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Conserved domains on  [gi|21361462|ref|NP_055416|]
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EH domain-containing protein 2 [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 ...
60-300 6.69e-161

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: 457.12  E-value: 6.69e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462  60 MVLVAGQYSTGKTSFIQYLLEQEVPGSRVGPEPTTDCFVAVMHGDTEGTVPGNALVVDPDKPFRKLNPFGNTFLNRFMCA 139
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 140 QLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRWFAERVDLIILLFDAHKLEISDEFSEAIGALRGHEDKIRVVLN 219
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 220 KADMVETQQLMRVYGALMWALGKVVGTPEVLRVYIGSFWSQPLLVPDNRRLFELEEQDLFRDIQGLPRHAALRKLNDLVK 299
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 21361462 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 3.28e-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: 202.08  E-value: 3.28e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462   288 HAALRKLNDLVKRARLVRVHAYIISYLKKEMPSVFGKENKKKQLILKLPVIFAKIQLEHHISPGDFPDCQKMQELLMAHD 367
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 21361462   368 FTKFHSLKPKLLEALDEMLTHDIAKLM 394
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
443-536 9.76e-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: 120.46  E-value: 9.76e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462    443 EWVVT-KDKSKYDEIFYNLAPA-DGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLEGH 520
Cdd:smart00027   1 PWAISpEDKAKYEQIFRSLDKNqDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 21361462    521 GLPANLPRRLVPPSKR 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 ...
24-56 2.21e-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: 67.04  E-value: 2.21e-14
                          10        20        30
                  ....*....|....*....|....*....|...
gi 21361462    24 ALKELYRTKLLPLEEHYRFGAFHSPALEDADFD 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 6.69e-161

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: 457.12  E-value: 6.69e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462  60 MVLVAGQYSTGKTSFIQYLLEQEVPGSRVGPEPTTDCFVAVMHGDTEGTVPGNALVVDPDKPFRKLNPFGNTFLNRFMCA 139
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 140 QLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRWFAERVDLIILLFDAHKLEISDEFSEAIGALRGHEDKIRVVLN 219
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 220 KADMVETQQLMRVYGALMWALGKVVGTPEVLRVYIGSFWSQPLLVPDNRRLFELEEQDLFRDIQGLPRHAALRKLNDLVK 299
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 21361462 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 3.28e-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: 202.08  E-value: 3.28e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462   288 HAALRKLNDLVKRARLVRVHAYIISYLKKEMPSVFGKENKKKQLILKLPVIFAKIQLEHHISPGDFPDCQKMQELLMAHD 367
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 21361462   368 FTKFHSLKPKLLEALDEMLTHDIAKLM 394
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
443-536 9.76e-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: 120.46  E-value: 9.76e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462    443 EWVVT-KDKSKYDEIFYNLAPA-DGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLEGH 520
Cdd:smart00027   1 PWAISpEDKAKYEQIFRSLDKNqDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 21361462    521 GLPANLPRRLVPPSKR 536
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
Dynamin_N pfam00350
Dynamin family;
61-221 3.15e-22

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 93.45  E-value: 3.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462    61 VLVAGQYSTGKTSFIQYLLEQEVPGSrvGPEPTTDCFVAVMHGDTEGTVPG--NALVVDPDKPFRKLNPFGNTFLNRFMC 138
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPR--GPGPTTRRPTVLRLGESPGASEGavKVEYKDGEKKFEDFSELREEIEKETEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462   139 -AQLPNQVLES-------------ISIIDTPGILSGAKQRVsrgydfpAVLRWFAERVDLIILLFDAHKLEISDEFSEAI 204
Cdd:pfam00350  79 iAGTGKGISSEpivleilsplvpgLTLVDTPGLDSVAVGDQ-------ELTKEYIKPADIILAVTPANVDLSTSEALFLA 151
                         170
                  ....*....|....*..
gi 21361462   205 GALRGHEDKIRVVLNKA 221
Cdd:pfam00350 152 REVDPNGKRTIGVLTKA 168
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
453-518 5.42e-22

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: 89.59  E-value: 5.42e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361462 453 YDEIFYNLAPA-DGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLE 518
Cdd:cd00052   1 YDQIFRSLDPDgDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
449-536 8.35e-20

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: 84.73  E-value: 8.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462   449 DKSKYDEIFYNLAPADGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLEGH--GLPANL 526
Cdd:pfam12763   8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPDEL 87
                          90
                  ....*....|
gi 21361462   527 PRRLVPPSKR 536
Cdd:pfam12763  88 PDWLVPGSKA 97
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
24-56 2.21e-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: 67.04  E-value: 2.21e-14
                          10        20        30
                  ....*....|....*....|....*....|...
gi 21361462    24 ALKELYRTKLLPLEEHYRFGAFHSPALEDADFD 56
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
YeeP COG3596
Predicted GTPase [General function prediction only];
57-225 9.25e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.84  E-value: 9.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462  57 GKPMVLVAGQYSTGKTSFIQYLLEQEVpgSRVG-PEPTTDcfvavmhgdtegtvpgnalvvdpdkpfrklnpfgntflnR 135
Cdd:COG3596  38 PPPVIALVGKTGAGKSSLINALFGAEV--AEVGvGRPCTR---------------------------------------E 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 136 FMCAQLPNQVLESISIIDTPGIlsgakQRVSRGYDFPAVLRWFAERVDLIILLFDAHK--LEISDEFSEAIgaLRGHED- 212
Cdd:COG3596  77 IQRYRLESDGLPGLVLLDTPGL-----GEVNERDREYRELRELLPEADLILWVVKADDraLATDEEFLQAL--RAQYPDp 149
                       170
                ....*....|...
gi 21361462 213 KIRVVLNKADMVE 225
Cdd:COG3596 150 PVLVVLTQVDRLE 162
 
Name Accession Description Interval E-value
EHD cd09913
Eps15 homology domain (EHD), C-terminal domain; Dynamin-like C-terminal Eps15 homology domain ...
60-300 6.69e-161

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: 457.12  E-value: 6.69e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462  60 MVLVAGQYSTGKTSFIQYLLEQEVPGSRVGPEPTTDCFVAVMHGDTEGTVPGNALVVDPDKPFRKLNPFGNTFLNRFMCA 139
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 140 QLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRWFAERVDLIILLFDAHKLEISDEFSEAIGALRGHEDKIRVVLN 219
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 220 KADMVETQQLMRVYGALMWALGKVVGTPEVLRVYIGSFWSQPLLVPDNRRLFELEEQDLFRDIQGLPRHAALRKLNDLVK 299
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 21361462 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 3.28e-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: 202.08  E-value: 3.28e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462   288 HAALRKLNDLVKRARLVRVHAYIISYLKKEMPSVFGKENKKKQLILKLPVIFAKIQLEHHISPGDFPDCQKMQELLMAHD 367
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 21361462   368 FTKFHSLKPKLLEALDEMLTHDIAKLM 394
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
443-536 9.76e-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: 120.46  E-value: 9.76e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462    443 EWVVT-KDKSKYDEIFYNLAPA-DGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLEGH 520
Cdd:smart00027   1 PWAISpEDKAKYEQIFRSLDKNqDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGY 80
                           90
                   ....*....|....*.
gi 21361462    521 GLPANLPRRLVPPSKR 536
Cdd:smart00027  81 PIPASLPPSLIPPSKR 96
Dynamin_N pfam00350
Dynamin family;
61-221 3.15e-22

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 93.45  E-value: 3.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462    61 VLVAGQYSTGKTSFIQYLLEQEVPGSrvGPEPTTDCFVAVMHGDTEGTVPG--NALVVDPDKPFRKLNPFGNTFLNRFMC 138
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPR--GPGPTTRRPTVLRLGESPGASEGavKVEYKDGEKKFEDFSELREEIEKETEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462   139 -AQLPNQVLES-------------ISIIDTPGILSGAKQRVsrgydfpAVLRWFAERVDLIILLFDAHKLEISDEFSEAI 204
Cdd:pfam00350  79 iAGTGKGISSEpivleilsplvpgLTLVDTPGLDSVAVGDQ-------ELTKEYIKPADIILAVTPANVDLSTSEALFLA 151
                         170
                  ....*....|....*..
gi 21361462   205 GALRGHEDKIRVVLNKA 221
Cdd:pfam00350 152 REVDPNGKRTIGVLTKA 168
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
453-518 5.42e-22

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: 89.59  E-value: 5.42e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361462 453 YDEIFYNLAPA-DGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLE 518
Cdd:cd00052   1 YDQIFRSLDPDgDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
449-536 8.35e-20

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: 84.73  E-value: 8.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462   449 DKSKYDEIFYNLAPADGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLEGH--GLPANL 526
Cdd:pfam12763   8 EIKKYWEIFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGNiaDVPDEL 87
                          90
                  ....*....|
gi 21361462   527 PRRLVPPSKR 536
Cdd:pfam12763  88 PDWLVPGSKA 97
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
62-244 3.07e-15

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: 73.26  E-value: 3.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462  62 LVAGQYSTGKTSFIQYLLEQEVPGSRVGPEPTTDCfvavmhgdtegtvpgNALVVDPDKPFRKLNpfgntflnrfmcaql 141
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDP---------------DVYVKELDKGKVKLV--------------- 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 142 pnqvlesisIIDTPGILSGAKQRVSRGYdfpavlRWFAERVDLIILLFDAHKLEISDEFSEAI-GALRGHEDKIRVVLNK 220
Cdd:cd00882  51 ---------LVDTPGLDEFGGLGREELA------RLLLRGADLILLVVDSTDRESEEDAKLLIlRRLRKEGIPIILVGNK 115
                       170       180
                ....*....|....*....|....
gi 21361462 221 ADMVETQQLMRVYGALMWALGKVV 244
Cdd:cd00882 116 IDLLEEREVEELLRLEELAKILGV 139
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
24-56 2.21e-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: 67.04  E-value: 2.21e-14
                          10        20        30
                  ....*....|....*....|....*....|...
gi 21361462    24 ALKELYRTKLLPLEEHYRFGAFHSPALEDADFD 56
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
148-220 2.29e-07

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: 49.54  E-value: 2.29e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361462   148 SISIIDTPGILSGAKQRVSRGYDFPAVlrwfaERVDLIILLFDAHKlEISDEFSEAIGALRGHEDKIRVVLNK 220
Cdd:pfam01926  47 QIILVDTPGLIEGASEGEGLGRAFLAI-----IEADLILFVVDSEE-GITPLDEELLELLRENKKPIILVLNK 113
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
61-229 2.50e-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: 51.01  E-value: 2.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462  61 VLVAGQYSTGKTSFIQYLLEQEV-PgsrVGPEPTTD--CFVAVmhgdtegtvpgnalvvdpdkpfrklnpfgntflnrfm 137
Cdd:cd09912   3 LAVVGEFSAGKSTLLNALLGEEVlP---TGVTPTTAviTVLRY------------------------------------- 42
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 138 caqlpnQVLESISIIDTPGILSGAKQRVsrgydfpAVLRWFAERVDLIILLFDA-HKLEISD-EFSEAIGALRGheDKIR 215
Cdd:cd09912  43 ------GLLKGVVLVDTPGLNSTIEHHT-------EITESFLPRADAVIFVLSAdQPLTESErEFLKEILKWSG--KKIF 107
                       170
                ....*....|....
gi 21361462 216 VVLNKADMVETQQL 229
Cdd:cd09912 108 FVLNKIDLLSEEEL 121
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
151-228 5.51e-06

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: 46.47  E-value: 5.51e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361462 151 IIDTPGILSGAKQRVSRGydfpAVLRWFAERVDLIILLFDAHKLEisDEFSEAIGALRGHEDKIRVVLNKADMVETQQ 228
Cdd:cd00880  50 LIDTPGLDEEGGLGRERV----EEARQVADRADLVLLVVDSDLTP--VEEEAKLGLLRERGKPVLLVLNKIDLVPESE 121
YeeP COG3596
Predicted GTPase [General function prediction only];
57-225 9.25e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.84  E-value: 9.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462  57 GKPMVLVAGQYSTGKTSFIQYLLEQEVpgSRVG-PEPTTDcfvavmhgdtegtvpgnalvvdpdkpfrklnpfgntflnR 135
Cdd:COG3596  38 PPPVIALVGKTGAGKSSLINALFGAEV--AEVGvGRPCTR---------------------------------------E 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 136 FMCAQLPNQVLESISIIDTPGIlsgakQRVSRGYDFPAVLRWFAERVDLIILLFDAHK--LEISDEFSEAIgaLRGHED- 212
Cdd:COG3596  77 IQRYRLESDGLPGLVLLDTPGL-----GEVNERDREYRELRELLPEADLILWVVKADDraLATDEEFLQAL--RAQYPDp 149
                       170
                ....*....|...
gi 21361462 213 KIRVVLNKADMVE 225
Cdd:COG3596 150 PVLVVLTQVDRLE 162
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
61-229 4.58e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 44.20  E-value: 4.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462  61 VLVAGQYSTGKTSFIQYLLEQEVPGSRVGPepttdcfvavmhgdTEGTVPGNALVVDPDKPFRklnpfgntflnrfmcaq 140
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLS--------------TNGVTIDKKELKLDGLDVD----------------- 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 141 lpnqvlesISIIDTPGILsgaKQRVSRgydfPAVLRWFAERvDLIILLFDAHKLEISDEFSEAIGALRGHEDKIR--VVL 218
Cdd:COG1100  55 --------LVIWDTPGQD---EFRETR----QFYARQLTGA-SLYLFVVDGTREETLQSLYELLESLRRLGKKSPiiLVL 118
                       170
                ....*....|.
gi 21361462 219 NKADMVETQQL 229
Cdd:COG1100 119 NKIDLYDEEEI 129
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
146-224 1.51e-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: 1.51e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361462 146 LESISIIDTPGIlsGAKQRVSRGYDfpAVLRWFAERVDLIILLFDAHKLEISDEFSEAIGALRGHEDKIRVVLNKADMV 224
Cdd:cd11383  44 GDGLVLLDLPGV--GERGRRDREYE--ELYRRLLPEADLVLWLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVDPV 118
Obg_like cd01881
Obg-like family of GTPases consist of five subfamilies: Obg, DRG, YyaF/YchF, Ygr210, and NOG1; ...
139-231 1.79e-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: 42.38  E-value: 1.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 139 AQLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRwfaeRVDLIILLFDAHKLEISDE-------FSEAIGALRGHE 211
Cdd:cd01881  37 GVFEFGDGVDIQIIDLPGLLDGASEGRGLGEQILAHLY----RSDLILHVIDASEDCVGDPledqktlNEEVSGSFLFLK 112
                        90       100
                ....*....|....*....|.
gi 21361462 212 DK-IRVVLNKADMVETQQLMR 231
Cdd:cd01881 113 NKpEMIVANKIDMASENNLKR 133
EngA2 cd01895
EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second ...
151-225 1.08e-03

EngA2 GTPase contains the second domain of EngA; This EngA2 subfamily CD represents the second 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: 206682 [Multi-domain]  Cd Length: 174  Bit Score: 40.11  E-value: 1.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361462 151 IIDTPGILSgaKQRVSRGYDFPAVLRWFA--ERVDLIILLFDAhkleiSDEFSE--------AIGALRGhedkIRVVLNK 220
Cdd:cd01895  54 LIDTAGIRK--KGKVTEGIEKYSVLRTLKaiERADVVLLVLDA-----SEGITEqdlriaglILEEGKA----LIIVVNK 122

                ....*
gi 21361462 221 ADMVE 225
Cdd:cd01895 123 WDLVE 127
DRG cd01896
Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding ...
149-220 3.16e-03

Developmentally Regulated GTP-binding protein (DRG); The developmentally regulated GTP-binding protein (DRG) subfamily is an uncharacterized member of the Obg family, an evolutionary branch of GTPase superfamily proteins. GTPases act as molecular switches regulating diverse cellular processes. DRG2 and DRG1 comprise the DRG subfamily in eukaryotes. In view of their widespread expression in various tissues and high conservation among distantly related species in eukaryotes and archaea, DRG proteins may regulate fundamental cellular processes. It is proposed that the DRG subfamily proteins play their physiological roles through RNA binding.


Pssm-ID: 206683 [Multi-domain]  Cd Length: 233  Bit Score: 39.45  E-value: 3.16e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361462 149 ISIIDTPGILSGAKQRVSRGYDFPAVLRwfaeRVDLIILLFDA-----HKLEISDEFsEAIGalrghedkIRvvLNK 220
Cdd:cd01896  49 IQLLDLPGIIEGASDGKGRGRQVIAVAR----TADLILIVLDAtkpegQREILEREL-EGVG--------IR--LNK 110
 
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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