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Conserved domains on  [gi|41056039|ref|NP_956357|]
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EH domain-containing protein 2b [Danio rerio]

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 ...
58-298 1.79e-158

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: 450.96  E-value: 1.79e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039  58 MVLVVGQYSTGKTTFIKYLLEQDVPGSRIGPEPTTDCFTAIMHGDVEGLIPGNALIVDPNKPFRKLNPFGNTFLNRFQCA 137
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 138 QLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRWFAERVDRIILLFDAHKLEISDEFSEAIGALKGNEDKLRVVLN 217
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 218 KADMVDTQQLMRVYGALMWSLGKVFGTPEVLRVYIGSFWSEPLMVTDNRKLFELEEEDLFADIQNLPRNAALRKLNDLVK 297
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 41056039 298 R 298
Cdd:cd09913 241 R 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
286-392 3.90e-60

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: 193.99  E-value: 3.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039   286 NAALRKLNDLVKRARLVRVHAHIISYLKQEMPSVFRKDNKKKNLIYQLPVIFSKIQLQHHISPGDFPDCAKMQEQLMAHD 365
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 41056039   366 FTKFKALKPNLMNMLDELLSSDIAKLM 392
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
443-536 2.28e-33

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: 2.28e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039    443 EWVVT-KDKPKYDEIFYNLAPN-EGKLSGTKAKDWMVSTRLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEVKLDGH 520
Cdd:smart00027   1 PWAISpEDKAKYEQIFRSLDKNqDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 41056039    521 GLPPELPARLVPPSKR 536
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 ...
22-54 1.44e-15

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: 70.12  E-value: 1.44e-15
                          10        20        30
                  ....*....|....*....|....*....|...
gi 41056039    22 GLKSLYRKKLLPLEQYYGFHDFHSPSLEDADFD 54
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 ...
58-298 1.79e-158

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: 450.96  E-value: 1.79e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039  58 MVLVVGQYSTGKTTFIKYLLEQDVPGSRIGPEPTTDCFTAIMHGDVEGLIPGNALIVDPNKPFRKLNPFGNTFLNRFQCA 137
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 138 QLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRWFAERVDRIILLFDAHKLEISDEFSEAIGALKGNEDKLRVVLN 217
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 218 KADMVDTQQLMRVYGALMWSLGKVFGTPEVLRVYIGSFWSEPLMVTDNRKLFELEEEDLFADIQNLPRNAALRKLNDLVK 297
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 41056039 298 R 298
Cdd:cd09913 241 R 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
286-392 3.90e-60

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: 193.99  E-value: 3.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039   286 NAALRKLNDLVKRARLVRVHAHIISYLKQEMPSVFRKDNKKKNLIYQLPVIFSKIQLQHHISPGDFPDCAKMQEQLMAHD 365
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 41056039   366 FTKFKALKPNLMNMLDELLSSDIAKLM 392
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
443-536 2.28e-33

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: 2.28e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039    443 EWVVT-KDKPKYDEIFYNLAPN-EGKLSGTKAKDWMVSTRLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEVKLDGH 520
Cdd:smart00027   1 PWAISpEDKAKYEQIFRSLDKNqDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 41056039    521 GLPPELPARLVPPSKR 536
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
Dynamin_N pfam00350
Dynamin family;
59-219 2.65e-24

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 99.61  E-value: 2.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039    59 VLVVGQYSTGKTTFIKYLLEQDVPGSriGPEPTTDCFTAIMHGDVEGLIPG--NALIVDPNKPFRKLNPFGNTFLNRFQC 136
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPR--GPGPTTRRPTVLRLGESPGASEGavKVEYKDGEKKFEDFSELREEIEKETEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039   137 -AQLPNQVLES-------------ISIIDTPGILSGAKQRVsrgydfpAVLRWFAERVDRIILLFDAHKLEISDEFSEAI 202
Cdd:pfam00350  79 iAGTGKGISSEpivleilsplvpgLTLVDTPGLDSVAVGDQ-------ELTKEYIKPADIILAVTPANVDLSTSEALFLA 151
                         170
                  ....*....|....*..
gi 41056039   203 GALKGNEDKLRVVLNKA 219
Cdd:pfam00350 152 REVDPNGKRTIGVLTKA 168
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
453-517 4.76e-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: 86.89  E-value: 4.76e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41056039 453 YDEIFYNLAPNE-GKLSGTKAKDWMVSTRLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEVKL 517
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 ...
442-536 3.33e-19

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: 82.81  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039   442 EEWvvtkDKPKYDEIFYNLAPNEGKLSGTKAKDWMVSTRLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEVKLDGH- 520
Cdd:pfam12763   5 EEW----EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80
                          90
                  ....*....|....*..
gi 41056039   521 -GLPPELPARLVPPSKR 536
Cdd:pfam12763  81 aDVPDELPDWLVPGSKA 97
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
22-54 1.44e-15

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: 70.12  E-value: 1.44e-15
                          10        20        30
                  ....*....|....*....|....*....|...
gi 41056039    22 GLKSLYRKKLLPLEQYYGFHDFHSPSLEDADFD 54
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
59-227 9.45e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 43.43  E-value: 9.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039  59 VLVVGQYSTGKTTFIKYLLEQDVPGSRIGPEpttdcftaimHGdveglipgnALIVdpnkpfRKlnpfgntflnRFQCAQ 138
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLST----------NG---------VTID------KK----------ELKLDG 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 139 LPNQVLesisIIDTPGILsgaKQRVSRgydfPAVLRWFAERvDRIILLFDAHKLEISDEFSEAIGALKGNEDKLR--VVL 216
Cdd:COG1100  51 LDVDLV----IWDTPGQD---EFRETR----QFYARQLTGA-SLYLFVVDGTREETLQSLYELLESLRRLGKKSPiiLVL 118
                       170
                ....*....|.
gi 41056039 217 NKADMVDTQQL 227
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 ...
58-298 1.79e-158

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: 450.96  E-value: 1.79e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039  58 MVLVVGQYSTGKTTFIKYLLEQDVPGSRIGPEPTTDCFTAIMHGDVEGLIPGNALIVDPNKPFRKLNPFGNTFLNRFQCA 137
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 138 QLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRWFAERVDRIILLFDAHKLEISDEFSEAIGALKGNEDKLRVVLN 217
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 218 KADMVDTQQLMRVYGALMWSLGKVFGTPEVLRVYIGSFWSEPLMVTDNRKLFELEEEDLFADIQNLPRNAALRKLNDLVK 297
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 41056039 298 R 298
Cdd:cd09913 241 R 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
286-392 3.90e-60

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: 193.99  E-value: 3.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039   286 NAALRKLNDLVKRARLVRVHAHIISYLKQEMPSVFRKDNKKKNLIYQLPVIFSKIQLQHHISPGDFPDCAKMQEQLMAHD 365
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 41056039   366 FTKFKALKPNLMNMLDELLSSDIAKLM 392
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
443-536 2.28e-33

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: 2.28e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039    443 EWVVT-KDKPKYDEIFYNLAPN-EGKLSGTKAKDWMVSTRLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEVKLDGH 520
Cdd:smart00027   1 PWAISpEDKAKYEQIFRSLDKNqDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 41056039    521 GLPPELPARLVPPSKR 536
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
Dynamin_N pfam00350
Dynamin family;
59-219 2.65e-24

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 99.61  E-value: 2.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039    59 VLVVGQYSTGKTTFIKYLLEQDVPGSriGPEPTTDCFTAIMHGDVEGLIPG--NALIVDPNKPFRKLNPFGNTFLNRFQC 136
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPR--GPGPTTRRPTVLRLGESPGASEGavKVEYKDGEKKFEDFSELREEIEKETEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039   137 -AQLPNQVLES-------------ISIIDTPGILSGAKQRVsrgydfpAVLRWFAERVDRIILLFDAHKLEISDEFSEAI 202
Cdd:pfam00350  79 iAGTGKGISSEpivleilsplvpgLTLVDTPGLDSVAVGDQ-------ELTKEYIKPADIILAVTPANVDLSTSEALFLA 151
                         170
                  ....*....|....*..
gi 41056039   203 GALKGNEDKLRVVLNKA 219
Cdd:pfam00350 152 REVDPNGKRTIGVLTKA 168
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
453-517 4.76e-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: 86.89  E-value: 4.76e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41056039 453 YDEIFYNLAPNE-GKLSGTKAKDWMVSTRLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEVKL 517
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 ...
442-536 3.33e-19

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: 82.81  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039   442 EEWvvtkDKPKYDEIFYNLAPNEGKLSGTKAKDWMVSTRLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEVKLDGH- 520
Cdd:pfam12763   5 EEW----EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNi 80
                          90
                  ....*....|....*..
gi 41056039   521 -GLPPELPARLVPPSKR 536
Cdd:pfam12763  81 aDVPDELPDWLVPGSKA 97
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
22-54 1.44e-15

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: 70.12  E-value: 1.44e-15
                          10        20        30
                  ....*....|....*....|....*....|...
gi 41056039    22 GLKSLYRKKLLPLEQYYGFHDFHSPSLEDADFD 54
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
60-238 8.62e-12

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: 63.24  E-value: 8.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039  60 LVVGQYSTGKTTFIKYLLEQDVPGSRIGPEPTTDCftaimhgdveglIPGNALIVDPNKPFRklnpfgntflnrfqcaql 139
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDP------------DVYVKELDKGKVKLV------------------ 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 140 pnqvlesisIIDTPGILSGAKQRVSRGYdfpavlRWFAERVDRIILLFDAHKLEISDEFSEAIGALKGNEDK-LRVVLNK 218
Cdd:cd00882  51 ---------LVDTPGLDEFGGLGREELA------RLLLRGADLILLVVDSTDRESEEDAKLLILRRLRKEGIpIILVGNK 115
                       170       180
                ....*....|....*....|
gi 41056039 219 ADMVDTQQLMRVYGALMWSL 238
Cdd:cd00882 116 IDLLEEREVEELLRLEELAK 135
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
59-218 6.94e-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: 50.70  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039    59 VLVVGQYSTGKTTFIKYLLEQDvpgSRIGPEP-TTdcftaimhgdveglipgnaliVDPNkpFRKLNPFGNTFLnrfqca 137
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAK---AIVSDYPgTT---------------------RDPN--EGRLELKGKQII------ 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039   138 qlpnqvlesisIIDTPGILSGAKQRVSRGYDFPAVlrwfaERVDRIILLFDAHKlEISDEFSEAIGALKGNEDKLRVVLN 217
Cdd:pfam01926  50 -----------LVDTPGLIEGASEGEGLGRAFLAI-----IEADLILFVVDSEE-GITPLDEELLELLRENKKPIILVLN 112

                  .
gi 41056039   218 K 218
Cdd:pfam01926 113 K 113
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
59-227 4.46e-07

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: 50.24  E-value: 4.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039  59 VLVVGQYSTGKTTFIKYLLEQDVPGSriGPEPTTDCFTAIMHGdveglipgnalivdpnkpfrklnpfgntflnrfqcaq 138
Cdd:cd09912   3 LAVVGEFSAGKSTLLNALLGEEVLPT--GVTPTTAVITVLRYG------------------------------------- 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 139 lpnqVLESISIIDTPGILSGAKQRVsrgydfpAVLRWFAERVDRIILLFDA-HKLEISD-EFSEAIgaLKGNEDKLRVVL 216
Cdd:cd09912  44 ----LLKGVVLVDTPGLNSTIEHHT-------EITESFLPRADAVIFVLSAdQPLTESErEFLKEI--LKWSGKKIFFVL 110
                       170
                ....*....|.
gi 41056039 217 NKADMVDTQQL 227
Cdd:cd09912 111 NKIDLLSEEEL 121
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
59-227 9.45e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 43.43  E-value: 9.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039  59 VLVVGQYSTGKTTFIKYLLEQDVPGSRIGPEpttdcftaimHGdveglipgnALIVdpnkpfRKlnpfgntflnRFQCAQ 138
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLST----------NG---------VTID------KK----------ELKLDG 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 139 LPNQVLesisIIDTPGILsgaKQRVSRgydfPAVLRWFAERvDRIILLFDAHKLEISDEFSEAIGALKGNEDKLR--VVL 216
Cdd:COG1100  51 LDVDLV----IWDTPGQD---EFRETR----QFYARQLTGA-SLYLFVVDGTREETLQSLYELLESLRRLGKKSPiiLVL 118
                       170
                ....*....|.
gi 41056039 217 NKADMVDTQQL 227
Cdd:COG1100 119 NKIDLYDEEEI 129
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
149-226 2.45e-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: 2.45e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41056039 149 IIDTPGILSGAKQRVSRGydfpAVLRWFAERVDRIILLFDAHKLEisDEFSEAIGALKGNEDKLRVVLNKADMVDTQQ 226
Cdd:cd00880  50 LIDTPGLDEEGGLGRERV----EEARQVADRADLVLLVVDSDLTP--VEEEAKLGLLRERGKPVLLVLNKIDLVPESE 121
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
61-229 4.19e-04

Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; The Obg-like subfamily consists of five well-delimited, ancient subfamilies, namely Obg, DRG, YyaF/YchF, Ygr210, and NOG1. Four of these groups (Obg, DRG, YyaF/YchF, and Ygr210) are characterized by a distinct glycine-rich motif immediately following the Walker B motif (G3 box). Obg/CgtA is an essential gene that is involved in the initiation of sporulation and DNA replication in the bacteria Caulobacter and Bacillus, but its exact molecular role is unknown. Furthermore, several OBG family members possess a C-terminal RNA-binding domain, the TGS domain, which is also present in threonyl-tRNA synthetase and in bacterial guanosine polyphosphatase SpoT. Nog1 is a nucleolar protein that might function in ribosome assembly. The DRG and Nog1 subfamilies are ubiquitous in archaea and eukaryotes, the Ygr210 subfamily is present in archaea and fungi, and the Obg and YyaF/YchF subfamilies are ubiquitous in bacteria and eukaryotes. The Obg/Nog1 and DRG subfamilies appear to form one major branch of the Obg family and the Ygr210 and YchF subfamilies form another branch. No GEFs, GAPs, or GDIs for Obg have been identified.


Pssm-ID: 206668 [Multi-domain]  Cd Length: 167  Bit Score: 41.23  E-value: 4.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039  61 VVGQYSTGKTTFIKYLLEQDVpgsRIGPEPttdcFTAImhgdveGLIPGnalivdpnkpfrklnpfgntflnrfqcaQLP 140
Cdd:cd01881   2 LVGLPNVGKSTLLSALTSAKV---EIASYP----FTTL------EPNVG----------------------------VFE 40
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056039 141 NQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRwfaeRVDRIILLFDAHKLEISDE-------FSEAIGALKGNEDKLR 213
Cdd:cd01881  41 FGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLY----RSDLILHVIDASEDCVGDPledqktlNEEVSGSFLFLKNKPE 116
                       170
                ....*....|....*..
gi 41056039 214 V-VLNKADMVDTQQLMR 229
Cdd:cd01881 117 MiVANKIDMASENNLKR 133
 
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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