSLLNALLGEEraivtdipgttrdvieETI-NIGGIPL-----------RLIDTAGI--RET---DD 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   66 KV-------SKNFLinGNVDVIIDIVDASN-LDRNLYLTTQLKQFNKPIILVLNMIDVAENKgikinyDILSKELNVKVI 137
Cdd:pfam12631 158 EVekigierAREAI--EEADLVLLVLDASRpLDEEDLEILELLKDKKPIIVVLNKSDLLGEI------DELEELKGKPVL 229
                         170       180       190
                  ....*....|....*....|....*....|
gi 500754663  138 PIIASKGIGIDKLIETLENKTFLSYKDNND 167
Cdd:pfam12631 230 AISAKTGEGLDELEEAIKELFLAGEIASDG 259
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
3-157 5.69e-10

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: 59.40  E-value: 5.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   3 TTALLGNPNVGKTSLFNQLTGSNQYVGN--------------WAGV-------TVekkeGFvndsikIVDLPgiyamdtf 61
Cdd:cd01878   43 TVALVGYTNAGKSTLFNALTGADVLAEDqlfatldpttrrikLPGGrevlltdTV----GF------IRDLP-------- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  62 sneekvskNFLIN---------GNVDVIIDIVDASNLDRNLYLTT------QLKQFNKPIILVLNMIDVAENKGIKINYD 126
Cdd:cd01878  105 --------HQLVEafrstleevAEADLLLHVVDASDPDREEQIETveevlkELGADDIPIILVLNKIDLLDDEELEERLR 176
                        170       180       190
                 ....*....|....*....|....*....|.
gi 500754663 127 ilskELNVKVIPIIASKGIGIDKLIETLENK 157
Cdd:cd01878  177 ----AGRPDAVFISAKTGEGLDLLKEAIEEL 203
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
5-154 6.45e-10

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 61.60  E-value: 6.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQ-YVGNWAGVTVEKKEG--FVND-SIKIVDLPGIyamdtFSNEEKVSKnfLINGNV--- 77
Cdd:PRK00093   5 AIVGRPNVGKSTLFNRLTGKRDaIVADTPGVTRDRIYGeaEWLGrEFILIDTGGI-----EPDDDGFEK--QIREQAela 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  78 ----DVIIDIVDA----SNLDRnlYLTTQLKQFNKPIILVLNMIDvaenkGIKINYDILS-KELNV-KVIPIIASKGIGI 147
Cdd:PRK00093  78 ieeaDVILFVVDGraglTPADE--EIAKILRKSNKPVILVVNKVD-----GPDEEADAYEfYSLGLgEPYPISAEHGRGI 150

                 ....*..
gi 500754663 148 DKLIETL 154
Cdd:PRK00093 151 GDLLDAI 157
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
6-154 1.04e-09

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: 57.82  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   6 LLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFVN----DSIKIVDLPGIYamdtfsneEKVSKN------FL--I 73
Cdd:cd01898    5 LVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRvddgRSFVIADIPGLI--------EGASEGkglghrFLrhI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  74 NgNVDVIIDIVDASNLDRNLY----LTTQLKQFN-----KPIILVLNMIDV-AENKGIKINYDILSKELNVKVIPIIASK 143
Cdd:cd01898   77 E-RTRVLLHVIDLSGEDDPVEdyetIRNELEAYNpglaeKPRIVVLNKIDLlDAEERFEKLKELLKELKGKKVFPISALT 155
                        170
                 ....*....|.
gi 500754663 144 GIGIDKLIETL 154
Cdd:cd01898  156 GEGLDELLKKL 166
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
2-170 3.81e-09

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 58.97  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   2 ITTALLGNPNVGKTSLFNQLTGSN----------------QYVgNWAGVTVekkegfvndsiKIVDLPGIyaMDTfsnEE 65
Cdd:PRK05291 216 LKVVIAGRPNVGKSSLLNALLGEEraivtdiagttrdvieEHI-NLDGIPL-----------RLIDTAGI--RET---DD 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  66 KVSK------NFLINgNVDVIIDIVDASNLDRNLYLTTQLKQFNKPIILVLNMIDVAENkgikinyDILSKELNVKVIPI 139
Cdd:PRK05291 279 EVEKigiersREAIE-EADLVLLVLDASEPLTEEDDEILEELKDKPVIVVLNKADLTGE-------IDLEEENGKPVIRI 350
                        170       180       190
                 ....*....|....*....|....*....|.
gi 500754663 140 IASKGIGIDKLIETLENKTFLSYKDNNDYNF 170
Cdd:PRK05291 351 SAKTGEGIDELREAIKELAFGGFGGNQEGVF 381
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
5-154 7.87e-09

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 58.11  E-value: 7.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQ-YVGNWAGVTVEKKEGFV--ND-SIKIVDLPGIyamdTFSNEEKVSKnfLINGNV--- 77
Cdd:COG1160    6 AIVGRPNVGKSTLFNRLTGRRDaIVDDTPGVTRDRIYGEAewGGrEFTLIDTGGI----EPDDDDGLEA--EIREQAela 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  78 ----DVIIDIVDASN----LDRnlYLTTQLKQFNKPIILVLNMIDvaenkGIKINYDILS-KELNV-KVIPIIASKGIGI 147
Cdd:COG1160   80 ieeaDVILFVVDGRAgltpLDE--EIAKLLRRSGKPVILVVNKVD-----GPKREADAAEfYSLGLgEPIPISAEHGRGV 152

                 ....*..
gi 500754663 148 DKLIETL 154
Cdd:COG1160  153 GDLLDAV 159
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
2-167 9.44e-09

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: 57.76  E-value: 9.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   2 ITTALLGNPNVGKTSLFNQLTGSN----------------QYVgNWAGVTVekkegfvndsiKIVDLPGIyaMDTfsnEE 65
Cdd:COG0486  214 IKVVIVGRPNVGKSSLLNALLGEEraivtdiagttrdvieERI-NIGGIPV-----------RLIDTAGL--RET---ED 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  66 KV-------SKNFLinGNVDVIIDIVDASN--LDRNLYLTTQLKqfNKPIILVLNMIDVAENKGIKINydilsKELNVKV 136
Cdd:COG0486  277 EVekigierAREAI--EEADLVLLLLDASEplTEEDEEILEKLK--DKPVIVVLNKIDLPSEADGELK-----SLPGEPV 347
                        170       180       190
                 ....*....|....*....|....*....|.
gi 500754663 137 IPIIASKGIGIDKLIETLENKTFLSYKDNND 167
Cdd:COG0486  348 IAISAKTGEGIDELKEAILELVGEGALEGEG 378
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
6-156 5.73e-08

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: 52.34  E-value: 5.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   6 LLGNPNVGKTSLFNQLTGS--NQYVGNWAGVTVEKKEGFVNDSIKIVdlpgIYAMDtFSNEEKVSKN---FLINGNVDVI 80
Cdd:cd09914    6 LVGQGGVGKTSLCKQLIGEkfDGDESSTHGINVQDWKIPAPERKKIR----LNVWD-FGGQEIYHAThqfFLTSRSLYLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  81 I-DIVDASNLDRNLYLTTQLKQF--NKPIILVLNMIDVAEnkgikiNYDILSKELNVKVIPII-------ASKGIGIDKL 150
Cdd:cd09914   81 VfDLRTGDEVSRVPYWLRQIKAFggVSPVILVGTHIDESC------DEDILKKALNKKFPAIIndihfvsCKNGKGIAEL 154

                 ....*.
gi 500754663 151 IETLEN 156
Cdd:cd09914  155 KKAIAK 160
EngB COG0218
GTP-binding protein EngB required for normal cell division [Cell cycle control, cell division, ...
5-156 5.87e-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: 53.15  E-value: 5.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQ--YVGNWAGVTVE----KkegfVNDSIKIVDLPGI-YAmdtfsneeKVSK-------- 69
Cdd:COG0218   27 AFAGRSNVGKSSLINALTNRKKlaRTSKTPGKTQLinffL----INDKFYLVDLPGYgYA--------KVSKaekekwqk 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  70 ---NFLINGN----VDVIIDI-VDASNLDRNLYltTQLKQFNKPIILVLNMID-VAENKgIKINYDILSKELN-----VK 135
Cdd:COG0218   95 lieDYLEGREnlkgVVLLIDIrHPPKELDLEML--EWLDEAGIPFLIVLTKADkLKKSE-LAKQLKAIKKALGkdpaaPE 171
                        170       180
                 ....*....|....*....|.
gi 500754663 136 VIPIIASKGIGIDKLIETLEN 156
Cdd:COG0218  172 VILFSSLKKEGIDELRAAIEE 192
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
5-157 3.62e-07

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 52.78  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQYVGNW--A--GVTVEKkegfvndsikiVDLPGIYAM---DT--FsneekVSK--NFLI 73
Cdd:COG2262  203 ALVGYTNAGKSTLFNRLTGADVLAEDKlfAtlDPTTRR-----------LELPDGRPVlltDTvgF-----IRKlpHQLV 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  74 N---------GNVDVIIDIVDASNLDRNLYLTT------QLKQFNKPIILVLNMIDVAENKGIKINydilsKELNVKVIP 138
Cdd:COG2262  267 EafrstleevREADLLLHVVDASDPDFEEQIETvnevleELGADDKPIILVFNKIDLLDDEELERL-----RAGYPDAVF 341
                        170
                 ....*....|....*....
gi 500754663 139 IIASKGIGIDKLIETLENK 157
Cdd:COG2262  342 ISAKTGEGIDELLEAIEER 360
YeeP COG3596
Predicted GTPase [General function prediction only];
5-117 3.69e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 52.08  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQY-VGNWAGVTVE----KKEGFVNDSIKIVDLPGIYAMDTFSNEEKVSKNFLinGNVDV 79
Cdd:COG3596   43 ALVGKTGAGKSSLINALFGAEVAeVGVGRPCTREiqryRLESDGLPGLVLLDTPGLGEVNERDREYRELRELL--PEADL 120
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 500754663  80 IIDIVDASN----LDRNLYLTTQLKQFNKPIILVLNMIDVAE 117
Cdd:COG3596  121 ILWVVKADDralaTDEEFLQALRAQYPDPPVLVVLTQVDRLE 162
obgE PRK12299
GTPase CgtA; Reviewed
6-154 1.03e-06

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 50.84  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   6 LLGNPNVGKTSLFNQLTGSNQYVGNWA--------GVtVEKKEGfvnDSIKIVDLPGIYamdtfsneEKVSKN------F 71
Cdd:PRK12299 163 LVGLPNAGKSTLISAVSAAKPKIADYPfttlhpnlGV-VRVDDY---KSFVIADIPGLI--------EGASEGaglghrF 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  72 LinGNVD---VIIDIVDASNLD-RNLYLTTQ--LKQFN-----KPIILVLNMIDVAENKGIKINYDILSKE-LNVKVIPI 139
Cdd:PRK12299 231 L--KHIErtrLLLHLVDIEAVDpVEDYKTIRneLEKYSpeladKPRILVLNKIDLLDEEEEREKRAALELAaLGGPVFLI 308
                        170
                 ....*....|....*
gi 500754663 140 IASKGIGIDKLIETL 154
Cdd:PRK12299 309 SAVTGEGLDELLRAL 323
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
5-156 1.51e-06

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: 48.52  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663    5 ALLGNPNVGKTSLFNQLTGSNQYVGN-WAGVTVE-KKEGFVNDSIK----IVDLPGI--YAMDTFSNEEKVSKNFLIngn 76
Cdd:TIGR00231   5 VIVGHPNVGKSTLLNSLLGNKGSITEyYPGTTRNyVTTVIEEDGKTykfnLLDTAGQedYDAIRRLYYPQVERSLRV--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   77 VDVIIDIVDASN-LDRNLYLTTQLKQFNKPIILVLNMIDvaeNKGIKINYDILSKELNVKVIPII---ASKGIGIDKLIE 152
Cdd:TIGR00231  82 FDIVILVLDVEEiLEKQTKEIIHHADSGVPIILVGNKID---LKDADLKTHVASEFAKLNGEPIIplsAETGKNIDSAFK 158

                  ....
gi 500754663  153 TLEN 156
Cdd:TIGR00231 159 IVEA 162
infB CHL00189
translation initiation factor 2; Provisional
5-154 2.15e-06

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 50.60  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQYVGNWAGVT-------VEKKEGFVNDSIKIVDLPGiyaMDTFSNEEKVSKNflingNV 77
Cdd:CHL00189 248 TILGHVDHGKTTLLDKIRKTQIAQKEAGGITqkigayeVEFEYKDENQKIVFLDTPG---HEAFSSMRSRGAN-----VT 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  78 DVIIDIVDAsnlDRNLYLTT-----QLKQFNKPIILVLNMIDVAENKGIKIN-----YDILSKEL--NVKVIPIIASKGI 145
Cdd:CHL00189 320 DIAILIIAA---DDGVKPQTieainYIQAANVPIIVAINKIDKANANTERIKqqlakYNLIPEKWggDTPMIPISASQGT 396

                 ....*....
gi 500754663 146 GIDKLIETL 154
Cdd:CHL00189 397 NIDKLLETI 405
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
77-155 9.43e-06

Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 47.41  E-value: 9.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  77 VDVIIDIVDA------SNLDrnlylttqLKQF--NKPIILVLNMIDVAENKGIK--INYdilSKELNVKVIPIIASKGIG 146
Cdd:COG1161   24 VDLVIEVVDAriplssRNPM--------LDELvgNKPRLLVLNKADLADPSVTKqwLKY---FEKQGVDALAISAKKGKG 92

                 ....*....
gi 500754663 147 IDKLIETLE 155
Cdd:COG1161   93 IKELIEAIR 101
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
6-181 1.58e-05

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 46.16  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   6 LLGNPNVGKTSLFNQLTGsnqyvGNWAG--------VTVEKKEGFVNDSIKIVDLPGiyamdtfsnEEKVSKNFL--ING 75
Cdd:cd04105    5 LLGPSDSGKTALFTKLTT-----GKVRStvtsiepnVASFYSNSSKGKKLTLVDVPG---------HEKLRDKLLeyLKA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  76 NVDVIIDIVDASNLDRN-------LY--LTTQLKQFNKPIILVL-NMIDVAENKGIKINYDILSKELNVkvipIIASKGI 145
Cdd:cd04105   71 SLKAIVFVVDSATFQKNirdvaefLYdiLTDLEKIKNKIPILIAcNKQDLFTAKPAKKIKELLEKEINT----LRESRSK 146
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 500754663 146 GIDKLIETLENKTFLSYKDNNDYNFESERDAYKFIG 181
Cdd:cd04105  147 SLESLDGDDGSKDTLGDKGGKDFEFDQLEGEVDFVE 182
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
99-154 2.75e-05

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: 44.77  E-value: 2.75e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500754663  99 LKQFNKPIILVLNMID----VAEN----KGIKINYDILSKEL--NVKVIPIIASKGIGIDKLIETL 154
Cdd:cd01887   97 AKAANVPIIVAINKIDkpygTEADpervKNELSELGLVGEEWggDVSIVPISAKTGEGIDDLLEAI 162
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
5-154 4.25e-05

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: 43.87  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSN-QYVGNWAGVTVEKKE---GFVNDSIKIVDLPGIYAMDTFSNEEKVSKNFLINgNVDVI 80
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEvAAVGDRRPTTRAAQAyvwQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLP-EADLV 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500754663  81 IDIVDASN----LDRNLYLtTQLKQFNKPIILVLNMIDvaenkgikinydilskelnvKVIPIIASKGIGIDKLIETL 154
Cdd:cd11383   80 LWLLDADDralaADHDFYL-LPLAGHDAPLLFVLNQVD--------------------PVLAVSARTGWGLDELAEAL 136
PRK04213 PRK04213
GTP-binding protein EngB;
1-157 7.87e-05

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 44.14  E-value: 7.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   1 MITTALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFVNDSIkIVDLPGIYAMDTFSNE--EKVSKNFL--INGN 76
Cdd:PRK04213   9 KPEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRKPNHYDWGDFI-LTDLPGFGFMSGVPKEvqEKIKDEIVryIEDN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  77 VDVI---IDIVDASNL----DR---------NLYLTTQLKQFNKPIILVLNMIDVAENKGIKINY--DILS-----KELN 133
Cdd:PRK04213  88 ADRIlaaVLVVDGKSFieiiERwegrgeipiDVEMFDFLRELGIPPIVAVNKMDKIKNRDEVLDEiaERLGlyppwRQWQ 167
                        170       180
                 ....*....|....*....|....
gi 500754663 134 VKVIPIIASKGiGIDKLIETLENK 157
Cdd:PRK04213 168 DIIAPISAKKG-GIEELKEAIRKR 190
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
5-116 8.69e-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: 43.93  E-value: 8.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSnqyVGNWAGVTVEKKEGFVNDSIKIVDLPGIYAMDTFSNEEK--VSKNFLINGNVDVII- 81
Cdd:cd04148    4 VLLGDSGVGKSSLANIFTAG---VYEDSAYEASGDDTYERTVSVDGEEATLVVYDHWEQEDGmwLEDSCMQVGDAYVIVy 80
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 500754663  82 DIVDASNLDRNLYLTTQLKQFN----KPIILVLNMIDVA 116
Cdd:cd04148   81 SVTDRSSFEKASELRIQLRRARqaedIPIILVGNKSDLV 119
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
5-55 8.78e-05

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 45.56  E-value: 8.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQ-YVGNWAGVTVEKKEGFVN---DSIKIVDLPGI 55
Cdd:PRK09518 454 ALVGRPNVGKSSLLNQLTHEERaVVNDLAGTTRDPVDEIVEidgEDWLFIDTAGI 508
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
1-55 9.07e-05

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: 43.33  E-value: 9.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 500754663   1 MITTALLGNPNVGKTSLFNQLTGSN-QYVGNWAGVTVEKKEGFVNDSIKIVDLPGI 55
Cdd:cd04178  116 SITVGVVGYPNVGKSSVINSLKRSRaCNVGATPGVTKSMQEVHLDKHVKLLDSPGV 171
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
5-37 1.50e-04

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 44.58  E-value: 1.50e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 500754663   5 ALLGNPNVGKTSLFNQLTGSNQ-YVGNWAGVTVE 37
Cdd:PRK03003 215 ALVGKPNVGKSSLLNKLAGEERsVVDDVAGTTVD 248
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
2-56 2.40e-04

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: 42.92  E-value: 2.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 500754663   2 ITTALLGNPNVGKTSLFNQLTGSNQYVGNWAGVTVEKKEGFVN---DSIKIVDLPGIY 56
Cdd:cd01896    1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEykgAKIQLLDLPGII 58
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
76-158 1.07e-03

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 40.84  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  76 NVDVIIdIVDASN--------LDRnlYLTtQLKQFNKPIILVLNMIDVAENKGIKinyDILS--KELNVKVIPIIASKGI 145
Cdd:cd01854    2 NVDQVL-IVFSLKepffnlrlLDR--YLV-AAEASGIEPVIVLNKADLVDDEELE---ELLEiyEKLGYPVLAVSAKTGE 74
                         90
                 ....*....|...
gi 500754663 146 GIDKLIETLENKT 158
Cdd:cd01854   75 GLDELRELLKGKT 87
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
7-55 1.27e-03

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 39.82  E-value: 1.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 500754663   7 LGNPNVGKTSLFNQLTGSNQY-VGNWAGVTVEKKEGFVNDSIKIVDLPGI 55
Cdd:cd01856  121 VGIPNVGKSTLINRLRGKKVAkVGNKPGVTRGQQWIRIGPNIELLDTPGI 170
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
98-156 2.09e-03

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


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 39.43  E-value: 2.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500754663   98 QLKQFNKPIILVLNMIDVAENKGIK-----INYDILSKEL----NVKVIPIIASKGIGIDKLIETLEN 156
Cdd:pfam00009 116 LARQLGVPIIVFINKMDRVDGAELEevveeVSRELLEKYGedgeFVPVVPGSALKGEGVQTLLDALDE 183
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
72-154 4.91e-03

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: 38.07  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  72 LINGNVDVIIDIVDASN--LDRNLYLTTQLKQFNKPIILVLNMID-----VAEnkGIKinyDILSKElNVKVIPIIASKG 144
Cdd:cd01859    7 RIIKEADVVLEVVDARDpeLTRSRKLERMALELGKKLIIVLNKADlvpreVLE--KWK---EVFESE-GLPVVYVSARER 80
                         90
                 ....*....|
gi 500754663 145 IGIDKLIETL 154
Cdd:cd01859   81 LGTRILRRTI 90
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
76-152 9.12e-03

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 37.51  E-value: 9.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500754663  76 NVDVIIDIVDA-----SnldRNLYLTTQLKqfNKPIILVLNMIDVAENKGIK--INYdilSKELNVKVIPIIASKGIGID 148
Cdd:cd01856   19 LVDVVIEVRDAriplsS---RNPDLDKILG--NKPRLIVLNKADLADPAKTKkwLKY---FKSQGEPVLFVNAKNGKGVK 90

                 ....
gi 500754663 149 KLIE 152
Cdd:cd01856   91 KLLK 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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