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Conserved domains on  [gi|15218697|ref|NP_171804|]
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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 ...
 33-322 7.73e-115

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: 343.13  E-value: 7.73e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697    33 ELDVAIVKATRHEEFPAEEKYIREILSLTSYSrSYINACVSTLSRRLNKTKCWTVALKTLILIQRLLGEGDQAYEQEIFF 112
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSS-AKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697   113 ATRRGTRLLNMSDFrdvsrSNSWDYSAFVRTYALYLDERLDFRMQARHGKrgvycvgGEADEEEQDqaaadlstAIVVRS 192
Cdd:pfam07651  80 ARRRISSLLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRDP-------GTFERVEYG--------SLVAVG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697   193 QPI---AEMKTEQIFIRIQHLQQLLDRFLACRPTGNARNNRVVIVALYPIVKESFQIYYDVTEIMGILIERFMELDIPDS 269
Cdd:pfam07651 140 DPNeryLTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDA 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15218697   270 IKVYDIFCRVSKQFEELDQFYSWCKNMGIARSSEYPEIEKITQKKLDLMDEFI 322
Cdd:pfam07651 220 DRALGIYKRFVKQFERLKEFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
PLN03229 super family cl31989
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 295-396 3.38e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


The actual alignment was detected with superfamily member PLN03229:

Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 40.61  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697  295 NMGIARSSEYPEIekitQKKLDLMDEFIRDKSALEHTKQSKSVKSEADEDDDEARTEEvnEEQEDMNAIKALPEPPPKEE 374
Cdd:PLN03229 521 NKRLSRAPNYLSL----KYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRP--EIKEKMEALKAEVASSGASS 594

                         90       100
                 ....*....|....*....|..
gi 15218697  375 DDVKPeEEAKEEVIIEKKQEEM 396
Cdd:PLN03229 595 GDELD-DDLKEKVEKMKKEIEL 615
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 33-322 7.73e-115

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: 343.13  E-value: 7.73e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697    33 ELDVAIVKATRHEEFPAEEKYIREILSLTSYSrSYINACVSTLSRRLNKTKCWTVALKTLILIQRLLGEGDQAYEQEIFF 112
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSS-AKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697   113 ATRRGTRLLNMSDFrdvsrSNSWDYSAFVRTYALYLDERLDFRMQARHGKrgvycvgGEADEEEQDqaaadlstAIVVRS 192
Cdd:pfam07651  80 ARRRISSLLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRDP-------GTFERVEYG--------SLVAVG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697   193 QPI---AEMKTEQIFIRIQHLQQLLDRFLACRPTGNARNNRVVIVALYPIVKESFQIYYDVTEIMGILIERFMELDIPDS 269
Cdd:pfam07651 140 DPNeryLTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDA 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15218697   270 IKVYDIFCRVSKQFEELDQFYSWCKNMGIARSSEYPEIEKITQKKLDLMDEFI 322
Cdd:pfam07651 220 DRALGIYKRFVKQFERLKEFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 34-155 2.38e-66

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: 212.10  E-value: 2.38e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697  34 LDVAIVKATRHEEFPAEEKYIREILSLTSYSRSYINACVSTLSRRLNKTKCWTVALKTLILIQRLLGEGDQAYEQEIFFA 113
Cdd:cd16987   1 LEVAVVKATSHDDAPPDEKYVREILSLGSSSRAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELSLA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15218697 114 TRRGTRLLNMSDFRDVSRSNSWDYSAFVRTYALYLDERLDFR 155
Cdd:cd16987  81 PSGGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
32-157 4.31e-41

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 145.08  E-value: 4.31e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697     32 SELDVAIVKATRHEEFPAEEKYIREILSLTSYSRSYINACVSTLSRRLNKTKCWTVALKTLILIQRLLGEGDqayEQEIF 111
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNWRVVYKALILLHYLLRNGS---PRVIL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 15218697    112 FATRRGTRLLNMSDFRDVSrSNSWDYSAFVRTYALYLDERLDFRMQ 157
Cdd:smart00273  78 EALRNRNRILNLSDFQDID-SRGKDQGANIRTYAKYLLERLEDDRR 122
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 295-396 3.38e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 40.61  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697  295 NMGIARSSEYPEIekitQKKLDLMDEFIRDKSALEHTKQSKSVKSEADEDDDEARTEEvnEEQEDMNAIKALPEPPPKEE 374
Cdd:PLN03229 521 NKRLSRAPNYLSL----KYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRP--EIKEKMEALKAEVASSGASS 594

                         90       100
                 ....*....|....*....|..
gi 15218697  375 DDVKPeEEAKEEVIIEKKQEEM 396
Cdd:PLN03229 595 GDELD-DDLKEKVEKMKKEIEL 615
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 33-322 7.73e-115

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: 343.13  E-value: 7.73e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697    33 ELDVAIVKATRHEEFPAEEKYIREILSLTSYSrSYINACVSTLSRRLNKTKCWTVALKTLILIQRLLGEGDQAYEQEIFF 112
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSS-AKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697   113 ATRRGTRLLNMSDFrdvsrSNSWDYSAFVRTYALYLDERLDFRMQARHGKrgvycvgGEADEEEQDqaaadlstAIVVRS 192
Cdd:pfam07651  80 ARRRISSLLRISSF-----SLSWDYGAFIRAYAKYLDERLDFHRKLPRDP-------GTFERVEYG--------SLVAVG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697   193 QPI---AEMKTEQIFIRIQHLQQLLDRFLACRPTGNARNNRVVIVALYPIVKESFQIYYDVTEIMGILIERFMELDIPDS 269
Cdd:pfam07651 140 DPNeryLTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDA 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15218697   270 IKVYDIFCRVSKQFEELDQFYSWCKNMGIARSSEYPEIEKITQKKLDLMDEFI 322
Cdd:pfam07651 220 DRALGIYKRFVKQFERLKEFYEVCKNLGYFRSLEIPKLPHIPPNLLEALEEYL 272
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 34-155 2.38e-66

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: 212.10  E-value: 2.38e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697  34 LDVAIVKATRHEEFPAEEKYIREILSLTSYSRSYINACVSTLSRRLNKTKCWTVALKTLILIQRLLGEGDQAYEQEIFFA 113
Cdd:cd16987   1 LEVAVVKATSHDDAPPDEKYVREILSLGSSSRAYASACVSALSRRLNRTRDWVVALKCLMLLHRLLRDGSPILEQELSLA 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15218697 114 TRRGTRLLNMSDFRDVSRSNSWDYSAFVRTYALYLDERLDFR 155
Cdd:cd16987  81 PSGGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDERLIFS 122
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
32-157 4.31e-41

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 145.08  E-value: 4.31e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697     32 SELDVAIVKATRHEEFPAEEKYIREILSLTSYSRSYINACVSTLSRRLNKTKCWTVALKTLILIQRLLGEGDqayEQEIF 111
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTKNWRVVYKALILLHYLLRNGS---PRVIL 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 15218697    112 FATRRGTRLLNMSDFRDVSrSNSWDYSAFVRTYALYLDERLDFRMQ 157
Cdd:smart00273  78 EALRNRNRILNLSDFQDID-SRGKDQGANIRTYAKYLLERLEDDRR 122
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 34-154 6.14e-38

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: 136.25  E-value: 6.14e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697  34 LDVAIVKATRHEEFPAEEKYIREILSLTS--YSRSYINACVSTLSRRLNKTKcWTVALKTLILIQRLLGEGDQAYEQEIF 111
Cdd:cd03564   1 LDVAVVKATNHDEVPPKEKHVRKLLLATSngGGRADVAYIVHALAKRLHKKN-WIVVLKTLIVIHRLLREGSPSFLEELL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15218697 112 fatRRGTRLLNMSDFRDVSRSNSWDYSAFVRTYALYLDERLDF 154
Cdd:cd03564  80 ---RYSGHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLEC 119
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 37-152 5.41e-12

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: 62.82  E-value: 5.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697  37 AIVKATRHEEFPAEEKYIREILSLTSYSRSYINACVSTLSRRLNKTKcWTVALKTLILIQRLLGEGDQAYEQeiFFATRr 116
Cdd:cd16985   4 AVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSS-WVVVFKALITTHHLMVYGNERFIQ--YLASR- 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15218697 117 gTRLLNMSDFRDVSRSNSWDYSAFVRTYALYLDERL 152
Cdd:cd16985  80 -NSLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKA 114
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 35-151 1.52e-11

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: 61.43  E-value: 1.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697  35 DVAIVKATRHEEFPAEEKYIREILSLTSYSRSYINACVSTLSRRLNKTKcWTVALKTLILIQRLLGEGDQAYeqeiffAT 114
Cdd:cd16988   2 EKLVKGATKIKLAPPKAKYLDPILLATYSSDASFGEIVRALSRRLRDNS-WTVVFKSLIVLHLMIREGETDD------VL 74

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15218697 115 RRGTRLLNMSDFRDVSRSNSWDYS--AFVRTYALYLDER 151
Cdd:cd16988  75 LYYLSRPDFLDLRKIRNGSSAGSGqlQNIQRYAAYLKER 113
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
 36-154 1.13e-06

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: 47.76  E-value: 1.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697  36 VAIVKATRHEEFPAEEKYIREILsLTSYSRSYINACVSTLSRRL---NKTKCWtvalKTLILIQRLLGEGDQayEQEIFF 112
Cdd:cd16986   3 KAVNKATNKTDSPPKPKHVRTII-VKSWTHQKGPQFYEELSKRLllnNPVVQF----KALVTLHKVLRDGPP--ELSLLG 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15218697 113 ATRRGTrLLNMSDFRDVSRSNSWDYSAFVRTYALYLDERLDF 154
Cdd:cd16986  76 GYLDAW-LPELVRVKNTQQSLSEFYSQLIKKYVRYLELKVVF 116
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 40-148 1.97e-04

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: 41.26  E-value: 1.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697  40 KATRHEEFPAEEKYIREILSLTSYSRSYINACVSTLSRRLNKtKCWTVALKTLILIQRLLGEGDQAYEQEifFATRRgtR 119
Cdd:cd00197   7 KATSNENMGPDWPLIMEICDLINETNVGPKEAVDAIKKRINN-KNPHVVLKALTLLEYCVKNCGERFHQE--VASND--F 81

                        90       100
                ....*....|....*....|....*....
gi 15218697 120 LLNMSDFRDVSRSNSwDYSAFVRTYALYL 148
Cdd:cd00197  82 AVELLKFDKSGLLGD-DVSTNVREKAIEL 109
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 295-396 3.38e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 40.61  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697  295 NMGIARSSEYPEIekitQKKLDLMDEFIRDKSALEHTKQSKSVKSEADEDDDEARTEEvnEEQEDMNAIKALPEPPPKEE 374
Cdd:PLN03229 521 NKRLSRAPNYLSL----KYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRP--EIKEKMEALKAEVASSGASS 594

                         90       100
                 ....*....|....*....|..
gi 15218697  375 DDVKPeEEAKEEVIIEKKQEEM 396
Cdd:PLN03229 595 GDELD-DDLKEKVEKMKKEIEL 615
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 32-152 5.00e-03

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: 37.54  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218697    32 SELDVAIVKATRHEEFPAEEKYIREILSLTsYSRSYINACVSTLSRRLNKT-KCWTVALKTLILIQRLLGEGDQAYEQEI 110
Cdd:pfam01417   2 SETELKVREATNNDPWGPSGTLMDEIARLT-YNYVEFPEIMKMLWKRLNDKgKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 15218697   111 ffatrRGTRLL--NMSDFRDVSrSNSWDYSAFVRTYALYL------DERL 152
Cdd:pfam01417  81 -----RENIYIirTLTDFHYID-ENGKDQGINVRKKAKEIlnlledDELL 124
 
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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