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Conserved domains on  [gi|16130386|ref|NP_416956|]
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putative ethanolamine utilization acetate kinase EutP [Escherichia coli str. K-12 substr. MG1655]

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;
1-158 5.12e-119

ethanolamine utilization acetate kinase EutP;


:

Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 332.32  E-value: 5.12e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386    1 MKRIAFVGSVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFNHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130386   81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPMFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
Cdd:PRK15467  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
 
Name Accession Description Interval E-value
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-158 5.12e-119

ethanolamine utilization acetate kinase EutP;


Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 332.32  E-value: 5.12e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386    1 MKRIAFVGSVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFNHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130386   81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPMFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
Cdd:PRK15467  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
EutP TIGR02528
ethanolamine utilization protein, EutP; This protein is found within operons which code for ...
 2-144 1.56e-75

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: 221.55  E-value: 1.56e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386     2 KRIAFVGSVGAGKTTLFNALQGNYTLARKTQAVEFNDkGDIDTPGEYFNHPRWYHALITTLQDVDMLIYVHGANDPESRL 81
Cdd:TIGR02528   1 KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYND-GAIDTPGEYVENRRLYSALIVTAADADVIALVQSATDPESRF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130386    82 PAGLLDIGVsKRQIAVISKTDMPDADVAATR-KLLLETGFEEPMFELNSHDPQSVQQLVDYLAS 144
Cdd:TIGR02528  80 PPGFASIFV-KPVIGLVTKIDLAEADVDIERaKELLETAGAEPIFEISSVDEQGLEALVDYLNS 142
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 1-148 8.51e-71

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: 209.66  E-value: 8.51e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   1 MKRIAFVGSVGAGKTTLFNALQGNYTLARKTQAVEFNDkGDIDTPGEYFNHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:COG4917   1 MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYD-NIIDTPGEYIENPRFYKALIATAQDADVIVLVQDATEPRSV 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130386  81 LPAGLLDIGvSKRQIAVISKTDMPDADVAATRKLLLETGFeEPMFELNSHDPQSVQQLVDYLASLTKQ 148
Cdd:COG4917  80 FPPGFAKAF-NKPVIGVITKIDLPEADVERARKWLKSAGV-EPIFIVSSVTGEGIEELKEYLEELGDE 145
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-138 2.13e-31

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: 109.68  E-value: 2.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386     1 MKRIAFVGSVGAGKTTLFNALQGNYTLARKTQAVEFNDkGDIDTPGEYFNHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYD-NAIDTPGEYLENRRYYSALIVTSADADVIALVQDATEPEST 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386    81 LPAGLLDIgVSKRQIAVISKTDMP--DADVAATRKLLLETGFEEPmFELNSHDPQSVQQL 138
Cdd:pfam10662  80 FPPGFASM-FNKPVIGIITKIDLAkdEANIEIAEEWLSLAGAQKI-FRISAVEKIGIEEL 137
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 5-144 1.10e-12

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: 62.09  E-value: 1.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   5 AFVGSVGAGKTTLFNALQGNY----------TLARKTQAVEFNDKGD----IDTPG-EYFNHPRWYHALITTLQDVDMLI 69
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEvgevsdvpgtTRDPDVYVKELDKGKVklvlVDTPGlDEFGGLGREELARLLLRGADLIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386  70 YVHGANDPESRLPAGLLDI----GVSKRQIAVISKTDMPDADV--AATRKLLLETGFEEPMFELNSHDPQSVQQLVDYLA 143
Cdd:cd00882  81 LVVDSTDRESEEDAKLLILrrlrKEGIPIILVGNKIDLLEEREveELLRLEELAKILGVPVFEVSAKTGEGVDELFEKLI 160


                .
gi 16130386 144 S 144
Cdd:cd00882 161 E 161
 
Name Accession Description Interval E-value
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-158 5.12e-119

ethanolamine utilization acetate kinase EutP;


Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 332.32  E-value: 5.12e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386    1 MKRIAFVGSVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFNHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130386   81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPMFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
Cdd:PRK15467  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
EutP TIGR02528
ethanolamine utilization protein, EutP; This protein is found within operons which code for ...
 2-144 1.56e-75

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: 221.55  E-value: 1.56e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386     2 KRIAFVGSVGAGKTTLFNALQGNYTLARKTQAVEFNDkGDIDTPGEYFNHPRWYHALITTLQDVDMLIYVHGANDPESRL 81
Cdd:TIGR02528   1 KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYND-GAIDTPGEYVENRRLYSALIVTAADADVIALVQSATDPESRF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130386    82 PAGLLDIGVsKRQIAVISKTDMPDADVAATR-KLLLETGFEEPMFELNSHDPQSVQQLVDYLAS 144
Cdd:TIGR02528  80 PPGFASIFV-KPVIGLVTKIDLAEADVDIERaKELLETAGAEPIFEISSVDEQGLEALVDYLNS 142
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 1-148 8.51e-71

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: 209.66  E-value: 8.51e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   1 MKRIAFVGSVGAGKTTLFNALQGNYTLARKTQAVEFNDkGDIDTPGEYFNHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:COG4917   1 MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYD-NIIDTPGEYIENPRFYKALIATAQDADVIVLVQDATEPRSV 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130386  81 LPAGLLDIGvSKRQIAVISKTDMPDADVAATRKLLLETGFeEPMFELNSHDPQSVQQLVDYLASLTKQ 148
Cdd:COG4917  80 FPPGFAKAF-NKPVIGVITKIDLPEADVERARKWLKSAGV-EPIFIVSSVTGEGIEELKEYLEELGDE 145
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-138 2.13e-31

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: 109.68  E-value: 2.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386     1 MKRIAFVGSVGAGKTTLFNALQGNYTLARKTQAVEFNDkGDIDTPGEYFNHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYD-NAIDTPGEYLENRRYYSALIVTSADADVIALVQDATEPEST 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386    81 LPAGLLDIgVSKRQIAVISKTDMP--DADVAATRKLLLETGFEEPmFELNSHDPQSVQQL 138
Cdd:pfam10662  80 FPPGFASM-FNKPVIGIITKIDLAkdEANIEIAEEWLSLAGAQKI-FRISAVEKIGIEEL 137
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 5-144 1.10e-12

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: 62.09  E-value: 1.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   5 AFVGSVGAGKTTLFNALQGNY----------TLARKTQAVEFNDKGD----IDTPG-EYFNHPRWYHALITTLQDVDMLI 69
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEvgevsdvpgtTRDPDVYVKELDKGKVklvlVDTPGlDEFGGLGREELARLLLRGADLIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386  70 YVHGANDPESRLPAGLLDI----GVSKRQIAVISKTDMPDADV--AATRKLLLETGFEEPMFELNSHDPQSVQQLVDYLA 143
Cdd:cd00882  81 LVVDSTDRESEEDAKLLILrrlrKEGIPIILVGNKIDLLEEREveELLRLEELAKILGVPVFEVSAKTGEGVDELFEKLI 160


                .
gi 16130386 144 S 144
Cdd:cd00882 161 E 161
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
2-150 1.37e-12

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 61.92  E-value: 1.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   2 KRIAFVGSVGAGKTTLFNALQGNYTLARKTQA--------VEFNDKGD------IDTPGEYFNHPrwYHA-LITTLQDVD 66
Cdd:COG1100   4 KKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLStngvtidkKELKLDGLdvdlviWDTPGQDEFRE--TRQfYARQLTGAS 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386  67 MLIYVHGANDPESRLPA-----GLLDIGVSKRQIAVISKTD-MPDADVAATRKL--LLETGFEEPMFELNSHDPQSVQQL 138
Cdd:COG1100  82 LYLFVVDGTREETLQSLyelleSLRRLGKKSPIILVLNKIDlYDEEEIEDEERLkeALSEDNIVEVVATSAKTGEGVEEL 161

                       170
                ....*....|..
gi 16130386 139 VDYLASLTKQEE 150
Cdd:COG1100 162 FAALAEILRGEG 173
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 2-142 2.82e-08

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 50.06  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386     2 KRIAFVGSVGAGKTTLFNALQGNY--------TLARKTQAVEFNDKGD------IDTPGEYFNHPRWYHALITT---LQD 64
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKgsiteyypGTTRNYVTTVIEEDGKtykfnlLDTAGQEDYDAIRRLYYPQVersLRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386    65 VDMLIYVHGAND---PESRLPAGLLDIGVSKrqIAVISKTDMPDADV-AATRKLLLETGFeEPMFELNSHDPQSVQQLVD 140
Cdd:TIGR00231  82 FDIVILVLDVEEileKQTKEIIHHADSGVPI--ILVGNKIDLKDADLkTHVASEFAKLNG-EPIIPLSAETGKNIDSAFK 158


                  ..
gi 16130386   141 YL 142
Cdd:TIGR00231 159 IV 160
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 5-145 7.15e-08

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: 49.17  E-value: 7.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   5 AFVGSVGAGKTTLFNALQGNY----------TLARKTQAVEFNDKGD---IDTPGEYFN---HPRWYHALITTLQDVDML 68
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNvgivspipgtTRDPVRKEWELLPLGPvvlIDTPGLDEEgglGRERVEEARQVADRADLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386  69 IYVHGANDPESRLPAGLLDIGVS-KRQIAVISKTDMPDAD--VAATRKLLLETGFEEPMFELNSHDPQSVQQLVDYLASL 145
Cdd:cd00880  81 LLVVDSDLTPVEEEAKLGLLRERgKPVLLVLNKIDLVPESeeEELLRERKLELLPDLPVIAVSALPGEGIDELRKKIAEL 160
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 4-151 1.17e-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: 48.76  E-value: 1.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   4 IAFVGSVGAGKTTLFNALQGNYTLARKTQ--------------AVEFNDK-GDIDTPGeyfnHPRWYHALITTLQDVDML 68
Cdd:cd04171   2 IGTAGHIDHGKTTLIKALTGIETDRLPEEkkrgitidlgfaylDLPDGKRlGFIDVPG----HEKFVKNMLAGAGGIDAV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386  69 IYVHGAND---PESR---LPAGLLDIgvsKRQIAVISKTDMPDAD----VAATRKLLLETGFEE--PMFELNSHDPQSVQ 136
Cdd:cd04171  78 LLVVAADEgimPQTRehlEILELLGI---KKGLVVLTKADLVDEDrlelVEEEILELLAGTFLAdaPIFPVSSVTGEGIE 154

                       170
                ....*....|....*
gi 16130386 137 QLVDYLASLTKQEEA 151
Cdd:cd04171 155 ELKNYLDELAEPQSK 169
YeeP COG3596
Predicted GTPase [General function prediction only];
3-77 1.64e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 49.38  E-value: 1.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   3 RIAFVGSVGAGKTTLFNALQGNyTLA---------RKTQAVEFNDKGD-----IDTPG--EYFNHPRWYHALITTLQDVD 66
Cdd:COG3596  41 VIALVGKTGAGKSSLINALFGA-EVAevgvgrpctREIQRYRLESDGLpglvlLDTPGlgEVNERDREYRELRELLPEAD 119

                        90
                ....*....|.
gi 16130386  67 MLIYVHGANDP 77
Cdd:COG3596 120 LILWVVKADDR 130
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 1-145 6.52e-07

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


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 47.07  E-value: 6.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   1 MKRIAFVGSVGAGKTTLFNALQGNYTLAR---------KTQAVEFNDKGDI---DTPGeyF--NHPrwyHALI----TTL 62
Cdd:cd01878  41 VPTVALVGYTNAGKSTLFNALTGADVLAEdqlfatldpTTRRIKLPGGREVlltDTVG--FirDLP---HQLVeafrSTL 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386  63 QDV---DMLIYVHGANDP--ESRLPAG---LLDIGVS-KRQIAVISKTDMPDADVAATRkllLETGFEEPMFeLNSHDPQ 133
Cdd:cd01878 116 EEVaeaDLLLHVVDASDPdrEEQIETVeevLKELGADdIPIILVLNKIDLLDDEELEER---LRAGRPDAVF-ISAKTGE 191

                       170
                ....*....|..
gi 16130386 134 SVQQLVDYLASL 145
Cdd:cd01878 192 GLDLLKEAIEEL 203
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 3-100 1.07e-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: 44.92  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386     3 RIAFVGSVGAGKTTLFNALQGNYTLA-------RKTQAVEFNDKGD----IDTPGEYFNHPRWYHALIT--TLQDVDMLI 69
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVsdypgttRDPNEGRLELKGKqiilVDTPGLIEGASEGEGLGRAflAIIEADLIL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 16130386    70 YVHGANDPESRLPAGLLDIGVS--KRQIAVISK 100
Cdd:pfam01926  81 FVVDSEEGITPLDEELLELLREnkKPIILVLNK 113
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 2-46 6.12e-06

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: 44.31  E-value: 6.12e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130386   2 KRIAFVGSVGAGKTTLFNALQGNytLARKTQAV-----------------EFNDKGD-IDTPG 46
Cdd:cd01854  86 KTSVLVGQSGVGKSTLLNALLPE--LVLATGEIseklgrgrhttthrelfPLPGGGLiIDTPG 146
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-48 8.85e-06

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 44.34  E-value: 8.85e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16130386   1 MKRIAFVGSVGAGKTTLFNAL----Q--GNY---TLARKTQAVEFNDKGD--IDTPGEY 48
Cdd:COG0370   3 MITIALVGNPNVGKTTLFNALtgsrQkvGNWpgvTVEKKEGKFKLKGKEIelVDLPGTY 61
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 5-80 1.22e-05

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: 42.71  E-value: 1.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   5 AFVGSVGAGKTTLFNAL-QGNYTL-------ARKTQAVEFNDKGD----IDTPG--EYFNHPRWYHALI-TTLQDVDMLI 69
Cdd:cd11383   1 GLMGKTGAGKSSLCNALfGTEVAAvgdrrptTRAAQAYVWQTGGDglvlLDLPGvgERGRRDREYEELYrRLLPEADLVL 80

                        90
                ....*....|.
gi 16130386  70 YVhgaNDPESR 80
Cdd:cd11383  81 WL---LDADDR 88
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 2-48 1.46e-05

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: 42.44  E-value: 1.46e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130386     2 KRIAFVGSVGAGKTTLFNALQG------NY---TLARKTQAVEFNDKGD--IDTPGEY 48
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGanqhvgNWpgvTVEKKEGKFKYKGYEIeiVDLPGIY 58
PRK01889 PRK01889
GTPase RsgA; Reviewed
 2-46 1.70e-05

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 43.38  E-value: 1.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130386    2 KRIAFVGSVGAGKTTLFNALQGNYTLArkTQAV-EFNDKGD-----------------IDTPG 46
Cdd:PRK01889 196 KTVALLGSSGVGKSTLVNALLGEEVQK--TGAVrEDDSKGRhttthrelhplpsggllIDTPG 256
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 2-46 2.09e-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: 42.53  E-value: 2.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130386     2 KRIAFVGSVGAGKTTLFNALQGNYTLA---------------RKTQAVEFNDKGD-IDTPG 46
Cdd:pfam03193 107 KTTVLAGQSGVGKSTLLNALLPELDLRtgeiseklgrgrhttTHVELFPLPGGGLlIDTPG 167
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 5-48 1.73e-04

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: 39.75  E-value: 1.73e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16130386   5 AFVGSVGAGKTTLFNAL----Q--GNY---TLARKTQAVEFNDKGD--IDTPGEY 48
Cdd:cd01879   1 ALVGNPNVGKTTLFNALtgarQkvGNWpgvTVEKKEGEFKLGGKEIeiVDLPGTY 55
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 2-26 2.43e-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: 40.20  E-value: 2.43e-04
                        10        20
                ....*....|....*....|....*
gi 16130386   2 KRIAFVGSVGAGKTTLFNALQGNYT 26
Cdd:COG2274 502 ERVAIVGRSGSGKSTLLKLLLGLYE 526
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 2-26 3.30e-04

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: 38.78  E-value: 3.30e-04
                          10        20
                  ....*....|....*....|....*
gi 16130386     2 KRIAFVGSVGAGKTTLFNALQGNYT 26
Cdd:pfam00005  12 EILALVGPNGAGKSTLLKLIAGLLS 36
era PRK00089
GTPase Era; Reviewed
 4-145 3.47e-04

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 39.65  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386    4 IAFVGSVGAGKTTLFNAL-------------------QGNYTLArKTQAVeFndkgdIDTPGeyFNHPRwyHAL------ 58
Cdd:PRK00089   8 VAIVGRPNVGKSTLLNALvgqkisivspkpqttrhriRGIVTED-DAQII-F-----VDTPG--IHKPK--RALnramnk 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   59 --ITTLQDVDMLIYVHGAND---PESRLPAGLLdIGVSKRQIAVISKTDM--PDADVAATRKLLLETGFEEPMFELNSHD 131
Cdd:PRK00089  77 aaWSSLKDVDLVLFVVDADEkigPGDEFILEKL-KKVKTPVILVLNKIDLvkDKEELLPLLEELSELMDFAEIVPISALK 155

                        170
                 ....*....|....
gi 16130386  132 PQSVQQLVDYLASL 145
Cdd:PRK00089 156 GDNVDELLDVIAKY 169
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 4-102 8.67e-04

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 37.83  E-value: 8.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   4 IAFVGSVGAGKTTLFNAL-------------------QGNYTLArKTQAVeFndkgdIDTPGEYFNHPRWYHAL----IT 60
Cdd:cd04163   6 VAIIGRPNVGKSTLLNALvgqkisivspkpqttrnriRGIYTDD-DAQII-F-----VDTPGIHKPKKKLGERMvkaaWS 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 16130386  61 TLQDVDMLIYVHGANDPESRLPAGLLDI--GVSKRQIAVISKTD 102
Cdd:cd04163  79 ALKDVDLVLFVVDASEWIGEGDEFILELlkKSKTPVILVLNKID 122
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 2-25 1.33e-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: 37.36  E-value: 1.33e-03
                        10        20
                ....*....|....*....|....
gi 16130386   2 KRIAFVGSVGAGKTTLFNALQGNY 25
Cdd:cd03228  29 EKVAIVGPSGSGKSTLLKLLLRLY 52
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 2-38 1.92e-03

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 37.52  E-value: 1.92e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 16130386    2 KRIAFVGSVGAGKTTLFNALQGN--YTLARKTQAVEFND 38
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLGFlpYQGSLKINGIELRE 415
feoB PRK09554
Fe(2+) transporter permease subunit FeoB;
1-148 2.15e-03

Fe(2+) transporter permease subunit FeoB;


Pssm-ID: 236563 [Multi-domain]  Cd Length: 772  Bit Score: 37.39  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386    1 MKR--IAFVGSVGAGKTTLFNALQ------GNY---TLARKT-------QAVEFndkgdIDTPGEYFnhprwyhalITTL 62
Cdd:PRK09554   1 MKKltIGLIGNPNSGKTTLFNQLTgarqrvGNWagvTVERKEgqfsttdHQVTL-----VDLPGTYS---------LTTI 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   63 Q-----------------DVDMLIYVHGANDPESRL-----------PA----GLLDIGVSKR---QIAVISKT-DMPDA 106
Cdd:PRK09554  67 SsqtsldeqiachyilsgDADLLINVVDASNLERNLyltlqllelgiPCivalNMLDIAEKQNiriDIDALSARlGCPVI 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 16130386  107 DVAATRKllleTGFEEPMFELNSHDPQSVQQLVDYLASLTKQ 148
Cdd:PRK09554 147 PLVSTRG----RGIEALKLAIDRHQANENVELVHYPQPLLNE 184
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 3-150 2.46e-03

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 36.99  E-value: 2.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   3 RIAFVGSVGAGKTTLFNALQGNYTLAR---------KTQAVEFNDKGDI---DTPGeyF--NHPrwyHALI----TTLQD 64
Cdd:COG2262 201 TVALVGYTNAGKSTLFNRLTGADVLAEdklfatldpTTRRLELPDGRPVlltDTVG--FirKLP---HQLVeafrSTLEE 275

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386  65 V---DMLIYVHGANDPESRLPAG-----LLDIGVS-KRQIAVISKTDMPDADVAATrkllLETGFEEPMFeLNSHDPQSV 135
Cdd:COG2262 276 VreaDLLLHVVDASDPDFEEQIEtvnevLEELGADdKPIILVFNKIDLLDDEELER----LRAGYPDAVF-ISAKTGEGI 350

                       170
                ....*....|....*
gi 16130386 136 QQLVDYLASLTKQEE 150
Cdd:COG2262 351 DELLEAIEERLPEDR 365
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 2-71 2.85e-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: 36.53  E-value: 2.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130386   2 KRIAFVGSVGAGKTTLFNAL-QGNYtlaRKTQA------VEFNDKGD-------IDTPGeyfnHPRWYHALITTLQDVDM 67
Cdd:cd04105   1 PTVLLLGPSDSGKTALFTKLtTGKV---RSTVTsiepnvASFYSNSSkgkkltlVDVPG----HEKLRDKLLEYLKASLK 73


                ....*
gi 16130386  68 -LIYV 71
Cdd:cd04105  74 aIVFV 78
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 1-44 3.44e-03

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


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 36.19  E-value: 3.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 16130386   1 MKRIAFVGSVGAGKTTL----FNALQGNYTLArktqAVEfndkGDIDT 44
Cdd:COG0378  13 VLAVNLMGSPGSGKTTLlektIRALKDRLRIA----VIE----GDIYT 52
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-25 3.52e-03

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 36.68  E-value: 3.52e-03
                        10        20
                ....*....|....*....|....
gi 16130386   2 KRIAFVGSVGAGKTTLFNALQGNY 25
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLRFY 390
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 7-27 4.12e-03

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 36.22  E-value: 4.12e-03
                        10        20
                ....*....|....*....|.
gi 16130386   7 VGSVGAGKTTLFNALQGNYTL 27
Cdd:COG1101  38 IGSNGAGKSTLLNAIAGSLPP 58
obgE PRK12299
GTPase CgtA; Reviewed
 84-154 5.25e-03

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 36.20  E-value: 5.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130386   84 GLLDigvsKRQIAVISKTDMPDADVAATRKLLLE-TGFEEPMFELNSHDPQSVQQLVDYLASLTKQEEAGEK 154
Cdd:PRK12299 268 ELAD----KPRILVLNKIDLLDEEEEREKRAALElAALGGPVFLISAVTGEGLDELLRALWELLEEARREEE 335
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 4-42 6.25e-03

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. 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: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 35.66  E-value: 6.25e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 16130386   4 IAFVGSVGAGKTTLFNALQGNYTlarktqavefNDKGDI 42
Cdd:cd03254  32 VAIVGPTGAGKTTLINLLMRFYD----------PQKGQI 60
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 3-23 7.72e-03

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 34.73  E-value: 7.72e-03
                        10        20
                ....*....|....*....|.
gi 16130386   3 RIAFVGSVGAGKTTLFNALQG 23
Cdd:cd03221  28 RIGLVGRNGAGKSTLLKLIAG 48
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 3-23 9.30e-03

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 35.43  E-value: 9.30e-03
                        10        20
                ....*....|....*....|.
gi 16130386   3 RIAFVGSVGAGKTTLFNALQG 23
Cdd:COG0488 343 RIGLIGPNGAGKSTLLKLLAG 363
 
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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