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Conserved domains on  [gi|647263443|ref|WP_025711469|]
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MULTISPECIES: ethanolamine utilization acetate kinase EutP [Klebsiella]

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 8.47e-115

ethanolamine utilization acetate kinase EutP;


:

Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 321.53  E-value: 8.47e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   1 MKRIAIVGAVGAGKTTLFNALQGNYSLARKTQALEFNDRGDIDTPGEYFSHPRWYHALITTLQDVDTLIYVHAANDTESR 80
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647263443  81 LPPGLLDIGSRKHLIVAISKTDLPDANVAAVRQLLEGMGFQAPVFALNGCDPQSVAPLENYLSELSQKEEgPGEETHYR 159
Cdd:PRK15467  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEE-AGEKTHHS 158
 
Name Accession Description Interval E-value
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-159 8.47e-115

ethanolamine utilization acetate kinase EutP;


Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 321.53  E-value: 8.47e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   1 MKRIAIVGAVGAGKTTLFNALQGNYSLARKTQALEFNDRGDIDTPGEYFSHPRWYHALITTLQDVDTLIYVHAANDTESR 80
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647263443  81 LPPGLLDIGSRKHLIVAISKTDLPDANVAAVRQLLEGMGFQAPVFALNGCDPQSVAPLENYLSELSQKEEgPGEETHYR 159
Cdd:PRK15467  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEE-AGEKTHHS 158
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 1-148 2.28e-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: 2.28e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   1 MKRIAIVGAVGAGKTTLFNALQGNYSLARKTQALEFNDrGDIDTPGEYFSHPRWYHALITTLQDVDTLIYVHAANDTESR 80
Cdd:COG4917    1 MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYD-NIIDTPGEYIENPRFYKALIATAQDADVIVLVQDATEPRSV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263443  81 LPPGLLDIGsRKHLIVAISKTDLPDANVAAVRQLLEGMGFQaPVFALNGCDPQSVAPLENYLSELSQK 148
Cdd:COG4917   80 FPPGFAKAF-NKPVIGVITKIDLPEADVERARKWLKSAGVE-PIFIVSSVTGEGIEELKEYLEELGDE 145
EutP TIGR02528
ethanolamine utilization protein, EutP; This protein is found within operons which code for ...
 2-142 6.07e-56

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: 172.24  E-value: 6.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443    2 KRIAIVGAVGAGKTTLFNALQGNYSLARKTQALEFNDrGDIDTPGEYFSHPRWYHALITTLQDVDTLIYVHAANDTESRL 81
Cdd:TIGR02528   1 KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYND-GAIDTPGEYVENRRLYSALIVTAADADVIALVQSATDPESRF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647263443   82 PPGLLDIGSRKhLIVAISKTDLPDANVAAVR--QLLEgMGFQAPVFALNGCDPQSVAPLENYL 142
Cdd:TIGR02528  80 PPGFASIFVKP-VIGLVTKIDLAEADVDIERakELLE-TAGAEPIFEISSVDEQGLEALVDYL 140
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-121 9.42e-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: 107.75  E-value: 9.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443    1 MKRIAIVGAVGAGKTTLFNALQGNYSLARKTQALEFNDrGDIDTPGEYFSHPRWYHALITTLQDVDTLIYVHAANDTESR 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYD-NAIDTPGEYLENRRYYSALIVTSADADVIALVQDATEPEST 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 647263443   81 LPPGLLDIgSRKHLIVAISKTDLP--DANVAAVRQLLEGMGFQ 121
Cdd:pfam10662  80 FPPGFASM-FNKPVIGIITKIDLAkdEANIEIAEEWLSLAGAQ 121
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 5-144 1.07e-09

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: 54.00  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   5 AIVGAVGAGKTTLFNALQGNYSLAR-----KTQALEF------NDRGDI---DTPG-EYFSHPRWYHALITTLQDVDTLI 69
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVsdvpgTTRDPDVyvkeldKGKVKLvlvDTPGlDEFGGLGREELARLLLRGADLIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443  70 YVHAANDTES----RLPPGLLDIGSRKHLIVAISKTDLPDANV--AAVRQLLEGMGFQAPVFALNGCDPQSVAPLENYLS 143
Cdd:cd00882   81 LVVDSTDRESeedaKLLILRRLRKEGIPIILVGNKIDLLEEREveELLRLEELAKILGVPVFEVSAKTGEGVDELFEKLI 160


                 .
gi 647263443 144 E 144
Cdd:cd00882  161 E 161
 
Name Accession Description Interval E-value
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-159 8.47e-115

ethanolamine utilization acetate kinase EutP;


Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 321.53  E-value: 8.47e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   1 MKRIAIVGAVGAGKTTLFNALQGNYSLARKTQALEFNDRGDIDTPGEYFSHPRWYHALITTLQDVDTLIYVHAANDTESR 80
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647263443  81 LPPGLLDIGSRKHLIVAISKTDLPDANVAAVRQLLEGMGFQAPVFALNGCDPQSVAPLENYLSELSQKEEgPGEETHYR 159
Cdd:PRK15467  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEE-AGEKTHHS 158
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 1-148 2.28e-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: 2.28e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   1 MKRIAIVGAVGAGKTTLFNALQGNYSLARKTQALEFNDrGDIDTPGEYFSHPRWYHALITTLQDVDTLIYVHAANDTESR 80
Cdd:COG4917    1 MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYD-NIIDTPGEYIENPRFYKALIATAQDADVIVLVQDATEPRSV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263443  81 LPPGLLDIGsRKHLIVAISKTDLPDANVAAVRQLLEGMGFQaPVFALNGCDPQSVAPLENYLSELSQK 148
Cdd:COG4917   80 FPPGFAKAF-NKPVIGVITKIDLPEADVERARKWLKSAGVE-PIFIVSSVTGEGIEELKEYLEELGDE 145
EutP TIGR02528
ethanolamine utilization protein, EutP; This protein is found within operons which code for ...
 2-142 6.07e-56

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: 172.24  E-value: 6.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443    2 KRIAIVGAVGAGKTTLFNALQGNYSLARKTQALEFNDrGDIDTPGEYFSHPRWYHALITTLQDVDTLIYVHAANDTESRL 81
Cdd:TIGR02528   1 KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYND-GAIDTPGEYVENRRLYSALIVTAADADVIALVQSATDPESRF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647263443   82 PPGLLDIGSRKhLIVAISKTDLPDANVAAVR--QLLEgMGFQAPVFALNGCDPQSVAPLENYL 142
Cdd:TIGR02528  80 PPGFASIFVKP-VIGLVTKIDLAEADVDIERakELLE-TAGAEPIFEISSVDEQGLEALVDYL 140
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-121 9.42e-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: 107.75  E-value: 9.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443    1 MKRIAIVGAVGAGKTTLFNALQGNYSLARKTQALEFNDrGDIDTPGEYFSHPRWYHALITTLQDVDTLIYVHAANDTESR 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYD-NAIDTPGEYLENRRYYSALIVTSADADVIALVQDATEPEST 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 647263443   81 LPPGLLDIgSRKHLIVAISKTDLP--DANVAAVRQLLEGMGFQ 121
Cdd:pfam10662  80 FPPGFASM-FNKPVIGIITKIDLAkdEANIEIAEEWLSLAGAQ 121
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 5-144 1.07e-09

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: 54.00  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   5 AIVGAVGAGKTTLFNALQGNYSLAR-----KTQALEF------NDRGDI---DTPG-EYFSHPRWYHALITTLQDVDTLI 69
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVsdvpgTTRDPDVyvkeldKGKVKLvlvDTPGlDEFGGLGREELARLLLRGADLIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443  70 YVHAANDTES----RLPPGLLDIGSRKHLIVAISKTDLPDANV--AAVRQLLEGMGFQAPVFALNGCDPQSVAPLENYLS 143
Cdd:cd00882   81 LVVDSTDRESeedaKLLILRRLRKEGIPIILVGNKIDLLEEREveELLRLEELAKILGVPVFEVSAKTGEGVDELFEKLI 160


                 .
gi 647263443 144 E 144
Cdd:cd00882  161 E 161
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
2-129 8.88e-09

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.91  E-value: 8.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   2 KRIAIVGAVGAGKTTLFNALQGNYSLARKTQA--------LEFNDRGD------IDTPGEYFshprwYHA----LITTLQ 63
Cdd:COG1100    4 KKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLStngvtidkKELKLDGLdvdlviWDTPGQDE-----FREtrqfYARQLT 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647263443  64 DVDTLIYVhAANDTESRLPP------GLLDIGSRKHLIVAISKTDLPDA----NVAAVRQLLEGMGFQAPVF--ALNG 129
Cdd:COG1100   79 GASLYLFV-VDGTREETLQSlyelleSLRRLGKKSPIILVLNKIDLYDEeeieDEERLKEALSEDNIVEVVAtsAKTG 155
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 4-150 1.63e-08

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: 51.07  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   4 IAIVGAVGAGKTTLFNALQG----------------NYSLARktQALEFNDR-GDIDTPGeyfsHPRWYHALITTLQDVD 66
Cdd:cd04171    2 IGTAGHIDHGKTTLIKALTGietdrlpeekkrgitiDLGFAY--LDLPDGKRlGFIDVPG----HEKFVKNMLAGAGGID 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443  67 TLIYVHAAND-----TESRLP-PGLLDIgsrKHLIVAISKTDLPDANVAA-----VRQLLEGMGFQ-APVFALNGCDPQS 134
Cdd:cd04171   76 AVLLVVAADEgimpqTREHLEiLELLGI---KKGLVVLTKADLVDEDRLElveeeILELLAGTFLAdAPIFPVSSVTGEG 152

                        170
                 ....*....|....*.
gi 647263443 135 VAPLENYLSELSQKEE 150
Cdd:cd04171  153 IEELKNYLDELAEPQS 168
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 2-116 4.12e-08

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: 50.40  E-value: 4.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   2 KRIAIVGAVGAGKTTLFNAL-QGNYslaRKTQA-LEFNDRGD------------IDTPGeyfsHPRWYHALITTLQD--- 64
Cdd:cd04105    1 PTVLLLGPSDSGKTALFTKLtTGKV---RSTVTsIEPNVASFysnsskgkkltlVDVPG----HEKLRDKLLEYLKAslk 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647263443  65 -----VDTLIYVHAANDTESRLPPGLLD---IGSRKHLIVAISKTDLPDA-NVAAVRQLLE 116
Cdd:cd04105   74 aivfvVDSATFQKNIRDVAEFLYDILTDlekIKNKIPILIACNKQDLFTAkPAKKIKELLE 134
YeeP COG3596
Predicted GTPase [General function prediction only];
3-76 1.87e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 48.99  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   3 RIAIVGAVGAGKTTLFNALQGNySLA---------RKTQALEFNDRGD-----IDTPGeYFS---HPRWYHALITTLQDV 65
Cdd:COG3596   41 VIALVGKTGAGKSSLINALFGA-EVAevgvgrpctREIQRYRLESDGLpglvlLDTPG-LGEvneRDREYRELRELLPEA 118

                         90
                 ....*....|.
gi 647263443  66 DTLIYVHAAND 76
Cdd:COG3596  119 DLILWVVKADD 129
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 5-128 3.00e-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: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   5 AIVGAVGAGKTTLFNALQGNYSLA----------RKTQALEFNDRGD---IDTPGEYF---SHPRWYHALITTLQDVDTL 68
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIvspipgttrdPVRKEWELLPLGPvvlIDTPGLDEeggLGRERVEEARQVADRADLV 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647263443  69 IYVHAANDTESRLPPGLLDI-GSRKHLIVAISKTDLP--DANVAAVRQLLEGMGFQAPVFALN 128
Cdd:cd00880   81 LLVVDSDLTPVEEEAKLGLLrERGKPVLLVLNKIDLVpeSEEEELLRERKLELLPDLPVIAVS 143
infB CHL00189
translation initiation factor 2; Provisional
 4-157 1.59e-06

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 46.75  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   4 IAIVGAVGAGKTTLFNALQgNYSLARK-----TQAL-----EFNDRGD------IDTPG-EYFSHPRWYHALITtlqdvD 66
Cdd:CHL00189 247 VTILGHVDHGKTTLLDKIR-KTQIAQKeaggiTQKIgayevEFEYKDEnqkivfLDTPGhEAFSSMRSRGANVT-----D 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443  67 TLIYVHAANDTesrLPPGllDIGSRKHL-------IVAISKTDLPDANVAAVRQLL-------EGMGFQAPVFALNGCDP 132
Cdd:CHL00189 321 IAILIIAADDG---VKPQ--TIEAINYIqaanvpiIVAINKIDKANANTERIKQQLakynlipEKWGGDTPMIPISASQG 395

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 647263443 133 Q----------SVAPLENYLSELSQKEEGPGEETH 157
Cdd:CHL00189 396 TnidklletilLLAEIEDLKADPTQLAQGIILEAH 430
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 3-100 3.35e-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: 3.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443    3 RIAIVGAVGAGKTTLFNALQGNYSLA-------RKTQALEFNDRGD----IDTPGEYFSHPRWYHALIT--TLQDVDTLI 69
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVsdypgttRDPNEGRLELKGKqiilVDTPGLIEGASEGEGLGRAflAIIEADLIL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 647263443   70 YVHaanDTESRLPPGLLDI-----GSRKHLIVAISK 100
Cdd:pfam01926  81 FVV---DSEEGITPLDEELlellrENKKPIILVLNK 113
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 5-76 1.05e-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: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   5 AIVGAVGAGKTTLFNAL-QGNYSL-------ARKTQALEFNDRGD----IDTPG--EYFSHPRWYHALI-TTLQDVDTLI 69
Cdd:cd11383    1 GLMGKTGAGKSSLCNALfGTEVAAvgdrrptTRAAQAYVWQTGGDglvlLDLPGvgERGRRDREYEELYrRLLPEADLVL 80


                 ....*..
gi 647263443  70 YVHAAND 76
Cdd:cd11383   81 WLLDADD 87
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 2-108 1.07e-05

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


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 43.13  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443    2 KRIAIVGAVGAGKTTLFNALQGNYslARKTQALEFNDRGD----------------IDTPGEYFSHPRWYHALITT---L 62
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNK--GSITEYYPGTTRNYvttvieedgktykfnlLDTAGQEDYDAIRRLYYPQVersL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 647263443   63 QDVDTLIYVHAANDTESRLPP---GLLDIGSRkhLIVAISKTDLPDANV 108
Cdd:TIGR00231  80 RVFDIVILVLDVEEILEKQTKeiiHHADSGVP--IILVGNKIDLKDADL 126
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 1-129 2.41e-05

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


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 42.45  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   1 MKRIAIVGAVGAGKTTLFNALQGNYSLAR---------KTQALEFNDRGDI---DTPGeyF-SH-PrwyHALI----TTL 62
Cdd:cd01878   41 VPTVALVGYTNAGKSTLFNALTGADVLAEdqlfatldpTTRRIKLPGGREVlltDTVG--FiRDlP---HQLVeafrSTL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443  63 QDV---DTLIYV------------HAANDTesrlppgLLDIG-SRKHLIVAISKTDLpdANVAAVRQLLEGMGFQA-PVF 125
Cdd:cd01878  116 EEVaeaDLLLHVvdasdpdreeqiETVEEV-------LKELGaDDIPIILVLNKIDL--LDDEELEERLRAGRPDAvFIS 186


                 ....
gi 647263443 126 ALNG 129
Cdd:cd01878  187 AKTG 190
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 2-25 4.83e-05

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: 42.13  E-value: 4.83e-05
                         10        20
                 ....*....|....*....|....
gi 647263443   2 KRIAIVGAVGAGKTTLFNALQGNY 25
Cdd:COG2274  502 ERVAIVGRSGSGKSTLLKLLLGLY 525
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 2-26 1.32e-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: 39.94  E-value: 1.32e-04
                          10        20
                  ....*....|....*....|....*
gi 647263443    2 KRIAIVGAVGAGKTTLFNALQGNYS 26
Cdd:pfam00005  12 EILALVGPNGAGKSTLLKLIAGLLS 36
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-48 1.50e-04

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 40.87  E-value: 1.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 647263443   1 MKRIAIVGAVGAGKTTLFNAL----Q--GNYS---LARKTQALEFNDRGD--IDTPGEY 48
Cdd:COG0370    3 MITIALVGNPNVGKTTLFNALtgsrQkvGNWPgvtVEKKEGKFKLKGKEIelVDLPGTY 61
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 2-26 1.56e-04

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: 40.06  E-value: 1.56e-04
                         10        20
                 ....*....|....*....|....*
gi 647263443   2 KRIAIVGAVGAGKTTLFNALQGNYS 26
Cdd:cd03228   29 EKVAIVGPSGSGKSTLLKLLLRLYD 53
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 2-23 1.85e-04

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 40.60  E-value: 1.85e-04
                         10        20
                 ....*....|....*....|..
gi 647263443   2 KRIAIVGAVGAGKTTLFNALQG 23
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLG 398
VI_IcmF TIGR03348
type VI secretion protein IcmF; Members of this protein family are IcmF homologs and tend to ...
 6-149 2.07e-04

type VI secretion protein IcmF; Members of this protein family are IcmF homologs and tend to be associated with type VI secretion systems. [Cellular processes, Pathogenesis]


Pssm-ID: 274531 [Multi-domain]  Cd Length: 1169  Bit Score: 40.40  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443     6 IVGAVGAGKTTLFNALQGNYSLARKTQALEFNDRGD--------------IDTPGEYfshprwyhalitTLQDVDtliyv 71
Cdd:TIGR03348  116 VIGPPGSGKTTLLQNSGLKFPLAERLGAAALRGVGGtrncdwwftdeavlIDTAGRY------------TTQDSD----- 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443    72 hAANDTESRLppGLLDiGSRKH--------LIVAISKTDLPDANVA-------AVRQ----LLEGMGFQAPV-FALNGCD 131
Cdd:TIGR03348  179 -PEEDAAAWL--GFLG-LLRKHrrrqplngVVVTVSLADLLTADPAerkaharAIRQrlqeLREQLGARFPVyLVLTKAD 254

                          170
                   ....*....|....*...
gi 647263443   132 pqSVAPLENYLSELSQKE 149
Cdd:TIGR03348  255 --LLAGFEEFFADLDAEE 270
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 2-46 2.10e-04

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: 39.69  E-value: 2.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647263443   2 KRIAIVGAVGAGKTTLFNALQGNYSLA---------------RKTQALEFNDRGD-IDTPG 46
Cdd:cd01854   86 KTSVLVGQSGVGKSTLLNALLPELVLAtgeiseklgrgrhttTHRELFPLPGGGLiIDTPG 146
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 2-48 2.18e-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: 39.36  E-value: 2.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 647263443    2 KRIAIVGAVGAGKTTLFNALQG------NYS---LARKTQALEFNDRGD--IDTPGEY 48
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGanqhvgNWPgvtVEKKEGKFKYKGYEIeiVDLPGIY 58
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 2-23 7.12e-04

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 38.97  E-value: 7.12e-04
                         10        20
                 ....*....|....*....|..
gi 647263443   2 KRIAIVGAVGAGKTTLFNALQG 23
Cdd:COG4988  364 ERVALVGPSGAGKSTLLNLLLG 385
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 3-23 7.13e-04

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 38.89  E-value: 7.13e-04
                         10        20
                 ....*....|....*....|.
gi 647263443   3 RIAIVGAVGAGKTTLFNALQG 23
Cdd:COG0488  343 RIGLIGPNGAGKSTLLKLLAG 363
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 4-149 7.35e-04

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 37.84  E-value: 7.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443   4 IAIVGAVGAGKTTLFNALQGNySLARK-----TQ---ALEFNDRGD------IDTPG-EYFSHPRWYHALITtlqdvDTL 68
Cdd:cd01887    3 VTVMGHVDHGKTTLLDKIRKT-NVAAGeaggiTQhigAYQVPIDVKipgitfIDTPGhEAFTNMRARGASVT-----DIA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443  69 IYVHAANDtesrlppGL--LDIGSRKHL-------IVAISKTDLP---DANVAAVRQLLEGMGFQ----------APVFA 126
Cdd:cd01887   77 ILVVAADD-------GVmpQTIEAINHAkaanvpiIVAINKIDKPygtEADPERVKNELSELGLVgeewggdvsiVPISA 149

                        170       180
                 ....*....|....*....|...
gi 647263443 127 LNGcdpQSVAPLENYLSELSQKE 149
Cdd:cd01887  150 KTG---EGIDDLLEAILLLAEVL 169
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 3-23 9.47e-04

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: 37.43  E-value: 9.47e-04
                         10        20
                 ....*....|....*....|.
gi 647263443   3 RIAIVGAVGAGKTTLFNALQG 23
Cdd:cd03221   28 RIGLVGRNGAGKSTLLKLIAG 48
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 2-46 1.29e-03

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: 37.52  E-value: 1.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647263443    2 KRIAIVGAVGAGKTTLFNALQGNYSLA---------------RKTQALEFNDRGD-IDTPG 46
Cdd:pfam03193 107 KTTVLAGQSGVGKSTLLNALLPELDLRtgeiseklgrgrhttTHVELFPLPGGGLlIDTPG 167
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-25 1.39e-03

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 37.84  E-value: 1.39e-03
                         10        20
                 ....*....|....*....|....
gi 647263443   2 KRIAIVGAVGAGKTTLFNALQGNY 25
Cdd:COG1132  367 ETVALVGPSGSGKSTLVNLLLRFY 390
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 85-159 1.55e-03

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 37.97  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443  85 LLDIgsrKHLIVAISKTDLPD----ANVAA-VRQLLEGMGF-QAPVFALNGCDPQSVAPLENYLSELSQKEEGPGEETHY 158
Cdd:COG3276  101 LLGI---KRGIVVLTKADLVDeewlELVEEeIRELLAGTFLeDAPIVPVSAVTGEGIDELRAALDALAAAVPARDADGPF 177


                 .
gi 647263443 159 R 159
Cdd:COG3276  178 R 178
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 5-48 1.75e-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: 36.67  E-value: 1.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 647263443   5 AIVGAVGAGKTTLFNAL----Q--GNYS---LARKTQALEFNDRGD--IDTPGEY 48
Cdd:cd01879    1 ALVGNPNVGKTTLFNALtgarQkvGNWPgvtVEKKEGEFKLGGKEIeiVDLPGTY 55
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 4-42 1.78e-03

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 37.37  E-value: 1.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 647263443   4 IAIVGAVGAGKTTLFNALQGNYSLarktqalefnDRGDI 42
Cdd:COG1101   35 VTVIGSNGAGKSTLLNAIAGSLPP----------DSGSI 63
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 65-143 2.25e-03

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: 36.99  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647263443  65 VDTLIYVHAANDTEsrLPPGLLDigsrKHLIVA----------ISKTDL-PDANVAAVRQLLEGMGFqaPVFALNGCDPQ 133
Cdd:cd01854    3 VDQVLIVFSLKEPF--FNLRLLD----RYLVAAeasgiepvivLNKADLvDDEELEELLEIYEKLGY--PVLAVSAKTGE 74

                         90
                 ....*....|
gi 647263443 134 SVAPLENYLS 143
Cdd:cd01854   75 GLDELRELLK 84
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
 2-58 2.81e-03

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.


Pssm-ID: 410874 [Multi-domain]  Cd Length: 177  Bit Score: 36.36  E-value: 2.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647263443   2 KRIAIVGAVGAGKTTLFNALqgnyslarkTQALEFNDRgdI----DTPGEYFSHPRWYHAL 58
Cdd:cd01130   13 KNILISGGTGSGKTTLLNAL---------LSFIPPDER--IvtieDTRELQLPHPNVVHLL 62
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 3-23 2.99e-03

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 36.97  E-value: 2.99e-03
                         10        20
                 ....*....|....*....|.
gi 647263443   3 RIAIVGAVGAGKTTLFNALQG 23
Cdd:COG0488   26 RIGLVGRNGAGKSTLLKILAG 46
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 4-46 4.95e-03

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: 35.56  E-value: 4.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 647263443   4 IAIVGAVGAGKTTLFNALQGNYSLAR------KTQALEFNDRGD----IDTPG 46
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTNRKKLARtsktpgRTQLINFFNVGDkfrlVDLPG 54
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 4-24 5.21e-03

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily 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-resisting 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.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 35.91  E-value: 5.21e-03
                         10        20
                 ....*....|....*....|.
gi 647263443   4 IAIVGAVGAGKTTLFNALQGN 24
Cdd:cd03250   34 VAIVGPVGSGKSSLLSALLGE 54
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
4-22 5.42e-03

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 36.09  E-value: 5.42e-03
                         10
                 ....*....|....*....
gi 647263443   4 IAIVGAVGAGKTTLFNALQ 22
Cdd:PRK13657 364 VAIVGPTGAGKSTLINLLQ 382
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 2-23 6.41e-03

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 35.77  E-value: 6.41e-03
                         10        20
                 ....*....|....*....|..
gi 647263443   2 KRIAIVGAVGAGKTTLFNALQG 23
Cdd:COG1122   28 EFVAIIGPNGSGKSTLLRLLNG 49
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 1-44 8.13e-03

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


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 35.04  E-value: 8.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 647263443   1 MKRIAIVGAVGAGKTTL----FNALQGNYSLArktqALEfndrGDIDT 44
Cdd:COG0378   13 VLAVNLMGSPGSGKTTLlektIRALKDRLRIA----VIE----GDIYT 52
PRK01889 PRK01889
GTPase RsgA; Reviewed
 2-46 8.31e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 35.68  E-value: 8.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647263443   2 KRIAIVGAVGAGKTTLFNALQGNYSLArkTQAL-EFNDRGD-----------------IDTPG 46
Cdd:PRK01889 196 KTVALLGSSGVGKSTLVNALLGEEVQK--TGAVrEDDSKGRhttthrelhplpsggllIDTPG 256
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 2-23 8.74e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. 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: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 34.91  E-value: 8.74e-03
                         10        20
                 ....*....|....*....|..
gi 647263443   2 KRIAIVGAVGAGKTTLFNALQG 23
Cdd:cd00267   26 EIVALVGPNGSGKSTLLRAIAG 47
Dck COG1428
Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];
1-21 8.86e-03

Deoxyadenosine/deoxycytidine kinase [Nucleotide transport and metabolism];


Pssm-ID: 441037 [Multi-domain]  Cd Length: 205  Bit Score: 35.15  E-value: 8.86e-03
                         10        20
                 ....*....|....*....|.
gi 647263443   1 MKRIAIVGAVGAGKTTLFNAL 21
Cdd:COG1428    3 PRYIAVEGNIGAGKTTLARLL 23
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 4-23 9.22e-03

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 34.83  E-value: 9.22e-03
                         10        20
                 ....*....|....*....|
gi 647263443   4 IAIVGAVGAGKTTLFNALQG 23
Cdd:cd03213   38 TAIMGPSGAGKSTLLNALAG 57
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 4-25 9.37e-03

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 35.35  E-value: 9.37e-03
                         10        20
                 ....*....|....*....|..
gi 647263443   4 IAIVGAVGAGKTTLFNALQGNY 25
Cdd:PRK11300  34 VSLIGPNGAGKTTVFNCLTGFY 55
 
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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