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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  40 GIMGKSGAGKSSLCNALFQGEVTPVSDVHAGTREVRRFRLSGHGHSMVITDLPGVGESRNRDAEYEALYRDILPELDLVL 119
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1604915319 120 WLIKADDRALSVDEYFWRHILHRGHQQVLFVVTQADK 156
Cdd:cd11383    81 WLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVDP 117

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  40 GIMGKSGAGKSSLCNALFQGEVTPVSDVHAGTREVRRFRLSGHGHSMVITDLPGVGESRNRDAEYEALYRDILPELDLVL 119
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1604915319 120 WLIKADDRALSVDEYFWRHILHRGHQQVLFVVTQADK 156
Cdd:cd11383    81 WLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVDP 117

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  39 IGIMGKSGAGKSSLCNALFqGEVTPVSDVHAGTREVRRFRLSGHGHSMVITDLPGVGESRNRDAEYEALYRDILpELDLV 118
Cdd:pfam01926   2 VALVGRPNVGKSTLINALT-GAKAIVSDYPGTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAII-EADLI 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1604915319 119 LWLIKADDRALSVDEYFwRHILHRGHQQVLFVVT 152
Cdd:pfam01926  80 LFVVDSEEGITPLDEEL-LELLRENKKPIILVLN 112

ABC transporter C family member; Provisional

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604915319    3 PSDAIEAIE--KPLSSLPYSLSRHILE-HLRKLTSHEPV-------------IGIMGKSGAGKSSLCNALFQ 58
Cdd:PLN03232  1213 PSEATAIIEnnRPVSGWPSRGSIKFEDvHLRYRPGLPPVlhglsffvspsekVGVVGRTGAGKSSMLNALFR 1284

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1604915319   6 AIEAIEKPLSSlPYSLSRHILEHLRKLTSHEPVIGIMGKSGAGKSSLCNAL 56
Cdd:cd03114    17 AITLVESGRPD-HRELAQELLDALLPQAGRAFRVGITGPPGAGKSTLIEAL 66

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  40 GIMGKSGAGKSSLCNALFQGEVTPVSDVHAGTREVRRFRLSGHGHSMVITDLPGVGESRNRDAEYEALYRDILPELDLVL 119
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTGGDGLVLLDLPGVGERGRRDREYEELYRRLLPEADLVL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1604915319 120 WLIKADDRALSVDEYFWRHILHRGHQQVLFVVTQADK 156
Cdd:cd11383    81 WLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVDP 117

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  40 GIMGKSGAGKSSLCNALFQGEVTPVSDVHAGTRE--VRRFRLSGHGHSMVITDLPGVGESRNRDaeYEALYRDILPELDL 117
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDpdVYVKELDKGKVKLVLVDTPGLDEFGGLG--REELARLLLRGADL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1604915319 118 VLWLIKADDRALSVDEYFWRHILHRGHQQ-VLFVVTQADKTEPCHEW 163
Cdd:cd00882    79 ILLVVDSTDRESEEDAKLLILRRLRKEGIpIILVGNKIDLLEEREVE 125

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  40 GIMGKSGAGKSSLCNALFQGEVTPVSDVHAGTREVRRFRL-SGHGHSMVITDLPGVGESRNRDAEYEALYRDILPELDLV 118
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWeLLPLGPVVLIDTPGLDEEGGLGRERVEEARQVADRADLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1604915319 119 LWLIKADdraLSVDEYFWRHI-LHRGHQQVLFVVTQADK 156
Cdd:cd00880    81 LLVVDSD---LTPVEEEAKLGlLRERGKPVLLVLNKIDL 116

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  39 IGIMGKSGAGKSSLCNALF-QGEVTPVSDVHAGTREVRRFRLsghGHSMVITDLPGVGE---SRNRDAEYEALYRDIL-- 112
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTnRKKLARTSKTPGRTQLINFFNV---GDKFRLVDLPGYGYakvSKEVREKWGKLIEEYLen 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1604915319 113 -PELDLVLWLIKADDRALSVDEYFWRHILHRGhQQVLFVVTQADK 156
Cdd:cd01876    79 rENLKGVVLLIDARHGPTPIDLEMLEFLEELG-IPFLIVLTKADK 122

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  41 IMGKSGAGKSSLCNALFQGEVTPVSDVHAGTREVRRFRLSGHGHSMVITDLPGVgesRNRDAEYEAL----YRDILPELD 116
Cdd:cd04164     8 IAGKPNVGKSSLLNALAGRDRAIVSDIAGTTRDVIEEEIDLGGIPVRLIDTAGL---RETEDEIEKIgierAREAIEEAD 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1604915319 117 LVLWLIkadDRALSVDEYFWRHILHRGHQQVLFVVTQAD 155
Cdd:cd04164    85 LVLLVV---DASEGLDEEDLEILELPAKKPVIVVLNKSD 120

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1604915319  25 ILEHLRKLTShepviGIMGKSGAGKSSLCNALFQGE---VTPVSDVHA-G---TREVRRFRLSGHGhsMVItDLPGVGE 96
Cdd:cd01854    79 LRELLKGKTS-----VLVGQSGVGKSTLLNALLPELvlaTGEISEKLGrGrhtTTHRELFPLPGGG--LII-DTPGFRE 149

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  39 IGIMGKSGAGKSSLCNALFQGEVTPVSDVhAGTrevRRFRLSG---HGHS-MVITDLPGV-------GESRNRDAeyeal 107
Cdd:cd04163     6 VAIIGRPNVGKSTLLNALVGQKISIVSPK-PQT---TRNRIRGiytDDDAqIIFVDTPGIhkpkkklGERMVKAA----- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1604915319 108 yRDILPELDLVLWLIKADDRALSVDEYFwRHILHRGHQQVLFVVTQADKTEP 159
Cdd:cd04163    77 -WSALKDVDLVLFVVDASEWIGEGDEFI-LELLKKSKTPVILVLNKIDLVKD 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  41 IMGKSGAGKSSLCNALFQGEVTPVSDVhAG-TREVRRFRLSGHGHSMVITDLPGVGES----------RNRDAEYEAlyr 109
Cdd:COG0486   218 IVGRPNVGKSSLLNALLGEERAIVTDI-AGtTRDVIEERINIGGIPVRLIDTAGLRETedevekigieRAREAIEEA--- 293

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1604915319 110 dilpelDLVLWLIKADDRALSVDEYFWRHILHRghqQVLFVVTQADKTEP 159
Cdd:COG0486   294 ------DLVLLLLDASEPLTEEDEEILEKLKDK---PVIVVLNKIDLPSE 334

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1604915319  38 VIGIMGKSGAGKSSLCNALfQGEVTPVS--------DVHAGTREVRRFRLS 80
Cdd:pfam00005  13 ILALVGPNGAGKSTLLKLI-AGLLSPTEgtilldgqDLTDDERKSLRKEIG 62

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1604915319  39 IGIMGKSGAGKSSLCNALFQGEVTPVSDVHAGTREVRRFRLSGHGHSMVITDLPGVGES 97
Cdd:cd01853    34 ILVLGKTGVGKSSTINSIFGERKVSVSAFQSETLRPREVSRTVDGFKLNIIDTPGLLES 92

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  41 IMGKSGAGKSSLCNALFQGEVTPVSDVhAG-TREVRRFRLSGHGHSMVITDLPGVGESrnrDAEYEAL----YRDILPEL 115
Cdd:PRK05291  220 IAGRPNVGKSSLLNALLGEERAIVTDI-AGtTRDVIEEHINLDGIPLRLIDTAGIRET---DDEVEKIgierSREAIEEA 295

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1604915319 116 DLVLWLIKADDRALSVDEYFWRHILHRghqQVLFVVTQADKTEP 159
Cdd:PRK05291  296 DLVLLVLDASEPLTEEDDEILEELKDK---PVIVVLNKADLTGE 336

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.

                          10
                  ....*....|....*....
gi 1604915319  39 IGIMGKSGAGKSSLCNALF 57
Cdd:cd03244    33 VGIVGRTGSGKSSLLLALF 51

GTPase Era; Reviewed

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604915319  39 IGIMGKSGAGKSSLCNALFQGEVTPVSDVhAGTrevRRFRLSG---HGHS-MVITDLPGVGESRNR------DAEYEALy 108
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQKISIVSPK-PQT---TRHRIRGivtEDDAqIIFVDTPGIHKPKRAlnramnKAAWSSL- 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1604915319 109 RDIlpelDLVLWLIKADDRALSVDEYFWRhILHRGHQQVLFVVTQADKTEP 159
Cdd:PRK00089   83 KDV----DLVLFVVDADEKIGPGDEFILE-KLKKVKTPVILVLNKIDLVKD 128

ABC transporter C family member; Provisional

                           10        20
                   ....*....|....*....|
gi 1604915319   39 IGIMGKSGAGKSSLCNALFQ 58
Cdd:PLN03130  1268 VGIVGRTGAGKSSMLNALFR 1287