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Conserved domains on  [gi|1562733470|gb|RXI66396|]
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ferrous iron transport protein B [Clostridium tetani]

Protein Classification

ferrous iron transporter B( domain architecture ID 11417566)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-666 0e+00

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


:

Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 994.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   1 MSTFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTP 80
Cdd:COG0370     3 MITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTYSLSAYSPDEKVARDFLLEEKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  81 DVVINVVDATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLIKESMKF 160
Cdd:COG0370    83 DVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAIIEA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 161 IEEDSFKPISISYGKELDDKKEKLTNILKEEKfklPLPYNWISLKILEGDEYVLNIInKNNPSEILKKELNLLAEKKDDY 240
Cdd:COG0370   163 AEGKKPRPLRIDYPEEIEEAIEELEELLEEDG---PYPSRWLAIKLLEGDEEVLELL-SELLELLEEIREELEEELGEDL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 241 ELTIVDKRYELISKIVSQAVSRPNINNVTLSDKIDKWVTNKWLGIPIFAAIMYLIFQLTFTIGQdMLGELAAGAIEFLGE 320
Cdd:COG0370   239 ESIIADARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTVGA-PLMDLIDGGFGWLGD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 321 STTDFLVglnsPEWLVSFVGDGIFGGVGAVVEFLPLIMVLYLLMGILEDTGYMARAAYVMDRVMRSLGLHGKTFVSMIVG 400
Cdd:COG0370   318 WVAALLP----PGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 401 FGCNVPGIMAARTLENKKDRMIAILINPFMSCGARIPIYLVFIAAFFPNNGVLVIFLLYVLGIITALIIGKIFSKTLFKG 480
Cdd:COG0370   394 FGCNVPAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKG 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 481 ESSYFIMELPPYRLPTLKGVLLNMWDKVGAFLKRAGTIIFSVVTILWVLGVLPYGVE-PNSEASILGQIGSFIAPLFKPA 559
Cdd:COG0370   474 EPSPFVMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGEsEDLENSYLGRIGKALEPVFAPL 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 560 GFgTWQASVGLFTGIVAKEAVVATLGMVYA---GVEEGTKLITAIQGTFTPLSAVSFMVMTLFYTPCAAVIATIKKETNS 636
Cdd:COG0370   554 GF-DWQIGVALITGFAAKEVVVGTLGTLYGvgeDAEESASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGS 632
                         650       660       670
                  ....*....|....*....|....*....|
gi 1562733470 637 TKWTLFAVGYTFVLGWLAAVLIYQIGSLLG 666
Cdd:COG0370   633 WKWTLFAVGYMTVLAYLVAFLVYQIGRLLG 662
 
Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-666 0e+00

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 994.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   1 MSTFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTP 80
Cdd:COG0370     3 MITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTYSLSAYSPDEKVARDFLLEEKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  81 DVVINVVDATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLIKESMKF 160
Cdd:COG0370    83 DVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAIIEA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 161 IEEDSFKPISISYGKELDDKKEKLTNILKEEKfklPLPYNWISLKILEGDEYVLNIInKNNPSEILKKELNLLAEKKDDY 240
Cdd:COG0370   163 AEGKKPRPLRIDYPEEIEEAIEELEELLEEDG---PYPSRWLAIKLLEGDEEVLELL-SELLELLEEIREELEEELGEDL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 241 ELTIVDKRYELISKIVSQAVSRPNINNVTLSDKIDKWVTNKWLGIPIFAAIMYLIFQLTFTIGQdMLGELAAGAIEFLGE 320
Cdd:COG0370   239 ESIIADARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTVGA-PLMDLIDGGFGWLGD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 321 STTDFLVglnsPEWLVSFVGDGIFGGVGAVVEFLPLIMVLYLLMGILEDTGYMARAAYVMDRVMRSLGLHGKTFVSMIVG 400
Cdd:COG0370   318 WVAALLP----PGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 401 FGCNVPGIMAARTLENKKDRMIAILINPFMSCGARIPIYLVFIAAFFPNNGVLVIFLLYVLGIITALIIGKIFSKTLFKG 480
Cdd:COG0370   394 FGCNVPAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKG 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 481 ESSYFIMELPPYRLPTLKGVLLNMWDKVGAFLKRAGTIIFSVVTILWVLGVLPYGVE-PNSEASILGQIGSFIAPLFKPA 559
Cdd:COG0370   474 EPSPFVMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGEsEDLENSYLGRIGKALEPVFAPL 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 560 GFgTWQASVGLFTGIVAKEAVVATLGMVYA---GVEEGTKLITAIQGTFTPLSAVSFMVMTLFYTPCAAVIATIKKETNS 636
Cdd:COG0370   554 GF-DWQIGVALITGFAAKEVVVGTLGTLYGvgeDAEESASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGS 632
                         650       660       670
                  ....*....|....*....|....*....|
gi 1562733470 637 TKWTLFAVGYTFVLGWLAAVLIYQIGSLLG 666
Cdd:COG0370   633 WKWTLFAVGYMTVLAYLVAFLVYQIGRLLG 662
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
8-633 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: 593.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   8 GNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTPDVVINVV 87
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGIYSLTTFSLEEEVARDYLLNEKPDLVVNVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  88 DATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLIKESMKFIEedsfk 167
Cdd:TIGR00437  81 DASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGRGIERLKDAIRKAIG----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 168 pisisYGKELDDKKEKLTNILKEEKFKLPLpyNWISLKILEGDEYVLNIINKNNPSEILKKElnllaekKDDYELTIVDK 247
Cdd:TIGR00437 156 -----LKELKKRAIEIVPEAYQVVEVVEGL--IEIIYSISKRGLEILLGLLEDLSLEIEKIE-------RNLAEVVIKES 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 248 RYELISKIVSqavsrpNINNVTLSDKIDKWVTNKWLGIPIFAAIMYLIFQLTFTIGQDmLGELAAGAIEFLGESTTDFLv 327
Cdd:TIGR00437 222 PSNLSPTEIA------DEDRVLVEKSIGRKILDRFLGLPIFLFVMFILFLLTFLVGQP-LVDLIETGFSFLSEAVKSFI- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 328 glnSPEWLVSFVGDGIFGGVGAVVEFLPLIMVLYLLMGILEDTGYMARAAYVMDRVMRSLGLHGKTFVSMIVGFGCNVPG 407
Cdd:TIGR00437 294 ---GNYWLASLLGDGLIGGVGAVLSFVPLIAILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPA 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 408 IMAARTLENKKDRMIAILINPFMSCGARIPIYLVFIAAFFP-NNGVLVIFLLYVLGIITALIIGKIFSKTLFKGESSYFI 486
Cdd:TIGR00437 371 IMATRTLETRRERLLTALVIPFMSCSARLPVIVLLFAAAFPgKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFI 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 487 MELPPYRLPTLKGVLLNMWDKVGAFLKRAGTIIFSVVTILWVLGVLPYGvepNSEASILGQIGSFIAPLFKPAGFGT-WQ 565
Cdd:TIGR00437 451 MELPPYRLPRFRVVFIQTWTRLRSFIKKAGTIIVIGSVLIWFLSSFPGG---KILESWLAAIGSIMAPLFVPLGKILdWF 527
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1562733470 566 ASVGLFTGIVAKEAVVATLGMVYAGVEEGtkliTAIQGTFTPLSAVSFMVMTLFYTPCAAVIATIKKE 633
Cdd:TIGR00437 528 ASVALIFGFVAKEVVVATLGVLYGLGNIL----SSIGHAMVPVEALSYMLFVLLYVPCLATLAAIARE 591
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
3-663 0e+00

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 584.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSE----DELVARNYILGD 78
Cdd:PRK09554    5 TIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSqtslDEQIACHYILSG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  79 TPDVVINVVDATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLiKESM 158
Cdd:PRK09554   85 DADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEAL-KLAI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 159 KFIEEDSFKPIsISYGKELDDKKEKLTNILKEEkfkLPLPYN-WISLKILEGDEYVLNIinKNNPSEILKKELNLLAEKK 237
Cdd:PRK09554  164 DRHQANENVEL-VHYPQPLLNEADSLAKVMPSD---IPLQQRrWLGLQMLEGDIYSRAY--AGEASQHLDAALARLRNEM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 238 DDYELTIVDKRYELISKIvSQAVSR-----PNinnvTLSDKIDKWVTNKWLGIPIFAAIMYLIFQLTFTIGqdmlgelaa 312
Cdd:PRK09554  238 DDPALHIADARYQCIAAI-CDAVSNtltaePS----RLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIG--------- 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 313 GAIE--FLGESTTDFLVG-------LNSPEWLVSFVGDGIFGGVGAVVEFLPLIMVLYLLMGILEDTGYMARAAYVMDRV 383
Cdd:PRK09554  304 GALQplFDVGSVAIFIHGiqwlgytLHFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 384 MRSLGLHGKTFVSMIVGFGCNVPGIMAARTLENKKDRMIAILINPFMSCGARIPIYLVFIAAFFPNNGVLVIFLLYVLGI 463
Cdd:PRK09554  384 MQALGLPGKSFVPLIVGFGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLGI 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 464 ITALIIGKIFSKTLFKGESSYFIMELPPYRLPTLKGVLLNMWDKVGAFLKRAGTIIFSVVTILWVLGVLPYGVEP--NSE 541
Cdd:PRK09554  464 VMAILTGLMLKYTIMRGEASPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIvdNIN 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 542 ASILGQIGSFIAPLFKPAGF--GTWQASVGLFTGIVAKEAVVATLGMVY------------AGVEEGTKLITAI------ 601
Cdd:PRK09554  544 DSALASVSRVITPVLKPIGVheDNWQATVGLFTGAMAKEVVVGTLNTLYtaeniqdeefnpAEFNLGDELFGAVdetwqs 623
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 602 -QGTFT-------------------------------PLSAVSFMVMTLFYTPCAAVIATIKKETnSTKWTLFAVGYTFV 649
Cdd:PRK09554  624 lKDTFSlsvlanpieaskgdgemgtgamgvmsqkfgsAAAAYSYLIFVLLYVPCISVMGAIARES-SRGWMGFSILWGLN 702
                         730
                  ....*....|....
gi 1562733470 650 LGWLAAVLIYQIGS 663
Cdd:PRK09554  703 IAYSLATLFYQVAS 716
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
3-156 3.58e-99

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: 300.52  E-value: 3.58e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTPDV 82
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGIYSLSPYSEEERVARDYLLNEKPDV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562733470  83 VINVVDATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLIKE 156
Cdd:pfam02421  82 IVNVVDATNLERNLYLTLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSARKGEGIDELLDA 155
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
5-153 1.08e-96

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: 293.98  E-value: 1.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTPDVVI 84
Cdd:cd01879     1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTYSLTPYSEDEKVARDFLLGEEPDLIV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562733470  85 NVVDATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDL 153
Cdd:cd01879    81 NVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDEL 149
 
Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-666 0e+00

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 994.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   1 MSTFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTP 80
Cdd:COG0370     3 MITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKGKEIELVDLPGTYSLSAYSPDEKVARDFLLEEKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  81 DVVINVVDATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLIKESMKF 160
Cdd:COG0370    83 DVVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGKGIDELKEAIIEA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 161 IEEDSFKPISISYGKELDDKKEKLTNILKEEKfklPLPYNWISLKILEGDEYVLNIInKNNPSEILKKELNLLAEKKDDY 240
Cdd:COG0370   163 AEGKKPRPLRIDYPEEIEEAIEELEELLEEDG---PYPSRWLAIKLLEGDEEVLELL-SELLELLEEIREELEEELGEDL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 241 ELTIVDKRYELISKIVSQAVSRPNINNVTLSDKIDKWVTNKWLGIPIFAAIMYLIFQLTFTIGQdMLGELAAGAIEFLGE 320
Cdd:COG0370   239 ESIIADARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTVGA-PLMDLIDGGFGWLGD 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 321 STTDFLVglnsPEWLVSFVGDGIFGGVGAVVEFLPLIMVLYLLMGILEDTGYMARAAYVMDRVMRSLGLHGKTFVSMIVG 400
Cdd:COG0370   318 WVAALLP----PGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSG 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 401 FGCNVPGIMAARTLENKKDRMIAILINPFMSCGARIPIYLVFIAAFFPNNGVLVIFLLYVLGIITALIIGKIFSKTLFKG 480
Cdd:COG0370   394 FGCNVPAIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKG 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 481 ESSYFIMELPPYRLPTLKGVLLNMWDKVGAFLKRAGTIIFSVVTILWVLGVLPYGVE-PNSEASILGQIGSFIAPLFKPA 559
Cdd:COG0370   474 EPSPFVMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGEsEDLENSYLGRIGKALEPVFAPL 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 560 GFgTWQASVGLFTGIVAKEAVVATLGMVYA---GVEEGTKLITAIQGTFTPLSAVSFMVMTLFYTPCAAVIATIKKETNS 636
Cdd:COG0370   554 GF-DWQIGVALITGFAAKEVVVGTLGTLYGvgeDAEESASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGS 632
                         650       660       670
                  ....*....|....*....|....*....|
gi 1562733470 637 TKWTLFAVGYTFVLGWLAAVLIYQIGSLLG 666
Cdd:COG0370   633 WKWTLFAVGYMTVLAYLVAFLVYQIGRLLG 662
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
8-633 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: 593.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   8 GNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTPDVVINVV 87
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGFQGEDIEIVDLPGIYSLTTFSLEEEVARDYLLNEKPDLVVNVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  88 DATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLIKESMKFIEedsfk 167
Cdd:TIGR00437  81 DASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGRGIERLKDAIRKAIG----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 168 pisisYGKELDDKKEKLTNILKEEKFKLPLpyNWISLKILEGDEYVLNIINKNNPSEILKKElnllaekKDDYELTIVDK 247
Cdd:TIGR00437 156 -----LKELKKRAIEIVPEAYQVVEVVEGL--IEIIYSISKRGLEILLGLLEDLSLEIEKIE-------RNLAEVVIKES 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 248 RYELISKIVSqavsrpNINNVTLSDKIDKWVTNKWLGIPIFAAIMYLIFQLTFTIGQDmLGELAAGAIEFLGESTTDFLv 327
Cdd:TIGR00437 222 PSNLSPTEIA------DEDRVLVEKSIGRKILDRFLGLPIFLFVMFILFLLTFLVGQP-LVDLIETGFSFLSEAVKSFI- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 328 glnSPEWLVSFVGDGIFGGVGAVVEFLPLIMVLYLLMGILEDTGYMARAAYVMDRVMRSLGLHGKTFVSMIVGFGCNVPG 407
Cdd:TIGR00437 294 ---GNYWLASLLGDGLIGGVGAVLSFVPLIAILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPA 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 408 IMAARTLENKKDRMIAILINPFMSCGARIPIYLVFIAAFFP-NNGVLVIFLLYVLGIITALIIGKIFSKTLFKGESSYFI 486
Cdd:TIGR00437 371 IMATRTLETRRERLLTALVIPFMSCSARLPVIVLLFAAAFPgKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFI 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 487 MELPPYRLPTLKGVLLNMWDKVGAFLKRAGTIIFSVVTILWVLGVLPYGvepNSEASILGQIGSFIAPLFKPAGFGT-WQ 565
Cdd:TIGR00437 451 MELPPYRLPRFRVVFIQTWTRLRSFIKKAGTIIVIGSVLIWFLSSFPGG---KILESWLAAIGSIMAPLFVPLGKILdWF 527
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1562733470 566 ASVGLFTGIVAKEAVVATLGMVYAGVEEGtkliTAIQGTFTPLSAVSFMVMTLFYTPCAAVIATIKKE 633
Cdd:TIGR00437 528 ASVALIFGFVAKEVVVATLGVLYGLGNIL----SSIGHAMVPVEALSYMLFVLLYVPCLATLAAIARE 591
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
3-663 0e+00

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 584.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSE----DELVARNYILGD 78
Cdd:PRK09554    5 TIGLIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSTTDHQVTLVDLPGTYSLTTISSqtslDEQIACHYILSG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  79 TPDVVINVVDATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLiKESM 158
Cdd:PRK09554   85 DADLLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEAL-KLAI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 159 KFIEEDSFKPIsISYGKELDDKKEKLTNILKEEkfkLPLPYN-WISLKILEGDEYVLNIinKNNPSEILKKELNLLAEKK 237
Cdd:PRK09554  164 DRHQANENVEL-VHYPQPLLNEADSLAKVMPSD---IPLQQRrWLGLQMLEGDIYSRAY--AGEASQHLDAALARLRNEM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 238 DDYELTIVDKRYELISKIvSQAVSR-----PNinnvTLSDKIDKWVTNKWLGIPIFAAIMYLIFQLTFTIGqdmlgelaa 312
Cdd:PRK09554  238 DDPALHIADARYQCIAAI-CDAVSNtltaePS----RLTTALDKIILNRWLGLPIFLFVMYLMFLLAINIG--------- 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 313 GAIE--FLGESTTDFLVG-------LNSPEWLVSFVGDGIFGGVGAVVEFLPLIMVLYLLMGILEDTGYMARAAYVMDRV 383
Cdd:PRK09554  304 GALQplFDVGSVAIFIHGiqwlgytLHFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRL 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 384 MRSLGLHGKTFVSMIVGFGCNVPGIMAARTLENKKDRMIAILINPFMSCGARIPIYLVFIAAFFPNNGVLVIFLLYVLGI 463
Cdd:PRK09554  384 MQALGLPGKSFVPLIVGFGCNVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLGI 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 464 ITALIIGKIFSKTLFKGESSYFIMELPPYRLPTLKGVLLNMWDKVGAFLKRAGTIIFSVVTILWVLGVLPYGVEP--NSE 541
Cdd:PRK09554  464 VMAILTGLMLKYTIMRGEASPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIvdNIN 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 542 ASILGQIGSFIAPLFKPAGF--GTWQASVGLFTGIVAKEAVVATLGMVY------------AGVEEGTKLITAI------ 601
Cdd:PRK09554  544 DSALASVSRVITPVLKPIGVheDNWQATVGLFTGAMAKEVVVGTLNTLYtaeniqdeefnpAEFNLGDELFGAVdetwqs 623
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 602 -QGTFT-------------------------------PLSAVSFMVMTLFYTPCAAVIATIKKETnSTKWTLFAVGYTFV 649
Cdd:PRK09554  624 lKDTFSlsvlanpieaskgdgemgtgamgvmsqkfgsAAAAYSYLIFVLLYVPCISVMGAIARES-SRGWMGFSILWGLN 702
                         730
                  ....*....|....
gi 1562733470 650 LGWLAAVLIYQIGS 663
Cdd:PRK09554  703 IAYSLATLFYQVAS 716
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
3-156 3.58e-99

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: 300.52  E-value: 3.58e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTPDV 82
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKYKGYEIEIVDLPGIYSLSPYSEEERVARDYLLNEKPDV 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1562733470  83 VINVVDATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLIKE 156
Cdd:pfam02421  82 IVNVVDATNLERNLYLTLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSARKGEGIDELLDA 155
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
5-153 1.08e-96

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: 293.98  E-value: 1.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTPDVVI 84
Cdd:cd01879     1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKLGGKEIEIVDLPGTYSLTPYSEDEKVARDFLLGEEPDLIV 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1562733470  85 NVVDATNIERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDL 153
Cdd:cd01879    81 NVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDEL 149
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
3-115 1.78e-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: 95.76  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAaySEDELVARNYILGDTPDV 82
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGA--SEGEGLGRAFLAIIEADL 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1562733470  83 VINVVDATN--IERNLYLTSQLMEMGAKVVVALNM 115
Cdd:pfam01926  79 ILFVVDSEEgiTPLDEELLELLRENKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
5-156 2.69e-22

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: 93.85  E-value: 2.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGTNQ-HVGNWPGVTVEKKEGTFKFKDK-SFKVIDLPGTYSfAAYSEDELVARNYILGDTPDV 82
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVgIVSPIPGTTRDPVRKEWELLPLgPVVLIDTPGLDE-EGGLGRERVEEARQVADRADL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562733470  83 VINVVDATNIERNLYLTSQLM-EMGAKVVVALNMMD--EATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLIKE 156
Cdd:cd00880    80 VLLVVDSDLTPVEEEAKLGLLrERGKPVLLVLNKIDlvPESEEEELLRERKLELLPDLPVIAVSALPGEGIDELRKK 156
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
5-156 1.46e-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: 80.19  E-value: 1.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGTNQ-HVGNWPGVTVEKKEGTFKFKDKSFKV--IDLPGTYSFaAYSEDELVARNYIlgDTPD 81
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVgEVSDVPGTTRDPDVYVKELDKGKVKLvlVDTPGLDEF-GGLGREELARLLL--RGAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  82 VVINVVDATN----IERNLYLTSQLMEMGAKVVVALNMMD--EATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLIK 155
Cdd:cd00882    78 LILLVVDSTDreseEDAKLLILRRLRKEGIPIILVGNKIDllEEREVEELLRLEELAKILGVPVFEVSAKTGEGVDELFE 157

                  .
gi 1562733470 156 E 156
Cdd:cd00882   158 K 158
FeoB_C pfam07664
Ferrous iron transport protein B C terminus; Escherichia coli has an iron(II) transport system ...
455-504 3.54e-17

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: 75.52  E-value: 3.54e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1562733470 455 IFLLYVLGIITALIIGKIFSK-TLFKGESSYFIMELPPYRLPTLKGVLLNM 504
Cdd:pfam07664   1 LFSLYLLGILVALLVALLLKKtTLLKGEPSPFVMELPPYRLPTLKNVLRKT 51
FeoB_Cyto pfam17910
FeoB cytosolic helical domain; FeoB is a G-protein coupled membrane protein essential for Fe ...
173-261 5.26e-16

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: 73.43  E-value: 5.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 173 YGKELDDKKEKLTNILKEEKfKLPLPYNWISLKILEGDEYVLNIINKNNP-SEILKKELNLLAEK-KDDYELTIVDKRYE 250
Cdd:pfam17910   1 YGEEIEEAISEIEPLLEEDL-EDKYPPRWLAIKLLEGDEEVLEKLKLSEElLEELEEIREELEKElGEDLESIIADARYG 79
                          90
                  ....*....|.
gi 1562733470 251 LISKIVSQAVS 261
Cdd:pfam17910  80 FIEGILKEVVK 90
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
350-443 1.23e-15

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


Pssm-ID: 429586 [Multi-domain]  Cd Length: 101  Bit Score: 72.67  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 350 VVEFLPLIMVLYLLMGILEDTGYMARAAYVMDRVMRSLG---LHGKTFVSMIVGFGCN---VPGIMAARTLENKKDRMIA 423
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYSGLLDRIGKLLGPLMRPLGlfpLPGKAAIALLLGFGAKevgVPLLATPYGIDTPRERLAA 80
                          90       100
                  ....*....|....*....|.
gi 1562733470 424 ILINPFMS-CGARIPIYLVFI 443
Cdd:pfam07670  81 LLFTSFSTpCGATLPVYAGEL 101
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
5-161 3.08e-14

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


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 70.54  E-value: 3.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGTNQH-VGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTPDVV 83
Cdd:cd01894     1 AIVGRPNVGKSTLFNRLTGRRDAiVSDTPGVTRDRKYGEAEWGGREFILIDTGGIEPDDEGISKEIREQAEIAIEEADVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  84 INVVDATNI--ERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSkeLGVPvIPIVAKRKTGISDLIKESMKFI 161
Cdd:cd01894    81 LFVVDGREGltPADEEIAKYLRKSKKPVILVVNKIDNIKEEEEAAEFYSLG--FGEP-IPISAEHGRGIGDLLDAILELL 157
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
5-156 1.69e-13

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: 68.96  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKD-KSFKVIDLPGTYSFAaySEDElVARNYILGD--TPD 81
Cdd:cd01881     1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEFGDgVDIQIIDLPGLLDGA--SEGR-GLGEQILAHlyRSD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  82 VVINVVDATNIERNLYLTSQ-----------LMEMGAKVVVALNMMDEATSQNIKIDTnKLSKELGVPVIPIVAKRKTGI 150
Cdd:cd01881    78 LILHVIDASEDCVGDPLEDQktlneevsgsfLFLKNKPEMIVANKIDMASENNLKRLK-LDKLKRGIPVVPTSALTRLGL 156

                  ....*.
gi 1562733470 151 SDLIKE 156
Cdd:cd01881   157 DRVIRT 162
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
4-159 8.25e-13

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: 67.07  E-value: 8.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   4 FALVGNPNSGKTTLFNALTGTNQH-VGNWPGVTVEKKEGTFKFKDKSFKVIDLPG-------TYSFAAYSedelVARNYI 75
Cdd:cd01895     5 IAIIGRPNVGKSSLLNALLGEERViVSDIAGTTRDSIDVPFEYDGQKYTLIDTAGirkkgkvTEGIEKYS----VLRTLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  76 LGDTPDVVINVVDATNI--ERNLYLTSQLMEMGAKVVVALNMMD-----EATSQNIKIDTN-KLSKELGVPVIPIVAKRK 147
Cdd:cd01895    81 AIERADVVLLVLDASEGitEQDLRIAGLILEEGKALIIVVNKWDlvekdEKTMKEFEKELRrKLPFLDYAPIVFISALTG 160
                         170
                  ....*....|..
gi 1562733470 148 TGISDLIKESMK 159
Cdd:cd01895   161 QGVDKLFDAIKE 172
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
1-165 1.36e-12

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 70.05  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   1 MS-TFALVGNPNSGKTTLFNALTGTNQH-VGNWPGVTVEKKEGTFKFKDKSFKVIDLPGtysFAAYSEDELVARnyILG- 77
Cdd:COG1160     1 MSpVVAIVGRPNVGKSTLFNRLTGRRDAiVDDTPGVTRDRIYGEAEWGGREFTLIDTGG---IEPDDDDGLEAE--IREq 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  78 -----DTPDVVINVVDATNiernlYLTSQ-------LMEMGAKVVVALNmmdeatsqniKIDTNKLSK------ELGV-P 138
Cdd:COG1160    76 aelaiEEADVILFVVDGRA-----GLTPLdeeiaklLRRSGKPVILVVN----------KVDGPKREAdaaefySLGLgE 140
                         170       180
                  ....*....|....*....|....*..
gi 1562733470 139 VIPIVAKRKTGISDLIKESMKFIEEDS 165
Cdd:COG1160   141 PIPISAEHGRGVGDLLDAVLELLPEEE 167
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
512-634 5.29e-12

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: 62.66  E-value: 5.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470 512 LKRAGTIIFSVVTILWVLgvlpygvepnSEASILGQIGSFIAPLFKPAGFG--TWQASVGLFTGIVAKEAVVATLGMVYa 589
Cdd:pfam07670   1 LLKVLPIILFFSVLISIL----------EYSGLLDRIGKLLGPLMRPLGLFplPGKAAIALLLGFGAKEVGVPLLATPY- 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1562733470 590 gveegtklitaiqGTFTPLSAVSFMVMTLFYTPCAAVIATIKKET 634
Cdd:pfam07670  70 -------------GIDTPRERLAALLFTSFSTPCGATLPVYAGEL 101
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
1-171 1.69e-10

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 63.53  E-value: 1.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   1 MSTFALVGNPNSGKTTLFNALTGTNQH-VGNWPGVTVEKKEGTFKFKDKSFKVIDLPGtYSFaaySEDELVARnyILG-- 77
Cdd:PRK00093    1 KPVVAIVGRPNVGKSTLFNRLTGKRDAiVADTPGVTRDRIYGEAEWLGREFILIDTGG-IEP---DDDGFEKQ--IREqa 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  78 ----DTPDVVINVVDATNIernlyLTSQ---LMEM----GAKVVVALNmmdeatsqniKIDTNKLSK------ELGVP-V 139
Cdd:PRK00093   75 elaiEEADVILFVVDGRAG-----LTPAdeeIAKIlrksNKPVILVVN----------KVDGPDEEAdayefySLGLGeP 139
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1562733470 140 IPIVAKRKTGISDL---IKESMKFIEEDSFKPISI 171
Cdd:PRK00093  140 YPISAEHGRGIGDLldaILEELPEEEEEDEEDEPI 174
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
6-161 2.39e-10

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: 59.75  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   6 LVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKD-KSFKVIDLPGtysfaaysedeLV---ARNYILGD--- 78
Cdd:cd01898     5 LVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDgRSFVIADIPG-----------LIegaSEGKGLGHrfl 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  79 -----TpDVVINVVDATN----------IERNLYLTSQLMEmGAKVVVALNMMDEATSQNIKIDTNKLSKEL-GVPVIPI 142
Cdd:cd01898    74 rhierT-RVLLHVIDLSGeddpvedyetIRNELEAYNPGLA-EKPRIVVLNKIDLLDAEERFEKLKELLKELkGKKVFPI 151
                         170
                  ....*....|....*....
gi 1562733470 143 VAKRKTGISDLIKESMKFI 161
Cdd:cd01898   152 SALTGEGLDELLKKLAKLL 170
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
5-156 2.07e-09

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 57.30  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGtnQHVGNWP-----GVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSedELVARNYilgDT 79
Cdd:COG1100     7 VVVGTGGVGKTSLVNRLVG--DIFSLEKylstnGVTIDKKELKLDGLDVDLVIWDTPGQDEFRETR--QFYARQL---TG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  80 PDVVINVVDATNIERN---LYLTSQLMEMG--AKVVVALNMMDEATSQNIKID---TNKLSKELGVPVIPIVAKRKTGIS 151
Cdd:COG1100    80 ASLYLFVVDGTREETLqslYELLESLRRLGkkSPIILVLNKIDLYDEEEIEDEerlKEALSEDNIVEVVATSAKTGEGVE 159

                  ....*
gi 1562733470 152 DLIKE 156
Cdd:COG1100   160 ELFAA 164
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
4-159 3.27e-09

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 59.68  E-value: 3.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   4 FALVGNPNSGKTTLFNALTGTNQH-VGNWPGVTVEKKEGTFKFKDKSFKVIDLPG-------TYSFAAYSedelVAR--N 73
Cdd:PRK00093  176 IAIIGRPNVGKSSLINALLGEERViVSDIAGTTRDSIDTPFERDGQKYTLIDTAGirrkgkvTEGVEKYS----VIRtlK 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  74 YIlgDTPDVVINVVDATN--IERNLYLTSQLMEMGAKVVVALN---MMDEATSQNIKidtNKLSKEL----GVPVIPIVA 144
Cdd:PRK00093  252 AI--ERADVVLLVIDATEgiTEQDLRIAGLALEAGRALVIVVNkwdLVDEKTMEEFK---KELRRRLpfldYAPIVFISA 326
                         170
                  ....*....|....*
gi 1562733470 145 KRKTGISDLIKESMK 159
Cdd:PRK00093  327 LTGQGVDKLLEAIDE 341
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
2-93 3.51e-09

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: 57.56  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   2 STFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDE-----LVARnyil 76
Cdd:cd01896     1 ARVALVGFPSVGKSTLLSKLTNTKSEVAAYEFTTLTCVPGVMEYKGAKIQLLDLPGIIEGASDGKGRgrqviAVAR---- 76
                          90
                  ....*....|....*..
gi 1562733470  77 gdTPDVVINVVDATNIE 93
Cdd:cd01896    77 --TADLILIVLDATKPE 91
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
2-136 9.16e-09

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: 55.79  E-value: 9.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   2 STFALVGNPNSGKTTLFNALTGtnqhvGNWPGvTV---EKKEGTFKF---KDKSFKVIDLPGTYSFAAYSEDElvarnyi 75
Cdd:cd04105     1 PTVLLLGPSDSGKTALFTKLTT-----GKVRS-TVtsiEPNVASFYSnssKGKKLTLVDVPGHEKLRDKLLEY------- 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1562733470  76 LGDTPDVVINVVDATNIERNL-----YLTSQLMEM-----GAKVVVALNMMDEATSQNIKIDTNKLSKELG 136
Cdd:cd04105    68 LKASLKAIVFVVDSATFQKNIrdvaeFLYDILTDLekiknKIPILIACNKQDLFTAKPAKKIKELLEKEIN 138
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
5-156 1.09e-08

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 54.69  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGTNQHVGN-WPGVTVEKKEGTFKFKDKSFKV--IDLPGTYSFAAYSEDELVARNYILGDTpD 81
Cdd:TIGR00231   5 VIVGHPNVGKSTLLNSLLGNKGSITEyYPGTTRNYVTTVIEEDGKTYKFnlLDTAGQEDYDAIRRLYYPQVERSLRVF-D 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562733470  82 VVINVVDATNI-ERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSKELGVPVIPIVAKRKTGISDLIKE 156
Cdd:TIGR00231  84 IVILVLDVEEIlEKQTKEIIHHADSGVPIILVGNKIDLKDADLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKI 159
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
4-156 2.44e-08

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: 54.05  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   4 FALVGNPNSGKTTLFNALTGTNQH--VGNWPGVTveKKEGTFKFKDKsFKVIDLPGtYSFAAYSEDELVA-----RNYIL 76
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTNRKKLarTSKTPGRT--QLINFFNVGDK-FRLVDLPG-YGYAKVSKEVREKwgkliEEYLE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  77 G-DTPDVVINVVDATN--IERNLYLTSQLMEMGAKVVVALNMMD-----EATSQNIKIDTNKLSKELGVPVIPIVAKRKT 148
Cdd:cd01876    78 NrENLKGVVLLIDARHgpTPIDLEMLEFLEELGIPFLIVLTKADklkksELAKVLKKIKEELNLFNILPPVILFSSKKGT 157

                  ....*...
gi 1562733470 149 GISDLIKE 156
Cdd:cd01876   158 GIDELRAL 165
PRK04213 PRK04213
GTP-binding protein EngB;
1-146 2.74e-08

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 54.54  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   1 MSTFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEgtfkFKDKSFKVIDLPGtYSFAAYSEDELVAR------NY 74
Cdd:PRK04213    9 KPEIVFVGRSNVGKSTLVRELTGKKVRVGKRPGVTRKPNH----YDWGDFILTDLPG-FGFMSGVPKEVQEKikdeivRY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  75 IL--GDTPDVVINVVDATN----IER---------NLYLTSQLMEMGAKVVVALNMMDeatsqniKIDT-----NKLSKE 134
Cdd:PRK04213   84 IEdnADRILAAVLVVDGKSfieiIERwegrgeipiDVEMFDFLRELGIPPIVAVNKMD-------KIKNrdevlDEIAER 156
                         170       180
                  ....*....|....*....|.
gi 1562733470 135 LGVP---------VIPIVAKR 146
Cdd:PRK04213  157 LGLYppwrqwqdiIAPISAKK 177
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
3-159 4.50e-08

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 56.34  E-value: 4.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTGTNQH-VGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAYSEDELVARNYILGDTPD 81
Cdd:PRK09518  277 VVAIVGRPNVGKSTLVNRILGRREAvVEDTPGVTRDRVSYDAEWAGTDFKLVDTGGWEADVEGIDSAIASQAQIAVSLAD 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  82 VVINVVDA-----TNIERnlyLTSQLMEMGAKVVVALNMMDEATSQNIKIDTNKLSkeLGVPViPIVAKRKTGISDLIKE 156
Cdd:PRK09518  357 AVVFVVDGqvgltSTDER---IVRMLRRAGKPVVLAVNKIDDQASEYDAAEFWKLG--LGEPY-PISAMHGRGVGDLLDE 430

                  ...
gi 1562733470 157 SMK 159
Cdd:PRK09518  431 ALD 433
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
4-190 1.09e-07

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 54.64  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   4 FALVGNPNSGKTTLFNALTGTNQH-VGNWPGVTVEKKEGTFKFKDKSFKVIDLPG-------TYSFAAYSedelVARNY- 74
Cdd:COG1160   178 IAIVGRPNVGKSSLINALLGEERViVSDIAGTTRDSIDTPFERDGKKYTLIDTAGirrkgkvDEGIEKYS----VLRTLr 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  75 -IlgDTPDVVINVVDATN--IERNLYLTSQLMEMGAKVVVALNMMDEATSQNIKID--TNKLSKEL----GVPVIPIVAK 145
Cdd:COG1160   254 aI--ERADVVLLVIDATEgiTEQDLKIAGLALEAGKALVIVVNKWDLVEKDRKTREelEKEIRRRLpfldYAPIVFISAL 331
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1562733470 146 RKTGISDLIkESMKFIEEDSFKPISISygkelddkkeKLTNILKE 190
Cdd:COG1160   332 TGQGVDKLL-EAVDEVYESANKRISTS----------KLNRVLEE 365
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
3-159 2.00e-07

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: 51.02  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSfaaYSEDElvaRNYI------- 75
Cdd:cd01897     2 TLVIAGYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKYLRWQVIDTPGILD---RPLEE---RNTIemqaita 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  76 LGDTPDVVINVVDATN-----IERNLYLTSQLMEMGAK-VVVALNMMDEATSQNIKIDTNKLSKElGVPVIPIVAKRKTG 149
Cdd:cd01897    76 LAHLRAAVLFFIDPSEtcgysIEEQLSLFKEIKPLFNKpVIVVLNKIDLLTEEDLSEIEKELEKE-GEEVIKISTLTEEG 154
                         170
                  ....*....|
gi 1562733470 150 ISDLIKESMK 159
Cdd:cd01897   155 VDELKNKACE 164
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
3-136 3.54e-07

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: 50.90  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTgTNQHVgnwPGVTVEKKEGTFKF---KDKSFKVIDLPGTYSFAAYSEDELVARNYILGdt 79
Cdd:pfam09439   5 AVIIAGLCDSGKTSLFTLLT-TDSVR---PTVTSQEPSAAYRYmlnKGNSFTLIDFPGHVKLRYKLLETLKDSSSLKG-- 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1562733470  80 pdvVINVVDATNIERNL-----YLTSQLME-MGAK----VVVALNMMDEATSQNIKIDTNKLSKELG 136
Cdd:pfam09439  79 ---IVFVVDSTIFPKEVtdtaeFLYDILSItELLKngidILIACNKQESFTARPPKKIKQALEKEIN 142
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
1-158 4.43e-07

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


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 50.92  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   1 MSTFALVGNPNSGKTTLFNALTGTNQHVgnwpgvtvekkegtfkfKDKSF-------KVIDLPGtysfaaysedelvARN 73
Cdd:cd01878    41 VPTVALVGYTNAGKSTLFNALTGADVLA-----------------EDQLFatldpttRRIKLPG-------------GRE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  74 YILGDT-------P-----------------DVVINVVDATNIERNLYL-TSQ--LMEMGAK---VVVALNMMDEATSQN 123
Cdd:cd01878    91 VLLTDTvgfirdlPhqlveafrstleevaeaDLLLHVVDASDPDREEQIeTVEevLKELGADdipIILVLNKIDLLDDEE 170
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1562733470 124 IKidtnKLSKELGVPVIPIVAKRKTGIsDLIKESM 158
Cdd:cd01878   171 LE----ERLRAGRPDAVFISAKTGEGL-DLLKEAI 200
YeeP COG3596
Predicted GTPase [General function prediction only];
3-119 2.15e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 50.15  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTGTNQ-HVGNWPGVTVEKKEGTFK-FKDKSFKVIDLPGTYSFAAYSEDELVARNYIlgDTP 80
Cdd:COG3596    41 VIALVGKTGAGKSSLINALFGAEVaEVGVGRPCTREIQRYRLEsDGLPGLVLLDTPGLGEVNERDREYRELRELL--PEA 118
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1562733470  81 DVVINVVDATN----IERNLYltSQLME--MGAKVVVALNMMDEA 119
Cdd:COG3596   119 DLILWVVKADDralaTDEEFL--QALRAqyPDPPVLVVLTQVDRL 161
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
13-154 7.67e-06

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: 46.70  E-value: 7.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  13 GKTTLFNALTGTN----------QHVGnwpGVTVEKKEgtfkfKDKSFKVIDLPGTYSFAaysedELVARNYILGdtpDV 82
Cdd:cd01887    12 GKTTLLDKIRKTNvaageaggitQHIG---AYQVPIDV-----KIPGITFIDTPGHEAFT-----NMRARGASVT---DI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  83 VINVVDATN------IErnlylTSQLMEM-GAKVVVALNMMDEATSQNIKID--------TNKLSKELG--VPVIPIVAK 145
Cdd:cd01887    76 AILVVAADDgvmpqtIE-----AINHAKAaNVPIIVAINKIDKPYGTEADPErvknelseLGLVGEEWGgdVSIVPISAK 150

                  ....*....
gi 1562733470 146 RKTGISDLI 154
Cdd:cd01887   151 TGEGIDDLL 159
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
4-154 1.91e-05

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


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 45.98  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   4 FALVGNPNSGKTTLFNALT--------GTNQHVGNWP-----------GVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAy 64
Cdd:pfam00009   6 IGIIGHVDHGKTTLTDRLLyytgaiskRGEVKGEGEAgldnlpeererGITIKSAAVSFETKDYLINLIDTPGHVDFVK- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  65 sedeLVARNyilGDTPDVVINVVDAT-----NIERNLYLTSQlmeMGAKVVVALNMMDEATSQNIKIDTNKLSKEL---- 135
Cdd:pfam00009  85 ----EVIRG---LAQADGAILVVDAVegvmpQTREHLRLARQ---LGVPIIVFINKMDRVDGAELEEVVEEVSRELleky 154
                         170       180
                  ....*....|....*....|....
gi 1562733470 136 -----GVPVIPIVAKRKTGISDLI 154
Cdd:pfam00009 155 gedgeFVPVVPGSALKGEGVQTLL 178
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
3-164 4.54e-05

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 46.23  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTGTnqhvgnwpGVTVEkkegtfkfkDKSF-------KVIDLPGTysfaaysedelvaRNYI 75
Cdd:COG2262   201 TVALVGYTNAGKSTLFNRLTGA--------DVLAE---------DKLFatldpttRRLELPDG-------------RPVL 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  76 LGDT-------P-----------------DVVINVVDAT--NIERNLYLTSQ-LMEMGA---KVVVALNMMDEATSQNIK 125
Cdd:COG2262   251 LTDTvgfirklPhqlveafrstleevreaDLLLHVVDASdpDFEEQIETVNEvLEELGAddkPIILVFNKIDLLDDEELE 330
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1562733470 126 IDtnklsKELGVPVIPIVAKRKTGISDLIKESMKFIEED 164
Cdd:COG2262   331 RL-----RAGYPDAVFISAKTGEGIDELLEAIEERLPED 364
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
5-118 5.57e-05

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 46.33  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGTNQH-VGNWPGVTVEKKEGTFKFKDKSFKVIDLPGT---------YSFAAYsedeLVARNY 74
Cdd:PRK09518  454 ALVGRPNVGKSSLLNQLTHEERAvVNDLAGTTRDPVDEIVEIDGEDWLFIDTAGIkrrqhkltgAEYYSS----LRTQAA 529
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1562733470  75 IlgDTPDVVINVVDATN--IERNLYLTSQLMEMGAKVVVALN---MMDE 118
Cdd:PRK09518  530 I--ERSELALFLFDASQpiSEQDLKVMSMAVDAGRALVLVFNkwdLMDE 576
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
5-156 8.11e-05

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: 43.25  E-value: 8.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTG------TNQhvgnwPGVTVEKKEGTFKFKDKSFKVIDLPG---TysfaayseDELV----- 70
Cdd:cd04164     7 VIAGKPNVGKSSLLNALAGrdraivSDI-----AGTTRDVIEEEIDLGGIPVRLIDTAGlreT--------EDEIekigi 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  71 --ARNYIlgDTPDVVINVVDATNIERNLYLTSQLMEMGAKVVVALNMMDeatsqnIKIDTNKLSKELGVPVIPIVAKRKT 148
Cdd:cd04164    74 erAREAI--EEADLVLLVVDASEGLDEEDLEILELPAKKPVIVVLNKSD------LLSDAEGISELNGKPIIAISAKTGE 145

                  ....*...
gi 1562733470 149 GISDLIKE 156
Cdd:cd04164   146 GIDELKEA 153
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
7-57 8.62e-05

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


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 43.67  E-value: 8.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1562733470   7 VGNPNSGKTTLFNALTGTN-QHVGNWPGVTveKKEGTFKFKDKsFKVIDLPG 57
Cdd:cd01856   121 VGIPNVGKSTLINRLRGKKvAKVGNKPGVT--RGQQWIRIGPN-IELLDTPG 169
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
5-37 2.96e-04

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


Pssm-ID: 206686 [Multi-domain]  Cd Length: 318  Bit Score: 43.37  E-value: 2.96e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1562733470   5 ALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVE 37
Cdd:cd01899     2 GLVGKPNVGKSTFFNAATLADVEIANYPFTTID 34
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
5-154 3.67e-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: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGTN-QHVGNWPGVTVEKKEGTFKFKDKSFKVIDLPGTYSFAAY-SEDELVARNYIlgDTPDV 82
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEvAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRdREYEELYRRLL--PEADL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1562733470  83 VINVVDATN----IERNLYLTsQLMEMGAKVVVALNMMDeatsqnikidtnklskelgvPVIPIVAKRKTGISDLI 154
Cdd:cd11383    79 VLWLLDADDralaADHDFYLL-PLAGHDAPLLFVLNQVD--------------------PVLAVSARTGWGLDELA 133
PRK09602 PRK09602
translation-associated GTPase; Reviewed
1-37 4.28e-04

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 43.26  E-value: 4.28e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1562733470   1 MSTFALVGNPNSGKTTLFNALTGTNQHVGNWPGVTVE 37
Cdd:PRK09602    1 MITIGLVGKPNVGKSTFFNAATLADVEIANYPFTTID 37
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
3-156 4.51e-04

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: 42.58  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNAL---TGTNQHVGN-WPGVTV------EKKEG--------TFKFKDKSFKVIDLPGTYSFAAY 64
Cdd:cd04170     1 NIALVGHSGSGKTTLAEALlyaTGAIDRLGRvEDGNTVsdydpeEKKRKmsietsvaPLEWNGHKINLIDTPGYADFVGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  65 SEDELVArnyilgdtPDVVINVVDA-TNIErnlYLTSQLMEMGAKV----VVALNMMDEATSqNIKIDTNKLSKELGVPV 139
Cdd:cd04170    81 TLSALRA--------VDAALIVVEAqSGVE---VGTEKVWEFLDDAklprIIFINKMDRARA-DFDKTLAALREAFGRPV 148
                         170       180
                  ....*....|....*....|..
gi 1562733470 140 IPIV-----AKRKTGISDLIKE 156
Cdd:cd04170   149 VPIQlpigeGDEFTGVVDLLSE 170
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
3-162 1.15e-03

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


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 40.36  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALT---GTNQHVGNWPGVTV-----EKKEG--------TFKFKDKSFKVIDLPGTYSFAaySE 66
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLyqtGAIDRRGTRKETFLdtlkeERERGitiktgvvEFEWPKRRINFIDTPGHEDFS--KE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  67 DELVARnyilgdTPDVVINVVDA-----TNIERNLYLtsqLMEMGAKVVVALNMMD-------EATSQNIKIDTNKL--- 131
Cdd:cd00881    79 TVRGLA------QADGALLVVDAnegvePQTREHLNI---ALAGGLPIIVAVNKIDrvgeedfDEVLREIKELLKLIgft 149
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1562733470 132 -SKELGVPVIPIVAKRKTGISDLIKESMKFIE 162
Cdd:cd00881   150 fLKGKDVPIIPISALTGEGIEELLDAIVEHLP 181
PRK03003 PRK03003
GTP-binding protein Der; Reviewed
3-90 1.17e-03

GTP-binding protein Der; Reviewed


Pssm-ID: 179525 [Multi-domain]  Cd Length: 472  Bit Score: 41.88  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   3 TFALVGNPNSGKTTLFNALTGTNQH-VGNWPGVTVEKKEGTFKFKDKSFKVIDlPGTYSFAAYSEDELVARNYILG-DTP 80
Cdd:PRK03003   40 VVAVVGRPNVGKSTLVNRILGRREAvVEDVPGVTRDRVSYDAEWNGRRFTVVD-TGGWEPDAKGLQASVAEQAEVAmRTA 118
                          90
                  ....*....|
gi 1562733470  81 DVVINVVDAT 90
Cdd:PRK03003  119 DAVLFVVDAT 128
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
6-57 1.42e-03

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 40.33  E-value: 1.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1562733470   6 LVGNPNSGKTTLFNALTGTNQH------------VGNWPGVTVekkeGTFKFK-DKSFKVIDLPG 57
Cdd:cd01855   130 VVGATNVGKSTLINALLKSNGGkvqaqalvqrltVSPIPGTTL----GLIKIPlGEGKKLYDTPG 190
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
6-155 2.83e-03

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 38.71  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   6 LVGNPNSGKTTLFNALTGtNQHVGNWP--GVTVEkkegTFKFKDKSFKVIDLPGTYSFAAYsedelvARNYilGDTPDVV 83
Cdd:cd00878     4 MLGLDGAGKTTILYKLKL-GEVVTTIPtiGFNVE----TVEYKNVKFTVWDVGGQDKIRPL------WKHY--YENTDGL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  84 INVVDATNIER-----NLyLTSQLME---MGAKVVVALNMMDEATSQNIKidtnKLSKELGVP--------VIPIVAKRK 147
Cdd:cd00878    71 IFVVDSSDRERieeakNE-LHKLLNEeelKGAPLLILANKQDLPGALTES----ELIELLGLEsikgrrwhIQPCSAVTG 145

                  ....*...
gi 1562733470 148 TGISDLIK 155
Cdd:cd00878   146 DGLDEGLD 153
PTZ00258 PTZ00258
GTP-binding protein; Provisional
6-51 6.06e-03

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 39.54  E-value: 6.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1562733470   6 LVGNPNSGKTTLFNALTGTNQHVGNWPGVTVEKKEGTFKFKDKSFK 51
Cdd:PTZ00258   26 IVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVNVPDERFD 71
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
5-156 8.26e-03

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: 37.83  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470   5 ALVGNPNSGKTTLFNALTGtnQHVgnwpgVTVEKKEGTFKFK------DKSFKVI--DLPGTYSFAAYSEDELV--ARNy 74
Cdd:cd04163     7 AIIGRPNVGKSTLLNALVG--QKI-----SIVSPKPQTTRNRirgiytDDDAQIIfvDTPGIHKPKKKLGERMVkaAWS- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1562733470  75 ILGDTpDVVINVVDATN--IERNLYLTSQLMEMGAKVVVALNMMDEATSQNI--KIDTNKLSKELGVPVIPIVAKRKTGI 150
Cdd:cd04163    79 ALKDV-DLVLFVVDASEwiGEGDEFILELLKKSKTPVILVLNKIDLVKDKEDllPLLEKLKELHPFAEIFPISALKGENV 157

                  ....*.
gi 1562733470 151 SDLIKE 156
Cdd:cd04163   158 DELLEY 163
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
5-57 8.39e-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: 37.68  E-value: 8.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1562733470   5 ALVGNPNSGKTTLFNALTG-----TNQHVGNwPGVTveKKEGTFKFkDKSFKVIDLPG 57
Cdd:cd01859   103 GVVGYPKVGKSSIINALKGrhsasTSPIPGS-PGYT--KGIQLVRI-DSKIYLIDTPG 156
 
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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