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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326523843  43 LDAAVIRATSHDDRFVDRGAAARVLDLARAS--SPSPLVWALARRAGRTRCWAVALK------ALMLAHRLLLLAQPR-- 112
Cdd:cd16987    1 LEVAVVKATSHDDAPPDEKYVREILSLGSSSraYASACVSALSRRLNRTRDWVVALKclmllhRLLRDGSPILEQELSla 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 326523843 113 -AGGRVPFDLADFRDRSSA---GFSVLVRAYFRFLDARSLFA 150
Cdd:cd16987   81 pSGGRNPLNLSDFRDGSSSkswDFSAFVRAYAAYLDERLIFS 122

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326523843  43 LDAAVIRATSHDDRFVDRGAAARVLDLARAS--SPSPLVWALARRAGRTRCWAVALK------ALMLAHRLLLLAQPR-- 112
Cdd:cd16987    1 LEVAVVKATSHDDAPPDEKYVREILSLGSSSraYASACVSALSRRLNRTRDWVVALKclmllhRLLRDGSPILEQELSla 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 326523843 113 -AGGRVPFDLADFRDRSSA---GFSVLVRAYFRFLDARSLFA 150
Cdd:cd16987   81 pSGGRNPLNLSDFRDGSSSkswDFSAFVRAYAAYLDERLIFS 122

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326523843  43 LDAAVIRATSHDDRFVDRGAAARVLDLARAS--SPSPLVWALARRAGRTRCWAVALK------ALMLAHRLLLLAQPR-- 112
Cdd:cd16987    1 LEVAVVKATSHDDAPPDEKYVREILSLGSSSraYASACVSALSRRLNRTRDWVVALKclmllhRLLRDGSPILEQELSla 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 326523843 113 -AGGRVPFDLADFRDRSSA---GFSVLVRAYFRFLDARSLFA 150
Cdd:cd16987   81 pSGGRNPLNLSDFRDGSSSkswDFSAFVRAYAAYLDERLIFS 122

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326523843  43 LDAAVIRATSHD-----DRFVDRGAAARVLDLARASSPsPLVWALARRAGRTRcWAVALKALMLAHRLLLLAQP------ 111
Cdd:cd03564    1 LDVAVVKATNHDevppkEKHVRKLLLATSNGGGRADVA-YIVHALAKRLHKKN-WIVVLKTLIVIHRLLREGSPsfleel 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 326523843 112 -RAGGRVpFDLADFRDRSS---AGFSVLVRAYFRFLDARS 147
Cdd:cd03564   79 lRYSGHI-FNLSNFKDDSSpeaWDLSAFIRRYARYLEERL 117