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Conserved domains on  [gi|15217515|ref|NP_174602|]
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ENTH/ANTH/VHS superfamily protein [Arabidopsis thaliana]

Protein Classification

ANTH domain-containing protein( domain architecture ID 10541692)

ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; similar to Homo sapiens phosphatidylinositol-binding clathrin assembly protein and clathrin coat assembly protein AP180

CATH:  1.20.58.150|1.25.40.90
Gene Ontology:  GO:0030276|GO:0048268|GO:0072583
PubMed:  12740367|12742163|22748146|14657269
SCOP:  4000571|4000581

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 37-303 2.07e-86

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: 262.62  E-value: 2.07e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515    37 DIEVAVVRATSHDDCPVDDKTMHEILFLVSNTpGSIPFLAEQISRRLAKTRDCLVAGKTLLLFHRLLRGSSRSIEQQLHI 116
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSS-AKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515   117 AHTSGHLQIGCSWFmmSLDSRSFVFLQNYVAYLQERVGWIINQA---GKLEPVMSG-----GTKFSRYKEKSMDLVFHIL 188
Cdd:pfam07651  80 ARRRISSLLRISSF--SLSWDYGAFIRAYAKYLDERLDFHRKLPrdpGTFERVEYGslvavGDPNERYLTMSMEDLLDSI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515   189 PKCQEFIAQVLKCSPVDAWPIDNLVQAATGNILKESFQVYMTYSDGMTALVSMLFDLSRPARDLACGMLRKASQQIQDLR 268
Cdd:pfam07651 158 PKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLK 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 15217515   269 ILYDKCRGFAGMKSLDYPSVQAISMDHIVALEECS 303
Cdd:pfam07651 238 EFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 37-303 2.07e-86

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: 262.62  E-value: 2.07e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515    37 DIEVAVVRATSHDDCPVDDKTMHEILFLVSNTpGSIPFLAEQISRRLAKTRDCLVAGKTLLLFHRLLRGSSRSIEQQLHI 116
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSS-AKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515   117 AHTSGHLQIGCSWFmmSLDSRSFVFLQNYVAYLQERVGWIINQA---GKLEPVMSG-----GTKFSRYKEKSMDLVFHIL 188
Cdd:pfam07651  80 ARRRISSLLRISSF--SLSWDYGAFIRAYAKYLDERLDFHRKLPrdpGTFERVEYGslvavGDPNERYLTMSMEDLLDSI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515   189 PKCQEFIAQVLKCSPVDAWPIDNLVQAATGNILKESFQVYMTYSDGMTALVSMLFDLSRPARDLACGMLRKASQQIQDLR 268
Cdd:pfam07651 158 PKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLK 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 15217515   269 ILYDKCRGFAGMKSLDYPSVQAISMDHIVALEECS 303
Cdd:pfam07651 238 EFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 38-155 3.37e-45

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly protein AP180 and similar proteins; This subfamily is composed of plant clathrin coat assembly protein AP180 and other ANTH domain containing proteins that are yet to be characterized. Arabidopsis thaliana AP180 (At-AP180) is a binding partner of plant alphaC-adaptin; it functions as a clathrin assembly protein that promotes the formation of cages with an almost uniform size distribution. In addition to At-AP180, Arabidopsis thaliana contains many ANTH domain containing proteins labelled as putative clathrin assembly proteins included in this subfamily such as At4g02650, At5g10410, At2g25430, and At1g33340, among others. 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: 340784  Cd Length: 122  Bit Score: 151.24  E-value: 3.37e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515  38 IEVAVVRATSHDDCPVDDKTMHEILFLVSNTPGSIPFLAEQISRRLAKTRDCLVAGKTLLLFHRLLRGSSRSIEQQLHIA 117
Cdd:cd16987   1 LEVAVVKATSHDDAPPDEKYVREILSLGSSSRAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELSLA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15217515 118 HTSGHLQIGCSWFMMSLDSRS---FVFLQNYVAYLQERVGW 155
Cdd:cd16987  81 PSGGRNPLNLSDFRDGSSSKSwdfSAFVRAYAAYLDERLIF 121
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
37-153 3.49e-15

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 71.51  E-value: 3.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515     37 DIEVAVVRATSHDDCPVDDKTMHEILFLVSNTPGSIPFLAEQISRRLAKTRDCLVAGKTLLLFHRLLR-GSSRSIEQ-QL 114
Cdd:smart00273   2 DLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNWRVVYKALILLHYLLRnGSPRVILEaLR 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 15217515    115 HIAHTsghLQIGCSWFMMSLDSRSFVFLQNYVAYLQERV 153
Cdd:smart00273  82 NRNRI---LNLSDFQDIDSRGKDQGANIRTYAKYLLERL 117
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 37-303 2.07e-86

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: 262.62  E-value: 2.07e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515    37 DIEVAVVRATSHDDCPVDDKTMHEILFLVSNTpGSIPFLAEQISRRLAKTRDCLVAGKTLLLFHRLLRGSSRSIEQQLHI 116
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSS-AKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515   117 AHTSGHLQIGCSWFmmSLDSRSFVFLQNYVAYLQERVGWIINQA---GKLEPVMSG-----GTKFSRYKEKSMDLVFHIL 188
Cdd:pfam07651  80 ARRRISSLLRISSF--SLSWDYGAFIRAYAKYLDERLDFHRKLPrdpGTFERVEYGslvavGDPNERYLTMSMEDLLDSI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515   189 PKCQEFIAQVLKCSPVDAWPIDNLVQAATGNILKESFQVYMTYSDGMTALVSMLFDLSRPARDLACGMLRKASQQIQDLR 268
Cdd:pfam07651 158 PKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLK 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 15217515   269 ILYDKCRGFAGMKSLDYPSVQAISMDHIVALEECS 303
Cdd:pfam07651 238 EFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 38-155 3.37e-45

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly protein AP180 and similar proteins; This subfamily is composed of plant clathrin coat assembly protein AP180 and other ANTH domain containing proteins that are yet to be characterized. Arabidopsis thaliana AP180 (At-AP180) is a binding partner of plant alphaC-adaptin; it functions as a clathrin assembly protein that promotes the formation of cages with an almost uniform size distribution. In addition to At-AP180, Arabidopsis thaliana contains many ANTH domain containing proteins labelled as putative clathrin assembly proteins included in this subfamily such as At4g02650, At5g10410, At2g25430, and At1g33340, among others. 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: 340784  Cd Length: 122  Bit Score: 151.24  E-value: 3.37e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515  38 IEVAVVRATSHDDCPVDDKTMHEILFLVSNTPGSIPFLAEQISRRLAKTRDCLVAGKTLLLFHRLLRGSSRSIEQQLHIA 117
Cdd:cd16987   1 LEVAVVKATSHDDAPPDEKYVREILSLGSSSRAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELSLA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15217515 118 HTSGHLQIGCSWFMMSLDSRS---FVFLQNYVAYLQERVGW 155
Cdd:cd16987  81 PSGGRNPLNLSDFRDGSSSKSwdfSAFVRAYAAYLDERLIF 121
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 38-153 1.63e-16

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: 75.00  E-value: 1.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515  38 IEVAVVRATSHDDCPVDDKTMHEILFLVSNTPG--SIPFLAEQISRRLAKtRDCLVAGKTLLLFHRLLRGSSRSIEQQLh 115
Cdd:cd03564   1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNGGGraDVAYIVHALAKRLHK-KNWIVVLKTLIVIHRLLREGSPSFLEEL- 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15217515 116 iAHTSGHL---------QIGCSWFMMSldsrsfvFLQNYVAYLQERV 153
Cdd:cd03564  79 -LRYSGHIfnlsnfkddSSPEAWDLSA-------FIRRYARYLEERL 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
37-153 3.49e-15

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 71.51  E-value: 3.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15217515     37 DIEVAVVRATSHDDCPVDDKTMHEILFLVSNTPGSIPFLAEQISRRLAKTRDCLVAGKTLLLFHRLLR-GSSRSIEQ-QL 114
Cdd:smart00273   2 DLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNWRVVYKALILLHYLLRnGSPRVILEaLR 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 15217515    115 HIAHTsghLQIGCSWFMMSLDSRSFVFLQNYVAYLQERV 153
Cdd:smart00273  82 NRNRI---LNLSDFQDIDSRGKDQGANIRTYAKYLLERL 117
 
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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