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Conserved domains on  [gi|45554264|ref|NP_996357|]
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mitochondrial assembly regulatory factor, isoform C [Drosophila melanogaster]

Protein Classification

Fzo-like mitofusin( domain architecture ID 10177731)

Fzo-like mitofusin such as Homo sapien mitofusin 2 (MFN2), a homolog of the Drosophila protein fuzzy onion (Fzo), is a dynamin-like GTPase that plays a central role in regulating mitochondrial fusion and cell metabolism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Fzo_mitofusin pfam04799
fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a ...
650-807 3.39e-84

fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a mediator of mitochondrial fusion. This conserved region is also found in the human mitofusin protein.


:

Pssm-ID: 461432  Cd Length: 159  Bit Score: 264.95  E-value: 3.39e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264   650 PEQLSLISRFAVSSIGSQGTVGGLVVAGVMLKTIGWRVLVGVGALYGCIYLYERLSWTNSAKERTFKSQYVRHATKKLKM 729
Cdd:pfam04799   1 QEELMLSLRLGLASVTSRGSLGVLVVGGVVWRTVGWRLIALSGALYGLLYLYERLTWTTKAKERAFKRQFVDHATQKLRL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45554264   730 IVDLTSANCSHQVQQELSSTFARLCRTVDTATTDMNDELKTLDSQLNILEANQKQLKLLRNKANYIQNELDIFEHNYI 807
Cdd:pfam04799  81 IVSFTSANCSHQVQQELSSTFARLCQQVDETQNELEEEIARLEREIQQLESVQSRSKTLRNKATFLENELDDFQETYL 158
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
138-389 4.37e-48

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: 168.11  E-value: 4.37e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 138 MKVAFFGRTSNGKSSVINAMLREKILPSGIGHTTNcfcqvegsnggeaylmtegseeKLNVVNIKqlanalcqeklcess 217
Cdd:cd09912   1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTA----------------------VITVLRYG--------------- 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 218 lvrifwprercslLRDDVVFVDSPGVDV-SANLDDWIDNHCLNADVFVLVLNAESTMTRAEKQFFHTVSQKlSKPNIFIL 296
Cdd:cd09912  44 -------------LLKGVVLVDTPGLNStIEHHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKIFFV 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 297 NNRWDASANEPECQESVKSQHtercidfltkELKVSNEKEAAERVFFVSARETLQARIEEAKGNpphmgaiaegfqIRYF 376
Cdd:cd09912 110 LNKIDLLSEEELEEVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEEL------------LEQS 167
                       250
                ....*....|...
gi 45554264 377 EFQDFERKFEECI 389
Cdd:cd09912 168 GFEELEEHLEEFL 180
 
Name Accession Description Interval E-value
Fzo_mitofusin pfam04799
fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a ...
650-807 3.39e-84

fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a mediator of mitochondrial fusion. This conserved region is also found in the human mitofusin protein.


Pssm-ID: 461432  Cd Length: 159  Bit Score: 264.95  E-value: 3.39e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264   650 PEQLSLISRFAVSSIGSQGTVGGLVVAGVMLKTIGWRVLVGVGALYGCIYLYERLSWTNSAKERTFKSQYVRHATKKLKM 729
Cdd:pfam04799   1 QEELMLSLRLGLASVTSRGSLGVLVVGGVVWRTVGWRLIALSGALYGLLYLYERLTWTTKAKERAFKRQFVDHATQKLRL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45554264   730 IVDLTSANCSHQVQQELSSTFARLCRTVDTATTDMNDELKTLDSQLNILEANQKQLKLLRNKANYIQNELDIFEHNYI 807
Cdd:pfam04799  81 IVSFTSANCSHQVQQELSSTFARLCQQVDETQNELEEEIARLEREIQQLESVQSRSKTLRNKATFLENELDDFQETYL 158
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
138-389 4.37e-48

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: 168.11  E-value: 4.37e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 138 MKVAFFGRTSNGKSSVINAMLREKILPSGIGHTTNcfcqvegsnggeaylmtegseeKLNVVNIKqlanalcqeklcess 217
Cdd:cd09912   1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTA----------------------VITVLRYG--------------- 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 218 lvrifwprercslLRDDVVFVDSPGVDV-SANLDDWIDNHCLNADVFVLVLNAESTMTRAEKQFFHTVSQKlSKPNIFIL 296
Cdd:cd09912  44 -------------LLKGVVLVDTPGLNStIEHHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKIFFV 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 297 NNRWDASANEPECQESVKSQHtercidfltkELKVSNEKEAAERVFFVSARETLQARIEEAKGNpphmgaiaegfqIRYF 376
Cdd:cd09912 110 LNKIDLLSEEELEEVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEEL------------LEQS 167
                       250
                ....*....|...
gi 45554264 377 EFQDFERKFEECI 389
Cdd:cd09912 168 GFEELEEHLEEFL 180
Dynamin_N pfam00350
Dynamin family;
140-298 1.96e-35

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 131.97  E-value: 1.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264   140 VAFFGRTSNGKSSVINAMLREKILPSGIGHTTNCFCQV---EGSNGGEAYLMTEGSEEKLNVVNIKQLANALCQEKLCES 216
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLrlgESPGASEGAVKVEYKDGEKKFEDFSELREEIEKETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264   217 ----SLVRIFWPRERCSLLRDDVVFVDSPGVDVSANLD-DWIDNHCLNADVFVLVLNAESTMTRAEKQFFHTVSQKLSKP 291
Cdd:pfam00350  81 gtgkGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDqELTKEYIKPADIILAVTPANVDLSTSEALFLAREVDPNGKR 160

                  ....*..
gi 45554264   292 NIFILNN 298
Cdd:pfam00350 161 TIGVLTK 167
YeeP COG3596
Predicted GTPase [General function prediction only];
130-352 1.70e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.00  E-value: 1.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 130 REVLQRDHMKVAFFGRTSNGKSSVINAMLREKIlpSGIGHTTNCfcqvegsnggeaylmTEGSEeklnvvnikqlanalc 209
Cdd:COG3596  32 RLLVELPPPVIALVGKTGAGKSSLINALFGAEV--AEVGVGRPC---------------TREIQ---------------- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 210 qeklcesslvRIFWPRERCSLLrddvVFVDSPGVDvSANLDDW----IDNHCLNADVFVLVLNAESTMTRAEKQFFHTVS 285
Cdd:COG3596  79 ----------RYRLESDGLPGL----VLLDTPGLG-EVNERDReyreLRELLPEADLILWVVKADDRALATDEEFLQALR 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45554264 286 QKLS-KPNIFILN--------NRWDASANEPecqESVKSQHTERCIDFLTKELKVsnekeAAERVFFVSARETLQA 352
Cdd:COG3596 144 AQYPdPPVLVVLTqvdrlepeREWDPPYNWP---SPPKEQNIRRALEAIAEQLGV-----PIDRVIPVSAAEDRTG 211
ProP COG0477
MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and ...
645-704 4.58e-03

MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and metabolism, Amino acid transport and metabolism, Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440245 [Multi-domain]  Cd Length: 295  Bit Score: 39.79  E-value: 4.58e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45554264 645 VAGITPEQLSLISRFA-----------VSSIGSQGTVGGLVVAGVMLKTIGWRVLVGVGALYGCIYLYERL 704
Cdd:COG0477 116 AGGLMPGALALIAELFparergralglWGAAIGLGLALGPLLGGLLVAALGWRWIFLINAPLGLLALVLRL 186
 
Name Accession Description Interval E-value
Fzo_mitofusin pfam04799
fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a ...
650-807 3.39e-84

fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a mediator of mitochondrial fusion. This conserved region is also found in the human mitofusin protein.


Pssm-ID: 461432  Cd Length: 159  Bit Score: 264.95  E-value: 3.39e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264   650 PEQLSLISRFAVSSIGSQGTVGGLVVAGVMLKTIGWRVLVGVGALYGCIYLYERLSWTNSAKERTFKSQYVRHATKKLKM 729
Cdd:pfam04799   1 QEELMLSLRLGLASVTSRGSLGVLVVGGVVWRTVGWRLIALSGALYGLLYLYERLTWTTKAKERAFKRQFVDHATQKLRL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45554264   730 IVDLTSANCSHQVQQELSSTFARLCRTVDTATTDMNDELKTLDSQLNILEANQKQLKLLRNKANYIQNELDIFEHNYI 807
Cdd:pfam04799  81 IVSFTSANCSHQVQQELSSTFARLCQQVDETQNELEEEIARLEREIQQLESVQSRSKTLRNKATFLENELDDFQETYL 158
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
138-389 4.37e-48

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: 168.11  E-value: 4.37e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 138 MKVAFFGRTSNGKSSVINAMLREKILPSGIGHTTNcfcqvegsnggeaylmtegseeKLNVVNIKqlanalcqeklcess 217
Cdd:cd09912   1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTA----------------------VITVLRYG--------------- 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 218 lvrifwprercslLRDDVVFVDSPGVDV-SANLDDWIDNHCLNADVFVLVLNAESTMTRAEKQFFHTVSQKlSKPNIFIL 296
Cdd:cd09912  44 -------------LLKGVVLVDTPGLNStIEHHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKIFFV 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 297 NNRWDASANEPECQESVKSQHtercidfltkELKVSNEKEAAERVFFVSARETLQARIEEAKGNpphmgaiaegfqIRYF 376
Cdd:cd09912 110 LNKIDLLSEEELEEVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEEL------------LEQS 167
                       250
                ....*....|...
gi 45554264 377 EFQDFERKFEECI 389
Cdd:cd09912 168 GFEELEEHLEEFL 180
Dynamin_N pfam00350
Dynamin family;
140-298 1.96e-35

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 131.97  E-value: 1.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264   140 VAFFGRTSNGKSSVINAMLREKILPSGIGHTTNCFCQV---EGSNGGEAYLMTEGSEEKLNVVNIKQLANALCQEKLCES 216
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLrlgESPGASEGAVKVEYKDGEKKFEDFSELREEIEKETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264   217 ----SLVRIFWPRERCSLLRDDVVFVDSPGVDVSANLD-DWIDNHCLNADVFVLVLNAESTMTRAEKQFFHTVSQKLSKP 291
Cdd:pfam00350  81 gtgkGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDqELTKEYIKPADIILAVTPANVDLSTSEALFLAREVDPNGKR 160

                  ....*..
gi 45554264   292 NIFILNN 298
Cdd:pfam00350 161 TIGVLTK 167
YeeP COG3596
Predicted GTPase [General function prediction only];
130-352 1.70e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.00  E-value: 1.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 130 REVLQRDHMKVAFFGRTSNGKSSVINAMLREKIlpSGIGHTTNCfcqvegsnggeaylmTEGSEeklnvvnikqlanalc 209
Cdd:COG3596  32 RLLVELPPPVIALVGKTGAGKSSLINALFGAEV--AEVGVGRPC---------------TREIQ---------------- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264 210 qeklcesslvRIFWPRERCSLLrddvVFVDSPGVDvSANLDDW----IDNHCLNADVFVLVLNAESTMTRAEKQFFHTVS 285
Cdd:COG3596  79 ----------RYRLESDGLPGL----VLLDTPGLG-EVNERDReyreLRELLPEADLILWVVKADDRALATDEEFLQALR 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45554264 286 QKLS-KPNIFILN--------NRWDASANEPecqESVKSQHTERCIDFLTKELKVsnekeAAERVFFVSARETLQA 352
Cdd:COG3596 144 AQYPdPPVLVVLTqvdrlepeREWDPPYNWP---SPPKEQNIRRALEAIAEQLGV-----PIDRVIPVSAAEDRTG 211
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
139-297 1.26e-04

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: 42.22  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264   139 KVAFFGRTSNGKSSVINAMLREKILPSGIGHTTncfcqvegsnggeaylmtegseeklnvvnikqlanalcqeklcessL 218
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPGTT----------------------------------------------R 34
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45554264   219 VRIFwprERCSLLRDDVVFVDSPGVDVSANLDDWIDNHCL---NADVFVLVLNAESTMTRAEKQFFHtVSQKLSKPNIFI 295
Cdd:pfam01926  35 DPNE---GRLELKGKQIILVDTPGLIEGASEGEGLGRAFLaiiEADLILFVVDSEEGITPLDEELLE-LLRENKKPIILV 110

                  ..
gi 45554264   296 LN 297
Cdd:pfam01926 111 LN 112
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
141-171 3.37e-04

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: 41.85  E-value: 3.37e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 45554264 141 AFFGRTSNGKSSVINAMLREKILP-SGIGHTT 171
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIvSPIPGTT 32
ProP COG0477
MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and ...
645-704 4.58e-03

MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and metabolism, Amino acid transport and metabolism, Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440245 [Multi-domain]  Cd Length: 295  Bit Score: 39.79  E-value: 4.58e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45554264 645 VAGITPEQLSLISRFA-----------VSSIGSQGTVGGLVVAGVMLKTIGWRVLVGVGALYGCIYLYERL 704
Cdd:COG0477 116 AGGLMPGALALIAELFparergralglWGAAIGLGLALGPLLGGLLVAALGWRWIFLINAPLGLLALVLRL 186
 
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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