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Conserved domains on  [gi|81910618|sp|Q641Z6|]
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RecName: Full=EH domain-containing protein 1

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
60-300 3.06e-166

Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling.


:

Pssm-ID: 206740  Cd Length: 241  Bit Score: 470.60  E-value: 3.06e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618  60 MVLLVGQYSTGKTTFIRHLIEQDFPGMRIGPEPTTDSFIAVMHGPTEGVVPGNALVVDPRRPFRKLNAFGNAFLNRFMCA 139
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 140 QLPNPVLDSISIIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKIRVVLN 219
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 220 KADQIETQQLMRVYGALMWSLGKIINTPEVVRVYIGSFWSHPLLIPDNRKLFEAEEQDLFKDIQSLPRNAALRKLNDLIK 299
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 81910618 300 R 300
Cdd:cd09913 241 R 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
288-394 2.49e-56

Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase 2 (EHD2) present in Mus musculus. The domain is helical in nature and has extensive contacts with the G-domain.


:

Pssm-ID: 465667  Cd Length: 107  Bit Score: 183.97  E-value: 2.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618   288 NAALRKLNDLIKRARLAKVHAYIISSLKKEMPNVFGKESKKKELVNNLGEIYQKIEREHQISSGDFPSLRKMQELLQTQD 367
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 81910618   368 FSKFQALKPKLLDTVDDMLANDIARLM 394
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
438-531 2.70e-38

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


:

Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 135.48  E-value: 2.70e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618    438 EWVV-GKDKPTYDEIFYTLSP-VNGKITGANAKKEMVKSKLPNTVLGKIWKLADVDKDGLLDDEEFALANHLIKVKLEGH 515
Cdd:smart00027   1 PWAIsPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 81910618    516 ELPADLPPHLIPPSKR 531
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
24-56 1.56e-14

N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins.


:

Pssm-ID: 465295 [Multi-domain]  Cd Length: 33  Bit Score: 67.42  E-value: 1.56e-14
                          10        20        30
                  ....*....|....*....|....*....|...
gi 81910618    24 GLRQLYAQKLLPLEEHYRFHEFHSPALEDADFD 56
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
 
Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
60-300 3.06e-166

Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling.


Pssm-ID: 206740  Cd Length: 241  Bit Score: 470.60  E-value: 3.06e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618  60 MVLLVGQYSTGKTTFIRHLIEQDFPGMRIGPEPTTDSFIAVMHGPTEGVVPGNALVVDPRRPFRKLNAFGNAFLNRFMCA 139
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 140 QLPNPVLDSISIIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKIRVVLN 219
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 220 KADQIETQQLMRVYGALMWSLGKIINTPEVVRVYIGSFWSHPLLIPDNRKLFEAEEQDLFKDIQSLPRNAALRKLNDLIK 299
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 81910618 300 R 300
Cdd:cd09913 241 R 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
288-394 2.49e-56

Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase 2 (EHD2) present in Mus musculus. The domain is helical in nature and has extensive contacts with the G-domain.


Pssm-ID: 465667  Cd Length: 107  Bit Score: 183.97  E-value: 2.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618   288 NAALRKLNDLIKRARLAKVHAYIISSLKKEMPNVFGKESKKKELVNNLGEIYQKIEREHQISSGDFPSLRKMQELLQTQD 367
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 81910618   368 FSKFQALKPKLLDTVDDMLANDIARLM 394
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
438-531 2.70e-38

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 135.48  E-value: 2.70e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618    438 EWVV-GKDKPTYDEIFYTLSP-VNGKITGANAKKEMVKSKLPNTVLGKIWKLADVDKDGLLDDEEFALANHLIKVKLEGH 515
Cdd:smart00027   1 PWAIsPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 81910618    516 ELPADLPPHLIPPSKR 531
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
448-513 2.06e-23

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 93.44  E-value: 2.06e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81910618 448 YDEIFYTLSPVN-GKITGANAKKEMVKSKLPNTVLGKIWKLADVDKDGLLDDEEFALANHLIKVKLE 513
Cdd:cd00052   1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
Dynamin_N pfam00350
Dynamin family;
61-221 1.44e-22

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 94.61  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618    61 VLLVGQYSTGKTTFIRHLIEQDFPGmrIGPEPTTDSFIAVMHGPTEGVVPG--NALVVDPRRPFRKLNAFGNAFLNRFMC 138
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILP--RGPGPTTRRPTVLRLGESPGASEGavKVEYKDGEKKFEDFSELREEIEKETEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618   139 AQLPN--------------PVLDSISIIDTPGILSGEKQRisrgydfAAVLEWFAERVDRIILLFDAHKLDISDEFSEVI 204
Cdd:pfam00350  79 IAGTGkgissepivleilsPLVPGLTLVDTPGLDSVAVGD-------QELTKEYIKPADIILAVTPANVDLSTSEALFLA 151
                         170
                  ....*....|....*..
gi 81910618   205 KALKNHEDKIRVVLNKA 221
Cdd:pfam00350 152 REVDPNGKRTIGVLTKA 168
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
447-531 3.04e-18

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 80.11  E-value: 3.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618   447 TYDEIFYTLSPVNGKITGANAKKEMVKSKLPNTVLGKIWKLADVDKDGLLDDEEFALANHLIKVKLEGH--ELPADLPPH 524
Cdd:pfam12763  11 KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPDELPDW 90

                  ....*..
gi 81910618   525 LIPPSKR 531
Cdd:pfam12763  91 LVPGSKA 97
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
24-56 1.56e-14

N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins.


Pssm-ID: 465295 [Multi-domain]  Cd Length: 33  Bit Score: 67.42  E-value: 1.56e-14
                          10        20        30
                  ....*....|....*....|....*....|...
gi 81910618    24 GLRQLYAQKLLPLEEHYRFHEFHSPALEDADFD 56
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
61-229 2.85e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 41.89  E-value: 2.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618  61 VLLVGQYSTGKTTFIRHLIEQDFPgmrigpepttdsfiAVMHGPTEGVvpgnaLVVDPRRPFRKLNAfgnaflnrfmcaq 140
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIFS--------------LEKYLSTNGV-----TIDKKELKLDGLDV------------- 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 141 lpnpvldSISIIDTPGILsgEKQRISRGYdfaavLEWFAERvDRIILLFDAHKLDISDEFSEVIKALKNHEDKIR--VVL 218
Cdd:COG1100  54 -------DLVIWDTPGQD--EFRETRQFY-----ARQLTGA-SLYLFVVDGTREETLQSLYELLESLRRLGKKSPiiLVL 118
                       170
                ....*....|.
gi 81910618 219 NKADQIETQQL 229
Cdd:COG1100 119 NKIDLYDEEEI 129
 
Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
60-300 3.06e-166

Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain (EHD) proteins regulate endocytic events; they have been linked to a number of Rab proteins through their association with mutual effectors, suggesting a coordinate role in endocytic regulation. Eukaryotic EHDs comprise four members (EHD1-4) in mammals and single members in Caenorhabditis elegans (Rme-1), Drosophila melanogaster (Past1) as well as several eukaryotic parasites. EHD1 regulates trafficking of multiple receptors from the endocytic recycling compartment (ERC) to the plasma membrane; EHD2 regulates trafficking from the plasma membrane by controlling Rac1 activity; EHD3 regulates endosome-to-Golgi transport, and preserves Golgi morphology; EHD4 is involved in the control of trafficking at the early endosome and regulates exit of cargo toward the recycling compartment as well as late endocytic pathway. Rme-1, an ortholog of human EHD1, controls the recycling of internalized receptors from the endocytic recycling compartment to the plasma membrane. In D. melanogaster, deletion of the Past1 gene leads to infertility as well as premature death of adult flies. Arabidopsis thaliana also has homologs of EHD proteins (AtEHD1 and AtEHD2), possibly involved in regulating endocytosis and signaling.


Pssm-ID: 206740  Cd Length: 241  Bit Score: 470.60  E-value: 3.06e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618  60 MVLLVGQYSTGKTTFIRHLIEQDFPGMRIGPEPTTDSFIAVMHGPTEGVVPGNALVVDPRRPFRKLNAFGNAFLNRFMCA 139
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 140 QLPNPVLDSISIIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKIRVVLN 219
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 220 KADQIETQQLMRVYGALMWSLGKIINTPEVVRVYIGSFWSHPLLIPDNRKLFEAEEQDLFKDIQSLPRNAALRKLNDLIK 299
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 81910618 300 R 300
Cdd:cd09913 241 R 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
288-394 2.49e-56

Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase 2 (EHD2) present in Mus musculus. The domain is helical in nature and has extensive contacts with the G-domain.


Pssm-ID: 465667  Cd Length: 107  Bit Score: 183.97  E-value: 2.49e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618   288 NAALRKLNDLIKRARLAKVHAYIISSLKKEMPNVFGKESKKKELVNNLGEIYQKIEREHQISSGDFPSLRKMQELLQTQD 367
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 81910618   368 FSKFQALKPKLLDTVDDMLANDIARLM 394
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
438-531 2.70e-38

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 135.48  E-value: 2.70e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618    438 EWVV-GKDKPTYDEIFYTLSP-VNGKITGANAKKEMVKSKLPNTVLGKIWKLADVDKDGLLDDEEFALANHLIKVKLEGH 515
Cdd:smart00027   1 PWAIsPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 81910618    516 ELPADLPPHLIPPSKR 531
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
448-513 2.06e-23

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 93.44  E-value: 2.06e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81910618 448 YDEIFYTLSPVN-GKITGANAKKEMVKSKLPNTVLGKIWKLADVDKDGLLDDEEFALANHLIKVKLE 513
Cdd:cd00052   1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
Dynamin_N pfam00350
Dynamin family;
61-221 1.44e-22

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 94.61  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618    61 VLLVGQYSTGKTTFIRHLIEQDFPGmrIGPEPTTDSFIAVMHGPTEGVVPG--NALVVDPRRPFRKLNAFGNAFLNRFMC 138
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILP--RGPGPTTRRPTVLRLGESPGASEGavKVEYKDGEKKFEDFSELREEIEKETEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618   139 AQLPN--------------PVLDSISIIDTPGILSGEKQRisrgydfAAVLEWFAERVDRIILLFDAHKLDISDEFSEVI 204
Cdd:pfam00350  79 IAGTGkgissepivleilsPLVPGLTLVDTPGLDSVAVGD-------QELTKEYIKPADIILAVTPANVDLSTSEALFLA 151
                         170
                  ....*....|....*..
gi 81910618   205 KALKNHEDKIRVVLNKA 221
Cdd:pfam00350 152 REVDPNGKRTIGVLTKA 168
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
447-531 3.04e-18

Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin cytoskeleton-regulatory complex END3 and similar proteins from fungi and closely related species.


Pssm-ID: 289529  Cd Length: 104  Bit Score: 80.11  E-value: 3.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618   447 TYDEIFYTLSPVNGKITGANAKKEMVKSKLPNTVLGKIWKLADVDKDGLLDDEEFALANHLIKVKLEGH--ELPADLPPH 524
Cdd:pfam12763  11 KYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPDELPDW 90

                  ....*..
gi 81910618   525 LIPPSKR 531
Cdd:pfam12763  91 LVPGSKA 97
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
24-56 1.56e-14

N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very N-terminus of many dynamins and EF-hand domain-containing proteins.


Pssm-ID: 465295 [Multi-domain]  Cd Length: 33  Bit Score: 67.42  E-value: 1.56e-14
                          10        20        30
                  ....*....|....*....|....*....|...
gi 81910618    24 GLRQLYAQKLLPLEEHYRFHEFHSPALEDADFD 56
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
62-244 2.38e-13

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: 67.87  E-value: 2.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618  62 LLVGQYSTGKTTFIRHLIEQDFpgmrigpepttdSFIAVMHGPTEGVVPGNALVVDPRRPFRklnafgnaflnrfmcaql 141
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEV------------GEVSDVPGTTRDPDVYVKELDKGKVKLV------------------ 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 142 pnpvldsisIIDTPGILSGEKQRISRGYdfaavlEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDK-IRVVLNK 220
Cdd:cd00882  51 ---------LVDTPGLDEFGGLGREELA------RLLLRGADLILLVVDSTDRESEEDAKLLILRRLRKEGIpIILVGNK 115
                       170       180
                ....*....|....*....|....
gi 81910618 221 ADQIETQQLMRVYGALMWSLGKII 244
Cdd:cd00882 116 IDLLEEREVEELLRLEELAKILGV 139
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
61-220 1.65e-08

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: 52.62  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618    61 VLLVGQYSTGKTTFIRHLIEQDfpgMRIGPEP--TTDsfiavmhgPTEGVVpgnalvvdprrpfrklnafgnaflnrfmc 138
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAK---AIVSDYPgtTRD--------PNEGRL----------------------------- 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618   139 aqlpNPVLDSISIIDTPGILSGEKQRISRGYDFAAVlewfaERVDRIILLFDAHKlDISDEFSEVIKALKNHEDKIRVVL 218
Cdd:pfam01926  42 ----ELKGKQIILVDTPGLIEGASEGEGLGRAFLAI-----IEADLILFVVDSEE-GITPLDEELLELLRENKKPIILVL 111

                  ..
gi 81910618   219 NK 220
Cdd:pfam01926 112 NK 113
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
61-229 3.52e-06

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: 47.54  E-value: 3.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618  61 VLLVGQYSTGKTTFIRHLIEQDFPGMriGPEPTTdsfiavmhgptegvvpgnalvvdprrpfrklnafGNAFLNRFMCaq 140
Cdd:cd09912   3 LAVVGEFSAGKSTLLNALLGEEVLPT--GVTPTT----------------------------------AVITVLRYGL-- 44
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 141 lpnpvLDSISIIDTPGILSGEKQRisrgydfAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKIRVVLNK 220
Cdd:cd09912  45 -----LKGVVLVDTPGLNSTIEHH-------TEITESFLPRADAVIFVLSADQPLTESEREFLKEILKWSGKKIFFVLNK 112

                ....*....
gi 81910618 221 ADQIETQQL 229
Cdd:cd09912 113 IDLLSEEEL 121
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
146-228 1.24e-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: 42.62  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 146 LDSISIIDTPGILSGEKQRISRgydFAAVLEWfAERVDRIILLFDAhKLDISDEFSEVIKALKNhEDKIRVVLNKADQIE 225
Cdd:cd00880  45 LGPVVLIDTPGLDEEGGLGRER---VEEARQV-ADRADLVLLVVDS-DLTPVEEEAKLGLLRER-GKPVLLVLNKIDLVP 118

                ...
gi 81910618 226 TQQ 228
Cdd:cd00880 119 ESE 121
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
146-224 1.54e-04

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 41.94  E-value: 1.54e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81910618 146 LDSISIIDTPGIlsGEKQRISRGYDfAAVLEwFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKIRVVLNKADQI 224
Cdd:cd11383  44 GDGLVLLDLPGV--GERGRRDREYE-ELYRR-LLPEADLVLWLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVDPV 118
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
61-229 2.85e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 41.89  E-value: 2.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618  61 VLLVGQYSTGKTTFIRHLIEQDFPgmrigpepttdsfiAVMHGPTEGVvpgnaLVVDPRRPFRKLNAfgnaflnrfmcaq 140
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIFS--------------LEKYLSTNGV-----TIDKKELKLDGLDV------------- 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 141 lpnpvldSISIIDTPGILsgEKQRISRGYdfaavLEWFAERvDRIILLFDAHKLDISDEFSEVIKALKNHEDKIR--VVL 218
Cdd:COG1100  54 -------DLVIWDTPGQD--EFRETRQFY-----ARQLTGA-SLYLFVVDGTREETLQSLYELLESLRRLGKKSPiiLVL 118
                       170
                ....*....|.
gi 81910618 219 NKADQIETQQL 229
Cdd:COG1100 119 NKIDLYDEEEI 129
YeeP COG3596
Predicted GTPase [General function prediction only];
61-225 3.05e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 39.75  E-value: 3.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618  61 VLLVGQYSTGKTTFIRHLIEQDFpgMRIG-PEPTTDSFIAVmhgptegvvpgnalvvdprrpfrklnafgnaflnrfmca 139
Cdd:COG3596  42 IALVGKTGAGKSSLINALFGAEV--AEVGvGRPCTREIQRY--------------------------------------- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 140 QLPNPVLDSISIIDTPGIlsGEKQRISRGYdfaAVLEWFAERVDRIILLFDAHKLDI-SDEfsEVIKALKNHEDKIRV-- 216
Cdd:COG3596  81 RLESDGLPGLVLLDTPGL--GEVNERDREY---RELRELLPEADLILWVVKADDRALaTDE--EFLQALRAQYPDPPVlv 153

                ....*....
gi 81910618 217 VLNKADQIE 225
Cdd:COG3596 154 VLTQVDRLE 162
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
152-228 3.27e-03

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: 38.60  E-value: 3.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81910618 152 IDTPGILSGEKQRISRGYDFAavleWFA-ERVDRIILLFDAHK-LDISDEFseVIKALKNHEDKIRVVLNKADQIETQQ 228
Cdd:cd04163  56 VDTPGIHKPKKKLGERMVKAA----WSAlKDVDLVLFVVDASEwIGEGDEF--ILELLKKSKTPVILVLNKIDLVKDKE 128
EngA1 cd01894
EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first ...
149-241 3.73e-03

EngA1 GTPase contains the first domain of EngA; This EngA1 subfamily CD represents the first GTPase domain of EngA and its orthologs, which are composed of two adjacent GTPase domains. 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. Although the exact function of these proteins has not been elucidated, studies have revealed that the E. coli EngA homolog, Der, and Neisseria gonorrhoeae EngA are essential for cell viability. A recent report suggests that E. coli Der functions in ribosome assembly and stability.


Pssm-ID: 206681 [Multi-domain]  Cd Length: 157  Bit Score: 38.19  E-value: 3.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 149 ISIIDTPGILSGEK---QRIsrgydfAAVLEWFAERVDRIILLFDAhKLDISDEFSEVIKALKNHEDKIRVVLNKADQIE 225
Cdd:cd01894  47 FILIDTGGIEPDDEgisKEI------REQAEIAIEEADVILFVVDG-REGLTPADEEIAKYLRKSKKPVILVVNKIDNIK 119
                        90
                ....*....|....*.
gi 81910618 226 tqqlMRVYGALMWSLG 241
Cdd:cd01894 120 ----EEEEAAEFYSLG 131
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
152-230 9.62e-03

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 38.05  E-value: 9.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81910618 152 IDTPGILSGEK---QRISRgydfaAVLEWFAErVDRIILLFDAHKlDISDEFSEVIKALKNHEDKIRVVLNKADQIETQQ 228
Cdd:COG1159  56 VDTPGIHKPKRklgRRMNK-----AAWSALED-VDVILFVVDATE-KIGEGDEFILELLKKLKTPVILVINKIDLVKKEE 128

                ..
gi 81910618 229 LM 230
Cdd:COG1159 129 LL 130
 
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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