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Conserved domains on  [gi|1347936489|gb|PPS52759|]
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ethanolamine utilization protein EutP [Citrobacter braakii]

Protein Classification

ethanolamine utilization acetate kinase EutP( domain architecture ID 10015132)

ethanolamine utilization acetate kinase EutP is a novel acetate kinase involved in ethanolamine catabolism

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-159 3.73e-119

ethanolamine utilization acetate kinase EutP;


:

Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 332.70  E-value: 3.73e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   1 MKRIAFVGTVGAGKTTLFNALQGNYSLARKTQAVEFNENGDIDTPGEYFSHPRWYHALITTLQDVDTLIYIHAANDKESR 80
Cdd:PRK15467    1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347936489  81 LPAGLLDIGASKRQIAVISKTDMPDADVAATRQLLRGIGFQEPIFELNSHDPRSVQHLVDYLTELSQKEErAGEKTHHS 159
Cdd:PRK15467   81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEE-AGEKTHHS 158
 
Name Accession Description Interval E-value
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-159 3.73e-119

ethanolamine utilization acetate kinase EutP;


Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 332.70  E-value: 3.73e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   1 MKRIAFVGTVGAGKTTLFNALQGNYSLARKTQAVEFNENGDIDTPGEYFSHPRWYHALITTLQDVDTLIYIHAANDKESR 80
Cdd:PRK15467    1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347936489  81 LPAGLLDIGASKRQIAVISKTDMPDADVAATRQLLRGIGFQEPIFELNSHDPRSVQHLVDYLTELSQKEErAGEKTHHS 159
Cdd:PRK15467   81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEE-AGEKTHHS 158
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 1-148 2.38e-69

Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];


Pssm-ID: 443945 [Multi-domain]  Cd Length: 145  Bit Score: 206.19  E-value: 2.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   1 MKRIAFVGTVGAGKTTLFNALQGNYSLARKTQAVEFNENgDIDTPGEYFSHPRWYHALITTLQDVDTLIYIHAANDKESR 80
Cdd:COG4917     1 MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYDN-IIDTPGEYIENPRFYKALIATAQDADVIVLVQDATEPRSV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347936489  81 LPAGLLDIgASKRQIAVISKTDMPDADVAATRQLLRGIGFqEPIFELNSHDPRSVQHLVDYLTELSQK 148
Cdd:COG4917    80 FPPGFAKA-FNKPVIGVITKIDLPEADVERARKWLKSAGV-EPIFIVSSVTGEGIEELKEYLEELGDE 145
EutP TIGR02528
ethanolamine utilization protein, EutP; This protein is found within operons which code for ...
 2-142 5.46e-65

ethanolamine utilization protein, EutP; This protein is found within operons which code for polyhedral organelles containing the enzyme ethanolamine ammonia lyase. The function of this gene is unknown, although the presence of an N-terminal GxxGxGK motif implies a GTP-binding site. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131580 [Multi-domain]  Cd Length: 142  Bit Score: 194.97  E-value: 5.46e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQGNYSLARKTQAVEFNENgDIDTPGEYFSHPRWYHALITTLQDVDTLIYIHAANDKESRL 81
Cdd:TIGR02528   1 KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYNDG-AIDTPGEYVENRRLYSALIVTAADADVIALVQSATDPESRF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347936489  82 PAGLLDIGAsKRQIAVISKTDMPDADVAATR-QLLRGIGFQEPIFELNSHDPRSVQHLVDYL 142
Cdd:TIGR02528  80 PPGFASIFV-KPVIGLVTKIDLAEADVDIERaKELLETAGAEPIFEISSVDEQGLEALVDYL 140
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-129 1.71e-30

Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.


Pssm-ID: 402341 [Multi-domain]  Cd Length: 137  Bit Score: 107.37  E-value: 1.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   1 MKRIAFVGTVGAGKTTLFNALQGNYSLARKTQAVEFNENGdIDTPGEYFSHPRWYHALITTLQDVDTLIYIHAANDKESR 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYDNA-IDTPGEYLENRRYYSALIVTSADADVIALVQDATEPEST 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1347936489  81 LPAGLLDIgASKRQIAVISKTDMP--DADVAATRQLLRGIGFQEpIFELNS 129
Cdd:pfam10662  80 FPPGFASM-FNKPVIGIITKIDLAkdEANIEIAEEWLSLAGAQK-IFRISA 128
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 5-144 2.18e-10

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: 55.93  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   5 AFVGTVGAGKTTLFNALQGNYSLAR-----KTQAVEF------NENGDI---DTPG-EYFSHPRWYHALITTLQDVDTLI 69
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVsdvpgTTRDPDVyvkeldKGKVKLvlvDTPGlDEFGGLGREELARLLLRGADLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489  70 YIHAANDKESRLPAGLLDI----GASKRQIAVISKTDMPDADV--AATRQLLRGIGFQEPIFELNSHDPRSVQHLVDYLT 143
Cdd:cd00882    81 LVVDSTDRESEEDAKLLILrrlrKEGIPIILVGNKIDLLEEREveELLRLEELAKILGVPVFEVSAKTGEGVDELFEKLI 160


                  .
gi 1347936489 144 E 144
Cdd:cd00882   161 E 161
 
Name Accession Description Interval E-value
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-159 3.73e-119

ethanolamine utilization acetate kinase EutP;


Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 332.70  E-value: 3.73e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   1 MKRIAFVGTVGAGKTTLFNALQGNYSLARKTQAVEFNENGDIDTPGEYFSHPRWYHALITTLQDVDTLIYIHAANDKESR 80
Cdd:PRK15467    1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347936489  81 LPAGLLDIGASKRQIAVISKTDMPDADVAATRQLLRGIGFQEPIFELNSHDPRSVQHLVDYLTELSQKEErAGEKTHHS 159
Cdd:PRK15467   81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEE-AGEKTHHS 158
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 1-148 2.38e-69

Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];


Pssm-ID: 443945 [Multi-domain]  Cd Length: 145  Bit Score: 206.19  E-value: 2.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   1 MKRIAFVGTVGAGKTTLFNALQGNYSLARKTQAVEFNENgDIDTPGEYFSHPRWYHALITTLQDVDTLIYIHAANDKESR 80
Cdd:COG4917     1 MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYDN-IIDTPGEYIENPRFYKALIATAQDADVIVLVQDATEPRSV 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347936489  81 LPAGLLDIgASKRQIAVISKTDMPDADVAATRQLLRGIGFqEPIFELNSHDPRSVQHLVDYLTELSQK 148
Cdd:COG4917    80 FPPGFAKA-FNKPVIGVITKIDLPEADVERARKWLKSAGV-EPIFIVSSVTGEGIEELKEYLEELGDE 145
EutP TIGR02528
ethanolamine utilization protein, EutP; This protein is found within operons which code for ...
 2-142 5.46e-65

ethanolamine utilization protein, EutP; This protein is found within operons which code for polyhedral organelles containing the enzyme ethanolamine ammonia lyase. The function of this gene is unknown, although the presence of an N-terminal GxxGxGK motif implies a GTP-binding site. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131580 [Multi-domain]  Cd Length: 142  Bit Score: 194.97  E-value: 5.46e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQGNYSLARKTQAVEFNENgDIDTPGEYFSHPRWYHALITTLQDVDTLIYIHAANDKESRL 81
Cdd:TIGR02528   1 KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYNDG-AIDTPGEYVENRRLYSALIVTAADADVIALVQSATDPESRF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347936489  82 PAGLLDIGAsKRQIAVISKTDMPDADVAATR-QLLRGIGFQEPIFELNSHDPRSVQHLVDYL 142
Cdd:TIGR02528  80 PPGFASIFV-KPVIGLVTKIDLAEADVDIERaKELLETAGAEPIFEISSVDEQGLEALVDYL 140
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-129 1.71e-30

Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.


Pssm-ID: 402341 [Multi-domain]  Cd Length: 137  Bit Score: 107.37  E-value: 1.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   1 MKRIAFVGTVGAGKTTLFNALQGNYSLARKTQAVEFNENGdIDTPGEYFSHPRWYHALITTLQDVDTLIYIHAANDKESR 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYDNA-IDTPGEYLENRRYYSALIVTSADADVIALVQDATEPEST 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1347936489  81 LPAGLLDIgASKRQIAVISKTDMP--DADVAATRQLLRGIGFQEpIFELNS 129
Cdd:pfam10662  80 FPPGFASM-FNKPVIGIITKIDLAkdEANIEIAEEWLSLAGAQK-IFRISA 128
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
2-154 2.15e-11

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 58.84  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQGNYSLARKTQA--------VEFNENGD------IDTPGEYFSHPrwYHA-LITTLQDVD 66
Cdd:COG1100     4 KKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLStngvtidkKELKLDGLdvdlviWDTPGQDEFRE--TRQfYARQLTGAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489  67 TLIYIHAANDKESRLPA-----GLLDIGASKRQIAVISKTDMPDADVAATRQLLRGIgFQE----PIFELNSHDPRSVQH 137
Cdd:COG1100    82 LYLFVVDGTREETLQSLyelleSLRRLGKKSPIILVLNKIDLYDEEEIEDEERLKEA-LSEdnivEVVATSAKTGEGVEE 160

                         170
                  ....*....|....*..
gi 1347936489 138 LVDYLTELSQKEERAGE 154
Cdd:COG1100   161 LFAALAEILRGEGDSLD 177
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 5-144 2.18e-10

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: 55.93  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   5 AFVGTVGAGKTTLFNALQGNYSLAR-----KTQAVEF------NENGDI---DTPG-EYFSHPRWYHALITTLQDVDTLI 69
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVsdvpgTTRDPDVyvkeldKGKVKLvlvDTPGlDEFGGLGREELARLLLRGADLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489  70 YIHAANDKESRLPAGLLDI----GASKRQIAVISKTDMPDADV--AATRQLLRGIGFQEPIFELNSHDPRSVQHLVDYLT 143
Cdd:cd00882    81 LVVDSTDRESEEDAKLLILrrlrKEGIPIILVGNKIDLLEEREveELLRLEELAKILGVPVFEVSAKTGEGVDELFEKLI 160


                  .
gi 1347936489 144 E 144
Cdd:cd00882   161 E 161
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 5-125 2.77e-07

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: 47.24  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   5 AFVGTVGAGKTTLFNALQGNYSLA----------RKTQAVEFNENGD---IDTPGEYF---SHPRWYHALITTLQDVDTL 68
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIvspipgttrdPVRKEWELLPLGPvvlIDTPGLDEeggLGRERVEEARQVADRADLV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347936489  69 IYIHAANDKESRLPAGLLDIGAS-KRQIAVISKTDMPDAD---VAATRQLLRGIGFQEPIF 125
Cdd:cd00880    81 LLVVDSDLTPVEEEAKLGLLRERgKPVLLVLNKIDLVPESeeeELLRERKLELLPDLPVIA 141
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 7-152 2.80e-07

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


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 47.60  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   7 VGTVGA---GKTTLFNALQG----------------NYSLARKTQAVEFNEnGDIDTPGeyfsHPRWYHALITTLQDVDT 67
Cdd:cd04171     2 IGTAGHidhGKTTLIKALTGietdrlpeekkrgitiDLGFAYLDLPDGKRL-GFIDVPG----HEKFVKNMLAGAGGIDA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489  68 LIYIHAAND------KESRLPAGLLDIgasKRQIAVISKTDMPDADVAA-----TRQLLRGIGFQE-PIFELNSHDPRSV 135
Cdd:cd04171    77 VLLVVAADEgimpqtREHLEILELLGI---KKGLVVLTKADLVDEDRLElveeeILELLAGTFLADaPIFPVSSVTGEGI 153

                         170
                  ....*....|....*..
gi 1347936489 136 QHLVDYLTELSQKEERA 152
Cdd:cd04171   154 EELKNYLDELAEPQSKD 170
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 3-100 2.73e-06

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: 43.76  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   3 RIAFVGTVGAGKTTLFNALQGNYSLA-------RKTQAVEFNENGD----IDTPGEYFSHPRWYHALIT--TLQDVDTLI 69
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVsdypgttRDPNEGRLELKGKqiilVDTPGLIEGASEGEGLGRAflAIIEADLIL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1347936489  70 YIHAANDKESRLPAGLLDIG--ASKRQIAVISK 100
Cdd:pfam01926  81 FVVDSEEGITPLDEELLELLreNKKPIILVLNK 113
YeeP COG3596
Predicted GTPase [General function prediction only];
3-76 3.02e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 45.53  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   3 RIAFVGTVGAGKTTLFNALQGNySLA---------RKTQAVEFNENGD-----IDTPGeYFS---HPRWYHALITTLQDV 65
Cdd:COG3596    41 VIALVGKTGAGKSSLINALFGA-EVAevgvgrpctREIQRYRLESDGLpglvlLDTPG-LGEvneRDREYRELRELLPEA 118

                          90
                  ....*....|.
gi 1347936489  66 DTLIYIHAAND 76
Cdd:COG3596   119 DLILWVVKADD 129
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 2-142 4.61e-06

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 44.28  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQGNYS--------LARKTQAVEFNENGD------IDTPGEYFSHPRWYHALITT---LQD 64
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGsiteyypgTTRNYVTTVIEEDGKtykfnlLDTAGQEDYDAIRRLYYPQVersLRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489  65 VDTLIYIHAAND---KESRLPAGLLDIGASKrqIAVISKTDMPDADVAATRQLLRGIGFQEPIFELNSHDPRSVQHLVDY 141
Cdd:TIGR00231  82 FDIVILVLDVEEileKQTKEIIHHADSGVPI--ILVGNKIDLKDADLKTHVASEFAKLNGEPIIPLSAETGKNIDSAFKI 159


                  .
gi 1347936489 142 L 142
Cdd:TIGR00231 160 V 160
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 2-46 1.13e-05

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 43.54  E-value: 1.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQGNYSLA---------------RKTQAVEFNENGD-IDTPG 46
Cdd:cd01854    86 KTSVLVGQSGVGKSTLLNALLPELVLAtgeiseklgrgrhttTHRELFPLPGGGLiIDTPG 146
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 2-46 7.41e-05

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 40.99  E-value: 7.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQGNYSLA---------------RKTQAVEFNENGD-IDTPG 46
Cdd:pfam03193 107 KTTVLAGQSGVGKSTLLNALLPELDLRtgeiseklgrgrhttTHVELFPLPGGGLlIDTPG 167
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 2-25 4.62e-04

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 39.43  E-value: 4.62e-04
                          10        20
                  ....*....|....*....|....
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQGNY 25
Cdd:COG2274   502 ERVAIVGRSGSGKSTLLKLLLGLY 525
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 2-48 5.15e-04

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: 38.20  E-value: 5.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347936489   2 KRIAFVGTVGAGKTTLFNAL----Q--GNYSlaRKTqaVE-----FNENGD----IDTPGEY 48
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALtganQhvGNWP--GVT--VEkkegkFKYKGYeieiVDLPGIY 58
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-48 6.14e-04

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 38.95  E-value: 6.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347936489   1 MKRIAFVGTVGAGKTTLFNAL----Q--GNYslARKTqaVE-----FNENGD----IDTPGEY 48
Cdd:COG0370     3 MITIALVGNPNVGKTTLFNALtgsrQkvGNW--PGVT--VEkkegkFKLKGKeielVDLPGTY 61
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 1-112 6.82e-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: 38.21  E-value: 6.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   1 MKRIAFVGTVGAGKTTLFNALQGNYSLAR---------KTQAVEFNENGDI---DTPGeyF-SH-PrwyHALI----TTL 62
Cdd:cd01878    41 VPTVALVGYTNAGKSTLFNALTGADVLAEdqlfatldpTTRRIKLPGGREVlltDTVG--FiRDlP---HQLVeafrSTL 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1347936489  63 QDV---DTLIY-IHAAN-DKESRLPAG---LLDIGAS-KRQIAVISKTDMPDADVAATR 112
Cdd:cd01878   116 EEVaeaDLLLHvVDASDpDREEQIETVeevLKELGADdIPIILVLNKIDLLDDEELEER 174
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 4-46 8.85e-04

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: 37.88  E-value: 8.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1347936489   4 IAFVGTVGAGKTTLFNALQGNYSLAR------KTQAVEFNENGD----IDTPG 46
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTNRKKLARtsktpgRTQLINFFNVGDkfrlVDLPG 54
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 2-26 1.02e-03

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.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 37.24  E-value: 1.02e-03
                          10        20
                  ....*....|....*....|....*
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQGNYS 26
Cdd:pfam00005  12 EILALVGPNGAGKSTLLKLIAGLLS 36
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 2-23 2.13e-03

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 37.52  E-value: 2.13e-03
                          10        20
                  ....*....|....*....|..
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQG 23
Cdd:PRK11174  377 QRIALVGPSGAGKTSLLNALLG 398
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 5-102 2.55e-03

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 36.16  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347936489   5 AFVGTVGAGKTTLFNAL-QGNYSL-------ARKTQAVEFNENGD----IDTPG--EYFSHPRWYHALI-TTLQDVDTLI 69
Cdd:cd11383     1 GLMGKTGAGKSSLCNALfGTEVAAvgdrrptTRAAQAYVWQTGGDglvlLDLPGvgERGRRDREYEELYrRLLPEADLVL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1347936489  70 YIHAANDKE-SRLPAGLLDIGASKRQ--IAVISKTD 102
Cdd:cd11383    81 WLLDADDRAlAADHDFYLLPLAGHDAplLFVLNQVD 116
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 2-26 2.98e-03

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 36.21  E-value: 2.98e-03
                          10        20
                  ....*....|....*....|....*
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQGNYS 26
Cdd:cd03228    29 EKVAIVGPSGSGKSTLLKLLLRLYD 53
PRK01889 PRK01889
GTPase RsgA; Reviewed
 2-34 4.38e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 36.45  E-value: 4.38e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1347936489   2 KRIAFVGTVGAGKTTLFNALQGNYSLArkTQAV 34
Cdd:PRK01889  196 KTVALLGSSGVGKSTLVNALLGEEVQK--TGAV 226
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 2-64 5.16e-03

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


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 35.76  E-value: 5.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347936489   2 KRIAFVGTVGAGKTTLFNAL-QGNYslaRKTQA------VEFNENGD-------IDTPGeyfsHPRWYHALITTLQD 64
Cdd:cd04105     1 PTVLLLGPSDSGKTALFTKLtTGKV---RSTVTsiepnvASFYSNSSkgkkltlVDVPG----HEKLRDKLLEYLKA 70
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 5-48 5.48e-03

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: 35.51  E-value: 5.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1347936489   5 AFVGTVGAGKTTLFNAL----Q--GNYSlaRKTqaVEFNE-----NGD----IDTPGEY 48
Cdd:cd01879     1 ALVGNPNVGKTTLFNALtgarQkvGNWP--GVT--VEKKEgefklGGKeieiVDLPGTY 55
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 1-44 7.05e-03

Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 35.42  E-value: 7.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1347936489   1 MKRIAFVGTVGAGKTTL----FNALQGNYSLArktqAVEfnenGDIDT 44
Cdd:COG0378    13 VLAVNLMGSPGSGKTTLlektIRALKDRLRIA----VIE----GDIYT 52
 
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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