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Conserved domains on  [gi|15238436|ref|NP_201340|]
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ENTH/ANTH/VHS superfamily protein [Arabidopsis thaliana]

Protein Classification

VHS/ENTH/ANTH domain-containing protein; ENTH domain-containing protein( domain architecture ID 13016533)

VHS (Vps27/Hrs/STAM) /ENTH (Epsin N-Terminal Homology) /ANTH (AP180 N-Terminal Homology) domain-containing protein similar to Homo sapiens ADP-ribosylation factor-binding protein GGA3 that plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes| 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
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 34-162 3.08e-34

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: 120.81  E-value: 3.08e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238436  34 IDLALLKATSHTsNNPPSDKYVTFLQSTIDT--CYGPDTVDAILHRLRVTTDVCVAAKCLILLHKMVKSESgyngeDSLR 111
Cdd:cd16987   1 LEVAVVKATSHD-DAPPDEKYVREILSLGSSsrAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGS-----PILE 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15238436 112 NNInhrtLIYTQGGSN-LKLNDLNVNSSRFTRELTPWVQWYKQYLDCYLSIA 162
Cdd:cd16987  75 QEL----SLAPSGGRNpLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122
 
Name Accession Description Interval E-value
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 34-162 3.08e-34

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: 120.81  E-value: 3.08e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238436  34 IDLALLKATSHTsNNPPSDKYVTFLQSTIDT--CYGPDTVDAILHRLRVTTDVCVAAKCLILLHKMVKSESgyngeDSLR 111
Cdd:cd16987   1 LEVAVVKATSHD-DAPPDEKYVREILSLGSSsrAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGS-----PILE 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15238436 112 NNInhrtLIYTQGGSN-LKLNDLNVNSSRFTRELTPWVQWYKQYLDCYLSIA 162
Cdd:cd16987  75 QEL----SLAPSGGRNpLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 33-248 5.37e-08

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: 53.07  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238436    33 TIDLALLKATSHtSNNPPSDKYVTFLQSTI-DTCYGPDTVDAILHRLRVTTDVCVAAKCLILLHKMVKSESGYNGEDSLR 111
Cdd:pfam07651   1 DLEVAVVKATSH-DEAPPKEKHVREILVGTsSSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238436   112 NNINHRTLiytqggsnlklndLNVNSSRFTRELTPWVQWYKQYLDCYLSIAEVLGITPNIKEKNEDKRLETQ-----RVS 186
Cdd:pfam07651  80 ARRRISSL-------------LRISSFSLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVgdpneRYL 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238436   187 SYPMDCILKQIDFLVE-LFEHISDRPKApQSKLNKIVIEMTELMVQDYF-------SAIRLMRIRFEELN 248
Cdd:pfam07651 147 TMSMEDLLDSIPKLQKlLFRLLKCRPTG-NALSNECIIAALILLVKESFglyrainEGIINLLEKFFELS 215
 
Name Accession Description Interval E-value
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 34-162 3.08e-34

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: 120.81  E-value: 3.08e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238436  34 IDLALLKATSHTsNNPPSDKYVTFLQSTIDT--CYGPDTVDAILHRLRVTTDVCVAAKCLILLHKMVKSESgyngeDSLR 111
Cdd:cd16987   1 LEVAVVKATSHD-DAPPDEKYVREILSLGSSsrAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGS-----PILE 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15238436 112 NNInhrtLIYTQGGSN-LKLNDLNVNSSRFTRELTPWVQWYKQYLDCYLSIA 162
Cdd:cd16987  75 QEL----SLAPSGGRNpLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 33-248 5.37e-08

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: 53.07  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238436    33 TIDLALLKATSHtSNNPPSDKYVTFLQSTI-DTCYGPDTVDAILHRLRVTTDVCVAAKCLILLHKMVKSESGYNGEDSLR 111
Cdd:pfam07651   1 DLEVAVVKATSH-DEAPPKEKHVREILVGTsSSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238436   112 NNINHRTLiytqggsnlklndLNVNSSRFTRELTPWVQWYKQYLDCYLSIAEVLGITPNIKEKNEDKRLETQ-----RVS 186
Cdd:pfam07651  80 ARRRISSL-------------LRISSFSLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVgdpneRYL 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238436   187 SYPMDCILKQIDFLVE-LFEHISDRPKApQSKLNKIVIEMTELMVQDYF-------SAIRLMRIRFEELN 248
Cdd:pfam07651 147 TMSMEDLLDSIPKLQKlLFRLLKCRPTG-NALSNECIIAALILLVKESFglyrainEGIINLLEKFFELS 215
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 34-156 4.33e-06

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: 44.96  E-value: 4.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238436  34 IDLALLKATSHtSNNPPSDKYV-TFLQSTIDTCYGPDT---VDAILHRLRvTTDVCVAAKCLILLHKMVKSesgynGEDS 109
Cdd:cd03564   1 LDVAVVKATNH-DEVPPKEKHVrKLLLATSNGGGRADVayiVHALAKRLH-KKNWIVVLKTLIVIHRLLRE-----GSPS 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15238436 110 -LRNNINHRTLIytqggsnlkLNDLNV--NSSRFTRELTPWVQWYKQYLD 156
Cdd:cd03564  74 fLEELLRYSGHI---------FNLSNFkdDSSPEAWDLSAFIRRYARYLE 114
ECH_2 pfam16113
Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: ...
 37-97 4.86e-03

Enoyl-CoA hydratase/isomerase; This family contains a diverse set of enzymes including: enoyl-CoA hydratase, napthoate synthase, carnitate racemase, 3-hydroxybutyryl-CoA dehydratase and dodecanoyl-CoA delta-isomerase. This family differs from pfam00378 in the structure of it's C-terminus.


Pssm-ID: 465024 [Multi-domain]  Cd Length: 331  Bit Score: 37.83  E-value: 4.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15238436    37 ALLKATSHTSNNPPSDkyVTFLQSTIDTCYGPDTVDAILHRLRVTTDVCV-AAKCLILLHKM 97
Cdd:pfam16113 198 AVLAEFAEESDPPPSP--LAAHREAIDRCFSADTVEEIIAALEAEADGDEwAAETLKTLRKR 257
 
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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