NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1776842870|ref|NP_001363657|]
View 

clathrin coat assembly protein AP180 isoform v [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-224 5.34e-80

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: 258.77  E-value: 5.34e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870   1 MADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYLNEKAFS 79
Cdd:pfam07651  38 LFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRARRRISSLLRIS-SFSLSWDYGAFIRAYAKYLDERLDF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  80 YRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKL 149
Cdd:pfam07651 117 HRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGL 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776842870 150 FACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKG-DIPDLTQAPSSLMETLEQHL 224
Cdd:pfam07651 197 YRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKEFYEVCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 667-837 1.58e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  667 PTMAPAGQPAPVSMVPP-SPAMAASKALGSDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWS 745
Cdd:PHA03247  2771 PPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPP 2843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  746 AGVPPSAPLQGAV---------PPTSSVPPVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVM 798
Cdd:PHA03247  2844 GPPPPSLPLGGSVapggdvrrrPPSRSPAAKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQP 2923

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1776842870  799 FAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 837
Cdd:PHA03247  2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 1-224 5.34e-80

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: 258.77  E-value: 5.34e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870   1 MADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYLNEKAFS 79
Cdd:pfam07651  38 LFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRARRRISSLLRIS-SFSLSWDYGAFIRAYAKYLDERLDF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  80 YRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKL 149
Cdd:pfam07651 117 HRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGL 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776842870 150 FACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKG-DIPDLTQAPSSLMETLEQHL 224
Cdd:pfam07651 197 YRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKEFYEVCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 1-80 1.81e-52

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: 178.38  E-value: 1.81e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870   1 MADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSY 80
Cdd:cd16985    38 LADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRNSLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKAISY 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
1-87 1.85e-26

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 105.02  E-value: 1.85e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870    1 MADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFI-QYLASRNTLFNLSNFLDKsGSHGYDMSTFIRRYSRYLNEKAF 78
Cdd:smart00273  40 IMAVLWRRLNDTkNWRVVYKALILLHYLLRNGSPRVIlEALRNRNRILNLSDFQDI-DSRGKDQGANIRTYAKYLLERLE 118


                   ....*....
gi 1776842870   79 SYRQMAFDF 87
Cdd:smart00273 119 DDRRLKEER 127
PHA03247 PHA03247
large tegument protein UL36; Provisional
 667-837 1.58e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  667 PTMAPAGQPAPVSMVPP-SPAMAASKALGSDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWS 745
Cdd:PHA03247  2771 PPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPP 2843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  746 AGVPPSAPLQGAV---------PPTSSVPPVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVM 798
Cdd:PHA03247  2844 GPPPPSLPLGGSVapggdvrrrPPSRSPAAKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQP 2923

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1776842870  799 FAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 837
Cdd:PHA03247  2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
 661-834 1.16e-03

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 42.36  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 661 LGDLLMPTMAPAgQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTT--TKKGDLQWNAGEKKLTGGANWQPK 738
Cdd:TIGR01645 278 VGKCVTPPDALL-QPATVSAIPAAAAVAAAAATAKIMAAEAVAGAAVLGPRAQSpaTPSSSLPTDIGNKAVVSSAKKEAE 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 739 VAPAtwsagVPPSAPLQGAVPPTSSVPPVAgAPSVGQPGagfGMPPAGTGMPMMPqQPVMFAQPmmRPPFGAAAVPGTQL 818
Cdd:TIGR01645 357 EVPP-----LPQAAPAVVKPGPMEIPTPVP-PPGLAIPS---LVAPPGLVAPTEI-NPSFLASP--RKKMKREKLPVTFG 424

                         170
                  ....*....|....*.
gi 1776842870 819 SPSPTPASQSPKKPPA 834
Cdd:TIGR01645 425 ALDDTLAWKEPSKEDQ 440
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 665-835 3.10e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 665 LMPTMAPAGQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTTTKKGDLQWNAGEKKL-TGGANWQPKVAPAt 743
Cdd:pfam03154 166 ILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLiQQTPTLHPQRLPS- 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 744 wsagvpPSAPLQGAVPPTSsvPPVAGAPSVGQPGAGFGMPPAG----TGMPMMPQqPVMfAQPMMRPP-FGAAAVPGTQL 818
Cdd:pfam03154 245 ------PHPPLQPMTQPPP--PSQVSPQPLPQPSLHGQMPPMPhslqTGPSHMQH-PVP-PQPFPLTPqSSQSQVPPGPS 314

                         170
                  ....*....|....*..
gi 1776842870 819 SPSPTPASQSPKKPPAK 835
Cdd:pfam03154 315 PAAPGQSQQRIHTPPSQ 331
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 1-224 5.34e-80

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: 258.77  E-value: 5.34e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870   1 MADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYLNEKAFS 79
Cdd:pfam07651  38 LFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRARRRISSLLRIS-SFSLSWDYGAFIRAYAKYLDERLDF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  80 YRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKL 149
Cdd:pfam07651 117 HRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGL 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776842870 150 FACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKG-DIPDLTQAPSSLMETLEQHL 224
Cdd:pfam07651 197 YRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKEFYEVCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 1-80 1.81e-52

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: 178.38  E-value: 1.81e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870   1 MADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSY 80
Cdd:cd16985    38 LADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRNSLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKAISY 117
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 2-80 1.68e-27

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: 107.74  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870   2 ADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRN-TLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSY 80
Cdd:cd03564    41 VHALAKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYSgHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLECF 120
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
1-87 1.85e-26

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 105.02  E-value: 1.85e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870    1 MADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFI-QYLASRNTLFNLSNFLDKsGSHGYDMSTFIRRYSRYLNEKAF 78
Cdd:smart00273  40 IMAVLWRRLNDTkNWRVVYKALILLHYLLRNGSPRVIlEALRNRNRILNLSDFQDI-DSRGKDQGANIRTYAKYLLERLE 118


                   ....*....
gi 1776842870   79 SYRQMAFDF 87
Cdd:smart00273 119 DDRRLKEER 127
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 2-79 6.28e-20

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: 85.94  E-value: 6.28e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776842870   2 ADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFlDKSGSHGYDMSTFIRRYSRYLNEKAFS 79
Cdd:cd00197    39 VDAIKKRINNKNPHVVLKALTLLEYCVKNCGERFHQEVASNDFAVELLKF-DKSGLLGDDVSTNVREKAIELVQLWAS 115
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 3-80 3.58e-14

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: 69.52  E-value: 3.58e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776842870   3 DTLFERATNSSWVVVFKALVTTHHLMVHGN-ERFIQYLASRNTLFNLSNFLDKSgSHGYDMSTFIRRYSRYLNEKAFSY 80
Cdd:cd16988    40 RALSRRLRDNSWTVVFKSLIVLHLMIREGEtDDVLLYYLSRPDFLDLRKIRNGS-SAGSGQLQNIQRYAAYLKERVKEY 117
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 1-73 1.01e-10

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: 59.88  E-value: 1.01e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776842870   1 MADTLFERA--TNSSWVVVFKALVTTHHLMVHGNERFIQYL-ASRNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYL 73
Cdd:pfam01417  40 IMKMLWKRLndKGKNWRHIYKALTLLEYLLKNGSERVVDDLrENIYIIRTLTDFHY-IDENGKDQGINVRKKAKEI 114
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 13-76 8.58e-10

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: 57.25  E-value: 8.58e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776842870  13 SWVVVFKALVTTHHLMVHGNERFIQ----YLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEK 76
Cdd:cd16987    51 DWVVALKCLMLLHRLLRDGSPILEQelslAPSGGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDER 118
PHA03247 PHA03247
large tegument protein UL36; Provisional
 667-837 1.58e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  667 PTMAPAGQPAPVSMVPP-SPAMAASKALGSDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWS 745
Cdd:PHA03247  2771 PPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPP 2843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  746 AGVPPSAPLQGAV---------PPTSSVPPVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVM 798
Cdd:PHA03247  2844 GPPPPSLPLGGSVapggdvrrrPPSRSPAAKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQP 2923

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1776842870  799 FAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 837
Cdd:PHA03247  2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 730-834 1.40e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 730 TGGANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPV-------AGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQP 802
Cdd:PRK07764  387 VAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPApaaapqpAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQP 466

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1776842870 803 MMRPPFGAAAVPGTQLSPSPTPASQSPKKPPA 834
Cdd:PRK07764  467 APAPAAAPEPTAAPAPAPPAAPAPAAAPAAPA 498
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
737-839 2.06e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 737 PKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPgt 816
Cdd:PRK12323  381 PVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAP-- 458

                          90       100
                  ....*....|....*....|...
gi 1776842870 817 qlSPSPTPASQSPKKPPAKDPLA 839
Cdd:PRK12323  459 --AAAARPAAAGPRPVAAAAAAA 479
PHA03247 PHA03247
large tegument protein UL36; Provisional
 535-833 2.72e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  535 SSPPQGASPvpeSSLTADLLSVDAFAAPSP--ATTASPAKVDSSGVIDLFGDAFGSSASEPQPASQAASSSSASADLLAG 612
Cdd:PHA03247  2677 SSPPQRPRR---RAARPTVGSLTSLADPPPppPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  613 ----------FGGSFMAPSPSPVTPAQNNLLQPnfEAAFGTTPSTSSSSSFDPSVFDGLGDLLMPTMAPAGQPAPVSMVP 682
Cdd:PHA03247  2754 parparppttAGPPAPAPPAAPAAGPPRRLTRP--AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  683 PSPAMAASKALGSDLDSSLaSLVGNLGISGTTTKKGDLQ----WNAGEKKLTGGANWQPKVAPATWSAGVPPsapLQGAV 758
Cdd:PHA03247  2832 TSAQPTAPPPPPGPPPPSL-PLGGSVAPGGDVRRRPPSRspaaKPAAPARPPVRRLARPAVSRSTESFALPP---DQPER 2907

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  759 PPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRP------PFGAAAVPGT-----QLSPSPTPASQ 827
Cdd:PHA03247  2908 PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsgavpqPWLGALVPGRvavprFRVPQPAPSRE 2987


                   ....*.
gi 1776842870  828 SPKKPP 833
Cdd:PHA03247  2988 APASST 2993
PHA03378 PHA03378
EBNA-3B; Provisional
 737-837 7.61e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 7.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 737 PKVAPATwsAGVPPSAPLQG---AVPPTSSVPPvAGAPSVGQPGA---GFGMPPAGTGMPMMP-------QQPVMFAQPM 803
Cdd:PHA03378  687 IQWAPGT--MQPPPRAPTPMrppAAPPGRAQRP-AAATGRARPPAaapGRARPPAAAPGRARPpaaapgrARPPAAAPGR 763

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1776842870 804 MRPPFGAAAVPGTQLSPSPTPAS-QSPKKPPAKDP 837
Cdd:PHA03378  764 ARPPAAAPGAPTPQPPPQAPPAPqQRPRGAPTPQP 798
PHA03247 PHA03247
large tegument protein UL36; Provisional
 737-837 8.74e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 8.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  737 PKVAPATWSAGVP-PSAPLQG-----AVPPTSSVPPVAGAPSVGQPGAGFGMPP--AGTGMPMMPQQPVMFAQPMMRPPF 808
Cdd:PHA03247  2708 PEPAPHALVSATPlPPGPAAArqaspALPAAPAPPAVPAGPATPGGPARPARPPttAGPPAPAPPAAPAAGPPRRLTRPA 2787

                           90       100
                   ....*....|....*....|....*....
gi 1776842870  809 GAAAVPGTQLSPSPTPASQSPKKPPAKDP 837
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAA 2816
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
 661-834 1.16e-03

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 42.36  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 661 LGDLLMPTMAPAgQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTT--TKKGDLQWNAGEKKLTGGANWQPK 738
Cdd:TIGR01645 278 VGKCVTPPDALL-QPATVSAIPAAAAVAAAAATAKIMAAEAVAGAAVLGPRAQSpaTPSSSLPTDIGNKAVVSSAKKEAE 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 739 VAPAtwsagVPPSAPLQGAVPPTSSVPPVAgAPSVGQPGagfGMPPAGTGMPMMPqQPVMFAQPmmRPPFGAAAVPGTQL 818
Cdd:TIGR01645 357 EVPP-----LPQAAPAVVKPGPMEIPTPVP-PPGLAIPS---LVAPPGLVAPTEI-NPSFLASP--RKKMKREKLPVTFG 424

                         170
                  ....*....|....*.
gi 1776842870 819 SPSPTPASQSPKKPPA 834
Cdd:TIGR01645 425 ALDDTLAWKEPSKEDQ 440
PHA03247 PHA03247
large tegument protein UL36; Provisional
 739-837 1.50e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  739 VAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAgfgmPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAV----- 813
Cdd:PHA03247  2740 APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP----PRRLTRPAVASLSESRESLPSPWDPADPPAAvlapa 2815

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1776842870  814 --------PGTQLSPSPTPASQSPKKPPAKDP 837
Cdd:PHA03247  2816 aalppaasPAGPLPPPTSAQPTAPPPPPGPPP 2847
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 670-840 2.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 670 APAGQPAPVSMVPPSPAMAASKAlgsdldSSLASLVGNLGISGTTTKKGDLQWNAGEkkltGGANWQPKVAPATWSAGVP 749
Cdd:PRK07764  614 RPAAPAAPAAPAAPAPAGAAAAP------AEASAAPAPGVAAPEHHPKHVAVPDASD----GGDGWPAKAGGAAPAAPPP 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 750 PSAPlQGAVPPTSSVPPVAGAPSVGQPGAGfgmpPAGTGMPMMPQQPVMFAQPmmrPPFGAAAVPGTQLSPSPTPASQSP 829
Cdd:PRK07764  684 APAP-AAPAAPAGAAPAQPAPAPAATPPAG----QADDPAAQPPQAAQGASAP---SPAADDPVPLPPEPDDPPDPAGAP 755

                         170
                  ....*....|.
gi 1776842870 830 KKPPAKDPLAD 840
Cdd:PRK07764  756 AQPPPPPAPAP 766
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
714-834 2.50e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.30  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 714 TTKKGDLQWNAGEKKLTGGANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPgagfgmppagtgmpmmp 793
Cdd:PRK14971  363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPP----------------- 425

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1776842870 794 qqpvmfaQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPA 834
Cdd:PRK14971  426 -------TVSVDPPAAVPVNPPSTAPQAVRPAQFKEEKKIP 459
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 737-839 2.70e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.24  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 737 PKVAPATWSAGVPPSAPLQGAVPPtsSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGT 816
Cdd:PRK14951  371 EAAAPAEKKTPARPEAAAPAAAPV--AQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALA 448

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1776842870 817 QLSP--------------SPTPASQSPKKPPAKDPLA 839
Cdd:PRK14951  449 PAPPaqaapetvaipvrvAPEPAVASAAPAPAAAPAA 485
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 665-835 3.10e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 665 LMPTMAPAGQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTTTKKGDLQWNAGEKKL-TGGANWQPKVAPAt 743
Cdd:pfam03154 166 ILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLiQQTPTLHPQRLPS- 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 744 wsagvpPSAPLQGAVPPTSsvPPVAGAPSVGQPGAGFGMPPAG----TGMPMMPQqPVMfAQPMMRPP-FGAAAVPGTQL 818
Cdd:pfam03154 245 ------PHPPLQPMTQPPP--PSQVSPQPLPQPSLHGQMPPMPhslqTGPSHMQH-PVP-PQPFPLTPqSSQSQVPPGPS 314

                         170
                  ....*....|....*..
gi 1776842870 819 SPSPTPASQSPKKPPAK 835
Cdd:pfam03154 315 PAAPGQSQQRIHTPPSQ 331
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 733-834 3.29e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.17  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 733 ANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM-----MPQQPVMFAQPMMRPP 807
Cdd:pfam09770 205 AQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilqrPQSPQPDPAQPSIQPQ 284

                          90       100
                  ....*....|....*....|....*..
gi 1776842870 808 FGAAAVPGTQLSPSPTPASQSPKKPPA 834
Cdd:pfam09770 285 AQQFHQQPPPVPVQPTQILQNPNRLSA 311
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 740-834 3.40e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.82  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 740 APATWSAGVPPSAPLQGAVPPTSSVPPVAGAP------SVGQPGAGfgmPPAGTGMPMMPQQPVMFAQPMMR-PPFGAAA 812
Cdd:PRK14959  379 SAPSGSAAEGPASGGAATIPTPGTQGPQGTAPaagmtpSSAAPATP---APSAAPSPRVPWDDAPPAPPRSGiPPRPAPR 455

                          90       100
                  ....*....|....*....|...
gi 1776842870 813 VPGTQLSP-SPTPASQSPKKPPA 834
Cdd:PRK14959  456 MPEASPVPgAPDSVASASDAPPT 478
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
737-841 3.47e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 737 PKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM---MPQQPVMFAQPmmRPPFGAAAV 813
Cdd:PRK12323  401 APPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAaapAAAARPAAAGP--RPVAAAAAA 478

                          90       100
                  ....*....|....*....|....*...
gi 1776842870 814 PGTQLSPSPTPASQSPKKPPAKDPLADL 841
Cdd:PRK12323  479 APARAAPAAAPAPADDDPPPWEELPPEF 506
PHA03247 PHA03247
large tegument protein UL36; Provisional
 667-837 3.61e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  667 PTMAPAGQPAPvSMVPPSPAMAASKALGSDLDSSL-------ASLVGNLGISGTTTKKGDLQWNAGEKKLTGGANWQPKV 739
Cdd:PHA03247  2614 PSPLPPDTHAP-DPPPPSPSPAANEPDPHPPPTVPpperprdDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV 2692

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  740 APATWSAGvPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPgtqls 819
Cdd:PHA03247  2693 GSLTSLAD-PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP----- 2766

                          170
                   ....*....|....*...
gi 1776842870  820 PSPTPASQSPKKPPAKDP 837
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLT 2784
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
 15-76 5.26e-03

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: 37.67  E-value: 5.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776842870  15 VVVFKALVTTHHLMVHGNERFI-QYLASRNTLFNLSNFLDKSGSHGYdmSTFIRRYSRYLNEK 76
Cdd:cd17007    51 VQCFKALITIHKVLQEGHPSALkEAIRNIEWLESLGRQSSGSGAKGY--GRLIKEYVRYLLDK 111
PHA03247 PHA03247
large tegument protein UL36; Provisional
 670-842 6.37e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 6.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  670 APAGQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGnlgisgtttkKGDLQWNAGekkltgganwQPKVAPATWSagvP 749
Cdd:PHA03247   305 APLALPAPPDPPPPAPAGDAEEEDDEDGAMEVVSPLP----------RPRQHYPLG----------FPKRRRPTWT---P 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  750 PSAP---LQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMmPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPT--- 823
Cdd:PHA03247   362 PSSLedlSAGRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTR-PAAPVPASVPTPAPTPVPASAPPPPATPLPSaep 440

                          170
                   ....*....|....*....
gi 1776842870  824 PASQSPKKPPAKDPLADLN 842
Cdd:PHA03247   441 GSDDGPAPPPERQPPAPAT 459
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 750-837 7.26e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 39.85  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 750 PSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPASQSP 829
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKK 440


                  ....*...
gi 1776842870 830 KKPPAKDP 837
Cdd:PRK07994  441 SEPAAASR 448
PHA03247 PHA03247
large tegument protein UL36; Provisional
 729-839 8.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 8.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870  729 LTGGANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPP----VAGAPSVGQPGAGFGMPPAGT----GMPMMPQQPVMFA 800
Cdd:PHA03247  2721 LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPArpptTAGPPAPAPPAAPAAGPPRRLtrpaVASLSESRESLPS 2800

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1776842870  801 QPMMRPPFGAAAVPGTQLSPSPTPASQSPkKPPAKDPLA 839
Cdd:PHA03247  2801 PWDPADPPAAVLAPAAALPPAASPAGPLP-PPTSAQPTA 2838
PHA03378 PHA03378
EBNA-3B; Provisional
 737-847 9.18e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842870 737 PKVAPATWSAGVPPSAPLQGAVPPTSSVP----PVAGAPSVGQPGA---GFGMPPAGT-GMPMMPQQPVMFAQPMMRPPF 808
Cdd:PHA03378  713 RAQRPAAATGRARPPAAAPGRARPPAAAPgrarPPAAAPGRARPPAaapGRARPPAAApGAPTPQPPPQAPPAPQQRPRG 792

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1776842870 809 GAAAVPGTQLSPspTPASQSPKKPPAKDPLADLNIKDFL 847
Cdd:PHA03378  793 APTPQPPPQAGP--TSMQLMPRAAPGQQGPTKQILRQLL 829
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH