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Conserved domains on  [gi|17506539|ref|NP_493260|]
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ENTH domain-containing protein [Caenorhabditis elegans]

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 ...
 9-275 2.19e-95

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: 284.96  E-value: 2.19e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539     9 GQFQAVQKAITKDETPLKPKHLETILLGTH-TEKSSAIFWSSVKKIKLENHPVLTWKFCLLVHKLLRDGHPVVPKEAYRN 87
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSsSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539    88 EKRFTQLALHWK--DKRDYGPCIDAYCKLLHDRVIFHHKRPYFPGNLFVSPLQLDTMGRDLSRMLrLTGDMMHQMDSLLA 165
Cdd:pfam07651  81 RRRISSLLRISSfsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY-LTMSMEDLLDSIPK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539   166 FQEKVYLLSNSSPRWDPNTpqGQCLMLPLISVIMDTWPFFIYIVRMMYNLHSNVSP------HELEGYRSRFQTIFEKTK 239
Cdd:pfam07651 160 LQKLLFRLLKCRPTGNALS--NECIIAALILLVKESFGLYRAINEGIINLLEKFFElskpdaDRALGIYKRFVKQFERLK 237

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 17506539   240 QFYEECSKHQYFRCFVqIPTFPLHAPNFFTQSDLES 275
Cdd:pfam07651 238 EFYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
GrpE super family cl03075
nucleotide exchange factor GrpE; GrpE is the adenine nucleotide exchange factor of DnaK (Hsp70) ...
 295-333 1.04e-03

nucleotide exchange factor GrpE; GrpE is the adenine nucleotide exchange factor of DnaK (Hsp70)-type ATPases. In bacteria, the DnaK-DnaJ-GrpE (KJE) chaperone system functions at the fulcrum of protein homeostasis. GrpE participates actively in response to heat shock by preventing aggregation of stress-denatured proteins; unfolded proteins initially bind to DnaJ, the J-domain ATPase-activating protein (Hsp40 family), whereupon DnaK hydrolyzes its bound ATP, resulting in a stable complex. The GrpE dimer binds to the ATPase domain of Hsp70 catalyzing the dissociation of ADP, which enables rebinding of ATP, one step in the Hsp70 reaction cycle in protein folding. In eukaryotes, only the mitochondrial Hsp70, not the cytosolic form, is GrpE dependent. Over-expression of Hsp70 molecular chaperones is important in suppressing toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, as well as several polyQ-diseases such as Huntington's disease and ataxias.


The actual alignment was detected with superfamily member PRK14156:

Pssm-ID: 446000 [Multi-domain]  Cd Length: 177  Bit Score: 39.43  E-value: 1.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 17506539  295 EEARTRIEHYENRLKEMHGEFQHVRREADENREEVQRLR 333
Cdd:PRK14156  37 ELANERADEFENKYLRAHAEMQNIQRRANEERQQLQRYR 75
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 9-275 2.19e-95

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: 284.96  E-value: 2.19e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539     9 GQFQAVQKAITKDETPLKPKHLETILLGTH-TEKSSAIFWSSVKKIKLENHPVLTWKFCLLVHKLLRDGHPVVPKEAYRN 87
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSsSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539    88 EKRFTQLALHWK--DKRDYGPCIDAYCKLLHDRVIFHHKRPYFPGNLFVSPLQLDTMGRDLSRMLrLTGDMMHQMDSLLA 165
Cdd:pfam07651  81 RRRISSLLRISSfsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY-LTMSMEDLLDSIPK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539   166 FQEKVYLLSNSSPRWDPNTpqGQCLMLPLISVIMDTWPFFIYIVRMMYNLHSNVSP------HELEGYRSRFQTIFEKTK 239
Cdd:pfam07651 160 LQKLLFRLLKCRPTGNALS--NECIIAALILLVKESFGLYRAINEGIINLLEKFFElskpdaDRALGIYKRFVKQFERLK 237

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 17506539   240 QFYEECSKHQYFRCFVqIPTFPLHAPNFFTQSDLES 275
Cdd:pfam07651 238 EFYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
ANTH_N_HIP1_like cd17006
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 10-122 2.55e-48

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they 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. 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. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.


Pssm-ID: 340803  Cd Length: 114  Bit Score: 158.98  E-value: 2.55e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539  10 QFQAVQKAITKDETPLKPKHLETILLGTHTEKSSAIFWSSVKKIKLENHPVLTWKFCLLVHKLLRDGHPVVPKEAYRNEK 89
Cdd:cd17006   1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 17506539  90 RFTQLALHWKDKRD-YGPCIDAYCKLLHDRVIFH 122
Cdd:cd17006  81 RLKELGKLWGHLKDgYGKLIAQYCKLLITKLEFH 114
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
8-129 6.87e-39

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 134.68  E-value: 6.87e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539      8 RGQFQAVQKAITKDETPLKPKHLETILLGTHTEKSSAIFWSSVKKIKLENH--PVLTWKFCLLVHKLLRDGHPVVPKEAY 85
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTknWRVVYKALILLHYLLRNGSPRVILEAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 17506539     86 RNEKRFTQLALHWK---DKRDYGPCIDAYCKLLHDRVIFHHKRPYFP 129
Cdd:smart00273  81 RNRNRILNLSDFQDidsRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PRK14156 PRK14156
heat shock protein GrpE; Provisional
 295-333 1.04e-03

heat shock protein GrpE; Provisional


Pssm-ID: 237628 [Multi-domain]  Cd Length: 177  Bit Score: 39.43  E-value: 1.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 17506539  295 EEARTRIEHYENRLKEMHGEFQHVRREADENREEVQRLR 333
Cdd:PRK14156  37 ELANERADEFENKYLRAHAEMQNIQRRANEERQQLQRYR 75
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 9-275 2.19e-95

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: 284.96  E-value: 2.19e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539     9 GQFQAVQKAITKDETPLKPKHLETILLGTH-TEKSSAIFWSSVKKIKLENHPVLTWKFCLLVHKLLRDGHPVVPKEAYRN 87
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSsSAKLAALFWALSRRLPLTRSWVVAFKALILVHKLLREGHPSVLQELLRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539    88 EKRFTQLALHWK--DKRDYGPCIDAYCKLLHDRVIFHHKRPYFPGNLFVSPLQLDTMGRDLSRMLrLTGDMMHQMDSLLA 165
Cdd:pfam07651  81 RRRISSLLRISSfsLSWDYGAFIRAYAKYLDERLDFHRKLPRDPGTFERVEYGSLVAVGDPNERY-LTMSMEDLLDSIPK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539   166 FQEKVYLLSNSSPRWDPNTpqGQCLMLPLISVIMDTWPFFIYIVRMMYNLHSNVSP------HELEGYRSRFQTIFEKTK 239
Cdd:pfam07651 160 LQKLLFRLLKCRPTGNALS--NECIIAALILLVKESFGLYRAINEGIINLLEKFFElskpdaDRALGIYKRFVKQFERLK 237

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 17506539   240 QFYEECSKHQYFRCFVqIPTFPLHAPNFFTQSDLES 275
Cdd:pfam07651 238 EFYEVCKNLGYFRSLE-IPKLPHIPPNLLEALEEYL 272
ANTH_N_HIP1_like cd17006
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 10-122 2.55e-48

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1 and related proteins; This subfamily includes Huntingtin-interacting protein 1 (HIP1), HIP1-related protein (HIP1R), and similar proteins. Mammalian HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 is expressed only in neurons while HIP1R is ubiquitously expressed. Together with its interacting partner HIPPI, HIP1 regulates apoptosis and gene expression. Both HIP1 and HIP1R promote clathrin assembly in vitro, and they 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. 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. Mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively, instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of the ANTH domain of Huntingtin-interacting protein 1 and related proteins.


Pssm-ID: 340803  Cd Length: 114  Bit Score: 158.98  E-value: 2.55e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539  10 QFQAVQKAITKDETPLKPKHLETILLGTHTEKSSAIFWSSVKKIKLENHPVLTWKFCLLVHKLLRDGHPVVPKEAYRNEK 89
Cdd:cd17006   1 QAISINKAINPQEVPVKEKHVRSIIIGTHQEKGASTFWSIVSRLPLQGNPIVCWKFCHLLHKLLREGHPSVLRDSQRYRS 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 17506539  90 RFTQLALHWKDKRD-YGPCIDAYCKLLHDRVIFH 122
Cdd:cd17006  81 RLKELGKLWGHLKDgYGKLIAQYCKLLITKLEFH 114
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
8-129 6.87e-39

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 134.68  E-value: 6.87e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539      8 RGQFQAVQKAITKDETPLKPKHLETILLGTHTEKSSAIFWSSVKKIKLENH--PVLTWKFCLLVHKLLRDGHPVVPKEAY 85
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTknWRVVYKALILLHYLLRNGSPRVILEAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 17506539     86 RNEKRFTQLALHWK---DKRDYGPCIDAYCKLLHDRVIFHHKRPYFP 129
Cdd:smart00273  81 RNRNRILNLSDFQDidsRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ANTH_N_HIP1 cd17013
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 13-122 1.13e-25

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1; Huntingtin-interacting protein 1 (HIP1) was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. HIP1 promotes clathrin assembly in vitro. Together with its interacting partner HIPPI, it regulates apoptosis and gene expression. HIP1 contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. 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. The ANTH domain of mammalian HIP1 was found to preferentially bind PtdIns(3,4)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1.


Pssm-ID: 340810  Cd Length: 114  Bit Score: 99.73  E-value: 1.13e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539  13 AVQKAITKDETPLKPKHLETILLGTHTEKSSAIFWSSVKKIKLENHPVLTWKFCLLVHKLLRDGHPVVPKEAYRNEKRFT 92
Cdd:cd17013   4 SINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYKNELS 83

                        90       100       110
                ....*....|....*....|....*....|.
gi 17506539  93 QLALHWKD-KRDYGPCIDAYCKLLHDRVIFH 122
Cdd:cd17013  84 DMSRMWGHlSEGYGQLCSIYLKLLITKMEFH 114
ANTH_N_HIP1R cd17014
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein ...
 10-122 1.96e-25

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Huntingtin-interacting protein 1-related protein; Huntingtin-interacting protein 1-related protein (HIP1R), also called HIP12, promotes clathrin assembly in vitro. It is an endocytic protein involved in receptor trafficking, including regulating cell surface expression of receptor tyrosine kinases. Low HIP1R protein expression is associated with worse survival in diffuse large B-cell lymphoma (DLBCL) patients; it is preferentially expressed in germinal center B-cell (GCB)-like DLBCL, and may be potentially useful in subtyping DLBCL cases. HIP1R contains an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domain. 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. The ANTH domain of mammalian HIP1R was found to preferentially bind PtdIns(3,5)P2 instead of PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domain of Huntingtin-interacting protein 1-related protein.


Pssm-ID: 340811  Cd Length: 114  Bit Score: 98.78  E-value: 1.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539  10 QFQAVQKAITKDETPLKPKHLETILLGTHTEKSSAIFWSSVKKIKLENHPVLTWKFCLLVHKLLRDGHPVVPKEAYRNEK 89
Cdd:cd17014   1 QAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLQDCQRYRS 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 17506539  90 RFTQLALHWKDKRD-YGPCIDAYCKLLHDRVIFH 122
Cdd:cd17014  81 NIRETGSLWGHLHDrYGQLVSLYTKLLCTKIEFH 114
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
 12-122 9.03e-22

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; This subfamily is composed of Saccharomyces cerevisiae Sla2 protein (Sla2p, also called transmembrane protein MOP2), Schizosaccharomyces pombe endocytosis protein End4 (End4p, also called Sla2 protein homolog), and similar proteins. In yeast, cells lacking Sla2p have severe defects in actin organization, cell morphology, and endocytosis, suggesting roles in these processes. Sla2p regulates the Eps15-like Arp2/3 complex activator, Pan1p, controlling actin polymerization during endocytosis. In fission yeast, End4p has been implicated in cellular morphogenesis. Sla2p contains an N-terminal ANTH, a central colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. 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. The ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome. This model describes the N-terminal region of ANTH domains f Sla2p and similar proteins.


Pssm-ID: 340804  Cd Length: 115  Bit Score: 88.90  E-value: 9.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539  12 QAVQKAITKDETPLKPKHLETILLGTHTEKSSAIFWSSVKKIKLENHPVLTWKFCLLVHKLLRDGHPVVPKEAYRNEKRF 91
Cdd:cd17007   3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKPFWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALKEAIRNIEWL 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 17506539  92 TQLALHWKDK--RDYGPCIDAYCKLLHDRVIFH 122
Cdd:cd17007  83 ESLGRQSSGSgaKGYGRLIKEYVRYLLDKLAFH 115
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
 13-122 2.37e-18

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: 79.73  E-value: 2.37e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539  13 AVQKAITKDETPLKPKHLETILLGTHTEKSSAIFWSSVKKIKLENHPVLTWKFCLLVHKLLRDGHPVVPK-----EAYRN 87
Cdd:cd16986   4 AVNKATNKTDSPPKPKHVRTIIVKSWTHQKGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPELSLlggylDAWLP 83

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17506539  88 E----KRFTQLALHWkdkrdYGPCIDAYCKLLHDRVIFH 122
Cdd:cd16986  84 ElvrvKNTQQSLSEF-----YSQLIKKYVRYLELKVVFH 117
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 11-122 9.71e-11

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: 58.44  E-value: 9.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506539  11 FQAVQKAITKDETPLKPKHLETILLGTHTEKSSAIFWSSVKKI--KLENHPVLT-WKFCLLVHKLLRDGHPVVPKEAYRN 87
Cdd:cd03564   2 DVAVVKATNHDEVPPKEKHVRKLLLATSNGGGRADVAYIVHALakRLHKKNWIVvLKTLIVIHRLLREGSPSFLEELLRY 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17506539  88 EKRFTQLaLHWKDKR-----DYGPCIDAYCKLLHDRVIFH 122
Cdd:cd03564  82 SGHIFNL-SNFKDDSspeawDLSAFIRRYARYLEERLECF 120
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 13-76 3.99e-04

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: 39.47  E-value: 3.99e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17506539  13 AVQKAITKDETPLKPKHLETILLGTHTEKSSA--IFWSSVKKIKlENHPVLTWKFCLLVHKLLRDG 76
Cdd:cd16988   4 LVKGATKIKLAPPKAKYLDPILLATYSSDASFgeIVRALSRRLR-DNSWTVVFKSLIVLHLMIREG 68
PRK14156 PRK14156
heat shock protein GrpE; Provisional
 295-333 1.04e-03

heat shock protein GrpE; Provisional


Pssm-ID: 237628 [Multi-domain]  Cd Length: 177  Bit Score: 39.43  E-value: 1.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 17506539  295 EEARTRIEHYENRLKEMHGEFQHVRREADENREEVQRLR 333
Cdd:PRK14156  37 ELANERADEFENKYLRAHAEMQNIQRRANEERQQLQRYR 75
 
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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