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Conserved domains on  [gi|2241050087|ref|XP_002533971|]
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putative clathrin assembly protein At4g40080 [Ricinus communis]

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 ...
 34-157 8.04e-52

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: 167.80  E-value: 8.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087  34 LHLALLRATTHDPfTPPNSKHITTVLSYGHSSRATAASAIEALMDRLQSTHDSSVAVKCLIIVHHIIKHGSFILQDQLSV 113
Cdd:cd16987     1 LEVAVVKATSHDD-APPDEKYVREILSLGSSSRAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELSL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2241050087 114 YPStGGRNYLKLSSFRDNTTPLTWELSSWVRWYARYLEHLLSTS 157
Cdd:cd16987    80 APS-GGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 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 ...
 34-157 8.04e-52

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: 167.80  E-value: 8.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087  34 LHLALLRATTHDPfTPPNSKHITTVLSYGHSSRATAASAIEALMDRLQSTHDSSVAVKCLIIVHHIIKHGSFILQDQLSV 113
Cdd:cd16987     1 LEVAVVKATSHDD-APPDEKYVREILSLGSSSRAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELSL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2241050087 114 YPStGGRNYLKLSSFRDNTTPLTWELSSWVRWYARYLEHLLSTS 157
Cdd:cd16987    80 APS-GGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 37-199 2.31e-16

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: 78.11  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087  37 ALLRATTHDPfTPPNSKHITTVLSYGHSSrATAASAIEALMDRLQSTHDSSVAVKCLIIVHHIIKHGS-FILQDQLSvYP 115
Cdd:pfam07651   5 AVVKATSHDE-APPKEKHVREILVGTSSS-AKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHpSVLQELLR-AR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087 116 STGGRnYLKLSSFrdnttPLTWELSSWVRWYARYLEHLLSTSRVLGFFlcstSGTAEKDKEEEKVSALTNS--------- 186
Cdd:pfam07651  82 RRISS-LLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRD----PGTFERVEYGSLVAVGDPNeryltmsme 151

                         170
                  ....*....|...
gi 2241050087 187 DLLKEIDSLSNLI 199
Cdd:pfam07651 152 DLLDSIPKLQKLL 164
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
37-163 1.05e-15

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 72.66  E-value: 1.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087   37 ALLRATTHDPfTPPNSKHITTVLSYGHSSRATAASAIEALMDRLQSTHDSSVAVKCLIIVHHIIKHGS--FILQDQLSVY 114
Cdd:smart00273   6 KVRKATNNDE-WGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNWRVVYKALILLHYLLRNGSprVILEALRNRN 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2241050087  115 pstggrNYLKLSSFRDnTTPLTWELSSWVRWYARYLEHLLSTSRVLGFF 163
Cdd:smart00273  85 ------RILNLSDFQD-IDSRGKDQGANIRTYAKYLLERLEDDRRLKEE 126
 
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 ...
 34-157 8.04e-52

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: 167.80  E-value: 8.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087  34 LHLALLRATTHDPfTPPNSKHITTVLSYGHSSRATAASAIEALMDRLQSTHDSSVAVKCLIIVHHIIKHGSFILQDQLSV 113
Cdd:cd16987     1 LEVAVVKATSHDD-APPDEKYVREILSLGSSSRAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELSL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2241050087 114 YPStGGRNYLKLSSFRDNTTPLTWELSSWVRWYARYLEHLLSTS 157
Cdd:cd16987    80 APS-GGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 37-156 1.92e-20

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: 85.40  E-value: 1.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087  37 ALLRATTHDPfTPPNSKHITTVL--SYGHSSRATAASAIEALMDRLQsTHDSSVAVKCLIIVHHIIKHGSFILQDQLSVY 114
Cdd:cd03564     4 AVVKATNHDE-VPPKEKHVRKLLlaTSNGGGRADVAYIVHALAKRLH-KKNWIVVLKTLIVIHRLLREGSPSFLEELLRY 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2241050087 115 PstggRNYLKLSSFRDNTTPLTWELSSWVRWYARYLEHLLST 156
Cdd:cd03564    82 S----GHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLEC 119
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 37-199 2.31e-16

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: 78.11  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087  37 ALLRATTHDPfTPPNSKHITTVLSYGHSSrATAASAIEALMDRLQSTHDSSVAVKCLIIVHHIIKHGS-FILQDQLSvYP 115
Cdd:pfam07651   5 AVVKATSHDE-APPKEKHVREILVGTSSS-AKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHpSVLQELLR-AR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087 116 STGGRnYLKLSSFrdnttPLTWELSSWVRWYARYLEHLLSTSRVLGFFlcstSGTAEKDKEEEKVSALTNS--------- 186
Cdd:pfam07651  82 RRISS-LLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRD----PGTFERVEYGSLVAVGDPNeryltmsme 151

                         170
                  ....*....|...
gi 2241050087 187 DLLKEIDSLSNLI 199
Cdd:pfam07651 152 DLLDSIPKLQKLL 164
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
37-163 1.05e-15

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 72.66  E-value: 1.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087   37 ALLRATTHDPfTPPNSKHITTVLSYGHSSRATAASAIEALMDRLQSTHDSSVAVKCLIIVHHIIKHGS--FILQDQLSVY 114
Cdd:smart00273   6 KVRKATNNDE-WGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNWRVVYKALILLHYLLRNGSprVILEALRNRN 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2241050087  115 pstggrNYLKLSSFRDnTTPLTWELSSWVRWYARYLEHLLSTSRVLGFF 163
Cdd:smart00273  85 ------RILNLSDFQD-IDSRGKDQGANIRTYAKYLLERLEDDRRLKEE 126
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 37-150 3.48e-08

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) subfamily; The Adaptor Protein 180 (AP180) subfamily members are phosphatidylinositol-binding clathrin assembly proteins, including mammalian clathrin coat assembly protein AP180 and Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), Drosophila LAP (also called Like-AP180 or AP180), and Caenorhabditis elegans Uncoordinated protein 11 (unc-11, also called AP180-like adaptor protein). They are components of the adaptor complexes which link clathrin to receptors in coated vesicles. AP180 and CALM play important roles in clathrin-mediated endocytosis. AP180, also called 91 kDa synaptosomal-associated protein (SNAP91) or phosphoprotein F1-20, is a brain-specific clathrin-binding protein which stimulates clathrin assembly during the recycling of synaptic vesicles. CALM, also called phosphatidylinositol binding clathrin assembly protein (PICALM), is ubiquitously expressed. Members of this subfamily contain ANTH domains, which 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 the Adaptor Protein 180 (AP180) subfamily.


Pssm-ID: 340782  Cd Length: 117  Bit Score: 51.27  E-value: 3.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087  37 ALLRATTHDpFTPPNSKHITTVLSYGHSSRATAASAIEALMDRlqSTHDSSVAV-KCLIIVHHIIKHGSfilqDQLSVYP 115
Cdd:cd16985     4 AVCKATTHE-VMGPKKKHLDYLVQCTNEPNVNIPQLADLLFER--TQNSSWVVVfKALITTHHLMVYGN----ERFIQYL 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2241050087 116 STggRNYL-KLSSFRDNTTPLTWELSSWVRWYARYL 150
Cdd:cd16985    77 AS--RNSLfNLSNFLDKSGSQGYDMSTFIRRYAKYL 110
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 49-151 7.85e-05

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: 41.78  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087  49 PPNSKHITTVLSYGHSSRATAASAIEALMDRLQSTHdSSVAVKCLIIVHHIIKHGSfilQDQLSVYPSTgGRNYLKLSSF 128
Cdd:cd16988    15 PPKAKYLDPILLATYSSDASFGEIVRALSRRLRDNS-WTVVFKSLIVLHLMIREGE---TDDVLLYYLS-RPDFLDLRKI 89

                          90       100
                  ....*....|....*....|...
gi 2241050087 129 RDNTTPLTWELSSwVRWYARYLE 151
Cdd:cd16988    90 RNGSSAGSGQLQN-IQRYAAYLK 111
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
 37-151 1.39e-03

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton 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. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.


Pssm-ID: 340783  Cd Length: 117  Bit Score: 38.13  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241050087  37 ALLRATTHDPfTPPNSKHITTVLSYGHsSRATAASAIEALMDRLQSThDSSVAVKCLIIVHHIIKHGSfilqdqlSVYPS 116
Cdd:cd16986     4 AVNKATNKTD-SPPKPKHVRTIIVKSW-THQKGPQFYEELSKRLLLN-NPVVQFKALVTLHKVLRDGP-------PELSL 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2241050087 117 TGG---RNYLKLSSFRDNTTPLTWELSSWVRWYARYLE 151
Cdd:cd16986    74 LGGyldAWLPELVRVKNTQQSLSEFYSQLIKKYVRYLE 111
 
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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