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Conserved domains on  [gi|2755704908|ref|WP_354596972|]
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GTPase [Streptomyces sp. JL1001]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 126-323 2.95e-35

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd11383:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 140  Bit Score: 129.77  E-value: 2.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 126 AVAGATGSGKSTLFNALAGAPISDTGLRRPTTSQPIACSWTDGaaglldrlavpgrlrrrphpgpaafdeaLQGLVLVDL 205
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTG----------------------------GDGLVLLDL 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 206 PDHDSAAIEHRD---QVDRVLALVDAVIWVVDPEKYADAALHERYLRPLAGHAEVTFVVLNQTDrlpgeaadlvlddlrr 282
Cdd:cd11383    53 PGVGERGRRDREyeeLYRRLLPEADLVLWLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVD---------------- 116

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2755704908 283 lldedgialgehgepgaTVMSLSALTGDGVPELREMIGRFV 323
Cdd:cd11383   117 -----------------PVLAVSARTGWGLDELAEALITAL 140
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 179-612 2.96e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.09  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  179 PGRLRRRPHPGPAAFDEALQGLVLVDLPDHDSAAIEHRDQVDRVLALVDAVIWVVDPEKYADAALHERYLRPLAGHAEVT 258
Cdd:COG3321    854 PGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  259 FVVLNQTDRLPGEAADLVLDDLRRLLDEDGIALGEHGEPGATVMSLSALTGDGVPELREMIGRFVSDRTAATRRLSADVD 338
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  339 AAAARLRKVYVAQGRPGLGERAREEFADRLAEAVGAAAAGQAAEREW-----RRNASRACGTPWLRLWRWYENRGLPGSL 413
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAAlalalAALLLLAALAELALAAAALALAAALAAA 1093

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  414 DRLGQALTPPEEELTARQRVEQAVRIVADDAADGLPGPWAQAVREAAFTGAQGLPEALDELAVKAGAPGAAKRGGGTETG 493
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  494 KGKSAVDRLGGRPPKPPRPKWWPAAVLAQASMTLLQIFGGLWLVGQIIGVLEPGLVTPALIMLGGVVGGPLVEWACAAAI 573
Cdd:COG3321   1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2755704908  574 RGPARRYGQDAERRLREAAAGCGRARVLDPVAAELVRYR 612
Cdd:COG3321   1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAA 1292
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 103-145 2.43e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member PRK09270:

Pssm-ID: 450170  Cd Length: 229  Bit Score: 39.92  E-value: 2.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2755704908 103 AEAGRVLDEAAARQRLSSRHTVVAVAGATGSGKSTLFNALAGA 145
Cdd:PRK09270   14 AVHKPLLRRLAALQAEPQRRTIVGIAGPPGAGKSTLAEFLEAL 56
 
Name Accession Description Interval E-value
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 126-323 2.95e-35

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: 129.77  E-value: 2.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 126 AVAGATGSGKSTLFNALAGAPISDTGLRRPTTSQPIACSWTDGaaglldrlavpgrlrrrphpgpaafdeaLQGLVLVDL 205
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTG----------------------------GDGLVLLDL 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 206 PDHDSAAIEHRD---QVDRVLALVDAVIWVVDPEKYADAALHERYLRPLAGHAEVTFVVLNQTDrlpgeaadlvlddlrr 282
Cdd:cd11383    53 PGVGERGRRDREyeeLYRRLLPEADLVLWLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVD---------------- 116

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2755704908 283 lldedgialgehgepgaTVMSLSALTGDGVPELREMIGRFV 323
Cdd:cd11383   117 -----------------PVLAVSARTGWGLDELAEALITAL 140
YeeP COG3596
Predicted GTPase [General function prediction only];
103-341 6.01e-26

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 108.70  E-value: 6.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 103 AEAGRVLDEAAARQRLSSRHTVVAVAGATGSGKSTLFNALAGAPISDTGLRRPTTSQPIACSWTdgaaglldrlavpgrl 182
Cdd:COG3596    20 QVLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLE---------------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 183 rrrphpgpaafDEALQGLVLVDLPDHDSAAIEHR--DQVDRVLALVDAVIWVVDPEKYADAALHERYLRPLAGHA-EVTF 259
Cdd:COG3596    84 -----------SDGLPGLVLLDTPGLGEVNERDReyRELRELLPEADLILWVVKADDRALATDEEFLQALRAQYPdPPVL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 260 VVLNQTDRLPGEAADLVLDDLRRLLDEDGI-----ALGEH-GEPGATVMSLSALTGD---GVPELREMIGRFVSDrtAAT 330
Cdd:COG3596   153 VVLTQVDRLEPEREWDPPYNWPSPPKEQNIrraleAIAEQlGVPIDRVIPVSAAEDRtgyGLEELVDALAEALPE--AKR 230

                         250
                  ....*....|.
gi 2755704908 331 RRLSADVDAAA 341
Cdd:COG3596   231 SRLARLLRAKA 241
Dynamin_N pfam00350
Dynamin family;
125-264 5.06e-09

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 55.70  E-value: 5.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 125 VAVAGATGSGKSTLFNALAGAPISDTGLRrPTTSQPIA---------------CSWTDGAAGLLD----RLAVPGRLRRR 185
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPG-PTTRRPTVlrlgespgasegavkVEYKDGEKKFEDfselREEIEKETEKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 186 PHPGPAAFDEAL---------QGLVLVDLPDHDSAAIEHRDQVDRVLALVDAVIWVVD---PEKYADAALHERYLRPlag 253
Cdd:pfam00350  80 AGTGKGISSEPIvleilsplvPGLTLVDTPGLDSVAVGDQELTKEYIKPADIILAVTPanvDLSTSEALFLAREVDP--- 156

                         170
                  ....*....|.
gi 2755704908 254 HAEVTFVVLNQ 264
Cdd:pfam00350 157 NGKRTIGVLTK 167
era PRK00089
GTPase Era; Reviewed
 125-319 7.02e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 48.12  E-value: 7.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 125 VAVAGATGSGKSTLFNALAGAPISDTGlRRP-TTsqpiacswtdgaaglldrlavpgrlRRRPHpGPAAFDEAlQgLVLV 203
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQKISIVS-PKPqTT-------------------------RHRIR-GIVTEDDA-Q-IIFV 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 204 DLPD-HDSaaiEHR------DQVDRVLALVDAVIWVVDPEKYADAalHERY-LRPLAGHAEVTFVVLNQTDRLPGEAADL 275
Cdd:PRK00089   59 DTPGiHKP---KRAlnramnKAAWSSLKDVDLVLFVVDADEKIGP--GDEFiLEKLKKVKTPVILVLNKIDLVKDKEELL 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2755704908 276 VLDDlrrlldedgiALGEHGEPGATVMsLSALTGDGVPELREMI 319
Cdd:PRK00089  134 PLLE----------ELSELMDFAEIVP-ISALKGDNVDELLDVI 166
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 179-612 2.96e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.09  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  179 PGRLRRRPHPGPAAFDEALQGLVLVDLPDHDSAAIEHRDQVDRVLALVDAVIWVVDPEKYADAALHERYLRPLAGHAEVT 258
Cdd:COG3321    854 PGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  259 FVVLNQTDRLPGEAADLVLDDLRRLLDEDGIALGEHGEPGATVMSLSALTGDGVPELREMIGRFVSDRTAATRRLSADVD 338
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  339 AAAARLRKVYVAQGRPGLGERAREEFADRLAEAVGAAAAGQAAEREW-----RRNASRACGTPWLRLWRWYENRGLPGSL 413
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAAlalalAALLLLAALAELALAAAALALAAALAAA 1093

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  414 DRLGQALTPPEEELTARQRVEQAVRIVADDAADGLPGPWAQAVREAAFTGAQGLPEALDELAVKAGAPGAAKRGGGTETG 493
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  494 KGKSAVDRLGGRPPKPPRPKWWPAAVLAQASMTLLQIFGGLWLVGQIIGVLEPGLVTPALIMLGGVVGGPLVEWACAAAI 573
Cdd:COG3321   1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2755704908  574 RGPARRYGQDAERRLREAAAGCGRARVLDPVAAELVRYR 612
Cdd:COG3321   1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAA 1292
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 103-145 2.43e-03

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 39.92  E-value: 2.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2755704908 103 AEAGRVLDEAAARQRLSSRHTVVAVAGATGSGKSTLFNALAGA 145
Cdd:PRK09270   14 AVHKPLLRRLAALQAEPQRRTIVGIAGPPGAGKSTLAEFLEAL 56
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
 103-145 8.26e-03

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 38.99  E-value: 8.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2755704908 103 AEAGRVLdEAAARQRLSsrhtvVAVAGATGSGKSTLFNALAGA 145
Cdd:COG4962   169 PEMAEFL-RAAVRARLN-----ILVSGGTGSGKTTLLNALSGF 205
 
Name Accession Description Interval E-value
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 126-323 2.95e-35

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: 129.77  E-value: 2.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 126 AVAGATGSGKSTLFNALAGAPISDTGLRRPTTSQPIACSWTDGaaglldrlavpgrlrrrphpgpaafdeaLQGLVLVDL 205
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAAQAYVWQTG----------------------------GDGLVLLDL 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 206 PDHDSAAIEHRD---QVDRVLALVDAVIWVVDPEKYADAALHERYLRPLAGHAEVTFVVLNQTDrlpgeaadlvlddlrr 282
Cdd:cd11383    53 PGVGERGRRDREyeeLYRRLLPEADLVLWLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVD---------------- 116

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2755704908 283 lldedgialgehgepgaTVMSLSALTGDGVPELREMIGRFV 323
Cdd:cd11383   117 -----------------PVLAVSARTGWGLDELAEALITAL 140
YeeP COG3596
Predicted GTPase [General function prediction only];
103-341 6.01e-26

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 108.70  E-value: 6.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 103 AEAGRVLDEAAARQRLSSRHTVVAVAGATGSGKSTLFNALAGAPISDTGLRRPTTSQPIACSWTdgaaglldrlavpgrl 182
Cdd:COG3596    20 QVLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLE---------------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 183 rrrphpgpaafDEALQGLVLVDLPDHDSAAIEHR--DQVDRVLALVDAVIWVVDPEKYADAALHERYLRPLAGHA-EVTF 259
Cdd:COG3596    84 -----------SDGLPGLVLLDTPGLGEVNERDReyRELRELLPEADLILWVVKADDRALATDEEFLQALRAQYPdPPVL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 260 VVLNQTDRLPGEAADLVLDDLRRLLDEDGI-----ALGEH-GEPGATVMSLSALTGD---GVPELREMIGRFVSDrtAAT 330
Cdd:COG3596   153 VVLTQVDRLEPEREWDPPYNWPSPPKEQNIrraleAIAEQlGVPIDRVIPVSAAEDRtgyGLEELVDALAEALPE--AKR 230

                         250
                  ....*....|.
gi 2755704908 331 RRLSADVDAAA 341
Cdd:COG3596   231 SRLARLLRAKA 241
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 126-319 3.57e-19

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: 84.82  E-value: 3.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 126 AVAGATGSGKSTLFNALAGAPISDTGLRRPTTSQPIACSWTdgaaglldrlavpgrlrrrphpgpaaFDEALQGLVLVDL 205
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKE--------------------------LDKGKVKLVLVDT 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 206 PDHDSAAIEHRDQ-VDRVLALVDAVIWVVDPEKYADAALHER-YLRPLAGHAEVTFVVLNQTDRLPGEAADLVLddlrrl 283
Cdd:cd00882    55 PGLDEFGGLGREElARLLLRGADLILLVVDSTDRESEEDAKLlILRRLRKEGIPIILVGNKIDLLEEREVEELL------ 128

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2755704908 284 ldedgIALGEHGEPGATVMSLSALTGDGVPELREMI 319
Cdd:cd00882   129 -----RLEELAKILGVPVFEVSAKTGEGVDELFEKL 159
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 126-319 1.15e-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: 57.64  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 126 AVAGATGSGKSTLFNALAGAPISDTGLRRPTTSQPIACSWTdgaaglldrlavpgrlrrrPHPgpaafdeaLQGLVLVDL 205
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGIVSPIPGTTRDPVRKEWE-------------------LLP--------LGPVVLIDT 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 206 PDHDSAAIEHRDQVDR---VLALVDAVIWVVD-----PEKYADAALHERYLRPLaghaevtFVVLNQTDRLPGEAadlvl 277
Cdd:cd00880    54 PGLDEEGGLGRERVEEarqVADRADLVLLVVDsdltpVEEEAKLGLLRERGKPV-------LLVLNKIDLVPESE----- 121

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2755704908 278 ddlRRLLDEDGIALGEHGEPGATVmslSALTGDGVPELREMI 319
Cdd:cd00880   122 ---EEELLRERKLELLPDLPVIAV---SALPGEGIDELRKKI 157
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 125-268 1.50e-09

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: 57.56  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 125 VAVAGATGSGKSTLFNALAGAPISDTGLrRPTTSQPIACSWtdgaaGLLDrlavpgrlrrrphpgpaafdealqGLVLVD 204
Cdd:cd09912     3 LAVVGEFSAGKSTLLNALLGEEVLPTGV-TPTTAVITVLRY-----GLLK------------------------GVVLVD 52

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2755704908 205 LPDHDSAAIEHRDQVDRVLALVDAVIWVVDpekyADAALHE---RYLRPLAG-HAEVTFVVLNQTDRL 268
Cdd:cd09912    53 TPGLNSTIEHHTEITESFLPRADAVIFVLS----ADQPLTEserEFLKEILKwSGKKIFFVLNKIDLL 116
Dynamin_N pfam00350
Dynamin family;
125-264 5.06e-09

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 55.70  E-value: 5.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 125 VAVAGATGSGKSTLFNALAGAPISDTGLRrPTTSQPIA---------------CSWTDGAAGLLD----RLAVPGRLRRR 185
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPG-PTTRRPTVlrlgespgasegavkVEYKDGEKKFEDfselREEIEKETEKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 186 PHPGPAAFDEAL---------QGLVLVDLPDHDSAAIEHRDQVDRVLALVDAVIWVVD---PEKYADAALHERYLRPlag 253
Cdd:pfam00350  80 AGTGKGISSEPIvleilsplvPGLTLVDTPGLDSVAVGDQELTKEYIKPADIILAVTPanvDLSTSEALFLAREVDP--- 156

                         170
                  ....*....|.
gi 2755704908 254 HAEVTFVVLNQ 264
Cdd:pfam00350 157 NGKRTIGVLTK 167
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 125-319 3.99e-08

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: 53.23  E-value: 3.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 125 VAVAGATGSGKSTLFNALAGAPISDTGlRRP-TTSQPIACSWTDGAAglldrlavpgrlrrrphpgpaafdealQgLVLV 203
Cdd:cd04163     6 VAIIGRPNVGKSTLLNALVGQKISIVS-PKPqTTRNRIRGIYTDDDA---------------------------Q-IIFV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 204 DLP----DHDSAAIEHRDQVDRVLALVDAVIWVVDPEKYADAaLHERYLRPLAGHAEVTFVVLNQTDRLPGEAADLVLDD 279
Cdd:cd04163    57 DTPgihkPKKKLGERMVKAAWSALKDVDLVLFVVDASEWIGE-GDEFILELLKKSKTPVILVLNKIDLVKDKEDLLPLLE 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2755704908 280 lrrlldedgiALGEHGEPGATVMsLSALTGDGVPELREMI 319
Cdd:cd04163   136 ----------KLKELHPFAEIFP-ISALKGENVDELLEYI 164
CrfC COG0699
Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, ...
 114-268 8.69e-08

Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, recombination and repair];


Pssm-ID: 440463 [Multi-domain]  Cd Length: 582  Bit Score: 55.03  E-value: 8.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 114 ARQRLSSRHTVVAVAGATGSGKSTLFNALAGAPISDTGLRRpTTSQPIACSWTDG--------AAGLLDRLAVPG----- 180
Cdd:COG0699    24 ARLDLADPSLRIVMAGTTSQGKSQLVNALLGRRLLPSGAGE-TTGVPTEIKHAEGssarllptAGSVADTKRWPGldtee 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 181 -----------RLRRRPHPGPAAFDEAL---------QGLVLVDLPDHDSAAIEHRDQVDRVLALVDAVIWVVDPE---K 237
Cdd:COG0699   103 iynpihqvsqtKKRRARGSNGPEVLRALvglphpllrQGLVIVDTPGLGALVGSEAELTLAKLPDADAVLVVLDADaevT 182

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2755704908 238 YADAALHERYLRPLAGHaEVTFVVLNQTDRL 268
Cdd:COG0699   183 ASEMELLRRVIQNLRIC-PSVFVVLNKIDRR 212
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
125-319 9.02e-08

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 53.84  E-value: 9.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 125 VAVAGATGSGKSTLFNALAGAPISDTGlRRP-TTSQPIACSWTDGAAglldrlavpgrlrrrphpgpaafdealQgLVLV 203
Cdd:COG1159     6 VAIVGRPNVGKSTLLNALVGQKVSIVS-PKPqTTRHRIRGIVTREDA---------------------------Q-IVFV 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 204 DLPD-HdsaaiEHRDQVDRVL------AL--VDAVIWVVDPEKYADAAlHERYLRPLAGHAEVTFVVLNQTDRLPGEAAD 274
Cdd:COG1159    57 DTPGiH-----KPKRKLGRRMnkaawsALedVDVILFVVDATEKIGEG-DEFILELLKKLKTPVILVINKIDLVKKEELL 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2755704908 275 LVLDdlrrlldedgiALGEHGEPGATVMsLSALTGDGVPELREMI 319
Cdd:COG1159   131 PLLA-----------EYSELLDFAEIVP-ISALKGDNVDELLDEI 163
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 125-263 5.53e-07

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: 48.38  E-value: 5.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 125 VAVAGATGSGKSTLFNALAG--APISDTglrrP-TTsqpiacswtdgaaglldRLAVPGRLRRRPHPgpaafdealqgLV 201
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGakAIVSDY----PgTT-----------------RDPNEGRLELKGKQ-----------II 49

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2755704908 202 LVDLPDHDSAAIEHRDQVDRVLAL--VDAVIWVVDPEKYADAalHERYLRPLAGHAEV-TFVVLN 263
Cdd:pfam01926  50 LVDTPGLIEGASEGEGLGRAFLAIieADLILFVVDSEEGITP--LDEELLELLRENKKpIILVLN 112
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 115-323 1.17e-06

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: 49.38  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 115 RQRLSSRHTVVAVAGATGSGKSTLFNALAGAPIS---------DTGLRRPTTSQPIACSWTDgaaglldrlAVpGRLRRR 185
Cdd:cd01878    34 ARRKRSGVPTVALVGYTNAGKSTLFNALTGADVLaedqlfatlDPTTRRIKLPGGREVLLTD---------TV-GFIRDL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 186 PHPGPAAF----DEALQG---LVLVDL--PDHDsaaiEHRDQVDRVLALVDAviwvvdpekyadaalherylrplagHAE 256
Cdd:cd01878   104 PHQLVEAFrstlEEVAEAdllLHVVDAsdPDRE----EQIETVEEVLKELGA-------------------------DDI 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2755704908 257 VTFVVLNQTDRLPGEAADLVLddlrrlldedgialgEHGEPGAtvMSLSALTGDGVPELREMIGRFV 323
Cdd:cd01878   155 PIILVLNKIDLLDDEELEERL---------------RAGRPDA--VFISAKTGEGLDLLKEAIEELL 204
era PRK00089
GTPase Era; Reviewed
 125-319 7.02e-06

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 48.12  E-value: 7.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 125 VAVAGATGSGKSTLFNALAGAPISDTGlRRP-TTsqpiacswtdgaaglldrlavpgrlRRRPHpGPAAFDEAlQgLVLV 203
Cdd:PRK00089    8 VAIVGRPNVGKSTLLNALVGQKISIVS-PKPqTT-------------------------RHRIR-GIVTEDDA-Q-IIFV 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 204 DLPD-HDSaaiEHR------DQVDRVLALVDAVIWVVDPEKYADAalHERY-LRPLAGHAEVTFVVLNQTDRLPGEAADL 275
Cdd:PRK00089   59 DTPGiHKP---KRAlnramnKAAWSSLKDVDLVLFVVDADEKIGP--GDEFiLEKLKKVKTPVILVLNKIDLVKDKEELL 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2755704908 276 VLDDlrrlldedgiALGEHGEPGATVMsLSALTGDGVPELREMI 319
Cdd:PRK00089  134 PLLE----------ELSELMDFAEIVP-ISALKGDNVDELLDVI 166
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 115-345 5.77e-05

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


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 45.85  E-value: 5.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 115 RQRLSSRHTVVAVAGATGSGKSTLFNALAGAPIS---------DTGLRrpttsqpiacswtdgaaglldRLAVPGRL--- 182
Cdd:COG2262   192 KRRKRSGIPTVALVGYTNAGKSTLFNRLTGADVLaedklfatlDPTTR---------------------RLELPDGRpvl 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 183 --------RRRPHPGPAAF----DEALQG-LVL--VDLPDHDSAaiEHRDQVDRVLALVDAviwvvdpekyadaalhery 247
Cdd:COG2262   251 ltdtvgfiRKLPHQLVEAFrstlEEVREAdLLLhvVDASDPDFE--EQIETVNEVLEELGA------------------- 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 248 lrplaghAEV-TFVVLNQTDRLPGEAadlvlddlrrlldedgIALGEHGEPGAtvMSLSALTGDGVPELREMIGRFVSDR 326
Cdd:COG2262   310 -------DDKpIILVFNKIDLLDDEE----------------LERLRAGYPDA--VFISAKTGEGIDELLEAIEERLPED 364

                         250
                  ....*....|....*....
gi 2755704908 327 taaTRRLSADVDAAAARLR 345
Cdd:COG2262   365 ---RVEVELLLPYSDGDLV 380
trmE PRK05291
tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE;
68-325 1.40e-04

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


Pssm-ID: 235392 [Multi-domain]  Cd Length: 449  Bit Score: 44.72  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  68 QVEAYA--PADGPLPARLDALRELVGLSRARLDRdtlaeagrVLDEAAARQRLSSRHTVVaVAGATGSGKSTLFNALAG- 144
Cdd:PRK05291  168 LVEAAIdfPEEDIEFLSDEKILEKLEELIAELEA--------LLASARQGEILREGLKVV-IAGRPNVGKSSLLNALLGe 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 145 --APISDtglrrpttsqpiacswtdgaaglldrlaVPGRLRrrphpgpaafD--EA---LQG--LVLVdlpdhDSAAI-E 214
Cdd:PRK05291  239 erAIVTD----------------------------IAGTTR----------DviEEhinLDGipLRLI-----DTAGIrE 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 215 HRDQVDR--------VLALVDAVIWVVDPEKYADAALHERYLRPLAGHaevTFVVLNQTDrLPGEAADLVlddlrrllde 286
Cdd:PRK05291  276 TDDEVEKigiersreAIEEADLVLLVLDASEPLTEEDDEILEELKDKP---VIVVLNKAD-LTGEIDLEE---------- 341

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2755704908 287 dgialgehgEPGATVMSLSALTGDGVPELREMIGRFVSD 325
Cdd:PRK05291  342 ---------ENGKPVIRISAKTGEGIDELREAIKELAFG 371
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 179-612 2.96e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 44.09  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  179 PGRLRRRPHPGPAAFDEALQGLVLVDLPDHDSAAIEHRDQVDRVLALVDAVIWVVDPEKYADAALHERYLRPLAGHAEVT 258
Cdd:COG3321    854 PGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALV 933

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  259 FVVLNQTDRLPGEAADLVLDDLRRLLDEDGIALGEHGEPGATVMSLSALTGDGVPELREMIGRFVSDRTAATRRLSADVD 338
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  339 AAAARLRKVYVAQGRPGLGERAREEFADRLAEAVGAAAAGQAAEREW-----RRNASRACGTPWLRLWRWYENRGLPGSL 413
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAAlalalAALLLLAALAELALAAAALALAAALAAA 1093

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  414 DRLGQALTPPEEELTARQRVEQAVRIVADDAADGLPGPWAQAVREAAFTGAQGLPEALDELAVKAGAPGAAKRGGGTETG 493
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAAL 1173

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  494 KGKSAVDRLGGRPPKPPRPKWWPAAVLAQASMTLLQIFGGLWLVGQIIGVLEPGLVTPALIMLGGVVGGPLVEWACAAAI 573
Cdd:COG3321   1174 LLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAA 1253

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 2755704908  574 RGPARRYGQDAERRLREAAAGCGRARVLDPVAAELVRYR 612
Cdd:COG3321   1254 ALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAA 1292
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 123-151 1.30e-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: 39.92  E-value: 1.30e-03
                          10        20
                  ....*....|....*....|....*....
gi 2755704908 123 TVVAVAGATGSGKSTLFNALAGAPISDTG 151
Cdd:cd00267    26 EIVALVGPNGSGKSTLLRAIAGLLKPTSG 54
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 125-323 1.36e-03

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 39.79  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 125 VAVAGATGSGKSTLFNALAGAP---------------------------ISDT-GLRRptTSQPIacswtdgaagllDRL 176
Cdd:cd04164     6 VVIAGKPNVGKSSLLNALAGRDraivsdiagttrdvieeeidlggipvrLIDTaGLRE--TEDEI------------EKI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 177 AVpgrlRRrphpgpaAFDEAlqglvlvdlpdhdsaaiehrDQVDRVLALVDA-VIWVVDPEKYADAALHERYLrplagha 255
Cdd:cd04164    72 GI----ER-------AREAI--------------------EEADLVLLVVDAsEGLDEEDLEILELPAKKPVI------- 113

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2755704908 256 evtfVVLNQTDRLPGEAADLvlddlrrlldedgialgehGEPGATVMSLSALTGDGVPELREMIGRFV 323
Cdd:cd04164   114 ----VVLNKSDLLSDAEGIS-------------------ELNGKPIIAISAKTGEGIDELKEALLELA 158
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 123-144 1.39e-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: 40.23  E-value: 1.39e-03
                          10        20
                  ....*....|....*....|..
gi 2755704908 123 TVVAVAGATGSGKSTLFNALAG 144
Cdd:cd03213    36 ELTAIMGPSGAGKSTLLNALAG 57
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 125-151 1.51e-03

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 40.53  E-value: 1.51e-03
                          10        20
                  ....*....|....*....|....*..
gi 2755704908 125 VAVAGATGSGKSTLFNALAGAPISDTG 151
Cdd:cd03225    30 VLIVGPNGSGKSTLLRLLNGLLGPTSG 56
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 103-145 2.43e-03

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 39.92  E-value: 2.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2755704908 103 AEAGRVLDEAAARQRLSSRHTVVAVAGATGSGKSTLFNALAGA 145
Cdd:PRK09270   14 AVHKPLLRRLAALQAEPQRRTIVGIAGPPGAGKSTLAEFLEAL 56
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 123-144 2.47e-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: 39.29  E-value: 2.47e-03
                          10        20
                  ....*....|....*....|..
gi 2755704908 123 TVVAVAGATGSGKSTLFNALAG 144
Cdd:cd03228    29 EKVAIVGPSGSGKSTLLKLLLR 50
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 94-330 3.70e-03

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 40.04  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908  94 RARLDRdTLAEAGRVLDEAAARQRLSSRHTVVaVAGATGSGKSTLFNALAG---APISDT-GlrrpTTsqpiacswtdga 169
Cdd:COG0486   187 LERLEE-LREELEALLASARQGELLREGIKVV-IVGRPNVGKSSLLNALLGeerAIVTDIaG----TT------------ 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 170 aglldRLAVPGRLRRRPHPgpaafdealqgLVLVDlpdhdSAAIehRDQVDRV-----------LALVDAVIWVVDPEKY 238
Cdd:COG0486   249 -----RDVIEERINIGGIP-----------VRLID-----TAGL--RETEDEVekigierareaIEEADLVLLLLDASEP 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2755704908 239 ADAAlhERYLRPLAGHAEVTfVVLNQTDRLPGEAADLVLDdlrrlldedgialgehgePGATVMSLSALTGDGVPELREM 318
Cdd:COG0486   306 LTEE--DEEILEKLKDKPVI-VVLNKIDLPSEADGELKSL------------------PGEPVIAISAKTGEGIDELKEA 364

                         250
                  ....*....|..
gi 2755704908 319 IGRFVSDRTAAT 330
Cdd:COG0486   365 ILELVGEGALEG 376
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 125-151 3.82e-03

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 39.68  E-value: 3.82e-03
                          10        20
                  ....*....|....*....|....*..
gi 2755704908 125 VAVAGATGSGKSTLFNALAGAPISDTG 151
Cdd:COG1101    35 VTVIGSNGAGKSTLLNAIAGSLPPDSG 61
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 124-157 3.97e-03

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 39.23  E-value: 3.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2755704908 124 VVAVAGATGSGKSTLFNALAGAPIS-DTG-LRRPTT 157
Cdd:cd01851     9 VVSVFGSQSSGKSFLLNHLFGTSDGfDVMdTSQQTT 44
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 125-144 7.29e-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: 38.47  E-value: 7.29e-03
                          10        20
                  ....*....|....*....|
gi 2755704908 125 VAVAGATGSGKSTLFNALAG 144
Cdd:COG1122    30 VAIIGPNGSGKSTLLRLLNG 49
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
 103-145 8.26e-03

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 38.99  E-value: 8.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2755704908 103 AEAGRVLdEAAARQRLSsrhtvVAVAGATGSGKSTLFNALAGA 145
Cdd:COG4962   169 PEMAEFL-RAAVRARLN-----ILVSGGTGSGKTTLLNALSGF 205
 
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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