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Conserved domains on  [gi|2042715554|ref|XP_041564455|]
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epsin-1 isoform X3 [Drosophila elegans]

Protein Classification

ENTH domain-containing protein( domain architecture ID 13016865)

ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to epsin that plays an important role as accessory proteins in clathrin-mediated endocytosis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 28-150 1.03e-90

Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


:

Pssm-ID: 340787  Cd Length: 124  Bit Score: 281.17  E-value: 1.03e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  28 DAQVKVREATSNDPWGPSAAIMGEIADLTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQCKE 107
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2042715554 108 NIFAIQTLREFVYFEE-GKDQGTHVREKAKQLVTLLKDDERLKN 150
Cdd:cd16990    81 NIFAIQTLKDFQYIDRdGKDQGVNVREKAKQLVSLLKDDERLKN 124
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 236-396 1.56e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  236 VRLQLALSQSEQDFKDPNGRPIPAPKKEEPQshlldlldISLGATSISSPPLGAAGGAPAPVVDPWATPAPRAPSQLSDP 315
Cdd:PHA03247  2719 TPLPPGPAAARQASPALPAAPAPPAVPAGPA--------TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  316 WSGTSSPPVDPWHPSATSRTIMG--AGVPMSAAPMGGAPGNDA---WGGRTQSPSVASGSSNEGWLQTNGNANQNGRGAT 390
Cdd:PHA03247  2791 LSESRESLPSPWDPADPPAAVLApaAALPPAASPAGPLPPPTSaqpTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRS 2870


                   ....*.
gi 2042715554  391 PAGPPA 396
Cdd:PHA03247  2871 PAAKPA 2876
UIM smart00726
Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated ...
 208-227 3.09e-03

Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated proteins.


:

Pssm-ID: 197845  Cd Length: 20  Bit Score: 35.58  E-value: 3.09e-03
                           10        20
                   ....*....|....*....|
gi 2042715554  208 EEELQLQLAMAMSREEAEQE 227
Cdd:smart00726   1 DEDEDLQRALELSLQEAEES 20
 
Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 28-150 1.03e-90

Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340787  Cd Length: 124  Bit Score: 281.17  E-value: 1.03e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  28 DAQVKVREATSNDPWGPSAAIMGEIADLTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQCKE 107
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2042715554 108 NIFAIQTLREFVYFEE-GKDQGTHVREKAKQLVTLLKDDERLKN 150
Cdd:cd16990    81 NIFAIQTLKDFQYIDRdGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 26-148 1.15e-66

ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown.


Pssm-ID: 426255  Cd Length: 124  Bit Score: 217.04  E-value: 1.15e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  26 YSDAQVKVREATSNDPWGPSAAIMGEIADLTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQC 105
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2042715554 106 KENIFAIQTLREFVYFEE-GKDQGTHVREKAKQLVTLLKDDERL 148
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDEnGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
27-152 2.54e-45

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 158.56  E-value: 2.54e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554   27 SDAQVKVREATSNDPWGPSAAIMGEIADLTYNV-VAFSEIMQMIWKRLNDHGkNWRHVYKALILLEYLIKTGSEKVAQQC 105
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2042715554  106 KENIFAIQTLREFVYFEE-GKDQGTHVREKAKQLVTLLKDDERLKNER 152
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSrGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PHA03247 PHA03247
large tegument protein UL36; Provisional
 236-396 1.56e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  236 VRLQLALSQSEQDFKDPNGRPIPAPKKEEPQshlldlldISLGATSISSPPLGAAGGAPAPVVDPWATPAPRAPSQLSDP 315
Cdd:PHA03247  2719 TPLPPGPAAARQASPALPAAPAPPAVPAGPA--------TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  316 WSGTSSPPVDPWHPSATSRTIMG--AGVPMSAAPMGGAPGNDA---WGGRTQSPSVASGSSNEGWLQTNGNANQNGRGAT 390
Cdd:PHA03247  2791 LSESRESLPSPWDPADPPAAVLApaAALPPAASPAGPLPPPTSaqpTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRS 2870


                   ....*.
gi 2042715554  391 PAGPPA 396
Cdd:PHA03247  2871 PAAKPA 2876
UIM smart00726
Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated ...
 208-227 3.09e-03

Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated proteins.


Pssm-ID: 197845  Cd Length: 20  Bit Score: 35.58  E-value: 3.09e-03
                           10        20
                   ....*....|....*....|
gi 2042715554  208 EEELQLQLAMAMSREEAEQE 227
Cdd:smart00726   1 DEDEDLQRALELSLQEAEES 20
 
Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 28-150 1.03e-90

Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of CCVs. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340787  Cd Length: 124  Bit Score: 281.17  E-value: 1.03e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  28 DAQVKVREATSNDPWGPSAAIMGEIADLTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQCKE 107
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2042715554 108 NIFAIQTLREFVYFEE-GKDQGTHVREKAKQLVTLLKDDERLKN 150
Cdd:cd16990    81 NIFAIQTLKDFQYIDRdGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 26-152 7.96e-67

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This subfamily is composed of the two orthologs of epsin in Saccharomyces cerevisiae, Epsin-1 (Ent1 or Ent1p) and Epsin-2 (Ent2 or Ent2p), and similar proteins. Yeast single epsin knockouts, either Ent1 and Ent2, are viable while the double knockout is not. Yeast epsins are required for endocytosis and localization of actin. Ent2 also plays a signaling role during cell division. The ENTH domain of Ent2 interacts with the septin organizing, Cdc42 GTPase activating protein, Bem3, leading to increased cytokinesis failure when overexpressed. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340788  Cd Length: 132  Bit Score: 217.91  E-value: 7.96e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  26 YSDAQVKVREATSNDPWGPSAAIMGEIADLTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQC 105
Cdd:cd16991     2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2042715554 106 KENIFAIQTLREFVYF-EEGKDQGTHVREKAKQLVTLLKDDERLKNER 152
Cdd:cd16991    82 KENIYIIKTLREFQYIdDEGKDQGQNVRVKAKELTSLLLDDERLREER 129
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 26-148 1.15e-66

ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown.


Pssm-ID: 426255  Cd Length: 124  Bit Score: 217.04  E-value: 1.15e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  26 YSDAQVKVREATSNDPWGPSAAIMGEIADLTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQC 105
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2042715554 106 KENIFAIQTLREFVYFEE-GKDQGTHVREKAKQLVTLLKDDERL 148
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDEnGKDQGINVRKKAKEILNLLEDDELL 124
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 29-144 5.78e-57

Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, contributing to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340772  Cd Length: 117  Bit Score: 190.42  E-value: 5.78e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  29 AQVKVREATSNDPWGPSAAIMGEIADLTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQCKEN 108
Cdd:cd03571     1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2042715554 109 IFAIQTLREFVYFEE-GKDQGTHVREKAKQLVTLLKD 144
Cdd:cd03571    81 LYLIRTLQDFQYVDEnGDDQGINVREKAKQIVALLED 117
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 29-155 5.61e-53

Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein (EpsinR) is also called clathrin interactor 1 (Clint), enthoprotin, or epsin-4. It is a clathrin-coated vesicle (CCV) protein that binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). It contains an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. The ENTH domain of human epsinR binds directly to the helical bundle domain of the mouse SNARE Vti1b; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340786  Cd Length: 130  Bit Score: 180.18  E-value: 5.61e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  29 AQVKVREATSNDPWGPSAAIMGEIADLTYNVVAFSEIMQMIWKR-LNDHGKNWRHVYKALILLEYLIKTGSEKVAQQCKE 107
Cdd:cd16989     1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRmLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2042715554 108 NIFAIQTLREFVYFEE-GKDQGTHVREKAKQLVTLLKDDERLKNERVKA 155
Cdd:cd16989    81 HIYDLRSLENYHFIDEkGKDQGINVRQKVKEIIELLQDDERLREERKKA 129
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
27-152 2.54e-45

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 158.56  E-value: 2.54e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554   27 SDAQVKVREATSNDPWGPSAAIMGEIADLTYNV-VAFSEIMQMIWKRLNDHGkNWRHVYKALILLEYLIKTGSEKVAQQC 105
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2042715554  106 KENIFAIQTLREFVYFEE-GKDQGTHVREKAKQLVTLLKDDERLKNER 152
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSrGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 32-147 2.05e-40

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-3 (Ent3 or Ent3p), and similar proteins. Ent3 is an adaptor proteins at the Trans-Golgi Network (TGN); it cooperates with yeast SNARE Vti1p to regulate transport from the TGN to the prevacuolar endosome. Ent3 facilitates the interaction between Gga2p with both the endosomal syntaxin Pep12p and clathrin in the GGA-dependent transport to the late endosome. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. Similar to mammalian epsinR, The ENTH domain of Ent3 binds to the yeast SNARE Vti1p; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340789  Cd Length: 121  Bit Score: 144.52  E-value: 2.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  32 KVREATSNDPWGPSAAIMGEIADLTYNVVAFSEIMQMIWKRLND-HGKNWRHVYKALILLEYLIKTGSEKVAQQCKENIF 110
Cdd:cd16992     4 KVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGHLT 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2042715554 111 AIQTLREFVYFEE-GKDQGTHVREKAKQLVTLLKDDER 147
Cdd:cd16992    84 LIKMLRSFHYIDDkGKDQGINVRNRAKELIELLSDDEK 121
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 32-144 4.88e-30

VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a VHS, CID, ENTH, or ANTH domain. The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It is located at the N-termini of proteins involved in intracellular membrane trafficking. The CTD-Interacting Domain (CID) is present in several RNA-processing factors and binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase II (RNAP II or Pol II). The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. A set of proteins previously designated as harboring an ENTH domain in fact contains a highly similar, yet unique module referred to as an AP180 N-Terminal Homology (ANTH) domain. VHS, ENTH, and ANTH domains are structurally similar and are composed of a superhelix of eight alpha helices. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH domain-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340764  Cd Length: 115  Bit Score: 114.83  E-value: 4.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  32 KVREATSNDPWGPSAAIMGEIADLTYN-VVAFSEIMQMIWKRLNDHgkNWRHVYKALILLEYLIKTGSEKVAQQCKENIF 110
Cdd:cd00197     4 TVEKATSNENMGPDWPLIMEICDLINEtNVGPKEAVDAIKKRINNK--NPHVVLKALTLLEYCVKNCGERFHQEVASNDF 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2042715554 111 AIQTLREFVYFEEGKDQGTHVREKAKQLVTLLKD 144
Cdd:cd00197    82 AVELLKFDKSGLLGDDVSTNVREKAIELVQLWAS 115
ENTH_Ent4 cd16994
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 ...
 29-146 8.54e-18

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 (Ent4 or Ent4p) has been reported to be involved in the Trans-Golgi Network (TGN)-to-vacuole sorting of Arn1p, a transporter for the uptake of ferrichrome, an important nutritional source of iron. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340791  Cd Length: 126  Bit Score: 80.03  E-value: 8.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  29 AQVKVREAT-SNDPWGPSAAIMGEIADLTYNVVAFSEIMQMIWKRLNDHG-----KNWRHVYKALILLEYLIKTGSEKVA 102
Cdd:cd16994     1 TELKVKQATdDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSkksshKNCVHILKTLTLISYLINNGSNEFI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2042715554 103 QQCKENIFAIQTLREFVYFEEGKDQ-GTHVREKAKQLVTLLKDDE 146
Cdd:cd16994    81 AWLRSNLYLIERLKDFEVQDNRDLPmANQIRSLSQDICELINDDE 125
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 30-157 6.90e-08

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-5 (Ent5 or Ent5p), and similar proteins. Ent5 is required, together with Ent3 and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. It is also required for protein transport from the Trans-Golgi Network (TGN) to the vacuole. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. ENTH and ANTH (E/ANTH)-containing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.


Pssm-ID: 340790  Cd Length: 158  Bit Score: 52.85  E-value: 6.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  30 QVKVREATSNDPWGPSAAIMGEIADLTYNVVAFsEIMQMIWKRLNDH-------------------GKNWRHVYKALILL 90
Cdd:cd16993     2 QIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLY-LMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKCLIVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2042715554  91 EYLI---KTGSE-KVAQQCKEN---IFAIQTLREFVYF-EEGKDQgTH---VREKAKQLVTLLKDDERLKNERVKALK 157
Cdd:cd16993    81 EFLLlnvDTGDElNQVLSCLLNhkhIFTREIAQYKVKFsNDGKME-IHergIQKKCELILQLIEDSDFLRQERAKNKK 157
VHS cd03561
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ...
 33-139 8.97e-07

VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It has a superhelical structure similar to that of the ARM (Armadillo) repeats and is present at the N-termini of proteins involved in intracellular membrane trafficking. There are four general groups of VHS domain containing proteins based on their association with other domains. The first group consists of proteins of the STAM/EAST/Hbp family, which has the domain composition of VHS-SH3-ITAM. The second consists of proteins with a FYVE domain C-terminal to VHS. The third consists of GGA proteins with a domain composition of VHS-GAT (GGA and TOM)-GAE (Gamma-Adaptin Ear) domain. The fourth consists of proteins with a VHS domain alone or with domains other than those mentioned above. In GGA proteins, VHS domains are involved in cargo recognition in trans-Golgi, thereby having a general membrane targeting/cargo recognition role in vesicular trafficking.


Pssm-ID: 340765  Cd Length: 131  Bit Score: 48.80  E-value: 8.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  33 VREATSNDPWGPSAAIMGEIADLtYNVVAFS--EIMQMIWKRLNDhgKNWRHVYKALILLEYLIKTGSEKVAQQ-CKENI 109
Cdd:cd03561     5 VEKATSESLTEPDWALNLEICDL-VNSDPAQakDAVRALRKRLQS--KNPKVQLLALTLLETLVKNCGAPFHSEvASRDF 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 2042715554 110 faiqtLREFVYFEEGKDQGTHVREKAKQLV 139
Cdd:cd03561    82 -----LQELVKLVKKKKTSPEVREKALALI 106
PHA03247 PHA03247
large tegument protein UL36; Provisional
 236-396 1.56e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  236 VRLQLALSQSEQDFKDPNGRPIPAPKKEEPQshlldlldISLGATSISSPPLGAAGGAPAPVVDPWATPAPRAPSQLSDP 315
Cdd:PHA03247  2719 TPLPPGPAAARQASPALPAAPAPPAVPAGPA--------TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  316 WSGTSSPPVDPWHPSATSRTIMG--AGVPMSAAPMGGAPGNDA---WGGRTQSPSVASGSSNEGWLQTNGNANQNGRGAT 390
Cdd:PHA03247  2791 LSESRESLPSPWDPADPPAAVLApaAALPPAASPAGPLPPPTSaqpTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRS 2870


                   ....*.
gi 2042715554  391 PAGPPA 396
Cdd:PHA03247  2871 PAAKPA 2876
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 243-397 7.80e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 7.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554 243 SQSEQDFKDPNGRPIPAPKKEEPQSHLLDLLDISLGATSISSPPLGAAGGAPAPVVDPWATPAPRAPSQLSDPWSGTSSP 322
Cdd:PRK07764  634 AAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQ 713

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2042715554 323 PVDPW--HPSATSRTIMGAGVPMSAAPMGGAPGNDAWGGRTQSPSVASGSsnegwlqtNGNANQNGRGATPAGPPAE 397
Cdd:PRK07764  714 ADDPAaqPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPA--------PAPAAAPAAAPPPSPPSEE 782
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 52-102 1.75e-03

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins; This subfamily includes yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins. There are two YAP180 proteins in Saccharomyces cerevisiae, AP180A (yAP180A or YAP1801) and AP180B (yAP180B or YAP1802). They are involved in endocytosis and clathrin cage assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains of plant clathrin coat assembly protein AP180 and similar proteins.


Pssm-ID: 340785  Cd Length: 117  Bit Score: 39.09  E-value: 1.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2042715554  52 IADLTYN-VVAFSEIMQMIWKRLNDhgKNWRHVYKALILLEYLIKTGSEKVA 102
Cdd:cd16988    24 ILLATYSsDASFGEIVRALSRRLRD--NSWTVVFKSLIVLHLMIREGETDDV 73
UIM smart00726
Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated ...
 208-227 3.09e-03

Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated proteins.


Pssm-ID: 197845  Cd Length: 20  Bit Score: 35.58  E-value: 3.09e-03
                           10        20
                   ....*....|....*....|
gi 2042715554  208 EEELQLQLAMAMSREEAEQE 227
Cdd:smart00726   1 DEDEDLQRALELSLQEAEES 20
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 30-148 6.23e-03

ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.


Pssm-ID: 340767  Cd Length: 120  Bit Score: 37.25  E-value: 6.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  30 QVKVREATSNDPWGPSAAIMGEIADLTYN---VVAFSEIMQMIWKRLndHGKNWRHVYKALILLEYLIKTGSEKVAQQCK 106
Cdd:cd03564     2 DVAVVKATNHDEVPPKEKHVRKLLLATSNgggRADVAYIVHALAKRL--HKKNWIVVLKTLIVIHRLLREGSPSFLEELL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2042715554 107 ENIFAIQTLREFV--YFEEGKDQGTHVREKAKQLvtllkdDERL 148
Cdd:cd03564    80 RYSGHIFNLSNFKddSSPEAWDLSAFIRRYARYL------EERL 117
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 55-149 8.23e-03

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 39.20  E-value: 8.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2042715554  55 LTYNVVAFSEIMQMIWKRLNDHgKNWRHVYKALILLEYLIKTGSEKVAQQCKENIFAIQTLREFVYFEEGKDQGTHVREK 134
Cdd:pfam07651  28 GTSSSAKLAALFWALSRRLPLT-RSWVVAFKALILVHKLLREGHPSVLQELLRARRRISSLLRISSFSLSWDYGAFIRAY 106

                          90
                  ....*....|....*
gi 2042715554 135 AKQLvtllkdDERLK 149
Cdd:pfam07651 107 AKYL------DERLD 115
 
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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