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Conserved domains on  [gi|446743515|ref|WP_000820771|]
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MULTISPECIES: ethanolamine utilization acetate kinase EutP [Enterobacteriaceae]

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 1.75e-119

ethanolamine utilization acetate kinase EutP;


:

Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 333.47  E-value: 1.75e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   1 MKRIAFVGTVGAGKTTLFNALQGDYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446743515  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
Cdd:PRK15467  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
 
Name Accession Description Interval E-value
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-158 1.75e-119

ethanolamine utilization acetate kinase EutP;


Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 333.47  E-value: 1.75e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   1 MKRIAFVGTVGAGKTTLFNALQGDYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446743515  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
Cdd:PRK15467  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
EutP TIGR02528
ethanolamine utilization protein, EutP; This protein is found within operons which code for ...
 2-144 3.28e-73

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: 215.77  E-value: 3.28e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515    2 KRIAFVGTVGAGKTTLFNALQGDYTLARKTQAVEFNDkGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESRL 81
Cdd:TIGR02528   1 KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYND-GAIDTPGEYVENRRLYSALIVTAADADVIALVQSATDPESRF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446743515   82 PAGLLDIGVsKRQIAVISKTDMPDADVAATR-KLLLETGFEEPIFELNSHDPQSVQQLVDYLAS 144
Cdd:TIGR02528  80 PPGFASIFV-KPVIGLVTKIDLAEADVDIERaKELLETAGAEPIFEISSVDEQGLEALVDYLNS 142
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 1-148 6.77e-72

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: 212.74  E-value: 6.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   1 MKRIAFVGTVGAGKTTLFNALQGDYTLARKTQAVEFNDkGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:COG4917    1 MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYD-NIIDTPGEYIENPRFYKALIATAQDADVIVLVQDATEPRSV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446743515  81 LPAGLLDIGvSKRQIAVISKTDMPDADVAATRKLLLETGFeEPIFELNSHDPQSVQQLVDYLASLTKQ 148
Cdd:COG4917   80 FPPGFAKAF-NKPVIGVITKIDLPEADVERARKWLKSAGV-EPIFIVSSVTGEGIEELKEYLEELGDE 145
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-138 3.07e-32

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: 111.60  E-value: 3.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515    1 MKRIAFVGTVGAGKTTLFNALQGDYTLARKTQAVEFNDkGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYD-NAIDTPGEYLENRRYYSALIVTSADADVIALVQDATEPEST 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   81 LPAGLLDIgVSKRQIAVISKTDMP--DADVAATRKLLLETGFEEpIFELNSHDPQSVQQL 138
Cdd:pfam10662  80 FPPGFASM-FNKPVIGIITKIDLAkdEANIEIAEEWLSLAGAQK-IFRISAVEKIGIEEL 137
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 5-144 2.83e-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: 60.93  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   5 AFVGTVGAGKTTLFNALQGDY----------TLARKTQAVEFNDKGD----IDTPG-EYFSHPRWYHALITTLQDVDMLI 69
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEvgevsdvpgtTRDPDVYVKELDKGKVklvlVDTPGlDEFGGLGREELARLLLRGADLIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515  70 YVHGANDPESRLPAGLLDI----GVSKRQIAVISKTDMPDADV--AATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLA 143
Cdd:cd00882   81 LVVDSTDRESEEDAKLLILrrlrKEGIPIILVGNKIDLLEEREveELLRLEELAKILGVPVFEVSAKTGEGVDELFEKLI 160


                 .
gi 446743515 144 S 144
Cdd:cd00882  161 E 161
 
Name Accession Description Interval E-value
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-158 1.75e-119

ethanolamine utilization acetate kinase EutP;


Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 333.47  E-value: 1.75e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   1 MKRIAFVGTVGAGKTTLFNALQGDYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446743515  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
Cdd:PRK15467  81 LPAGLLDIGVSKRQIAVISKTDMPDADVAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASLTKQEEAGEKTHHS 158
EutP TIGR02528
ethanolamine utilization protein, EutP; This protein is found within operons which code for ...
 2-144 3.28e-73

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: 215.77  E-value: 3.28e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515    2 KRIAFVGTVGAGKTTLFNALQGDYTLARKTQAVEFNDkGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESRL 81
Cdd:TIGR02528   1 KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYND-GAIDTPGEYVENRRLYSALIVTAADADVIALVQSATDPESRF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446743515   82 PAGLLDIGVsKRQIAVISKTDMPDADVAATR-KLLLETGFEEPIFELNSHDPQSVQQLVDYLAS 144
Cdd:TIGR02528  80 PPGFASIFV-KPVIGLVTKIDLAEADVDIERaKELLETAGAEPIFEISSVDEQGLEALVDYLNS 142
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 1-148 6.77e-72

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: 212.74  E-value: 6.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   1 MKRIAFVGTVGAGKTTLFNALQGDYTLARKTQAVEFNDkGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:COG4917    1 MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYD-NIIDTPGEYIENPRFYKALIATAQDADVIVLVQDATEPRSV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446743515  81 LPAGLLDIGvSKRQIAVISKTDMPDADVAATRKLLLETGFeEPIFELNSHDPQSVQQLVDYLASLTKQ 148
Cdd:COG4917   80 FPPGFAKAF-NKPVIGVITKIDLPEADVERARKWLKSAGV-EPIFIVSSVTGEGIEELKEYLEELGDE 145
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-138 3.07e-32

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: 111.60  E-value: 3.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515    1 MKRIAFVGTVGAGKTTLFNALQGDYTLARKTQAVEFNDkGDIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYD-NAIDTPGEYLENRRYYSALIVTSADADVIALVQDATEPEST 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   81 LPAGLLDIgVSKRQIAVISKTDMP--DADVAATRKLLLETGFEEpIFELNSHDPQSVQQL 138
Cdd:pfam10662  80 FPPGFASM-FNKPVIGIITKIDLAkdEANIEIAEEWLSLAGAQK-IFRISAVEKIGIEEL 137
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
2-150 5.13e-14

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 65.77  E-value: 5.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   2 KRIAFVGTVGAGKTTLFNALQGDYTLARKTQA--------VEFNDKGD------IDTPGEYFSHPrwYHA-LITTLQDVD 66
Cdd:COG1100    4 KKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLStngvtidkKELKLDGLdvdlviWDTPGQDEFRE--TRQfYARQLTGAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515  67 MLIYVHGANDPESRLPA-----GLLDIGVSKRQIAVISKTD-MPDADVAATRKL--LLETGFEEPIFELNSHDPQSVQQL 138
Cdd:COG1100   82 LYLFVVDGTREETLQSLyelleSLRRLGKKSPIILVLNKIDlYDEEEIEDEERLkeALSEDNIVEVVATSAKTGEGVEEL 161

                        170
                 ....*....|..
gi 446743515 139 VDYLASLTKQEE 150
Cdd:COG1100  162 FAALAEILRGEG 173
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 5-144 2.83e-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: 60.93  E-value: 2.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   5 AFVGTVGAGKTTLFNALQGDY----------TLARKTQAVEFNDKGD----IDTPG-EYFSHPRWYHALITTLQDVDMLI 69
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEvgevsdvpgtTRDPDVYVKELDKGKVklvlVDTPGlDEFGGLGREELARLLLRGADLIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515  70 YVHGANDPESRLPAGLLDI----GVSKRQIAVISKTDMPDADV--AATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLA 143
Cdd:cd00882   81 LVVDSTDRESEEDAKLLILrrlrKEGIPIILVGNKIDLLEEREveELLRLEELAKILGVPVFEVSAKTGEGVDELFEKLI 160


                 .
gi 446743515 144 S 144
Cdd:cd00882  161 E 161
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 5-145 1.87e-09

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: 53.40  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   5 AFVGTVGAGKTTLFNALQGDY----------TLARKTQAVEFNDKGD---IDTPGEYF---SHPRWYHALITTLQDVDML 68
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNvgivspipgtTRDPVRKEWELLPLGPvvlIDTPGLDEeggLGRERVEEARQVADRADLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515  69 IYVHGANDPESRLPAGLLDIGVS-KRQIAVISKTDMPDAD--VAATRKLLLETGFEEPIFELNSHDPQSVQQLVDYLASL 145
Cdd:cd00880   81 LLVVDSDLTPVEEEAKLGLLRERgKPVLLVLNKIDLVPESeeEELLRERKLELLPDLPVIAVSALPGEGIDELRKKIAEL 160
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 1-145 1.05e-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: 48.99  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   1 MKRIAFVGTVGAGKTTLFNALQGDYTLAR---------KTQAVEFNDKGDI---DTPGeyF-SH-PrwyHALI----TTL 62
Cdd:cd01878   41 VPTVALVGYTNAGKSTLFNALTGADVLAEdqlfatldpTTRRIKLPGGREVlltDTVG--FiRDlP---HQLVeafrSTL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515  63 QDV---DMLIYVHGANDP--ESRLPAG---LLDIGVS-KRQIAVISKTDMPDADVAATRkllLETGFEEPIFeLNSHDPQ 133
Cdd:cd01878  116 EEVaeaDLLLHVVDASDPdrEEQIETVeevLKELGADdIPIILVLNKIDLLDDEELEER---LRAGRPDAVF-ISAKTGE 191

                        170
                 ....*....|..
gi 446743515 134 SVQQLVDYLASL 145
Cdd:cd01878  192 GLDLLKEAIEEL 203
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 7-151 1.14e-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: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   7 VGTVGA---GKTTLFNALQGDYTLARKTQ--------------AVEFNDK-GDIDTPGeyfsHPRWYHALITTLQDVDML 68
Cdd:cd04171    2 IGTAGHidhGKTTLIKALTGIETDRLPEEkkrgitidlgfaylDLPDGKRlGFIDVPG----HEKFVKNMLAGAGGIDAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515  69 IYVHGAND---PESR---LPAGLLDIgvsKRQIAVISKTDMPDAD----VAATRKLLLETGFEE--PIFELNSHDPQSVQ 136
Cdd:cd04171   78 LLVVAADEgimPQTRehlEILELLGI---KKGLVVLTKADLVDEDrlelVEEEILELLAGTFLAdaPIFPVSSVTGEGIE 154

                        170
                 ....*....|....*
gi 446743515 137 QLVDYLASLTKQEEA 151
Cdd:cd04171  155 ELKNYLDELAEPQSK 169
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 2-142 1.61e-07

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: 48.14  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515    2 KRIAFVGTVGAGKTTLFNALQGDY--------TLARKTQAVEFNDKGD------IDTPGEYFSHPRWYHALITT---LQD 64
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKgsiteyypGTTRNYVTTVIEEDGKtykfnlLDTAGQEDYDAIRRLYYPQVersLRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   65 VDMLIYVHGAND---PESRLPAGLLDIGVSKrqIAVISKTDMPDADV-AATRKLLLETGFeEPIFELNSHDPQSVQQLVD 140
Cdd:TIGR00231  82 FDIVILVLDVEEileKQTKEIIHHADSGVPI--ILVGNKIDLKDADLkTHVASEFAKLNG-EPIIPLSAETGKNIDSAFK 158


                  ..
gi 446743515  141 YL 142
Cdd:TIGR00231 159 IV 160
YeeP COG3596
Predicted GTPase [General function prediction only];
3-77 1.07e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.07  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   3 RIAFVGTVGAGKTTLFNALQG------DYTLA--RKTQAVEFNDKGD-----IDTPGeYFS---HPRWYHALITTLQDVD 66
Cdd:COG3596   41 VIALVGKTGAGKSSLINALFGaevaevGVGRPctREIQRYRLESDGLpglvlLDTPG-LGEvneRDREYRELRELLPEAD 119

                         90
                 ....*....|.
gi 446743515  67 MLIYVHGANDP 77
Cdd:COG3596  120 LILWVVKADDR 130
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 3-100 1.14e-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: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515    3 RIAFVGTVGAGKTTLFNALQGDYTLA-------RKTQAVEFNDKGD----IDTPGEYFSHPRWYHALIT--TLQDVDMLI 69
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVsdypgttRDPNEGRLELKGKqiilVDTPGLIEGASEGEGLGRAflAIIEADLIL 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 446743515   70 YVHGANDPESRLPAGLLDIGVS--KRQIAVISK 100
Cdd:pfam01926  81 FVVDSEEGITPLDEELLELLREnkKPIILVLNK 113
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 5-80 1.92e-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: 41.94  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   5 AFVGTVGAGKTTLFNAL-QGDYTL-------ARKTQAVEFNDKGD----IDTPG--EYFSHPRWYHALI-TTLQDVDMLI 69
Cdd:cd11383    1 GLMGKTGAGKSSLCNALfGTEVAAvgdrrptTRAAQAYVWQTGGDglvlLDLPGvgERGRRDREYEELYrRLLPEADLVL 80

                         90
                 ....*....|.
gi 446743515  70 YVhgaNDPESR 80
Cdd:cd11383   81 WL---LDADDR 88
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 2-46 2.64e-05

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


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 42.39  E-value: 2.64e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446743515   2 KRIAFVGTVGAGKTTLFNALQGDytLARKTQAV-----------------EFNDKGD-IDTPG 46
Cdd:cd01854   86 KTSVLVGQSGVGKSTLLNALLPE--LVLATGEIseklgrgrhttthrelfPLPGGGLiIDTPG 146
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 6-145 3.43e-05

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


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 41.68  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   6 FVGTVG---AGKTTLFNAL-------------------QGDYTLArKTQAVeFndkgdIDTPGEYFSHPRWYHAL----I 59
Cdd:cd04163    5 FVAIIGrpnVGKSTLLNALvgqkisivspkpqttrnriRGIYTDD-DAQII-F-----VDTPGIHKPKKKLGERMvkaaW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515  60 TTLQDVDMLIYVHGANDPESRLPAGLLDI--GVSKRQIAVISKTD--MPDADVAATRKLLLETGFEEPIFELNSHDPQSV 135
Cdd:cd04163   78 SALKDVDLVLFVVDASEWIGEGDEFILELlkKSKTPVILVLNKIDlvKDKEDLLPLLEKLKELHPFAEIFPISALKGENV 157

                        170
                 ....*....|
gi 446743515 136 QQLVDYLASL 145
Cdd:cd04163  158 DELLEYIVEY 167
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 2-48 6.18e-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: 40.90  E-value: 6.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446743515    2 KRIAFVGTVGAGKTTLFNALQGDY---------TLARKTQAVEFNDKGD--IDTPGEY 48
Cdd:pfam02421   1 ITIALVGNPNVGKTTLFNALTGANqhvgnwpgvTVEKKEGKFKYKGYEIeiVDLPGIY 58
era PRK00089
GTPase Era; Reviewed
 1-145 7.67e-05

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 41.57  E-value: 7.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   1 MKRIAFVGTVG---AGKTTLFNAL-------------------QGDYTLArKTQAVeFndkgdIDTPGeyFSHPRwyHAL 58
Cdd:PRK00089   2 GFKSGFVAIVGrpnVGKSTLLNALvgqkisivspkpqttrhriRGIVTED-DAQII-F-----VDTPG--IHKPK--RAL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515  59 --------ITTLQDVDMLIYVHGAND---PESRLPAGLLdIGVSKRQIAVISKTDM--PDADVAATRKLLLETGFEEPIF 125
Cdd:PRK00089  71 nramnkaaWSSLKDVDLVLFVVDADEkigPGDEFILEKL-KKVKTPVILVLNKIDLvkDKEELLPLLEELSELMDFAEIV 149

                        170       180
                 ....*....|....*....|
gi 446743515 126 ELNSHDPQSVQQLVDYLASL 145
Cdd:PRK00089 150 PISALKGDNVDELLDVIAKY 169
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 3-150 1.19e-04

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 40.84  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   3 RIAFVGTVGAGKTTLFNALQGDYTLAR---------KTQAVEFNDKGDI---DTPGeyF-SH-PrwyHALI----TTLQD 64
Cdd:COG2262  201 TVALVGYTNAGKSTLFNRLTGADVLAEdklfatldpTTRRLELPDGRPVlltDTVG--FiRKlP---HQLVeafrSTLEE 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515  65 V---DMLIYVHGANDPESRLPAG-----LLDIGVS-KRQIAVISKTDMPDADVAATrkllLETGFEEPIFeLNSHDPQSV 135
Cdd:COG2262  276 VreaDLLLHVVDASDPDFEEQIEtvnevLEELGADdKPIILVFNKIDLLDDEELER----LRAGYPDAVF-ISAKTGEGI 350

                        170
                 ....*....|....*
gi 446743515 136 QQLVDYLASLTKQEE 150
Cdd:COG2262  351 DELLEAIEERLPEDR 365
PRK01889 PRK01889
GTPase RsgA; Reviewed
 2-46 1.25e-04

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 41.07  E-value: 1.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446743515   2 KRIAFVGTVGAGKTTLFNALQGDYTLArkTQAV-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 1.43e-04

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


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 40.22  E-value: 1.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446743515    2 KRIAFVGTVGAGKTTLFNALQGDYTLA---------------RKTQAVEFNDKGD-IDTPG 46
Cdd:pfam03193 107 KTTVLAGQSGVGKSTLLNALLPELDLRtgeiseklgrgrhttTHVELFPLPGGGLlIDTPG 167
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 2-26 5.85e-04

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


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 39.05  E-value: 5.85e-04
                         10        20
                 ....*....|....*....|....*
gi 446743515   2 KRIAFVGTVGAGKTTLFNALQGDYT 26
Cdd:COG2274  502 ERVAIVGRSGSGKSTLLKLLLGLYE 526
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
 5-48 6.18e-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: 38.21  E-value: 6.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446743515   5 AFVGTVGAGKTTLFNALQGDY---------TLARKTQAVEFNDKGD--IDTPGEY 48
Cdd:cd01879    1 ALVGNPNVGKTTLFNALTGARqkvgnwpgvTVEKKEGEFKLGGKEIeiVDLPGTY 55
obgE PRK12299
GTPase CgtA; Reviewed
 84-154 1.08e-03

GTPase CgtA; Reviewed


Pssm-ID: 237048 [Multi-domain]  Cd Length: 335  Bit Score: 38.13  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446743515  84 GLLDigvsKRQIAVISKTDMPDADVAATRKLLLE-TGFEEPIFELNSHDPQSVQQLVDYLASLTKQEEAGEK 154
Cdd:PRK12299 268 ELAD----KPRILVLNKIDLLDEEEEREKRAALElAALGGPVFLISAVTGEGLDELLRALWELLEEARREEE 335
FeoB COG0370
Fe2+ transporter FeoB [Inorganic ion transport and metabolism];
1-48 1.59e-03

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


Pssm-ID: 440139 [Multi-domain]  Cd Length: 662  Bit Score: 37.79  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446743515   1 MKRIAFVGTVGAGKTTLFNAL----Q--GDY---TLARKTQAVEFNDKGD--IDTPGEY 48
Cdd:COG0370    3 MITIALVGNPNVGKTTLFNALtgsrQkvGNWpgvTVEKKEGKFKLKGKEIelVDLPGTY 61
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 2-25 1.80e-03

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 36.98  E-value: 1.80e-03
                         10        20
                 ....*....|....*....|....
gi 446743515   2 KRIAFVGTVGAGKTTLFNALQGDY 25
Cdd:cd03228   29 EKVAIVGPSGSGKSTLLKLLLRLY 52
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 2-23 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
                 ....*....|....*....|..
gi 446743515   2 KRIAFVGTVGAGKTTLFNALQG 23
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLG 398
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 2-71 2.00e-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: 36.92  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   2 KRIAFVGTVGAGKTTLFNALQGDYTlaRKTQA------VEFNDKGD-------IDTPGeyfsHPRWYHALITTLQDVDM- 67
Cdd:cd04105    1 PTVLLLGPSDSGKTALFTKLTTGKV--RSTVTsiepnvASFYSNSSkgkkltlVDVPG----HEKLRDKLLEYLKASLKa 74


                 ....
gi 446743515  68 LIYV 71
Cdd:cd04105   75 IVFV 78
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 2-26 2.75e-03

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 36.09  E-value: 2.75e-03
                          10        20
                  ....*....|....*....|....*
gi 446743515    2 KRIAFVGTVGAGKTTLFNALQGDYT 26
Cdd:pfam00005  12 EILALVGPNGAGKSTLLKLIAGLLS 36
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 1-44 5.66e-03

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


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 35.81  E-value: 5.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446743515   1 MKRIAFVGTVGAGKTTL----FNALQGDYTLArktqAVEfndkGDIDT 44
Cdd:COG0378   13 VLAVNLMGSPGSGKTTLlektIRALKDRLRIA----VIE----GDIYT 52
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 3-71 6.66e-03

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


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 35.21  E-value: 6.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446743515   3 RIAFVGTVGAGKTTLFNALQGD------------------YTLARKtqaVEFndkgdIDTPG--EYFSHprwyHALITT- 61
Cdd:cd09912    2 LLAVVGEFSAGKSTLLNALLGEevlptgvtpttavitvlrYGLLKG---VVL-----VDTPGlnSTIEH----HTEITEs 69

                         90
                 ....*....|.
gi 446743515  62 -LQDVDMLIYV 71
Cdd:cd09912   70 fLPRADAVIFV 80
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 4-64 7.14e-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: 7.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446743515   4 IAFVGTVGAGKTTLFNALQGDYTlarktqavefNDKGDI---DTPGEYFSHPRWYHALITTLQD 64
Cdd:cd03254   32 VAIVGPTGAGKTTLINLLMRFYD----------PQKGQIlidGIDIRDISRKSLRSMIGVVLQD 85
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-25 8.05e-03

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 35.53  E-value: 8.05e-03
                         10        20
                 ....*....|....*....|....
gi 446743515   2 KRIAFVGTVGAGKTTLFNALQGDY 25
Cdd:COG1132  367 ETVALVGPSGSGKSTLVNLLLRFY 390
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 3-24 9.66e-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: 9.66e-03
                         10        20
                 ....*....|....*....|..
gi 446743515   3 RIAFVGTVGAGKTTLFNALQGD 24
Cdd:COG0488  343 RIGLIGPNGAGKSTLLKLLAGE 364
 
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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