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Conserved domains on  [gi|24646379|ref|NP_731737|]
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putative achaete scute target 1, isoform A [Drosophila melanogaster]

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 ...
63-303 2.00e-165

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: 468.68  E-value: 2.00e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379  63 MILLVGQYSTGKTTFIRYLLERDFPGIRIGPEPTTDRFIAVMYDDKEGVIPGNALVVDPKKQFRPLSKYGNAFLNRFQCS 142
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379 143 SVASPVLNAISIVDTPGILSGEKQRIDRGYDFTGVLEWFAERVDRIILLFDAHKLDISDEFRRSIEALKGHDDKIRIILN 222
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379 223 KADMIDHQQLMRVYGALMWSLGKVLQTPEVARVYIGSFWDQPLRFDANRRLFEDEEQDLFRDLQSLPRNAALRKLNDLIK 302
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 24646379 303 R 303
Cdd:cd09913 241 R 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
291-397 5.93e-55

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: 180.12  E-value: 5.93e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379   291 NAALRKLNDLIKRARLAKVHAFIIAELRKDMPSVFGKDSKKKDLIKNLGQVYDRIQREHSISPGDFPDIKKMQEVLQHQD 370
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 24646379   371 FTKFHSLKPHLLDIVDNMLAKDIARLM 397
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
446-538 5.79e-31

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: 115.45  E-value: 5.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379    446 WICNKDKPRTDGIFNGLGP-VDGKISGATAKQELIKSKLPNSVLSKIWKLSDVDGDGFLDSDEFALALHLINVKLEGCEL 524
Cdd:smart00027   3 AISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPI 82
                           90
                   ....*....|....
gi 24646379    525 PTVLPEHLVPPSKR 538
Cdd:smart00027  83 PASLPPSLIPPSKR 96
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
27-59 8.22e-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: 68.19  E-value: 8.22e-15
                          10        20        30
                  ....*....|....*....|....*....|...
gi 24646379    27 ELKKIYRSKLLPLEEHYQFHDFHSPKLEDPDFD 59
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 ...
63-303 2.00e-165

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: 468.68  E-value: 2.00e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379  63 MILLVGQYSTGKTTFIRYLLERDFPGIRIGPEPTTDRFIAVMYDDKEGVIPGNALVVDPKKQFRPLSKYGNAFLNRFQCS 142
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379 143 SVASPVLNAISIVDTPGILSGEKQRIDRGYDFTGVLEWFAERVDRIILLFDAHKLDISDEFRRSIEALKGHDDKIRIILN 222
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379 223 KADMIDHQQLMRVYGALMWSLGKVLQTPEVARVYIGSFWDQPLRFDANRRLFEDEEQDLFRDLQSLPRNAALRKLNDLIK 302
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 24646379 303 R 303
Cdd:cd09913 241 R 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
291-397 5.93e-55

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: 180.12  E-value: 5.93e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379   291 NAALRKLNDLIKRARLAKVHAFIIAELRKDMPSVFGKDSKKKDLIKNLGQVYDRIQREHSISPGDFPDIKKMQEVLQHQD 370
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 24646379   371 FTKFHSLKPHLLDIVDNMLAKDIARLM 397
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
446-538 5.79e-31

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: 115.45  E-value: 5.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379    446 WICNKDKPRTDGIFNGLGP-VDGKISGATAKQELIKSKLPNSVLSKIWKLSDVDGDGFLDSDEFALALHLINVKLEGCEL 524
Cdd:smart00027   3 AISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPI 82
                           90
                   ....*....|....
gi 24646379    525 PTVLPEHLVPPSKR 538
Cdd:smart00027  83 PASLPPSLIPPSKR 96
Dynamin_N pfam00350
Dynamin family;
64-224 2.82e-23

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 96.53  E-value: 2.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379    64 ILLVGQYSTGKTTFIRYLLERDFPGirIGPEPTTDRFIAVMYDDKEGVIPG--NALVVDPKKQFRPLSKYGNAFLNRFQC 141
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILP--RGPGPTTRRPTVLRLGESPGASEGavKVEYKDGEKKFEDFSELREEIEKETEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379   142 SSVA--------------SPVLNAISIVDTPGILSGEKQRIDrgydftgVLEWFAERVDRIILLFDAHKLDISDEFRRSI 207
Cdd:pfam00350  79 IAGTgkgissepivleilSPLVPGLTLVDTPGLDSVAVGDQE-------LTKEYIKPADIILAVTPANVDLSTSEALFLA 151
                         170
                  ....*....|....*..
gi 24646379   208 EALKGHDDKIRIILNKA 224
Cdd:pfam00350 152 REVDPNGKRTIGVLTKA 168
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
456-520 1.83e-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: 90.74  E-value: 1.83e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24646379 456 DGIFNGLGPV-DGKISGATAKQELIKSKLPNSVLSKIWKLSDVDGDGFLDSDEFALALHLINVKLE 520
Cdd:cd00052   2 DQIFRSLDPDgDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
458-539 4.35e-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: 82.42  E-value: 4.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379   458 IFNGLGPVDGKISGATAKQELIKSKLPNSVLSKIWKLSDVDGDGFLDSDEFALALHLINVKLEG--CELPTVLPEHLVPP 535
Cdd:pfam12763  15 IFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGniADVPDELPDWLVPG 94

                  ....
gi 24646379   536 SKRY 539
Cdd:pfam12763  95 SKAH 98
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
27-59 8.22e-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: 68.19  E-value: 8.22e-15
                          10        20        30
                  ....*....|....*....|....*....|...
gi 24646379    27 ELKKIYRSKLLPLEEHYQFHDFHSPKLEDPDFD 59
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 ...
63-303 2.00e-165

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: 468.68  E-value: 2.00e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379  63 MILLVGQYSTGKTTFIRYLLERDFPGIRIGPEPTTDRFIAVMYDDKEGVIPGNALVVDPKKQFRPLSKYGNAFLNRFQCS 142
Cdd:cd09913   1 MVLFLGQYSTGKSTFINYLLGQDYPGLRTGPEPTTDRFTVVMHGEDDGTIPGNALVVDPDKPFRGLSKFGNGFLNKFEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379 143 SVASPVLNAISIVDTPGILSGEKQRIDRGYDFTGVLEWFAERVDRIILLFDAHKLDISDEFRRSIEALKGHDDKIRIILN 222
Cdd:cd09913  81 TLPHPLLESVTIVDTPGILSGEKQRQSRGYDFNAVCRWFAERADLIFLLFDPHKLDISDEFRRVIEQLKGHESKIRIVLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379 223 KADMIDHQQLMRVYGALMWSLGKVLQTPEVARVYIGSFWDQPLRFDANRRLFEDEEQDLFRDLQSLPRNAALRKLNDLIK 302
Cdd:cd09913 161 KADMVDTQQLMRVYGALMWSLSKVINTPEVPRVYIGSFWDQPYEPDTNRKLFLEEEIDLLRDLNSLPRNAALRKLNDLIK 240

                .
gi 24646379 303 R 303
Cdd:cd09913 241 R 241
DUF5600 pfam18150
Domain of unknown function (DUF5600); This domain can be found in EH-domain-containing ATPase ...
291-397 5.93e-55

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: 180.12  E-value: 5.93e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379   291 NAALRKLNDLIKRARLAKVHAFIIAELRKDMPSVFGKDSKKKDLIKNLGQVYDRIQREHSISPGDFPDIKKMQEVLQHQD 370
Cdd:pfam18150   1 NAAVRKLNDLVKRARLVKVHAYIIAHLKKEMPTVFGKESKKKELINNLPEIFRKVQREHQLPPGDFPDVEKFQEQLRAYD 80
                          90       100
                  ....*....|....*....|....*..
gi 24646379   371 FTKFHSLKPHLLDIVDNMLAKDIARLM 397
Cdd:pfam18150  81 FTKFPKLKPKLIEALDEMLTNDIPKLM 107
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
446-538 5.79e-31

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: 115.45  E-value: 5.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379    446 WICNKDKPRTDGIFNGLGP-VDGKISGATAKQELIKSKLPNSVLSKIWKLSDVDGDGFLDSDEFALALHLINVKLEGCEL 524
Cdd:smart00027   3 AISPEDKAKYEQIFRSLDKnQDGTVTGAQAKPILLKSGLPQTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPI 82
                           90
                   ....*....|....
gi 24646379    525 PTVLPEHLVPPSKR 538
Cdd:smart00027  83 PASLPPSLIPPSKR 96
Dynamin_N pfam00350
Dynamin family;
64-224 2.82e-23

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 96.53  E-value: 2.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379    64 ILLVGQYSTGKTTFIRYLLERDFPGirIGPEPTTDRFIAVMYDDKEGVIPG--NALVVDPKKQFRPLSKYGNAFLNRFQC 141
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILP--RGPGPTTRRPTVLRLGESPGASEGavKVEYKDGEKKFEDFSELREEIEKETEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379   142 SSVA--------------SPVLNAISIVDTPGILSGEKQRIDrgydftgVLEWFAERVDRIILLFDAHKLDISDEFRRSI 207
Cdd:pfam00350  79 IAGTgkgissepivleilSPLVPGLTLVDTPGLDSVAVGDQE-------LTKEYIKPADIILAVTPANVDLSTSEALFLA 151
                         170
                  ....*....|....*..
gi 24646379   208 EALKGHDDKIRIILNKA 224
Cdd:pfam00350 152 REVDPNGKRTIGVLTKA 168
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
456-520 1.83e-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: 90.74  E-value: 1.83e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24646379 456 DGIFNGLGPV-DGKISGATAKQELIKSKLPNSVLSKIWKLSDVDGDGFLDSDEFALALHLINVKLE 520
Cdd:cd00052   2 DQIFRSLDPDgDGLISGDEARPFLGKSGLPRSVLAQIWDLADTDKDGKLDKEEFAIAMHLIALALN 67
EF-hand_4 pfam12763
Cytoskeletal-regulatory complex EF hand; This is an efhand family from the N-terminal of actin ...
458-539 4.35e-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: 82.42  E-value: 4.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379   458 IFNGLGPVDGKISGATAKQELIKSKLPNSVLSKIWKLSDVDGDGFLDSDEFALALHLINVKLEG--CELPTVLPEHLVPP 535
Cdd:pfam12763  15 IFSGLKPENNKLTGDQVSPVLKNSRLPDDQLAKIWDLADIDSDGKLDFEEFCIAMRLIFDLVNGniADVPDELPDWLVPG 94

                  ....
gi 24646379   536 SKRY 539
Cdd:pfam12763  95 SKAH 98
EHD_N pfam16880
N-terminal EH-domain containing protein; EHD_N is a short domain that lies at the very ...
27-59 8.22e-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: 68.19  E-value: 8.22e-15
                          10        20        30
                  ....*....|....*....|....*....|...
gi 24646379    27 ELKKIYRSKLLPLEEHYQFHDFHSPKLEDPDFD 59
Cdd:pfam16880   1 GLKKLYKSKIKPLEEAYKFNDFHSPPLTDADFD 33
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
65-243 1.12e-11

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: 1.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379  65 LLVGQYSTGKTTFIRYLLERDFPGIRIGPEPTTDRFIAVMYDDKEGVIpgnalvvdpkkqfrplskygnaflnrfqcssv 144
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDKGKVK-------------------------------- 48
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379 145 aspvlnaISIVDTPGILSGEKQRIDRGYdftgvlEWFAERVDRIILLFDAHKLDISDEFRRSI-EALKGHDDKIRIILNK 223
Cdd:cd00882  49 -------LVLVDTPGLDEFGGLGREELA------RLLLRGADLILLVVDSTDRESEEDAKLLIlRRLRKEGIPIILVGNK 115
                       170       180
                ....*....|....*....|
gi 24646379 224 ADMIDHQQLMRVYGALMWSL 243
Cdd:cd00882 116 IDLLEEREVEELLRLEELAK 135
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
64-223 8.19e-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: 47.61  E-value: 8.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379    64 ILLVGQYSTGKTTFIRYLLER-----DFPGIrigpepTTDR-FIAVMYDDKEgvipgnalvvdpkkqfrplskygnafln 137
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGAkaivsDYPGT------TRDPnEGRLELKGKQ---------------------------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379   138 rfqcssvaspvlnaISIVDTPGILSGEKQRIDRGYDFTGVlewfaERVDRIILLFDAHKlDISDEFRRSIEALKGHDDKI 217
Cdd:pfam01926  48 --------------IILVDTPGLIEGASEGEGLGRAFLAI-----IEADLILFVVDSEE-GITPLDEELLELLRENKKPI 107

                  ....*.
gi 24646379   218 RIILNK 223
Cdd:pfam01926 108 ILVLNK 113
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
64-232 2.72e-06

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 47.93  E-value: 2.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379  64 ILLVGQYSTGKTTFIRYLLERDF-PgirIGPEPTTDRFIAVmyddkegvipgnalvvdpkkqfrplsKYGnaflnrfqcs 142
Cdd:cd09912   3 LAVVGEFSAGKSTLLNALLGEEVlP---TGVTPTTAVITVL--------------------------RYG---------- 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24646379 143 svaspVLNAISIVDTPGILSGEKQRidrgydfTGVLEWFAERVDRIILLFDA-HKLDISD-EFRRSIeaLKGHDDKIRII 220
Cdd:cd09912  44 -----LLKGVVLVDTPGLNSTIEHH-------TEITESFLPRADAVIFVLSAdQPLTESErEFLKEI--LKWSGKKIFFV 109
                       170
                ....*....|..
gi 24646379 221 LNKADMIDHQQL 232
Cdd:cd09912 110 LNKIDLLSEEEL 121
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
149-227 5.11e-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: 40.40  E-value: 5.11e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24646379 149 LNAISIVDTPGIlsGEKQRIDRGYdfTGVLEWFAERVDRIILLFDAHKLDISDEFRRSIEALKGHDDKIRIILNKADMI 227
Cdd:cd11383  44 GDGLVLLDLPGV--GERGRRDREY--EELYRRLLPEADLVLWLLDADDRALAADHDFYLLPLAGHDAPLLFVLNQVDPV 118
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
184-249 7.92e-03

cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.


Pssm-ID: 349766  Cd Length: 198  Bit Score: 37.89  E-value: 7.92e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24646379 184 RVDRIILLFDAHKL-------DISDEFRRSIEalkgHDDkiRIILNKADMIDHQQLMRVYGAL--MWSLGKVLQT 249
Cdd:cd03112 116 RLDGVVTVVDAKNFlkqldeeDVSDLAVDQIA----FAD--VIVLNKTDLVDEEELEALRARIraLNPGAKIVET 184
 
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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