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Conserved domains on  [gi|489009949|ref|WP_002920508|]
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MULTISPECIES: Fe(2+) transporter permease subunit FeoB [Klebsiella]

Protein Classification

ferrous iron transporter B( domain architecture ID 11484344)

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 Ontology:  GO:0015093|GO:0005525|GO:0006826
PubMed:  12446835
SCOP:  4004042
TCDB:  9.A.8

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
1-772 0e+00

Fe(2+) transporter permease subunit FeoB;


:

Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 1651.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   1 MQKLTVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTISSQTSLDEQIACHY 80
Cdd:PRK09554   1 MKKLTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSQTSLDEQIACHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  81 ILSGDADMLINVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALK 160
Cdd:PRK09554  81 ILSGDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEALK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 161 IALDRHQANSDLELVHYPQPLLREADLLAQQMSAQIPTRQRRWLGLQMLEGDIYSRAYAGDAADKLDIALANLSDEIDDP 240
Cdd:PRK09554 161 LAIDRHQANENVELVHYPQPLLNEADSLAKVMPSDIPLQQRRWLGLQMLEGDIYSRAYAGEASQHLDAALARLRNEMDDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 241 ALHIADARYQTIAAICDAVSNTLTAEPSRFTAAMDKVILNRFLGLPIFLFVMYLMFLLAINIGGALQPIFDAGSVAIFVH 320
Cdd:PRK09554 241 ALHIADARYQCIAAICDAVSNTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIGGALQPLFDVGSVAIFIH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 321 GIQWLGYTLHFPDWLTVFLAQGIGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVG 400
Cdd:PRK09554 321 GIQWLGYTLHFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 401 FGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYVLGIVMAILTGLMLKHTIMRG 480
Cdd:PRK09554 401 FGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLGIVMAILTGLMLKYTIMRG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 481 EASPFVMELPVYHVPHIKSLIIQTWQRLKGFVLRAGKVIVIVSIFLSALNSFSLSGKVVDNINDSALASVSRVITPVFKP 560
Cdd:PRK09554 481 EASPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIVDNINDSALASVSRVITPVLKP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 561 IGVHEDNWQATVGLFTGAMAKEVVVGTLNTLYTAEDIQNEEFNPQTFSLGEELLAAVDETWQGLKDTFSLSVLANPIEAS 640
Cdd:PRK09554 561 IGVHEDNWQATVGLFTGAMAKEVVVGTLNTLYTAENIQDEEFNPAEFNLGDELFGAVDETWQSLKDTFSLSVLANPIEAS 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 641 KGDGEMATGAMGVMGSKFGSAAAAYSYLIFVLLYIPCISVMGAIARESSRGWMTFSILWGLNIAYSLSTLYYQTVSFSDH 720
Cdd:PRK09554 641 KGDGEMGTGAMGVMSQKFGSAAAAYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQVASFSQH 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489009949 721 PRYSLVCILAVVLFNVVLFGLLRRARSRVDVSLLATRKTPASCCSSPAGDCH 772
Cdd:PRK09554 721 PTYSLVCILAVILFNIVVLGLLRRARSRVDVELLATRKSVSSCCAATTGDCH 772
 
Name Accession Description Interval E-value
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
1-772 0e+00

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 1651.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   1 MQKLTVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTISSQTSLDEQIACHY 80
Cdd:PRK09554   1 MKKLTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSQTSLDEQIACHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  81 ILSGDADMLINVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALK 160
Cdd:PRK09554  81 ILSGDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEALK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 161 IALDRHQANSDLELVHYPQPLLREADLLAQQMSAQIPTRQRRWLGLQMLEGDIYSRAYAGDAADKLDIALANLSDEIDDP 240
Cdd:PRK09554 161 LAIDRHQANENVELVHYPQPLLNEADSLAKVMPSDIPLQQRRWLGLQMLEGDIYSRAYAGEASQHLDAALARLRNEMDDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 241 ALHIADARYQTIAAICDAVSNTLTAEPSRFTAAMDKVILNRFLGLPIFLFVMYLMFLLAINIGGALQPIFDAGSVAIFVH 320
Cdd:PRK09554 241 ALHIADARYQCIAAICDAVSNTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIGGALQPLFDVGSVAIFIH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 321 GIQWLGYTLHFPDWLTVFLAQGIGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVG 400
Cdd:PRK09554 321 GIQWLGYTLHFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 401 FGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYVLGIVMAILTGLMLKHTIMRG 480
Cdd:PRK09554 401 FGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLGIVMAILTGLMLKYTIMRG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 481 EASPFVMELPVYHVPHIKSLIIQTWQRLKGFVLRAGKVIVIVSIFLSALNSFSLSGKVVDNINDSALASVSRVITPVFKP 560
Cdd:PRK09554 481 EASPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIVDNINDSALASVSRVITPVLKP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 561 IGVHEDNWQATVGLFTGAMAKEVVVGTLNTLYTAEDIQNEEFNPQTFSLGEELLAAVDETWQGLKDTFSLSVLANPIEAS 640
Cdd:PRK09554 561 IGVHEDNWQATVGLFTGAMAKEVVVGTLNTLYTAENIQDEEFNPAEFNLGDELFGAVDETWQSLKDTFSLSVLANPIEAS 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 641 KGDGEMATGAMGVMGSKFGSAAAAYSYLIFVLLYIPCISVMGAIARESSRGWMTFSILWGLNIAYSLSTLYYQTVSFSDH 720
Cdd:PRK09554 641 KGDGEMGTGAMGVMSQKFGSAAAAYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQVASFSQH 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489009949 721 PRYSLVCILAVVLFNVVLFGLLRRARSRVDVSLLATRKTPASCCSSPAGDCH 772
Cdd:PRK09554 721 PTYSLVCILAVILFNIVVLGLLRRARSRVDVELLATRKSVSSCCAATTGDCH 772
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-717 0e+00

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 824.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   1 MQKLTVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTissqTSLDEQIACHY 80
Cdd:COG0370    1 MKMITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTYSLSA----YSPDEKVARDF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  81 ILSGDADMLINVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALK 160
Cdd:COG0370   77 LLEEKPDVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 161 IALDRHQANSDLE--LVHYPQPLLREADLLAQQMSAQIPtRQRRWLGLQMLEGDIYSRAYAGDAADKLDIALANLSDEID 238
Cdd:COG0370  157 EAIIEAAEGKKPRplRIDYPEEIEEAIEELEELLEEDGP-YPSRWLAIKLLEGDEEVLELLSELLELLEEIREELEEELG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 239 -DPALHIADARYQTIAAICDAVSNTLTAEPSRFTAAMDKVILNRFLGLPIFLFVMYLMFLLAINIGGALQPIFDAGsVAI 317
Cdd:COG0370  236 eDLESIIADARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTVGAPLMDLIDGG-FGW 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 318 FVHGIQWLGytlhFPDWLTVFLAQGIGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPL 397
Cdd:COG0370  315 LGDWVAALL----PPGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPL 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 398 IVGFGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYVLGIVMAILTGLMLKHTI 477
Cdd:COG0370  391 LSGFGCNVPAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTL 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 478 MRGEASPFVMELPVYHVPHIKSLIIQTWQRLKGFVLRAGKVIVIVSIFLSALNSFSLSGkVVDNINDSALASVSRVITPV 557
Cdd:COG0370  471 LKGEPSPFVMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGG-ESEDLENSYLGRIGKALEPV 549
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 558 FKPIGVhedNWQATVGLFTGAMAKEVVVGTLNTLYTAEDiqneefnpqtfslgeellaavdetwqglkdtfslsvlanpi 637
Cdd:COG0370  550 FAPLGF---DWQIGVALITGFAAKEVVVGTLGTLYGVGE----------------------------------------- 585
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 638 easkgDGEMATGAMGVMGSKFgSAAAAYSYLIFVLLYIPCISVMGAIARES-SRGWMTFSILWGLNIAYSLSTLYYQTVS 716
Cdd:COG0370  586 -----DAEESASLAEALAAGF-TPATALSFLVFVLLYTPCVATLAAIKRETgSWKWTLFAVGYMTVLAYLVAFLVYQIGR 659

                 .
gi 489009949 717 F 717
Cdd:COG0370  660 L 660
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
10-687 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: 674.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   10 GNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTISsqtsLDEQIACHYILSGDADML 89
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGIYSLTTFS----LEEEVARDYLLNEKPDLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   90 INVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALKIALDrhQAN 169
Cdd:TIGR00437  77 VNVVDASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGRGIERLKDAIR--KAI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  170 SDLELVHYPQPLLREADLLAQQMSAQIPTRQRR-WLGLQMLEGDIYSRAYAGDAADKLDIALANLSDEIDDPALHIADAR 248
Cdd:TIGR00437 155 GLKELKKRAIEIVPEAYQVVEVVEGLIEIIYSIsKRGLEILLGLLEDLSLEIEKIERNLAEVVIKESPSNLSPTEIADED 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  249 yqtiaaicdavsnTLTAEPSRFTAamdkvILNRFLGLPIFLFVMYLMFLLAINIGGALQPIFDAGSVAIFVHGIQWLGyt 328
Cdd:TIGR00437 235 -------------RVLVEKSIGRK-----ILDRFLGLPIFLFVMFILFLLTFLVGQPLVDLIETGFSFLSEAVKSFIG-- 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  329 lhfPDWLTVFLAQGIGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFGCNVPSV 408
Cdd:TIGR00437 295 ---NYWLASLLGDGLIGGVGAVLSFVPLIAILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPAI 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  409 MGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFF-GQNGALAVFSLYVLGIVMAILTGLMLKHTIMRGEASPFVM 487
Cdd:TIGR00437 372 MATRTLETRRERLLTALVIPFMSCSARLPVIVLLFAAAFpGKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFIM 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  488 ELPVYHVPHIKSLIIQTWQRLKGFVLRAGKVIVIVSIFLSALNSFSLSgkvvdNINDSALASVSRVITPVFKPIGVHEDn 567
Cdd:TIGR00437 452 ELPPYRLPRFRVVFIQTWTRLRSFIKKAGTIIVIGSVLIWFLSSFPGG-----KILESWLAAIGSIMAPLFVPLGKILD- 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  568 WQATVGLFTGAMAKEVVVGTLNTLYTAEDIqneefnpqtfslgeellaavdetwqglkdTFSLSVLANPIEaskgdgema 647
Cdd:TIGR00437 526 WFASVALIFGFVAKEVVVATLGVLYGLGNI-----------------------------LSSIGHAMVPVE--------- 567
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 489009949  648 tgamgvmgskfgsaaaAYSYLIFVLLYIPCISVMGAIARE 687
Cdd:TIGR00437 568 ----------------ALSYMLFVLLYVPCLATLAAIARE 591
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
8-165 7.90e-77

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: 244.67  E-value: 7.90e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   8 LIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTISsqtsLDEQIACHYILSGDAD 87
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTYSLTPYS----EDEKVARDFLLGEEPD 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489009949  88 MLINVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALKIALDR 165
Cdd:cd01879   78 LIVNVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDELLDAIAK 155
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
4-160 2.57e-76

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: 243.13  E-value: 2.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949    4 LTVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTISsqtsLDEQIACHYILS 83
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGIYSLSPYS----EEERVARDYLLN 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489009949   84 GDADMLINVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALK 160
Cdd:pfam02421  77 EKPDVIVNVVDATNLERNLYLTLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSARKGEGIDELL 153
 
Name Accession Description Interval E-value
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
1-772 0e+00

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 1651.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   1 MQKLTVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTISSQTSLDEQIACHY 80
Cdd:PRK09554   1 MKKLTIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSQTSLDEQIACHY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  81 ILSGDADMLINVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALK 160
Cdd:PRK09554  81 ILSGDADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEALK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 161 IALDRHQANSDLELVHYPQPLLREADLLAQQMSAQIPTRQRRWLGLQMLEGDIYSRAYAGDAADKLDIALANLSDEIDDP 240
Cdd:PRK09554 161 LAIDRHQANENVELVHYPQPLLNEADSLAKVMPSDIPLQQRRWLGLQMLEGDIYSRAYAGEASQHLDAALARLRNEMDDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 241 ALHIADARYQTIAAICDAVSNTLTAEPSRFTAAMDKVILNRFLGLPIFLFVMYLMFLLAINIGGALQPIFDAGSVAIFVH 320
Cdd:PRK09554 241 ALHIADARYQCIAAICDAVSNTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIGGALQPLFDVGSVAIFIH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 321 GIQWLGYTLHFPDWLTVFLAQGIGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVG 400
Cdd:PRK09554 321 GIQWLGYTLHFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 401 FGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYVLGIVMAILTGLMLKHTIMRG 480
Cdd:PRK09554 401 FGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLGIVMAILTGLMLKYTIMRG 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 481 EASPFVMELPVYHVPHIKSLIIQTWQRLKGFVLRAGKVIVIVSIFLSALNSFSLSGKVVDNINDSALASVSRVITPVFKP 560
Cdd:PRK09554 481 EASPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIVDNINDSALASVSRVITPVLKP 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 561 IGVHEDNWQATVGLFTGAMAKEVVVGTLNTLYTAEDIQNEEFNPQTFSLGEELLAAVDETWQGLKDTFSLSVLANPIEAS 640
Cdd:PRK09554 561 IGVHEDNWQATVGLFTGAMAKEVVVGTLNTLYTAENIQDEEFNPAEFNLGDELFGAVDETWQSLKDTFSLSVLANPIEAS 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 641 KGDGEMATGAMGVMGSKFGSAAAAYSYLIFVLLYIPCISVMGAIARESSRGWMTFSILWGLNIAYSLSTLYYQTVSFSDH 720
Cdd:PRK09554 641 KGDGEMGTGAMGVMSQKFGSAAAAYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQVASFSQH 720
                        730       740       750       760       770
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489009949 721 PRYSLVCILAVVLFNVVLFGLLRRARSRVDVSLLATRKTPASCCSSPAGDCH 772
Cdd:PRK09554 721 PTYSLVCILAVILFNIVVLGLLRRARSRVDVELLATRKSVSSCCAATTGDCH 772
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-717 0e+00

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 824.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   1 MQKLTVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTissqTSLDEQIACHY 80
Cdd:COG0370    1 MKMITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTYSLSA----YSPDEKVARDF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  81 ILSGDADMLINVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALK 160
Cdd:COG0370   77 LLEEKPDVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 161 IALDRHQANSDLE--LVHYPQPLLREADLLAQQMSAQIPtRQRRWLGLQMLEGDIYSRAYAGDAADKLDIALANLSDEID 238
Cdd:COG0370  157 EAIIEAAEGKKPRplRIDYPEEIEEAIEELEELLEEDGP-YPSRWLAIKLLEGDEEVLELLSELLELLEEIREELEEELG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 239 -DPALHIADARYQTIAAICDAVSNTLTAEPSRFTAAMDKVILNRFLGLPIFLFVMYLMFLLAINIGGALQPIFDAGsVAI 317
Cdd:COG0370  236 eDLESIIADARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTVGAPLMDLIDGG-FGW 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 318 FVHGIQWLGytlhFPDWLTVFLAQGIGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPL 397
Cdd:COG0370  315 LGDWVAALL----PPGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPL 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 398 IVGFGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYVLGIVMAILTGLMLKHTI 477
Cdd:COG0370  391 LSGFGCNVPAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTL 470
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 478 MRGEASPFVMELPVYHVPHIKSLIIQTWQRLKGFVLRAGKVIVIVSIFLSALNSFSLSGkVVDNINDSALASVSRVITPV 557
Cdd:COG0370  471 LKGEPSPFVMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGG-ESEDLENSYLGRIGKALEPV 549
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 558 FKPIGVhedNWQATVGLFTGAMAKEVVVGTLNTLYTAEDiqneefnpqtfslgeellaavdetwqglkdtfslsvlanpi 637
Cdd:COG0370  550 FAPLGF---DWQIGVALITGFAAKEVVVGTLGTLYGVGE----------------------------------------- 585
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 638 easkgDGEMATGAMGVMGSKFgSAAAAYSYLIFVLLYIPCISVMGAIARES-SRGWMTFSILWGLNIAYSLSTLYYQTVS 716
Cdd:COG0370  586 -----DAEESASLAEALAAGF-TPATALSFLVFVLLYTPCVATLAAIKRETgSWKWTLFAVGYMTVLAYLVAFLVYQIGR 659

                 .
gi 489009949 717 F 717
Cdd:COG0370  660 L 660
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
10-687 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: 674.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   10 GNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTISsqtsLDEQIACHYILSGDADML 89
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGIYSLTTFS----LEEEVARDYLLNEKPDLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   90 INVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALKIALDrhQAN 169
Cdd:TIGR00437  77 VNVVDASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGRGIERLKDAIR--KAI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  170 SDLELVHYPQPLLREADLLAQQMSAQIPTRQRR-WLGLQMLEGDIYSRAYAGDAADKLDIALANLSDEIDDPALHIADAR 248
Cdd:TIGR00437 155 GLKELKKRAIEIVPEAYQVVEVVEGLIEIIYSIsKRGLEILLGLLEDLSLEIEKIERNLAEVVIKESPSNLSPTEIADED 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  249 yqtiaaicdavsnTLTAEPSRFTAamdkvILNRFLGLPIFLFVMYLMFLLAINIGGALQPIFDAGSVAIFVHGIQWLGyt 328
Cdd:TIGR00437 235 -------------RVLVEKSIGRK-----ILDRFLGLPIFLFVMFILFLLTFLVGQPLVDLIETGFSFLSEAVKSFIG-- 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  329 lhfPDWLTVFLAQGIGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFGCNVPSV 408
Cdd:TIGR00437 295 ---NYWLASLLGDGLIGGVGAVLSFVPLIAILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPAI 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  409 MGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFF-GQNGALAVFSLYVLGIVMAILTGLMLKHTIMRGEASPFVM 487
Cdd:TIGR00437 372 MATRTLETRRERLLTALVIPFMSCSARLPVIVLLFAAAFpGKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFIM 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  488 ELPVYHVPHIKSLIIQTWQRLKGFVLRAGKVIVIVSIFLSALNSFSLSgkvvdNINDSALASVSRVITPVFKPIGVHEDn 567
Cdd:TIGR00437 452 ELPPYRLPRFRVVFIQTWTRLRSFIKKAGTIIVIGSVLIWFLSSFPGG-----KILESWLAAIGSIMAPLFVPLGKILD- 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  568 WQATVGLFTGAMAKEVVVGTLNTLYTAEDIqneefnpqtfslgeellaavdetwqglkdTFSLSVLANPIEaskgdgema 647
Cdd:TIGR00437 526 WFASVALIFGFVAKEVVVATLGVLYGLGNI-----------------------------LSSIGHAMVPVE--------- 567
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 489009949  648 tgamgvmgskfgsaaaAYSYLIFVLLYIPCISVMGAIARE 687
Cdd:TIGR00437 568 ----------------ALSYMLFVLLYVPCLATLAAIARE 591
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
8-165 7.90e-77

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: 244.67  E-value: 7.90e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   8 LIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTISsqtsLDEQIACHYILSGDAD 87
Cdd:cd01879    2 LVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTYSLTPYS----EDEKVARDFLLGEEPD 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489009949  88 MLINVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALKIALDR 165
Cdd:cd01879   78 LIVNVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDELLDAIAK 155
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
4-160 2.57e-76

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: 243.13  E-value: 2.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949    4 LTVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYSLTTISsqtsLDEQIACHYILS 83
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGIYSLSPYS----EEERVARDYLLN 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489009949   84 GDADMLINVVDASNLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGCPVIPLVSTRGRGIEALK 160
Cdd:pfam02421  77 EKPDVIVNVVDATNLERNLYLTLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSARKGEGIDELL 153
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
5-121 1.47e-24

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


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 98.85  E-value: 1.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949    5 TVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPGTYslttisSQTSLDEQIACHYILSG 84
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLI------EGASEGEGLGRAFLAII 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 489009949   85 DADMLINVVDASNL--ERNLYLTLQLLELGIPCVVALNM 121
Cdd:pfam01926  75 EADLILFVVDSEEGitPLDEELLELLRENKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
7-166 1.89e-18

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: 83.06  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   7 GLIGNPNSGKTTLFNQLTGARQR-VGNWAGVTVERKEGIFaTTDH--QVTLVDLPGtysLTTISSQTSLDEQIAchYILS 83
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGiVSPIPGTTRDPVRKEW-ELLPlgPVVLIDTPG---LDEEGGLGRERVEEA--RQVA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  84 GDADMLINVVDAS-NLERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDID--ALAARLGCPVIPLVSTRGRGIEALK 160
Cdd:cd00880   75 DRADLVLLVVDSDlTPVEEEAKLGLLRERGKPVLLVLNKIDLVPESEEEELLRerKLELLPDLPVIAVSALPGEGIDELR 154

                 ....*.
gi 489009949 161 IALDRH 166
Cdd:cd00880  155 KKIAEL 160
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
7-163 2.90e-17

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: 79.81  E-value: 2.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   7 GLIGNPNSGKTTLFNQLTGARQ-RVGNWAGVTVE--RKEGIFATTDHQVTLVDLPGTYslttiSSQTSLDEQIACHYIls 83
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVgEVSDVPGTTRDpdVYVKELDKGKVKLVLVDTPGLD-----EFGGLGREELARLLL-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  84 GDADMLINVVDASNLE----RNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDA--LAARLGCPVIPLVSTRGRGIE 157
Cdd:cd00882   74 RGADLILLVVDSTDREseedAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLeeLAKILGVPVFEVSAKTGEGVD 153

                 ....*.
gi 489009949 158 ALKIAL 163
Cdd:cd00882  154 ELFEKL 159
FeoB_C pfam07664
Ferrous iron transport protein B C terminus; Escherichia coli has an iron(II) transport system ...
455-504 1.51e-16

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: 73.98  E-value: 1.51e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489009949  455 VFSLYVLGIVMAILTGLML-KHTIMRGEASPFVMELPVYHVPHIKSLIIQT 504
Cdd:pfam07664   1 LFSLYLLGILVALLVALLLkKTTLLKGEPSPFVMELPPYRLPTLKNVLRKT 51
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
350-436 5.09e-14

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: 68.43  E-value: 5.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  350 VLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALG---LPGKSFVPLIVGFGCN---VPSVMGARTLDAPRERLMT 423
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYSGLLDRIGKLLGPLMRPLGlfpLPGKAAIALLLGFGAKevgVPLLATPYGIDTPRERLAA 80
                          90
                  ....*....|....
gi 489009949  424 IMMAPFMS-CGARL 436
Cdd:pfam07670  81 LLFTSFSTpCGATL 94
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
5-166 2.24e-11

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: 63.63  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   5 TVGLIGNPNSGKTTLFNQLTGarqrvgnwAGVTVERKegIFATTD-----------HQVTLVD-------LPgtyslTTI 66
Cdd:cd01878   43 TVALVGYTNAGKSTLFNALTG--------ADVLAEDQ--LFATLDpttrriklpggREVLLTDtvgfirdLP-----HQL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  67 --SSQTSLDEqiachyilSGDADMLINVVDASNLERNLYLTLQLL------ELGIPCVVALNMLDIAEKQQVRIDIDALA 138
Cdd:cd01878  108 veAFRSTLEE--------VAEADLLLHVVDASDPDREEQIETVEEvlkelgADDIPIILVLNKIDLLDDEELEERLRAGR 179
                        170       180
                 ....*....|....*....|....*...
gi 489009949 139 ArlgcPVIPLVSTRGRGIEALKIALDRH 166
Cdd:cd01878  180 P----DAVFISAKTGEGLDLLKEAIEEL 203
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
7-162 5.71e-11

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: 61.64  E-value: 5.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   7 GLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTD-HQVTLVDLPGTysLTTISSQTSLDEQIACHYILSgd 85
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDgVDIQIIDLPGL--LDGASEGRGLGEQILAHLYRS-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  86 aDMLINVVDASNLE-----------RNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARlGCPVIPLVSTRGR 154
Cdd:cd01881   77 -DLILHVIDASEDCvgdpledqktlNEEVSGSFLFLKNKPEMIVANKIDMASENNLKRLKLDKLKR-GIPVVPTSALTRL 154

                 ....*...
gi 489009949 155 GIEALKIA 162
Cdd:cd01881  155 GLDRVIRT 162
FeoB_Cyto pfam17910
FeoB cytosolic helical domain; FeoB is a G-protein coupled membrane protein essential for Fe ...
186-259 3.43e-10

FeoB cytosolic helical domain; FeoB is a G-protein coupled membrane protein essential for Fe(II) uptake in prokaryotes. In the structures, a canonical G-protein domain (G domain) is followed by a helical bundle domain (S-domain) which is represented by this entry.


Pssm-ID: 465561 [Multi-domain]  Cd Length: 90  Bit Score: 57.25  E-value: 3.43e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489009949  186 DLLAQQMSAQIPtrqRRWLGLQMLEGDIYSRAYAGDAAD---KLDIALANLSDEI-DDPALHIADARYQTIAAICDAV 259
Cdd:pfam17910  14 PLLEEDLEDKYP---PRWLAIKLLEGDEEVLEKLKLSEElleELEEIREELEKELgEDLESIIADARYGFIEGILKEV 88
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
512-596 7.69e-09

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: 53.80  E-value: 7.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  512 VLRAGKVIVIVSIFLSALNSFSLsgkvvdnindsaLASVSRVITPVFKPIGVHEDNWQATVGLFTGAMAKEVVVGTLNTL 591
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYSGL------------LDRIGKLLGPLMRPLGLFPLPGKAAIALLLGFGAKEVGVPLLATP 68

                  ....*
gi 489009949  592 YTAED 596
Cdd:pfam07670  69 YGIDT 73
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
8-95 3.98e-08

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: 53.21  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   8 LIGNPNSGKTTLFNQLTGARQR-VGNWAGVTVERKEGIFATTDHQVTLVDLPG-TYSLTTISSQTSLDEQIACHyilsgD 85
Cdd:cd01894    2 IVGRPNVGKSTLFNRLTGRRDAiVSDTPGVTRDRKYGEAEWGGREFILIDTGGiEPDDEGISKEIREQAEIAIE-----E 76
                         90
                 ....*....|
gi 489009949  86 ADMLINVVDA 95
Cdd:cd01894   77 ADVILFVVDG 86
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
5-166 4.62e-08

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 56.25  E-value: 4.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   5 TVGLIGNPNSGKTTLFNQLTGArqrvgnwaGVTVERKegIFATTD-----------HQVTLVD-------LPgtyslTT- 65
Cdd:COG2262  201 TVALVGYTNAGKSTLFNRLTGA--------DVLAEDK--LFATLDpttrrlelpdgRPVLLTDtvgfirkLP-----HQl 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  66 ISS-QTSLDEqiachyilSGDADMLINVVDAS--NLERNLYLTLQ----LLELGIPCVVALNMLDIAEKQqvriDIDALA 138
Cdd:COG2262  266 VEAfRSTLEE--------VREADLLLHVVDASdpDFEEQIETVNEvleeLGADDKPIILVFNKIDLLDDE----ELERLR 333
                        170       180
                 ....*....|....*....|....*....
gi 489009949 139 ARLGCPVipLVSTR-GRGIEALKIALDRH 166
Cdd:COG2262  334 AGYPDAV--FISAKtGEGIDELLEAIEER 360
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
6-166 5.89e-08

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 54.99  E-value: 5.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   6 VGLIGNPNSGKTTLFNQLTGA------------RQRVgnwagvtveRkeGIFATTDHQVTLVDLPGtyslttI-SSQTSL 72
Cdd:COG1159    6 VAIVGRPNVGKSTLLNALVGQkvsivspkpqttRHRI---------R--GIVTREDAQIVFVDTPG------IhKPKRKL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  73 DE---QIAchyiLS--GDADMLINVVDASNL--ERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRIDIDALAARLGC-P 144
Cdd:COG1159   69 GRrmnKAA----WSalEDVDVILFVVDATEKigEGDEFILELLKKLKTPVILVINKIDLVKKEELLPLLAEYSELLDFaE 144
                        170       180
                 ....*....|....*....|..
gi 489009949 145 VIPLVSTRGRGIEALKIALDRH 166
Cdd:COG1159  145 IVPISALKGDNVDELLDEIAKL 166
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
6-160 6.61e-08

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: 52.85  E-value: 6.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   6 VGLIGNPNSGKTTLFNQLTGA------------RQRVgnwagvtverkEGIFATTDHQVTLVDLPGtysltTISSQTSLD 73
Cdd:cd04163    6 VAIIGRPNVGKSTLLNALVGQkisivspkpqttRNRI-----------RGIYTDDDAQIIFVDTPG-----IHKPKKKLG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  74 EQIAcHYILSG--DADMLINVVDASNL--ERNLYLTLQLLELGIPCVVALNMLDIAEKQQvriDIDALAARL-----GCP 144
Cdd:cd04163   70 ERMV-KAAWSAlkDVDLVLFVVDASEWigEGDEFILELLKKSKTPVILVLNKIDLVKDKE---DLLPLLEKLkelhpFAE 145
                        170
                 ....*....|....*.
gi 489009949 145 VIPLVSTRGRGIEALK 160
Cdd:cd04163  146 IFPISALKGENVDELL 161
PRK04213 PRK04213
GTP-binding protein EngB;
1-166 9.26e-08

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 53.00  E-value: 9.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   1 MQKLTVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTveRKEGIFATTDHqvTLVDLPGTYSLTTISSQTSldEQIA--- 77
Cdd:PRK04213   7 DRKPEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVT--RKPNHYDWGDF--ILTDLPGFGFMSGVPKEVQ--EKIKdei 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  78 CHYILSGDADML--INVVDASNL----ER---------NLYLTLQLLELGIPCVVALNMLD-IAEKQQVridIDALAARL 141
Cdd:PRK04213  81 VRYIEDNADRILaaVLVVDGKSFieiiERwegrgeipiDVEMFDFLRELGIPPIVAVNKMDkIKNRDEV---LDEIAERL 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 489009949 142 GCP---------VIPLVSTRGrGIEALKIALDRH 166
Cdd:PRK04213 158 GLYppwrqwqdiIAPISAKKG-GIEELKEAIRKR 190
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
5-166 1.08e-07

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


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 52.68  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   5 TVGLIGNPNSGKTTLFNQLT---GARQRVGNWAGVTV-----ERKEGIFATT--------DHQVTLVDLPG--TYSLTTI 66
Cdd:cd00881    1 NVGVIGHVDHGKTTLTGSLLyqtGAIDRRGTRKETFLdtlkeERERGITIKTgvvefewpKRRINFIDTPGheDFSKETV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  67 SSQTSldeqiachyilsgdADMLINVVDAS-----NLERNlylTLQLLELGIPCVVALN---MLDIAEKQQVRIDIDALA 138
Cdd:cd00881   81 RGLAQ--------------ADGALLVVDANegvepQTREH---LNIALAGGLPIIVAVNkidRVGEEDFDEVLREIKELL 143
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489009949 139 ARLGC--------PVIPLVSTRGRGIEALKIALDRH 166
Cdd:cd00881  144 KLIGFtflkgkdvPIIPISALTGEGIEELLDAIVEH 179
YeeP COG3596
Predicted GTPase [General function prediction only];
4-166 2.37e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 53.23  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   4 LTVGLIGNPNSGKTTLFNQLTGARQ-RVGNWAGVTVERKEGIFAT-TDHQVTLVDLPGTyslttisSQTSLDEQIACHYI 81
Cdd:COG3596   40 PVIALVGKTGAGKSSLINALFGAEVaEVGVGRPCTREIQRYRLESdGLPGLVLLDTPGL-------GEVNERDREYRELR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  82 -LSGDADMLINVVDASN----LERNLYLTLQLLELGIPCVVALNMLDIAE----------------KQQVRIDIDALAAR 140
Cdd:COG3596  113 eLLPEADLILWVVKADDralaTDEEFLQALRAQYPDPPVLVVLTQVDRLEperewdppynwpsppkEQNIRRALEAIAEQ 192
                        170       180       190
                 ....*....|....*....|....*....|..
gi 489009949 141 LGCP---VIPLV---STRGRGIEALKIALDRH 166
Cdd:COG3596  193 LGVPidrVIPVSaaeDRTGYGLEELVDALAEA 224
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
1-163 2.73e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.14  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   1 MQKLTVGLIGNPNSGKTTLFNQLtgARQRVGNWA-----GVTVERKEGIFATTDHQVTLVDLPGTYSLTTISSqtSLDEQ 75
Cdd:COG1100    1 MGEKKIVVVGTGGVGKTSLVNRL--VGDIFSLEKylstnGVTIDKKELKLDGLDVDLVIWDTPGQDEFRETRQ--FYARQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  76 IAchyilsgDADMLINVVDASNLERNLYLTLQLLE-----LGIPCVVALNMLDIAEKQQVRiDIDALAARLG----CPVI 146
Cdd:COG1100   77 LT-------GASLYLFVVDGTREETLQSLYELLESlrrlgKKSPIILVLNKIDLYDEEEIE-DEERLKEALSedniVEVV 148
                        170
                 ....*....|....*..
gi 489009949 147 PLVSTRGRGIEALKIAL 163
Cdd:COG1100  149 ATSAKTGEGVEELFAAL 165
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
5-59 3.05e-07

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


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 52.16  E-value: 3.05e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489009949   5 TVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDHQVTLVDLPG 59
Cdd:cd01896    2 RVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPG 56
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
5-95 6.21e-07

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 52.72  E-value: 6.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   5 TVGLIGNPNSGKTTLFNQLTGARQR-VGNWAGVTVERKEGIFATTDHQVTLVDLPGtyslTTISSQTSLDEQIAcHYILS 83
Cdd:COG1160    4 VVAIVGRPNVGKSTLFNRLTGRRDAiVDDTPGVTRDRIYGEAEWGGREFTLIDTGG----IEPDDDDGLEAEIR-EQAEL 78
                         90
                 ....*....|....
gi 489009949  84 G--DADMLINVVDA 95
Cdd:COG1160   79 AieEADVILFVVDG 92
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
3-95 2.08e-06

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 50.82  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   3 KLTVGLIGNPNSGKTTLFNQLTGARQR-VGNWAGVTVERKEGIFATTDHQVTLVDLPG-TYSLTTIS------SQTSLDE 74
Cdd:PRK00093   1 KPVVAIVGRPNVGKSTLFNRLTGKRDAiVADTPGVTRDRIYGEAEWLGREFILIDTGGiEPDDDGFEkqireqAELAIEE 80
                         90       100
                 ....*....|....*....|.
gi 489009949  75 qiachyilsgdADMLINVVDA 95
Cdd:PRK00093  81 -----------ADVILFVVDG 90
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
6-59 3.66e-06

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: 47.80  E-value: 3.66e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489009949   6 VGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGIFATTDH-QVTLVDLPG 59
Cdd:cd01898    3 VGLVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGrSFVIADIPG 57
era PRK00089
GTPase Era; Reviewed
6-160 4.01e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 49.28  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   6 VGLIGNPNSGKTTLFNQLTGA------------RQRVgnwagvtverkEGIFATTDHQVTLVDLPGTYslttiSSQTSLD 73
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALVGQkisivspkpqttRHRI-----------RGIVTEDDAQIIFVDTPGIH-----KPKRALN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  74 E---QIAchyiLS--GDADMLINVVDASN---------LERnlyltlqLLELGIPCVVALNMLD-IAEKQQVRIDIDALA 138
Cdd:PRK00089  72 RamnKAA----WSslKDVDLVLFVVDADEkigpgdefiLEK-------LKKVKTPVILVLNKIDlVKDKEELLPLLEELS 140
                        170       180
                 ....*....|....*....|...
gi 489009949 139 ARLG-CPVIPLVSTRGRGIEALK 160
Cdd:PRK00089 141 ELMDfAEIVPISALKGDNVDELL 163
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
6-159 4.13e-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: 47.37  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949    6 VGLIGNPNSGKTTLFNQLTGARQRVgnwagvtVERKEGI---FATTDHQV-------TLVDLPGTYSLTTISSQtSLDEQ 75
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSI-------TEYYPGTtrnYVTTVIEEdgktykfNLLDTAGQEDYDAIRRL-YYPQV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   76 IAchyiLSGDADMLINVVDASN-LERNLYLTLQLLELGIPCVVALNMLDI---AEKQQVRIDIDALAarlGCPVIPLVST 151
Cdd:TIGR00231  76 ER----SLRVFDIVILVLDVEEiLEKQTKEIIHHADSGVPIILVGNKIDLkdaDLKTHVASEFAKLN---GEPIIPLSAE 148

                  ....*...
gi 489009949  152 RGRGIEAL 159
Cdd:TIGR00231 149 TGKNIDSA 156
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
5-148 1.72e-05

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


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 47.20  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   5 TVGLIGNPNSGKTTLFNQL---TGARQRVGN-WAGVTV--------ERKEGIFATT------DHQVTLVDLPGtysltti 66
Cdd:cd04170    1 NIALVGHSGSGKTTLAEALlyaTGAIDRLGRvEDGNTVsdydpeekKRKMSIETSVaplewnGHKINLIDTPG------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  67 ssqtSLD---EQIAChyiLSGdADMLINVVDASN-----LERnlyLTLQLLELGIPCVVALNMLDiAEKQQVRIDIDALA 138
Cdd:cd04170   74 ----YADfvgETLSA---LRA-VDAALIVVEAQSgvevgTEK---VWEFLDDAKLPRIIFINKMD-RARADFDKTLAALR 141
                        170
                 ....*....|
gi 489009949 139 ARLGCPVIPL 148
Cdd:cd04170  142 EAFGRPVVPI 151
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
6-166 4.43e-05

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: 44.81  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   6 VGLIGNPNSGKTTLFNQLTGARQ--RVGNWAGVTverKEGIFATTDHQVTLVDLPGtYSLTTISSQTSLD-EQIACHYIL 82
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTNRKKlaRTSKTPGRT---QLINFFNVGDKFRLVDLPG-YGYAKVSKEVREKwGKLIEEYLE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  83 SGDA-DMLINVVDA------------SNLERNlyltlqllelGIPCVVALN---MLDIAEKQQVRIDI-DALAARLGCP- 144
Cdd:cd01876   78 NRENlKGVVLLIDArhgptpidlemlEFLEEL----------GIPFLIVLTkadKLKKSELAKVLKKIkEELNLFNILPp 147
                        170       180
                 ....*....|....*....|..
gi 489009949 145 VIPLVSTRGRGIEALKIALDRH 166
Cdd:cd01876  148 VILFSSKKGTGIDELRALIAEW 169
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
4-159 6.22e-05

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


Pssm-ID: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 44.35  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   4 LTVGLIGNPNSGKTTLFNQLTGA-RQRVGNWAGVT-------VERKegifattDHQVTLVDLPG----------TYSLTT 65
Cdd:cd01895    3 IKIAIIGRPNVGKSSLLNALLGEeRVIVSDIAGTTrdsidvpFEYD-------GQKYTLIDTAGirkkgkvtegIEKYSV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  66 ISSQTSLDeqiachyilsgDADMLINVVDASN--LERNLYLTLQLLELGIPCVVALNMLDIAEKQQVRID--IDALAARL 141
Cdd:cd01895   76 LRTLKAIE-----------RADVVLLVLDASEgiTEQDLRIAGLILEEGKALIIVVNKWDLVEKDEKTMKefEKELRRKL 144
                        170       180
                 ....*....|....*....|..
gi 489009949 142 ----GCPVIPLVSTRGRGIEAL 159
Cdd:cd01895  145 pfldYAPIVFISALTGQGVDKL 166
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
3-59 2.20e-04

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: 42.52  E-value: 2.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489009949   3 KLTVGLIGNPNSGKTTLFNQLTGAR-QRVGNWAGVTveRKEGIFaTTDHQVTLVDLPG 59
Cdd:cd01856  115 PLRAMVVGIPNVGKSTLINRLRGKKvAKVGNKPGVT--RGQQWI-RIGPNIELLDTPG 169
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
5-101 2.27e-04

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: 43.08  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   5 TVGLIGNPNSGKTTLFNQLTGarqrvGNWAGvTV---ERKEGIFATTDHQ---VTLVDLPGTYSLTTISSQTsldeqiac 78
Cdd:cd04105    2 TVLLLGPSDSGKTALFTKLTT-----GKVRS-TVtsiEPNVASFYSNSSKgkkLTLVDVPGHEKLRDKLLEY-------- 67
                         90       100
                 ....*....|....*....|...
gi 489009949  79 hyiLSGDADMLINVVDASNLERN 101
Cdd:cd04105   68 ---LKASLKAIVFVVDSATFQKN 87
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
6-160 2.53e-04

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 42.74  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   6 VGLIGNPNSGKTTLFNQLTG-----------ARQRVG-----NWAGVTVERKEGIFA-----TTDHQVTLVDLPGTYSLt 64
Cdd:cd01889    3 VGLLGHVDSGKTSLAKALSEiastaafdknpQSQERGitldlGFSSFEVDKPKHLEDnenpqIENYQITLVDCPGHASL- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  65 tissqtsldeqIAChyILSGDA--DMLINVVDASN------------LErnlyltlqllELGIPCVVALNMLDIAEKQQV 130
Cdd:cd01889   82 -----------IRT--IIGGAQiiDLMLLVVDAKKgiqtqtaeclviGE----------LLCKPLIVVLNKIDLIPEEER 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 489009949 131 RIDIDALAARL----------GCPVIPLVSTRGRGIEALK 160
Cdd:cd01889  139 KRKIEKMKKRLqktlektrlkDSPIIPVSAKPGEGEAELG 178
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
7-163 4.57e-04

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: 41.17  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   7 GLIGNPNSGKTTLFNQLTGAR-QRVGNWAGVTVERKEGIFATTDHQVTLVDLPG------TYSLTTISSQTSLDEqiach 79
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEvAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGvgergrRDREYEELYRRLLPE----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  80 yilsgdADMLINVVDA-----SNLERnlYLTLQLLELGIPCVVALNMLDiaekqqvrididalaarlgcPVIPLVSTRGR 154
Cdd:cd11383   76 ------ADLVLWLLDAddralAADHD--FYLLPLAGHDAPLLFVLNQVD--------------------PVLAVSARTGW 127

                 ....*....
gi 489009949 155 GIEALKIAL 163
Cdd:cd11383  128 GLDELAEAL 136
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
3-59 5.51e-04

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: 41.41  E-value: 5.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   3 KLTVGLIGNPNSGKTTLFNQLTgaRQR---VGNWAGVTVERKEGIFattDHQVTLVDLPG 59
Cdd:cd04178  116 SITVGVVGYPNVGKSSVINSLK--RSRacnVGATPGVTKSMQEVHL---DKHVKLLDSPG 170
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
4-166 6.83e-04

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: 41.36  E-value: 6.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949    4 LTVGLIGNPNSGKTTLFNQL---TGARQRVGNWAGVT--------VERKEGI--------FATTDHQVTLVDLPG----T 60
Cdd:pfam00009   4 RNIGIIGHVDHGKTTLTDRLlyyTGAISKRGEVKGEGeagldnlpEERERGItiksaavsFETKDYLINLIDTPGhvdfV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   61 YSLTTISSQtsldeqiachyilsgdADMLINVVDAS-----NLERNlylTLQLLELGIPCVVALN---MLDIAEKQQVRI 132
Cdd:pfam00009  84 KEVIRGLAQ----------------ADGAILVVDAVegvmpQTREH---LRLARQLGVPIIVFINkmdRVDGAELEEVVE 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 489009949  133 DI------DALAARLGCPVIPLVSTRGRGIEALKIALDRH 166
Cdd:pfam00009 145 EVsrelleKYGEDGEFVPVVPGSALKGEGVQTLLDALDEY 184
PRK09602 PRK09602
translation-associated GTPase; Reviewed
4-96 1.36e-03

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 41.72  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   4 LTVGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGI-FATTDHQ-----------------------VTLVDLPG 59
Cdd:PRK09602   2 ITIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVGVaYVRVECPckelgvkcnprngkcidgtrfipVELIDVAG 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489009949  60 tysLTTISSQ------TSLDEqiachyiLSgDADMLINVVDAS 96
Cdd:PRK09602  82 ---LVPGAHEgrglgnQFLDD-------LR-QADALIHVVDAS 113
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
5-164 1.39e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 42.09  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   5 TVGLIGNPNSGKTTLFNQLTGARQR-VGNWAGVTVER--KEGIFATTDhqVTLVDLPG-TYSLTTISSQTSLDEQIACHY 80
Cdd:PRK09518 277 VVAIVGRPNVGKSTLVNRILGRREAvVEDTPGVTRDRvsYDAEWAGTD--FKLVDTGGwEADVEGIDSAIASQAQIAVSL 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  81 ilsgdADMLINVVD------------ASNLERnlyltlqlleLGIPCVVALNMLDIAEKQQVRIDIDALAarLGCPViPL 148
Cdd:PRK09518 355 -----ADAVVFVVDgqvgltstderiVRMLRR----------AGKPVVLAVNKIDDQASEYDAAEFWKLG--LGEPY-PI 416
                        170
                 ....*....|....*..
gi 489009949 149 VSTRGRGI-EALKIALD 164
Cdd:PRK09518 417 SAMHGRGVgDLLDEALD 433
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
2-59 1.48e-03

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


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 39.68  E-value: 1.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489009949   2 QKLTVGLIGNPNSGKTTLFNQLTGAR-QRVGNWAGVTverKEGIFATTDHQVTLVDLPG 59
Cdd:cd01849   90 KGIRVGVVGLPNVGKSSFINALLNKFkLKVGSIPGTT---KLQQDVKLDKEIYLYDTPG 145
PRK13351 PRK13351
elongation factor G-like protein;
1-237 2.71e-03

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 41.09  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949   1 MQKLTVGLIGNPNSGKTTLFNQL---TGARQRVGNW-AGVTV------ERKEGI-----FATTD---HQVTLVDLPGTYS 62
Cdd:PRK13351   6 MQIRNIGILAHIDAGKTTLTERIlfyTGKIHKMGEVeDGTTVtdwmpqEQERGItiesaATSCDwdnHRINLIDTPGHID 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949  63 LT--TISSQTSLDEQIAchyILsgDADMLINVVDASNLErnlyltlQLLELGIPCVVALNMLDiAEKQQVRIDIDALAAR 140
Cdd:PRK13351  86 FTgeVERSLRVLDGAVV---VF--DAVTGVQPQTETVWR-------QADRYGIPRLIFINKMD-RVGADLFKVLEDIEER 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949 141 LGCPVIPLvstrgrgieALKIAldrhqANSDLELVhypqpllreADLLAQQMsaqiPTRQRRWLGLQMLEGDI--YSRAY 218
Cdd:PRK13351 153 FGKRPLPL---------QLPIG-----SEDGFEGV---------VDLITEPE----LHFSEGDGGSTVEEGPIpeELLEE 205
                        250
                 ....*....|....*....
gi 489009949 219 AGDAADKLDIALANLSDEI 237
Cdd:PRK13351 206 VEEAREKLIEALAEFDDEL 224
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
6-25 3.34e-03

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 40.02  E-value: 3.34e-03
                         10        20
                 ....*....|....*....|.
gi 489009949   6 VGLIGnPN-SGKTTLFNQLTG 25
Cdd:COG0411   33 VGLIG-PNgAGKTTLFNLITG 52
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
6-59 3.38e-03

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 40.93  E-value: 3.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489009949   6 VGLIGNPNSGKTTLFNQLTGA-RQRVGNWAGVTVERKEGIFATTDHQVTLVDLPG 59
Cdd:PRK09518 453 VALVGRPNVGKSSLLNQLTHEeRAVVNDLAGTTRDPVDEIVEIDGEDWLFIDTAG 507
obgE PRK12299
GTPase CgtA; Reviewed
6-32 5.72e-03

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 39.67  E-value: 5.72e-03
                         10        20
                 ....*....|....*....|....*..
gi 489009949   6 VGLIGNPNSGKTTLFNQLTGARQRVGN 32
Cdd:PRK12299 161 VGLVGLPNAGKSTLISAVSAAKPKIAD 187
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
5-101 7.38e-03

Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition particle receptor (SRP) is a transmembrane GTPase which anchors the alpha subunit to the endoplasmic reticulum membrane.


Pssm-ID: 462797 [Multi-domain]  Cd Length: 181  Bit Score: 38.19  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489009949    5 TVGLIGNPNSGKTTLFNQLTGARqrvgnwAGVTVERKEGIFA-----TTDHQVTLVDLPGTYSLTTISSQTSLDeqiach 79
Cdd:pfam09439   5 AVIIAGLCDSGKTSLFTLLTTDS------VRPTVTSQEPSAAyrymlNKGNSFTLIDFPGHVKLRYKLLETLKD------ 72
                          90       100
                  ....*....|....*....|..
gi 489009949   80 yilSGDADMLINVVDASNLERN 101
Cdd:pfam09439  73 ---SSSLKGIVFVVDSTIFPKE 91
 
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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