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Conserved domains on  [gi|503861074|ref|WP_014095068|]
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ferrous iron transporter B [Candidatus Arthromitus sp. SFB-rat-Yit]

Protein Classification

ferrous iron transporter B( domain architecture ID 11417566)

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

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

Graphical summary

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List of domain hits

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

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


:

Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 624.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   1 MRYALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKITNN---IELIDLPGIYSLDSISIEERISLEYLQNKNPD 77
Cdd:COG0370    4 ITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKgkeIELVDLPGTYSLSAYSPDEKVARDFLLEEKPD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  78 LIINVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKK-------------- 143
Cdd:COG0370   84 VVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGkgidelkeaiieaa 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 144 -----------------NTISSIENFIKNYEP----------------------------------IDIQKSKVDKSKSS 172
Cdd:COG0370  164 egkkprplridypeeieEAIEELEELLEEDGPypsrwlaikllegdeevlellsellelleeireeLEEELGEDLESIIA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 173 NEIYEEINSILKLCVKTSKSKNKNKSKYVDNIVLNKYLSFPILIIIFYLIFKITFSWvGGPMSDILSNLISNkFVPIIEN 252
Cdd:COG0370  244 DARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTV-GAPLMDLIDGGFGW-LGDWVAA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 253 LLShsSPIIKSFILDGIINAVSTIISFLPLILSMFICLTFLDNCGYIARSSVLLNRFMNMFGLSGKAFFPLLMSFGCTVP 332
Cdd:COG0370  322 LLP--PGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNVP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 333 AIMATRTFENDNDRKISIFLLPLMSCSARLPVFLLFTNIFFKNHKEIVLLFLYALSIILAVIIGIIMNKFSKTDNLEkSF 412
Cdd:COG0370  400 AIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPS-PF 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 413 ILELPDYKLPSLSYILKESLNKISSFFKKIGTLILSISIVIWFLSNFNIYG-FCSIEDSFLYSIGSYISKIFVPLGFgFW 491
Cdd:COG0370  479 VMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGeSEDLENSYLGRIGKALEPVFAPLGF-DW 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 492 QAGVSLIAGLMAKEFIISSMGVTFG--------ANLTQIIPTFFTSHSSISFLVFVLLYTPCISVLSTVKHEYG-IKFTL 562
Cdd:COG0370  558 QIGVALITGFAAKEVVVGTLGTLYGvgedaeesASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGsWKWTL 637
                        650       660
                 ....*....|....*....|....*
gi 503861074 563 ILTVYQLLLAYSVSFLVFNITNLLW 587
Cdd:COG0370  638 FAVGYMTVLAYLVAFLVYQIGRLLG 662
 
Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-587 0e+00

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 624.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   1 MRYALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKITNN---IELIDLPGIYSLDSISIEERISLEYLQNKNPD 77
Cdd:COG0370    4 ITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKgkeIELVDLPGTYSLSAYSPDEKVARDFLLEEKPD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  78 LIINVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKK-------------- 143
Cdd:COG0370   84 VVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGkgidelkeaiieaa 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 144 -----------------NTISSIENFIKNYEP----------------------------------IDIQKSKVDKSKSS 172
Cdd:COG0370  164 egkkprplridypeeieEAIEELEELLEEDGPypsrwlaikllegdeevlellsellelleeireeLEEELGEDLESIIA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 173 NEIYEEINSILKLCVKTSKSKNKNKSKYVDNIVLNKYLSFPILIIIFYLIFKITFSWvGGPMSDILSNLISNkFVPIIEN 252
Cdd:COG0370  244 DARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTV-GAPLMDLIDGGFGW-LGDWVAA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 253 LLShsSPIIKSFILDGIINAVSTIISFLPLILSMFICLTFLDNCGYIARSSVLLNRFMNMFGLSGKAFFPLLMSFGCTVP 332
Cdd:COG0370  322 LLP--PGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNVP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 333 AIMATRTFENDNDRKISIFLLPLMSCSARLPVFLLFTNIFFKNHKEIVLLFLYALSIILAVIIGIIMNKFSKTDNLEkSF 412
Cdd:COG0370  400 AIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPS-PF 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 413 ILELPDYKLPSLSYILKESLNKISSFFKKIGTLILSISIVIWFLSNFNIYG-FCSIEDSFLYSIGSYISKIFVPLGFgFW 491
Cdd:COG0370  479 VMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGeSEDLENSYLGRIGKALEPVFAPLGF-DW 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 492 QAGVSLIAGLMAKEFIISSMGVTFG--------ANLTQIIPTFFTSHSSISFLVFVLLYTPCISVLSTVKHEYG-IKFTL 562
Cdd:COG0370  558 QIGVALITGFAAKEVVVGTLGTLYGvgedaeesASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGsWKWTL 637
                        650       660
                 ....*....|....*....|....*
gi 503861074 563 ILTVYQLLLAYSVSFLVFNITNLLW 587
Cdd:COG0370  638 FAVGYMTVLAYLVAFLVYQIGRLLG 662
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
7-555 3.54e-139

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: 416.83  E-value: 3.54e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074    7 GNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT---NNIELIDLPGIYSLDSISIEERISLEYLQNKNPDLIINVL 83
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGfqgEDIEIVDLPGIYSLTTFSLEEEVARDYLLNEKPDLVVNVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   84 DSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKKNTIS---------------- 147
Cdd:TIGR00437  81 DASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGRGIErlkdairkaiglkelk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  148 -----------SIENFIKNYEPIDIQKSKVDKSKSSNEIYEE------INSILKLCVKTSKSKNKNKSKYVDNI------ 204
Cdd:TIGR00437 161 kraieivpeayQVVEVVEGLIEIIYSISKRGLEILLGLLEDLsleiekIERNLAEVVIKESPSNLSPTEIADEDrvlvek 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  205 -----VLNKYLSFPILIIIFYLIFKITFSwVGGPMSDILSNLISNKFVPIIENLLSHSspiIKSFILDGIINAVSTIISF 279
Cdd:TIGR00437 241 sigrkILDRFLGLPIFLFVMFILFLLTFL-VGQPLVDLIETGFSFLSEAVKSFIGNYW---LASLLGDGLIGGVGAVLSF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  280 LPLILSMFICLTFLDNCGYIARSSVLLNRFMNMFGLSGKAFFPLLMSFGCTVPAIMATRTFENDNDRKISIFLLPLMSCS 359
Cdd:TIGR00437 317 VPLIAILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPAIMATRTLETRRERLLTALVIPFMSCS 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  360 ARLPVFLLFTNIFFKNHKEIVLLFLYALSIILAVIIGIIMNKFSKTDNLEKSFILELPDYKLPSLSYILKESLNKISSFF 439
Cdd:TIGR00437 397 ARLPVIVLLFAAAFPGKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFIMELPPYRLPRFRVVFIQTWTRLRSFI 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  440 KKIGTLILSISIVIWFLSnfnIYGFCSIEDSFLYSIGSYISKIFVPLGFGF-WQAGVSLIAGLMAKEFIISSMGVTFGA- 517
Cdd:TIGR00437 477 KKAGTIIVIGSVLIWFLS---SFPGGKILESWLAAIGSIMAPLFVPLGKILdWFASVALIFGFVAKEVVVATLGVLYGLg 553
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 503861074  518 NLTQIIPTFFTSHSSISFLVFVLLYTPCISVLSTVKHE 555
Cdd:TIGR00437 554 NILSSIGHAMVPVEALSYMLFVLLYVPCLATLAAIARE 591
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
5-584 1.96e-97

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 313.96  E-value: 1.96e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   5 LIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT---NNIELIDLPGIYSLDSIS----IEERISLEYLQNKNPD 77
Cdd:PRK09554   8 LIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSttdHQVTLVDLPGTYSLTTISsqtsLDEQIACHYILSGDAD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  78 LIINVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKKNTISSIENFIKNYE 157
Cdd:PRK09554  88 LLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEALKLAIDRHQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 158 PIDIQKSKVDKSKSSNEI-------------------------------------------------------------- 175
Cdd:PRK09554 168 ANENVELVHYPQPLLNEAdslakvmpsdiplqqrrwlglqmlegdiysrayageasqhldaalarlrnemddpalhiada 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 176 -YEEINSILKLCVKTSKSKNKNKSKYVDNIVLNKYLSFPILIIIFYLIFKITFSwVGG---PMSDILSNLIsnkFVPIIE 251
Cdd:PRK09554 248 rYQCIAAICDAVSNTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAIN-IGGalqPLFDVGSVAI---FIHGIQ 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 252 NL--LSHSSPIIKSFILDGIINAVSTIISFLPLILSMFICLTFLDNCGYIARSSVLLNRFMNMFGLSGKAFFPLLMSFGC 329
Cdd:PRK09554 324 WLgyTLHFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFGC 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 330 TVPAIMATRTFENDNDRKISIFLLPLMSCSARLPVFLLFTNIFFKNHKEIVLLFLYALSiILAVIIGIIMNKFSKTDNLE 409
Cdd:PRK09554 404 NVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLG-IVMAILTGLMLKYTIMRGEA 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 410 KSFILELPDYKLPSLSYILKESLNKISSFFKKIGTLILSISIVIWFLSNFNIYGFC--SIEDSFLYSIGSYISKIFVPLG 487
Cdd:PRK09554 483 SPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIvdNINDSALASVSRVITPVLKPIG 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 488 F--GFWQAGVSLIAGLMAKEFIISSMGVTFGANLTQIIP-------------------------TF-------------- 526
Cdd:PRK09554 563 VheDNWQATVGLFTGAMAKEVVVGTLNTLYTAENIQDEEfnpaefnlgdelfgavdetwqslkdTFslsvlanpieaskg 642
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503861074 527 ---------------FTSHSS-ISFLVFVLLYTPCISVLSTVKHEYGIKFTLILTVYQLLLAYSVSFLVFNITN 584
Cdd:PRK09554 643 dgemgtgamgvmsqkFGSAAAaYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQVAS 716
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
4-156 2.70e-73

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: 231.19  E-value: 2.70e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT---NNIELIDLPGIYSLDSISIEERISLEYLQNKNPDLII 80
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKlggKEIEIVDLPGTYSLTPYSEDEKVARDFLLGEEPDLIV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503861074  81 NVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKKNTISSIENFIKNY 156
Cdd:cd01879   81 NVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDELLDAIAKL 156
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
2-143 3.06e-72

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: 228.49  E-value: 3.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074    2 RYALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT---NNIELIDLPGIYSLDSISIEERISLEYLQNKNPDL 78
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKykgYEIEIVDLPGIYSLSPYSEEERVARDYLLNEKPDV 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503861074   79 IINVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKK 143
Cdd:pfam02421  82 IVNVVDATNLERNLYLTLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSARKG 146
 
Name Accession Description Interval E-value
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-587 0e+00

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 624.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   1 MRYALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKITNN---IELIDLPGIYSLDSISIEERISLEYLQNKNPD 77
Cdd:COG0370    4 ITIALVGNPNVGKTTLFNALTGSRQKVGNWPGVTVEKKEGKFKLKgkeIELVDLPGTYSLSAYSPDEKVARDFLLEEKPD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  78 LIINVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKK-------------- 143
Cdd:COG0370   84 VVVNVVDATNLERNLYLTLQLLELGIPVVLALNMMDEAEKKGIKIDVEKLSKLLGVPVVPTSARKGkgidelkeaiieaa 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 144 -----------------NTISSIENFIKNYEP----------------------------------IDIQKSKVDKSKSS 172
Cdd:COG0370  164 egkkprplridypeeieEAIEELEELLEEDGPypsrwlaikllegdeevlellsellelleeireeLEEELGEDLESIIA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 173 NEIYEEINSILKLCVKTSKSKNKNKSKYVDNIVLNKYLSFPILIIIFYLIFKITFSWvGGPMSDILSNLISNkFVPIIEN 252
Cdd:COG0370  244 DARYAFIERILKEVVTKPGEKKLTLTDKIDRILLHPVLGIPIFLLIMFLVFQLTFTV-GAPLMDLIDGGFGW-LGDWVAA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 253 LLShsSPIIKSFILDGIINAVSTIISFLPLILSMFICLTFLDNCGYIARSSVLLNRFMNMFGLSGKAFFPLLMSFGCTVP 332
Cdd:COG0370  322 LLP--PGWLRSLLVDGIIGGVGGVLVFLPQIAILFLFLSLLEDSGYMARAAFLMDRLMRKFGLSGKSFIPLLSGFGCNVP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 333 AIMATRTFENDNDRKISIFLLPLMSCSARLPVFLLFTNIFFKNHKEIVLLFLYALSIILAVIIGIIMNKFSKTDNLEkSF 412
Cdd:COG0370  400 AIMATRTIESPRDRLITILVAPFMSCSARLPVYALLAAAFFPDNQGLVLFSLYLLGILVALLTALLLKKTLLKGEPS-PF 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 413 ILELPDYKLPSLSYILKESLNKISSFFKKIGTLILSISIVIWFLSNFNIYG-FCSIEDSFLYSIGSYISKIFVPLGFgFW 491
Cdd:COG0370  479 VMELPPYRLPTLKNVLLHTWERAKAFLKKAGTIILAASIVLWFLSSFPPGGeSEDLENSYLGRIGKALEPVFAPLGF-DW 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 492 QAGVSLIAGLMAKEFIISSMGVTFG--------ANLTQIIPTFFTSHSSISFLVFVLLYTPCISVLSTVKHEYG-IKFTL 562
Cdd:COG0370  558 QIGVALITGFAAKEVVVGTLGTLYGvgedaeesASLAEALAAGFTPATALSFLVFVLLYTPCVATLAAIKRETGsWKWTL 637
                        650       660
                 ....*....|....*....|....*
gi 503861074 563 ILTVYQLLLAYSVSFLVFNITNLLW 587
Cdd:COG0370  638 FAVGYMTVLAYLVAFLVYQIGRLLG 662
feoB TIGR00437
ferrous iron transporter FeoB; FeoB (773 amino acids in E. coli), a cytoplasmic membrane ...
7-555 3.54e-139

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: 416.83  E-value: 3.54e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074    7 GNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT---NNIELIDLPGIYSLDSISIEERISLEYLQNKNPDLIINVL 83
Cdd:TIGR00437   1 GNPNVGKSTLFNALTGANQTVGNWPGVTVEKKEGKLGfqgEDIEIVDLPGIYSLTTFSLEEEVARDYLLNEKPDLVVNVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   84 DSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKKNTIS---------------- 147
Cdd:TIGR00437  81 DASNLERNLYLTLQLLELGIPMILALNLVDEAEKKGIRIDEEKLEERLGVPVVPTSATEGRGIErlkdairkaiglkelk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  148 -----------SIENFIKNYEPIDIQKSKVDKSKSSNEIYEE------INSILKLCVKTSKSKNKNKSKYVDNI------ 204
Cdd:TIGR00437 161 kraieivpeayQVVEVVEGLIEIIYSISKRGLEILLGLLEDLsleiekIERNLAEVVIKESPSNLSPTEIADEDrvlvek 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  205 -----VLNKYLSFPILIIIFYLIFKITFSwVGGPMSDILSNLISNKFVPIIENLLSHSspiIKSFILDGIINAVSTIISF 279
Cdd:TIGR00437 241 sigrkILDRFLGLPIFLFVMFILFLLTFL-VGQPLVDLIETGFSFLSEAVKSFIGNYW---LASLLGDGLIGGVGAVLSF 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  280 LPLILSMFICLTFLDNCGYIARSSVLLNRFMNMFGLSGKAFFPLLMSFGCTVPAIMATRTFENDNDRKISIFLLPLMSCS 359
Cdd:TIGR00437 317 VPLIAILFLALSFLEDSGYLARAAFLMDGIMNKFGLSGRAFIPLILGFGCNVPAIMATRTLETRRERLLTALVIPFMSCS 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  360 ARLPVFLLFTNIFFKNHKEIVLLFLYALSIILAVIIGIIMNKFSKTDNLEKSFILELPDYKLPSLSYILKESLNKISSFF 439
Cdd:TIGR00437 397 ARLPVIVLLFAAAFPGKYGGIVIFSLYLLGFVAALITARLLPGEVFKGERSPFIMELPPYRLPRFRVVFIQTWTRLRSFI 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  440 KKIGTLILSISIVIWFLSnfnIYGFCSIEDSFLYSIGSYISKIFVPLGFGF-WQAGVSLIAGLMAKEFIISSMGVTFGA- 517
Cdd:TIGR00437 477 KKAGTIIVIGSVLIWFLS---SFPGGKILESWLAAIGSIMAPLFVPLGKILdWFASVALIFGFVAKEVVVATLGVLYGLg 553
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 503861074  518 NLTQIIPTFFTSHSSISFLVFVLLYTPCISVLSTVKHE 555
Cdd:TIGR00437 554 NILSSIGHAMVPVEALSYMLFVLLYVPCLATLAAIARE 591
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
5-584 1.96e-97

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 313.96  E-value: 1.96e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   5 LIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT---NNIELIDLPGIYSLDSIS----IEERISLEYLQNKNPD 77
Cdd:PRK09554   8 LIGNPNSGKTTLFNQLTGARQRVGNWAGVTVERKEGQFSttdHQVTLVDLPGTYSLTTISsqtsLDEQIACHYILSGDAD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  78 LIINVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKKNTISSIENFIKNYE 157
Cdd:PRK09554  88 LLINVVDASNLERNLYLTLQLLELGIPCIVALNMLDIAEKQNIRIDIDALSARLGCPVIPLVSTRGRGIEALKLAIDRHQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 158 PIDIQKSKVDKSKSSNEI-------------------------------------------------------------- 175
Cdd:PRK09554 168 ANENVELVHYPQPLLNEAdslakvmpsdiplqqrrwlglqmlegdiysrayageasqhldaalarlrnemddpalhiada 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 176 -YEEINSILKLCVKTSKSKNKNKSKYVDNIVLNKYLSFPILIIIFYLIFKITFSwVGG---PMSDILSNLIsnkFVPIIE 251
Cdd:PRK09554 248 rYQCIAAICDAVSNTLTAEPSRLTTALDKIILNRWLGLPIFLFVMYLMFLLAIN-IGGalqPLFDVGSVAI---FIHGIQ 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 252 NL--LSHSSPIIKSFILDGIINAVSTIISFLPLILSMFICLTFLDNCGYIARSSVLLNRFMNMFGLSGKAFFPLLMSFGC 329
Cdd:PRK09554 324 WLgyTLHFPDWLTIFLAQGLGGGINTVLPLVPQIGMMYLFLSFLEDSGYMARAAFVMDRLMQALGLPGKSFVPLIVGFGC 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 330 TVPAIMATRTFENDNDRKISIFLLPLMSCSARLPVFLLFTNIFFKNHKEIVLLFLYALSiILAVIIGIIMNKFSKTDNLE 409
Cdd:PRK09554 404 NVPSVMGARTLDAPRERLMTIMMAPFMSCGARLAIFAVFAAAFFGQNGALAVFSLYLLG-IVMAILTGLMLKYTIMRGEA 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 410 KSFILELPDYKLPSLSYILKESLNKISSFFKKIGTLILSISIVIWFLSNFNIYGFC--SIEDSFLYSIGSYISKIFVPLG 487
Cdd:PRK09554 483 SPFVMELPVYHVPHLKSLLIQTWQRLKGFVLRAGKVIIIVSIFIGALNSFSLSGKIvdNINDSALASVSRVITPVLKPIG 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074 488 F--GFWQAGVSLIAGLMAKEFIISSMGVTFGANLTQIIP-------------------------TF-------------- 526
Cdd:PRK09554 563 VheDNWQATVGLFTGAMAKEVVVGTLNTLYTAENIQDEEfnpaefnlgdelfgavdetwqslkdTFslsvlanpieaskg 642
                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503861074 527 ---------------FTSHSS-ISFLVFVLLYTPCISVLSTVKHEYGIKFTLILTVYQLLLAYSVSFLVFNITN 584
Cdd:PRK09554 643 dgemgtgamgvmsqkFGSAAAaYSYLIFVLLYVPCISVMGAIARESSRGWMGFSILWGLNIAYSLATLFYQVAS 716
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
4-156 2.70e-73

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: 231.19  E-value: 2.70e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT---NNIELIDLPGIYSLDSISIEERISLEYLQNKNPDLII 80
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGARQKVGNWPGVTVEKKEGEFKlggKEIEIVDLPGTYSLTPYSEDEKVARDFLLGEEPDLIV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503861074  81 NVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKKNTISSIENFIKNY 156
Cdd:cd01879   81 NVVDATNLERNLYLTLQLLELGLPVVVALNMIDEAEKRGIKIDLDKLSELLGVPVVPTSARKGEGIDELLDAIAKL 156
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
2-143 3.06e-72

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: 228.49  E-value: 3.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074    2 RYALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT---NNIELIDLPGIYSLDSISIEERISLEYLQNKNPDL 78
Cdd:pfam02421   2 TIALVGNPNVGKTTLFNALTGANQHVGNWPGVTVEKKEGKFKykgYEIEIVDLPGIYSLSPYSEEERVARDYLLNEKPDV 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503861074   79 IINVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKK 143
Cdd:pfam02421  82 IVNVVDATNLERNLYLTLQLLELGLPVVLALNMMDEAEKKGIKIDIKKLSELLGVPVVPTSARKG 146
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
4-111 1.20e-24

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


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 98.85  E-value: 1.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074    4 ALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKITNN---IELIDLPGIYslDSISIEERISLEYLQNKNPDLII 80
Cdd:pfam01926   3 ALVGRPNVGKSTLINALTGAKAIVSDYPGTTRDPNEGRLELKgkqIILVDTPGLI--EGASEGEGLGRAFLAIIEADLIL 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 503861074   81 NVLDSSNLYRNLFLTLQ--LINFNIPMVLVLNM 111
Cdd:pfam01926  81 FVVDSEEGITPLDEELLelLRENKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
4-156 1.15e-18

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


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 83.45  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQ-KVGNYPGVT---VQKKVGKITN-NIELIDLPGIYSLDsISIEERISLEYLQNKNPDL 78
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVgIVSPIPGTTrdpVRKEWELLPLgPVVLIDTPGLDEEG-GLGRERVEEARQVADRADL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  79 IINVLDSSNLYRNLFLTLQ-LINFNIPMVLVLNMIDV--AEKNNIKIHTNKLSTYLNCKVFTVNGNKKNTISSIENFIKN 155
Cdd:cd00880   80 VLLVVDSDLTPVEEEAKLGlLRERGKPVLLVLNKIDLvpESEEEELLRERKLELLPDLPVIAVSALPGEGIDELRKKIAE 159

                 .
gi 503861074 156 Y 156
Cdd:cd00880  160 L 160
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
4-149 1.11e-14

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: 71.72  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQ-KVGNYPGVTVQKKVGKITN-----NIELIDLPGIYSLDSISIEERISLEYlqnKNPD 77
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVgEVSDVPGTTRDPDVYVKELdkgkvKLVLVDTPGLDEFGGLGREELARLLL---RGAD 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503861074  78 LIINVLDSSNLYRNLFLTLQLINF----NIPMVLVLNMIDVAEKNNIK--IHTNKLSTYLNCKVFTVNGNKKNTISSI 149
Cdd:cd00882   78 LILLVVDSTDRESEEDAKLLILRRlrkeGIPIILVGNKIDLLEEREVEelLRLEELAKILGVPVFEVSAKTGEGVDEL 155
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
4-122 3.87e-12

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: 64.72  E-value: 3.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT----NNIELIDLPGIY---SLDSISIEERISLEYLQnknp 76
Cdd:cd01881    1 GLVGLPNVGKSTLLSALTSAKVEIASYPFTTLEPNVGVFEfgdgVDIQIIDLPGLLdgaSEGRGLGEQILAHLYRS---- 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503861074  77 DLIINVLDSSNL--------YRNLFLTLQLINF---NIPMVLVLNMIDVAEKNNIKI 122
Cdd:cd01881   77 DLILHVIDASEDcvgdpledQKTLNEEVSGSFLflkNKPEMIVANKIDMASENNLKR 133
GTPase_YlqF TIGR03596
ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding ...
2-81 1.92e-10

ribosome biogenesis GTP-binding protein YlqF; Members of this protein family are GTP-binding proteins involved in ribosome biogenesis, including the essential YlqF protein of Bacillus subtilis, which is an essential protein. They are related to Era, EngA, and other GTPases of ribosome biogenesis, but are circularly permuted. This family is not universal, and is not present in Escherichia coli, and so is not as well studied as some other GTPases. This model is built for bacterial members. [Protein synthesis, Other]


Pssm-ID: 274669 [Multi-domain]  Cd Length: 276  Bit Score: 61.76  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074    2 RYALIGNPNVGKTTIFNILTGSNQ-KVGNYPGVTVQKKVGKITNNIELIDLPGI-----------YSL-------DSISI 62
Cdd:TIGR03596 120 RAMIVGIPNVGKSTLINRLAGKKVaKVGNRPGVTKGQQWIKLSDNLELLDTPGIlwpkfedqevgLKLaatgaikDEALD 199
                          90       100
                  ....*....|....*....|..
gi 503861074   63 EERIS---LEYLQNKNPDLIIN 81
Cdd:TIGR03596 200 LEDVAlflLEYLLEHYPELLKE 221
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
6-54 5.56e-10

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: 58.69  E-value: 5.56e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 503861074   6 IGNPNVGKTTIFNILTGSNQ-KVGNYPGVTVQKKVGKITNNIELIDLPGI 54
Cdd:cd01856  121 VGIPNVGKSTLINRLRGKKVaKVGNKPGVTRGQQWIRIGPNIELLDTPGI 170
NOG cd01897
Nucleolar GTP-binding protein (NOG); NOG1 is a nucleolar GTP-binding protein present in ...
7-121 9.19e-10

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: 57.96  E-value: 9.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   7 GNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKITNN---IELIDLPGIysLDSiSIEER--------ISLEYLqnkn 75
Cdd:cd01897    7 GYPNVGKSSLVNKLTRAKPEVAPYPFTTKSLFVGHFDYKylrWQVIDTPGI--LDR-PLEERntiemqaiTALAHL---- 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503861074  76 PDLIINVLDSSN--LY-----RNLFLTLQLiNFNIPMVLVLNMIDVAEKNNIK 121
Cdd:cd01897   80 RAAVLFFIDPSEtcGYsieeqLSLFKEIKP-LFNKPVIVVLNKIDLLTEEDLS 131
RbgA COG1161
Ribosome biogenesis GTPase RbgA [Translation, ribosomal structure and biogenesis];
6-54 8.25e-09

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


Pssm-ID: 440775 [Multi-domain]  Cd Length: 279  Bit Score: 57.04  E-value: 8.25e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 503861074   6 IGNPNVGKTTIFNILTGSNQ-KVGNYPGVTVQKKVGKITNNIELIDLPGI 54
Cdd:COG1161  119 VGIPNVGKSTLINRLAGKKVaKTGNKPGVTKGQQWIKLDDGLELLDTPGI 168
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
4-66 8.51e-09

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: 54.75  E-value: 8.51e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQK-VGNYPGVTVQKKVGKI---TNNIELIDLPGIySLDSISIEERI 66
Cdd:cd01894    1 AIVGRPNVGKSTLFNRLTGRRDAiVSDTPGVTRDRKYGEAewgGREFILIDTGGI-EPDDEGISKEI 66
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
276-369 3.65e-08

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: 51.49  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  276 IISFLPLILSMFICLTFLDNCGYIARSSVLLNRFMNMFG---LSGKAFFPLLMSFGC---TVPAIMATRTFENDNDRKIS 349
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYSGLLDRIGKLLGPLMRPLGlfpLPGKAAIALLLGFGAkevGVPLLATPYGIDTPRERLAA 80
                          90       100
                  ....*....|....*....|.
gi 503861074  350 IFLLPLMS-CSARLPVFLLFT 369
Cdd:pfam07670  81 LLFTSFSTpCGATLPVYAGEL 101
Gate pfam07670
Nucleoside recognition; This region in the nucleoside transporter proteins are responsible for ...
439-552 1.57e-07

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: 49.56  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  439 FKKIGTLILSISIVIWFLSNFniygfcsiedSFLYSIGSYISKIFVPLGFGF--WQAGVSLIAGLMAKEFIISSMGVTFG 516
Cdd:pfam07670   1 LLKVLPIILFFSVLISILEYS----------GLLDRIGKLLGPLMRPLGLFPlpGKAAIALLLGFGAKEVGVPLLATPYG 70
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 503861074  517 anltqiiptFFTSHSSISFLVFVLLYTPCISVLSTV 552
Cdd:pfam07670  71 ---------IDTPRERLAALLFTSFSTPCGATLPVY 97
YeeP COG3596
Predicted GTPase [General function prediction only];
4-116 3.66e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 52.46  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQ-KVGNYPGVTVQKKVGKITNN----IELIDLPGiysLDSISIEERISLEYLQN-KNPD 77
Cdd:COG3596   43 ALVGKTGAGKSSLINALFGAEVaEVGVGRPCTREIQRYRLESDglpgLVLLDTPG---LGEVNERDREYRELRELlPEAD 119
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 503861074  78 LIINVLDSSNLYR----NLFLTLQLINFNIPMVLVLNMIDVAE 116
Cdd:COG3596  120 LILWVVKADDRALatdeEFLQALRAQYPDPPVLVVLTQVDRLE 162
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
2-55 4.36e-07

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


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 51.01  E-value: 4.36e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503861074   2 RYALIGNPNVGKTTIFNILTGSNQKVGNY--------PGVTVQKKVgkitnNIELIDLPGIY 55
Cdd:cd01896    2 RVALVGFPSVGKSTLLSKLTNTKSEVAAYefttltcvPGVMEYKGA-----KIQLLDLPGII 58
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
4-54 6.05e-07

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: 49.24  E-value: 6.05e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503861074   4 ALIGNPNVGKTTIFNILTG----SNQKVGNYPGVTVQKKVGKITNNIELIDLPGI 54
Cdd:cd01859  103 GVVGYPKVGKSSIINALKGrhsaSTSPIPGSPGYTKGIQLVRIDSKIYLIDTPGV 157
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
4-156 6.38e-07

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: 49.43  E-value: 6.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQ--KVGNYPGVTVQKKVGKITNNIELIDLPG-IYSLDSISIEERIS---LEYLQN-KNP 76
Cdd:cd01876    3 AFAGRSNVGKSSLINALTNRKKlaRTSKTPGRTQLINFFNVGDKFRLVDLPGyGYAKVSKEVREKWGkliEEYLENrENL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  77 DLIINVLDSSNLYRNLFLTL--QLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCK-----VFTVNGNKKNTISSI 149
Cdd:cd01876   83 KGVVLLIDARHGPTPIDLEMleFLEELGIPFLIVLTKADKLKKSELAKVLKKIKEELNLFnilppVILFSSKKGTGIDEL 162

                 ....*..
gi 503861074 150 ENFIKNY 156
Cdd:cd01876  163 RALIAEW 169
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
2-54 8.21e-07

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


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 48.92  E-value: 8.21e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503861074   2 RYALIGNPNVGKTTIFN-ILTGSNQKVGNYPGVTVQKKVGKITNNIELIDLPGI 54
Cdd:cd01849   93 RVGVVGLPNVGKSSFINaLLNKFKLKVGSIPGTTKLQQDVKLDKEIYLYDTPGI 146
Der COG1160
Double Era-like domain GTPase Der [Translation, ribosomal structure and biogenesis];
4-66 8.48e-07

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


Pssm-ID: 440774 [Multi-domain]  Cd Length: 438  Bit Score: 51.56  E-value: 8.48e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQK-VGNYPGVTVQKKVGKIT---NNIELIDLPGIYSLDSISIEERI 66
Cdd:COG1160    6 AIVGRPNVGKSTLFNRLTGRRDAiVDDTPGVTRDRIYGEAEwggREFTLIDTGGIEPDDDDGLEAEI 72
PRK00093 PRK00093
GTP-binding protein Der; Reviewed
4-66 1.28e-06

GTP-binding protein Der; Reviewed


Pssm-ID: 234628 [Multi-domain]  Cd Length: 435  Bit Score: 51.20  E-value: 1.28e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQK-VGNYPGVT--VQKKVGKITN-NIELIDLPGIySLDSISIEERI 66
Cdd:PRK00093   5 AIVGRPNVGKSTLFNRLTGKRDAiVADTPGVTrdRIYGEAEWLGrEFILIDTGGI-EPDDDGFEKQI 70
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
5-143 2.46e-06

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


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 47.80  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   5 LIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKITNNIE----LIDLPGIysldsisIE----------------E 64
Cdd:cd01898    5 LVGLPNAGKSTLLSAISNAKPKIADYPFTTLVPNLGVVRVDDGrsfvIADIPGL-------IEgasegkglghrflrhiE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  65 RISleylqnknpdLIINVLDSSNLYrNLFLTLQLIN----------FNIPMVLVLNMIDV-AEKNNIKIHTNKLSTYLNC 133
Cdd:cd01898   78 RTR----------VLLHVIDLSGED-DPVEDYETIRneleaynpglAEKPRIVVLNKIDLlDAEERFEKLKELLKELKGK 146
                        170
                 ....*....|
gi 503861074 134 KVFTVNGNKK 143
Cdd:cd01898  147 KVFPISALTG 156
GTP1 COG0012
Ribosome-binding ATPase YchF, GTP1/OBG family [Translation, ribosomal structure and biogenesis] ...
1-54 3.17e-06

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


Pssm-ID: 439783 [Multi-domain]  Cd Length: 362  Bit Score: 49.63  E-value: 3.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503861074   1 MRYALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVG-------------------KITNN-IELIDLPGI 54
Cdd:COG0012    1 LKCGIVGLPNVGKSTLFNALTKAGAEAANYPFCTIEPNVGvvpvpderldklaeivkpkKIVPAtIEFVDIAGL 74
Nucleostemin_like cd04178
A circularly permuted subfamily of the Ras GTPases; Nucleostemin (NS) is a nucleolar protein ...
4-54 4.37e-06

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


Pssm-ID: 206753 [Multi-domain]  Cd Length: 171  Bit Score: 47.18  E-value: 4.37e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503861074   4 ALIGNPNVGKTTIFNILTGSN-QKVGNYPGVTVQKKVGKITNNIELIDLPGI 54
Cdd:cd04178  120 GVVGYPNVGKSSVINSLKRSRaCNVGATPGVTKSMQEVHLDKHVKLLDSPGV 171
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
1-134 6.01e-06

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: 46.72  E-value: 6.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   1 MRYALIGNPNVGKTTIFNILTGSNQK-VGNYPGVT-----VQKKVGKItnNIELIDLPGI-YSLDSIsieERI----SLE 69
Cdd:cd04164    4 IKVVIAGKPNVGKSSLLNALAGRDRAiVSDIAGTTrdvieEEIDLGGI--PVRLIDTAGLrETEDEI---EKIgierARE 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503861074  70 YLQNKnpDLIINVLDSSNLYRNLFLTLQLINFNIPMVLVLNMID-VAEKNNIKIHTNKLSTYLNCK 134
Cdd:cd04164   79 AIEEA--DLVLLVVDASEGLDEEDLEILELPAKKPVIVVLNKSDlLSDAEGISELNGKPIIAISAK 142
Ygr210 cd01899
Ygr210 GTPase; Ygr210 is a member of Obg-like family and present in archaea and fungi. They ...
4-40 1.10e-05

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: 47.61  E-value: 1.10e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVG 40
Cdd:cd01899    2 GLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVG 38
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
1-113 2.13e-05

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 45.06  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074    1 MRYALIGNPNVGKTTIFNILTG-SNQKVGNYPGVT-----VQKKVGKITNNIELIDLPGIYSLDSI---SIEERI-SLEY 70
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGnKGSITEYYPGTTrnyvtTVIEEDGKTYKFNLLDTAGQEDYDAIrrlYYPQVErSLRV 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 503861074   71 LqnknpDLIINVLD-SSNLYRNLFLTLQLINFNIPMVLVLNMID 113
Cdd:TIGR00231  82 F-----DIVILVLDvEEILEKQTKEIIHHADSGVPIILVGNKID 120
PRK09602 PRK09602
translation-associated GTPase; Reviewed
1-40 2.47e-05

translation-associated GTPase; Reviewed


Pssm-ID: 236584 [Multi-domain]  Cd Length: 396  Bit Score: 46.72  E-value: 2.47e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 503861074   1 MRYALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVG 40
Cdd:PRK09602   2 ITIGLVGKPNVGKSTFFNAATLADVEIANYPFTTIDPNVG 41
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
4-113 2.61e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 44.97  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQKVGNYP---GVTVQKKVGKITN---NIELIDLPGIYSLDSISIEERISLeylqnKNPD 77
Cdd:COG1100    7 VVVGTGGVGKTSLVNRLVGDIFSLEKYLstnGVTIDKKELKLDGldvDLVIWDTPGQDEFRETRQFYARQL-----TGAS 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 503861074  78 LIINVLDSS--NLYRNLFLTLQLI---NFNIPMVLVLNMID 113
Cdd:COG1100   82 LYLFVVDGTreETLQSLYELLESLrrlGKKSPIILVLNKID 122
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
1-126 6.16e-05

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 45.87  E-value: 6.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   1 MRYALIGNPNVGKTTIFNILTGSNqK--VGNYPGVT-----VQKKVGKITnnIELIDLPGI-YSLDSIsieERI----SL 68
Cdd:PRK05291 216 LKVVIAGRPNVGKSSLLNALLGEE-RaiVTDIAGTTrdvieEHINLDGIP--LRLIDTAGIrETDDEV---EKIgierSR 289
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 503861074  69 EYLqnKNPDLIINVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNK 126
Cdd:PRK05291 290 EAI--EEADLVLLVLDASEPLTEEDDEILEELKDKPVIVVLNKADLTGEIDLEEENGK 345
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
4-156 8.02e-05

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: 43.60  E-value: 8.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGsnQK---VGNYPGVTVQKKVGKITNN---IELIDLPGIYSldsisiEERISLEYLqNKNP- 76
Cdd:cd04163    7 AIIGRPNVGKSTLLNALVG--QKisiVSPKPQTTRNRIRGIYTDDdaqIIFVDTPGIHK------PKKKLGERM-VKAAw 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  77 ------DLIINVLDSSNL--YRNLFLTLQLINFNIPMVLVLNMID-VAEKNNIKIHTNKLS-TYLNCKVFTVNGNKKNTI 146
Cdd:cd04163   78 salkdvDLVLFVVDASEWigEGDEFILELLKKSKTPVILVLNKIDlVKDKEDLLPLLEKLKeLHPFAEIFPISALKGENV 157
                        170
                 ....*....|
gi 503861074 147 SSIENFIKNY 156
Cdd:cd04163  158 DELLEYIVEY 167
PRK04213 PRK04213
GTP-binding protein EngB;
5-53 9.13e-05

GTP-binding protein EngB;


Pssm-ID: 179790 [Multi-domain]  Cd Length: 201  Bit Score: 43.75  E-value: 9.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503861074   5 LIGNPNVGKTTIFNILTGSNQKVGNYPGVTVqkkvgKITN----NIELIDLPG 53
Cdd:PRK04213  14 FVGRSNVGKSTLVRELTGKKVRVGKRPGVTR-----KPNHydwgDFILTDLPG 61
YchF cd01900
YchF GTPase; YchF is a member of the Obg family, which includes four other subfamilies of ...
6-42 1.17e-04

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


Pssm-ID: 206687 [Multi-domain]  Cd Length: 274  Bit Score: 44.37  E-value: 1.17e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 503861074   6 IGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKI 42
Cdd:cd01900    4 VGLPNVGKSTLFNALTKSNAEAANYPFCTIEPNVGIV 40
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
4-117 1.86e-04

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: 42.83  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT--NNIELI---------DLPgiYSLdsisIEE-RISLEYL 71
Cdd:cd01878   45 ALVGYTNAGKSTLFNALTGADVLAEDQLFATLDPTTRRIKlpGGREVLltdtvgfirDLP--HQL----VEAfRSTLEEV 118
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503861074  72 qnKNPDLIINVLDSSNLYRNLFL-----TLQLINF-NIPMVLVLNMIDVAEK 117
Cdd:cd01878  119 --AEADLLLHVVDASDPDREEQIetveeVLKELGAdDIPIILVLNKIDLLDD 168
obgE PRK12297
GTPase CgtA; Reviewed
4-118 2.26e-04

GTPase CgtA; Reviewed


Pssm-ID: 237046 [Multi-domain]  Cd Length: 424  Bit Score: 43.94  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNQKVGNYP--------GVtVQKKVGKitnNIELIDLPGIysldsisIE------------ 63
Cdd:PRK12297 162 GLVGFPNVGKSTLLSVVSNAKPKIANYHfttlvpnlGV-VETDDGR---SFVMADIPGL-------IEgasegvglghqf 230
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503861074  64 ----ERISleylqnknpdLIINVLDSSNLY-RNLFLTLQLIN-----FNI-----PMVLVLNMIDV--AEKN 118
Cdd:PRK12297 231 lrhiERTR----------VIVHVIDMSGSEgRDPIEDYEKINkelklYNPrllerPQIVVANKMDLpeAEEN 292
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
4-122 2.44e-04

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


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 43.62  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074    4 ALIGNPNVGKTTIFNILTGSNqK--VGNYPGVT-----VQKKVGKITnnIELIDLPGI-YSLDSIsieERI----SLEYL 71
Cdd:pfam12631  98 VIVGKPNVGKSSLLNALLGEE-RaiVTDIPGTTrdvieETINIGGIP--LRLIDTAGIrETDDEV---EKIgierAREAI 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 503861074   72 QNKnpDLIINVLDSSN-LYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKI 122
Cdd:pfam12631 172 EEA--DLVLLVLDASRpLDEEDLEILELLKDKKPIIVVLNKSDLLGEIDELE 221
PTZ00258 PTZ00258
GTP-binding protein; Provisional
5-43 6.23e-04

GTP-binding protein; Provisional


Pssm-ID: 240334 [Multi-domain]  Cd Length: 390  Bit Score: 42.24  E-value: 6.23e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 503861074   5 LIGNPNVGKTTIFNILTGSNQKVGNYPGVTVQKKVGKIT 43
Cdd:PTZ00258  26 IVGLPNVGKSTTFNALCKQQVPAENFPFCTIDPNTARVN 64
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
1-148 9.67e-04

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


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 40.61  E-value: 9.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   1 MRYALIGNPNVGKTTIFNILTGSN-QKVGNYPgVTvqkkvGKIT-------NNIELIDLPGiysLDSISIE-ERISLEYL 71
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEvLPTGVTP-TT-----AVITvlrygllKGVVLVDTPG---LNSTIEHhTEITESFL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074  72 qnKNPDLIINVLDSSNLYRNL---FLTLQLINFNIPMVLVLNMIDVAEKNNIKIHTNKLSTYLNCKVFTVNGNKKNTISS 148
Cdd:cd09912   72 --PRADAVIFVLSADQPLTESereFLKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREELGVLELGGGEPRIFPVSA 149
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
4-122 1.27e-03

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


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 41.59  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503861074   4 ALIGNPNVGKTTIFNILTGSNqK--VGNYPG-----VTVQKKVGKITnnIELIDLPGI-YSLDSIsieERI----SLEYL 71
Cdd:COG0486  217 VIVGRPNVGKSSLLNALLGEE-RaiVTDIAGttrdvIEERINIGGIP--VRLIDTAGLrETEDEV---EKIgierAREAI 290
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503861074  72 qnKNPDLIINVLDSSNLYRNLFLTLQLINFNIPMVLVLNMIDVAEKNNIKI 122
Cdd:COG0486  291 --EEADLVLLLLDASEPLTEEDEEILEKLKDKPVIVVLNKIDLPSEADGEL 339
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
5-54 2.86e-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: 39.17  E-value: 2.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503861074   5 LIGNPNVGKTTIFNILTGSNQK------------VGNYPGVTVQKKVGKITNNIELIDLPGI 54
Cdd:cd01855  130 VVGATNVGKSTLINALLKSNGGkvqaqalvqrltVSPIPGTTLGLIKIPLGEGKKLYDTPGI 191
NGP_1 cd01858
A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; ...
5-54 7.97e-03

A novel nucleolar GTP-binding protein, circularly permuted subfamily of the Ras GTPases; Autoantigen NGP-1 (Nucleolar G-protein gene 1) has been shown to localize in the nucleolus and nucleolar organizers in all cell types analyzed, which is indicative of a function in ribosomal assembly. NGP-1 and its homologs show a circular permutation of the GTPase signature motifs so that the C-terminal strands 5, 6, and 7 (strand 6 contains the G4 box with NKXD motif) are relocated to the N terminus.


Pssm-ID: 206751 [Multi-domain]  Cd Length: 157  Bit Score: 37.28  E-value: 7.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503861074   5 LIGNPNVGKTTIFNILTGSNQ-KVGNYPGVTvqkKVGK---ITNNIELIDLPGI 54
Cdd:cd01858  107 FIGYPNVGKSSVINTLRSKKVcKVAPIPGET---KVWQyitLMKRIYLIDCPGV 157
 
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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