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Conserved domains on  [gi|665400862|ref|NP_001286413|]
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optic atrophy 1, isoform E [Drosophila melanogaster]

Protein Classification

dynamin family protein( domain architecture ID 10171807)

dynamin family protein similar to dynamins and dynamin-like proteins (DLPs), which catalyze membrane fission during clathrin-mediated endocytosis

EC:  3.6.5.5
Gene Ontology:  GO:0005525|GO:0003924
SCOP:  4004047

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
259-533 9.48e-88

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. 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 interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


:

Pssm-ID: 206738  Cd Length: 278  Bit Score: 274.12  E-value: 9.48e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 259 HLPRVVVVGDQSSGKTSVLESIAKARIFPRGSGeMMTRAPVKVTLAEGPYH-VAQFRDSDREYDLTKE---SDLQDLRRD 334
Cdd:cd08771    2 DLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSG-ICTRRPLELQLRRSPSEsDEDEKEEWGEFLHLKSkefTDFEELREE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 335 VEFRMKASVRGGKTVSNEVIAMTVKGPGLQRMVLVDLPGIISTMTVDMASDTKDSIHQMTKHYMSNPNAIILCIQDGSVD 414
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 415 AERSNVTDLVMQCDPLGRRTIFVLTKVDLAEELADPDRIRKILSGKLFPMKaLGYYAVVTGRGRKDD---SIDAIRQYEE 491
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLLLQGKVIPLK-LGYVGVVNRSQKDIDsgkSIEEALEAEE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 665400862 492 DFFKNSKLFHRrgvIMPHQVTSRNLSLAVSDRFWKMVRETIE 533
Cdd:cd08771  240 EFFETHPWYKL---LPASRVGTPALRKRLSKLLQKHIRESLP 278
OPA1_C super family cl44852
Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of ...
590-617 2.07e-07

Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of Dynamin-like GTPase OPA1. This protein is involved in mitochondrial fusion and inner membrane remodelling, essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. Mutations in human OPA1 cause optic atrophy. This domain includes the helix bundle (HB) domains HB1 (C-terminal) and HB2 (equivalent to extreme C-terminal bundle signaling element (BSE) and to the stalk domain of dynamin-1, respectively) and the lipid-interacting stalk (LIS, equivalent to the PH domain of dynamin-1).


The actual alignment was detected with superfamily member pfam19434:

Pssm-ID: 466080  Cd Length: 345  Bit Score: 53.34  E-value: 2.07e-07
                          10        20
                  ....*....|....*....|....*...
gi 665400862  590 DALSTKLWEKLSNYVFESIYLPAAQSGS 617
Cdd:pfam19434   2 EALQKKLWEKVSSHVFENIYLPAAQSEN 29
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
259-533 9.48e-88

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. 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 interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206738  Cd Length: 278  Bit Score: 274.12  E-value: 9.48e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 259 HLPRVVVVGDQSSGKTSVLESIAKARIFPRGSGeMMTRAPVKVTLAEGPYH-VAQFRDSDREYDLTKE---SDLQDLRRD 334
Cdd:cd08771    2 DLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSG-ICTRRPLELQLRRSPSEsDEDEKEEWGEFLHLKSkefTDFEELREE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 335 VEFRMKASVRGGKTVSNEVIAMTVKGPGLQRMVLVDLPGIISTMTVDMASDTKDSIHQMTKHYMSNPNAIILCIQDGSVD 414
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 415 AERSNVTDLVMQCDPLGRRTIFVLTKVDLAEELADPDRIRKILSGKLFPMKaLGYYAVVTGRGRKDD---SIDAIRQYEE 491
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLLLQGKVIPLK-LGYVGVVNRSQKDIDsgkSIEEALEAEE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 665400862 492 DFFKNSKLFHRrgvIMPHQVTSRNLSLAVSDRFWKMVRETIE 533
Cdd:cd08771  240 EFFETHPWYKL---LPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_N pfam00350
Dynamin family;
263-441 2.20e-44

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 155.85  E-value: 2.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862  263 VVVVGDQSSGKTSVLESIAKARIFPRGSGeMMTRAPVKVTLAEGPYHVAQFRDSDREYDLTKESDLQDLRRDVEFRMKAS 342
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPG-PTTRRPTVLRLGESPGASEGAVKVEYKDGEKKFEDFSELREEIEKETEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862  343 VRGGKTVSNEVIAMTVKGPGLQRMVLVDLPGIISTMTVDMAsdtkdsihqMTKHYMsNPNAIILCIQDGSVDAERSNVTD 422
Cdd:pfam00350  80 AGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQE---------LTKEYI-KPADIILAVTPANVDLSTSEALF 149
                         170
                  ....*....|....*....
gi 665400862  423 LVMQCDPLGRRTIFVLTKV 441
Cdd:pfam00350 150 LAREVDPNGKRTIGVLTKA 168
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
253-480 1.85e-32

Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.


Pssm-ID: 197491  Cd Length: 240  Bit Score: 125.38  E-value: 1.85e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862   253 GYTMADHLPRVVVVGDQSSGKTSVLESIAKARIFPRGSGeMMTRAPVKVTLAEGPYHVAQFRdsdrEYDLTKESDLQDLR 332
Cdd:smart00053  19 GQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSG-IVTRRPLILQLIKSKTEYAEFL----HCKGKKFTDFDEVR 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862   333 RDVEFRMKASVRGGKTVSNEVIAMTVKGPGLQRMVLVDLPGIISTMTVDMASDTKDSIHQMTKHYMSNPNAIILCIQDGS 412
Cdd:smart00053  94 NEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFISREECLILAVTPAN 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665400862   413 VDAERSNVTDLVMQCDPLGRRTIFVLTKVDLAEELADpdrIRKILSGKLFPMKAlGYYAVVTgRGRKD 480
Cdd:smart00053 174 TDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTD---ARDILENKLLPLRR-GYIGVVN-RSQKD 236
OPA1_C pfam19434
Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of ...
590-617 2.07e-07

Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of Dynamin-like GTPase OPA1. This protein is involved in mitochondrial fusion and inner membrane remodelling, essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. Mutations in human OPA1 cause optic atrophy. This domain includes the helix bundle (HB) domains HB1 (C-terminal) and HB2 (equivalent to extreme C-terminal bundle signaling element (BSE) and to the stalk domain of dynamin-1, respectively) and the lipid-interacting stalk (LIS, equivalent to the PH domain of dynamin-1).


Pssm-ID: 466080  Cd Length: 345  Bit Score: 53.34  E-value: 2.07e-07
                          10        20
                  ....*....|....*....|....*...
gi 665400862  590 DALSTKLWEKLSNYVFESIYLPAAQSGS 617
Cdd:pfam19434   2 EALQKKLWEKVSSHVFENIYLPAAQSEN 29
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
259-533 9.48e-88

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. 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 interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206738  Cd Length: 278  Bit Score: 274.12  E-value: 9.48e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 259 HLPRVVVVGDQSSGKTSVLESIAKARIFPRGSGeMMTRAPVKVTLAEGPYH-VAQFRDSDREYDLTKE---SDLQDLRRD 334
Cdd:cd08771    2 DLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSG-ICTRRPLELQLRRSPSEsDEDEKEEWGEFLHLKSkefTDFEELREE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 335 VEFRMKASVRGGKTVSNEVIAMTVKGPGLQRMVLVDLPGIISTMTVDMASDTKDSIHQMTKHYMSNPNAIILCIQDGSVD 414
Cdd:cd08771   81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 415 AERSNVTDLVMQCDPLGRRTIFVLTKVDLAEELADPDRIRKILSGKLFPMKaLGYYAVVTGRGRKDD---SIDAIRQYEE 491
Cdd:cd08771  161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLLLQGKVIPLK-LGYVGVVNRSQKDIDsgkSIEEALEAEE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 665400862 492 DFFKNSKLFHRrgvIMPHQVTSRNLSLAVSDRFWKMVRETIE 533
Cdd:cd08771  240 EFFETHPWYKL---LPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_N pfam00350
Dynamin family;
263-441 2.20e-44

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 155.85  E-value: 2.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862  263 VVVVGDQSSGKTSVLESIAKARIFPRGSGeMMTRAPVKVTLAEGPYHVAQFRDSDREYDLTKESDLQDLRRDVEFRMKAS 342
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPG-PTTRRPTVLRLGESPGASEGAVKVEYKDGEKKFEDFSELREEIEKETEKI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862  343 VRGGKTVSNEVIAMTVKGPGLQRMVLVDLPGIISTMTVDMAsdtkdsihqMTKHYMsNPNAIILCIQDGSVDAERSNVTD 422
Cdd:pfam00350  80 AGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQE---------LTKEYI-KPADIILAVTPANVDLSTSEALF 149
                         170
                  ....*....|....*....
gi 665400862  423 LVMQCDPLGRRTIFVLTKV 441
Cdd:pfam00350 150 LAREVDPNGKRTIGVLTKA 168
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
253-480 1.85e-32

Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.


Pssm-ID: 197491  Cd Length: 240  Bit Score: 125.38  E-value: 1.85e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862   253 GYTMADHLPRVVVVGDQSSGKTSVLESIAKARIFPRGSGeMMTRAPVKVTLAEGPYHVAQFRdsdrEYDLTKESDLQDLR 332
Cdd:smart00053  19 GQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSG-IVTRRPLILQLIKSKTEYAEFL----HCKGKKFTDFDEVR 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862   333 RDVEFRMKASVRGGKTVSNEVIAMTVKGPGLQRMVLVDLPGIISTMTVDMASDTKDSIHQMTKHYMSNPNAIILCIQDGS 412
Cdd:smart00053  94 NEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFISREECLILAVTPAN 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665400862   413 VDAERSNVTDLVMQCDPLGRRTIFVLTKVDLAEELADpdrIRKILSGKLFPMKAlGYYAVVTgRGRKD 480
Cdd:smart00053 174 TDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTD---ARDILENKLLPLRR-GYIGVVN-RSQKD 236
OPA1_C pfam19434
Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of ...
590-617 2.07e-07

Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of Dynamin-like GTPase OPA1. This protein is involved in mitochondrial fusion and inner membrane remodelling, essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. Mutations in human OPA1 cause optic atrophy. This domain includes the helix bundle (HB) domains HB1 (C-terminal) and HB2 (equivalent to extreme C-terminal bundle signaling element (BSE) and to the stalk domain of dynamin-1, respectively) and the lipid-interacting stalk (LIS, equivalent to the PH domain of dynamin-1).


Pssm-ID: 466080  Cd Length: 345  Bit Score: 53.34  E-value: 2.07e-07
                          10        20
                  ....*....|....*....|....*...
gi 665400862  590 DALSTKLWEKLSNYVFESIYLPAAQSGS 617
Cdd:pfam19434   2 EALQKKLWEKVSSHVFENIYLPAAQSEN 29
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
264-489 1.04e-05

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: 45.91  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 264 VVVGDQSSGKTSVLESIAKARIFPRgsgemmtrapvkvtlaegpyhvaqfrdsdreydltkesdlqdlrrdvefrmkaSV 343
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEV-----------------------------------------------------SD 27
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 344 RGGKTVSNEVIAMTVKGPGLQrMVLVDLPGIISTmtvdmasdTKDSIHQMTKHYMSNPNAIILCIQDGSVDAERSNVTDL 423
Cdd:cd00882   28 VPGTTRDPDVYVKELDKGKVK-LVLVDTPGLDEF--------GGLGREELARLLLRGADLILLVVDSTDRESEEDAKLLI 98
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665400862 424 VMQCDPLGRRTIFVLTKVDLAEEladPDRIRKILSGKLFPMKALGYYAV--VTGRGrkddsIDAIRQY 489
Cdd:cd00882   99 LRRLRKEGIPIILVGNKIDLLEE---REVEELLRLEELAKILGVPVFEVsaKTGEG-----VDELFEK 158
FeoB cd01879
Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) ...
346-457 5.56e-03

Ferrous iron transport protein B (FeoB) family; Ferrous iron transport protein B (FeoB) subfamily. E. coli has an iron(II) transport system, known as feo, which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 206667 [Multi-domain]  Cd Length: 159  Bit Score: 37.82  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665400862 346 GKTVSNEVIAMTVKGpglQRMVLVDLPGIIStmtvdMASDTKDsiHQMTKHYMSNPNA-IILCIqdgsVDA---ERSNVt 421
Cdd:cd01879   29 GVTVEKKEGEFKLGG---KEIEIVDLPGTYS-----LTPYSED--EKVARDFLLGEEPdLIVNV----VDAtnlERNLY- 93
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 665400862 422 dLVMQCDPLGRRTIFVLTKVDLAEELA---DPDRIRKIL 457
Cdd:cd01879   94 -LTLQLLELGLPVVVALNMIDEAEKRGikiDLDKLSELL 131
 
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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