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Conserved domains on  [gi|2217300846|ref|XP_047288364|]
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EH domain-containing protein 4 isoform X1 [Homo sapiens]

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 ...
 1-215 1.49e-139

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: 399.73  E-value: 1.49e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846   1 MRIGPEPTTDSFIAVMYGETEGSTPGNALVVDPKKPFRKLSRFGNAFLNRFMCSQLPNQVLKSISVIDSPGILSGEKQRI 80
Cdd:cd09913    27 LRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGSTLPHPLLESVTIVDTPGILSGEKQRQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846  81 SRGYDFCQVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVIN 160
Cdd:cd09913   107 SRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLNKADMVDTQQLMRVYGALMWSLSKVIN 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217300846 161 TPEVLRVYIGSFWAQPLQNTDNRRLFEAEAQDLFRDIQSLPQKAAVRKLNDLIKR 215
Cdd:cd09913   187 TPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIKR 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
 204-309 9.99e-63

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: 198.22  E-value: 9.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846 204 AAVRKLNDLIKRARLAKVHAYIISYLKKEMPSVFGKENKKRELISRLPEIYIQLQREYQISAGDFPEVKAMQEQLENYDF 283
Cdd:pfam18150   2 AAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYDF 81

                          90       100
                  ....*....|....*....|....*.
gi 2217300846 284 TKFHSLKPKLIEAVDNMLSNKISPLM 309
Cdd:pfam18150  82 TKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 353-446 6.10e-34

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: 122.39  E-value: 6.10e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846  353 EWVV-AKDKPVYDELFYTLSP-INGKISGVNAKKEMVTSKLPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIKLDGY 430
Cdd:smart00027   1 PWAIsPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....*.
gi 2217300846  431 ELPSSLPPHLVPPSHR 446
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
 
Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 1-215 1.49e-139

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: 399.73  E-value: 1.49e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846   1 MRIGPEPTTDSFIAVMYGETEGSTPGNALVVDPKKPFRKLSRFGNAFLNRFMCSQLPNQVLKSISVIDSPGILSGEKQRI 80
Cdd:cd09913    27 LRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGSTLPHPLLESVTIVDTPGILSGEKQRQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846  81 SRGYDFCQVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVIN 160
Cdd:cd09913   107 SRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLNKADMVDTQQLMRVYGALMWSLSKVIN 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217300846 161 TPEVLRVYIGSFWAQPLQNTDNRRLFEAEAQDLFRDIQSLPQKAAVRKLNDLIKR 215
Cdd:cd09913   187 TPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIKR 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
 204-309 9.99e-63

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: 198.22  E-value: 9.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846 204 AAVRKLNDLIKRARLAKVHAYIISYLKKEMPSVFGKENKKRELISRLPEIYIQLQREYQISAGDFPEVKAMQEQLENYDF 283
Cdd:pfam18150   2 AAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYDF 81

                          90       100
                  ....*....|....*....|....*.
gi 2217300846 284 TKFHSLKPKLIEAVDNMLSNKISPLM 309
Cdd:pfam18150  82 TKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 353-446 6.10e-34

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: 122.39  E-value: 6.10e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846  353 EWVV-AKDKPVYDELFYTLSP-INGKISGVNAKKEMVTSKLPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIKLDGY 430
Cdd:smart00027   1 PWAIsPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....*.
gi 2217300846  431 ELPSSLPPHLVPPSHR 446
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 363-427 5.43e-21

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: 86.12  E-value: 5.43e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217300846 363 YDELFYTLSPIN-GKISGVNAKKEMVTSKLPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIKL 427
Cdd:cd00052     1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 352-444 4.55e-17

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: 76.64  E-value: 4.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846 352 EEWVVAKdkpvYDELFYTLSPINGKISGVNAKKEMVTSKLPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIKLDGY- 430
Cdd:pfam12763   5 EEWEIKK----YWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80

                          90
                  ....*....|....*
gi 2217300846 431 -ELPSSLPPHLVPPS 444
Cdd:pfam12763  81 aDVPDELPDWLVPGS 95
Dynamin_N pfam00350
Dynamin family;
3-136 1.06e-12

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 66.10  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846   3 IGPEPTTDSFIAVMYGETEGSTPG--NALVVDPKKPFRKLSRFGNAFLNRFMCSQLPNQ--------------VLKSISV 66
Cdd:pfam00350  26 RGPGPTTRRPTVLRLGESPGASEGavKVEYKDGEKKFEDFSELREEIEKETEKIAGTGKgissepivleilspLVPGLTL 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846  67 IDSPGILSGEKQRISrgydfcqVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKA 136
Cdd:pfam00350 106 VDTPGLDSVAVGDQE-------LTKEYIKPADIILAVTPANVDLSTSEALFLAREVDPNGKRTIGVLTKA 168
 
Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
 1-215 1.49e-139

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: 399.73  E-value: 1.49e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846   1 MRIGPEPTTDSFIAVMYGETEGSTPGNALVVDPKKPFRKLSRFGNAFLNRFMCSQLPNQVLKSISVIDSPGILSGEKQRI 80
Cdd:cd09913    27 LRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGSTLPHPLLESVTIVDTPGILSGEKQRQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846  81 SRGYDFCQVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVIN 160
Cdd:cd09913   107 SRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLNKADMVDTQQLMRVYGALMWSLSKVIN 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217300846 161 TPEVLRVYIGSFWAQPLQNTDNRRLFEAEAQDLFRDIQSLPQKAAVRKLNDLIKR 215
Cdd:cd09913   187 TPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIKR 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
 204-309 9.99e-63

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: 198.22  E-value: 9.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846 204 AAVRKLNDLIKRARLAKVHAYIISYLKKEMPSVFGKENKKRELISRLPEIYIQLQREYQISAGDFPEVKAMQEQLENYDF 283
Cdd:pfam18150   2 AAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYDF 81

                          90       100
                  ....*....|....*....|....*.
gi 2217300846 284 TKFHSLKPKLIEAVDNMLSNKISPLM 309
Cdd:pfam18150  82 TKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 353-446 6.10e-34

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: 122.39  E-value: 6.10e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846  353 EWVV-AKDKPVYDELFYTLSP-INGKISGVNAKKEMVTSKLPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIKLDGY 430
Cdd:smart00027   1 PWAIsPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80

                           90
                   ....*....|....*.
gi 2217300846  431 ELPSSLPPHLVPPSHR 446
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 363-427 5.43e-21

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: 86.12  E-value: 5.43e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217300846 363 YDELFYTLSPIN-GKISGVNAKKEMVTSKLPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIKL 427
Cdd:cd00052     1 YDQIFRSLDPDGdGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALAL 66
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
 352-444 4.55e-17

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: 76.64  E-value: 4.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846 352 EEWVVAKdkpvYDELFYTLSPINGKISGVNAKKEMVTSKLPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIKLDGY- 430
Cdd:pfam12763   5 EEWEIKK----YWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80

                          90
                  ....*....|....*
gi 2217300846 431 -ELPSSLPPHLVPPS 444
Cdd:pfam12763  81 aDVPDELPDWLVPGS 95
Dynamin_N pfam00350
Dynamin family;
3-136 1.06e-12

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 66.10  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846   3 IGPEPTTDSFIAVMYGETEGSTPG--NALVVDPKKPFRKLSRFGNAFLNRFMCSQLPNQ--------------VLKSISV 66
Cdd:pfam00350  26 RGPGPTTRRPTVLRLGESPGASEGavKVEYKDGEKKFEDFSELREEIEKETEKIAGTGKgissepivleilspLVPGLTL 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846  67 IDSPGILSGEKQRISrgydfcqVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKA 136
Cdd:pfam00350 106 VDTPGLDSVAVGDQE-------LTKEYIKPADIILAVTPANVDLSTSEALFLAREVDPNGKRTIGVLTKA 168
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 60-155 1.20e-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: 45.53  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846  60 VLKSISVIDSPGILSGEKQRISRGYDfcqvlqWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDK-IRVVLNKADQ 138
Cdd:cd00882    45 GKVKLVLVDTPGLDEFGGLGREELAR------LLLRGADLILLVVDSTDRESEEDAKLLILRRLRKEGIpIILVGNKIDL 118

                          90
                  ....*....|....*..
gi 2217300846 139 VDTQQLMRVYGALMWSL 155
Cdd:cd00882   119 LEEREVEELLRLEELAK 135
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 62-135 1.12e-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: 41.45  E-value: 1.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217300846  62 KSISVIDSPGILSGEKQRISRGYDFCQVlqwfaERVDRIILLFDAHKlDISDEFSEAIKAFRGQDDKIRVVLNK 135
Cdd:pfam01926  46 KQIILVDTPGLIEGASEGEGLGRAFLAI-----IEADLILFVVDSEE-GITPLDEELLELLRENKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 61-143 3.95e-03

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: 38.00  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217300846  61 LKSISVIDSPGILSGEKQRISRGYDFCQVlqwfAERVDRIILLFDAhKLDISDEFsEAIKAFRGQDDKIRVVLNKADQVD 140
Cdd:cd00880    45 LGPVVLIDTPGLDEEGGLGRERVEEARQV----ADRADLVLLVVDS-DLTPVEEE-AKLGLLRERGKPVLLVLNKIDLVP 118


                  ...
gi 2217300846 141 TQQ 143
Cdd:cd00880   119 ESE 121
 
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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