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Conserved domains on  [gi|375493604|ref|NP_001243646|]
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clathrin coat assembly protein AP180 isoform d [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; ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; similar to phosphatidylinositol-binding clathrin assembly protein (PICALM) and clathrin coat assembly protein AP180 (SNAP91); ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; similar to phosphatidylinositol-binding clathrin assembly protein (PICALM) and clathrin coat assembly protein AP180 (SNAP91)

CATH:  1.20.58.150|1.25.40.90
Gene Ontology:  GO:0030136|GO:0005545|GO:0030276|GO:0048268
PubMed:  12740367|12742163|22748146

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 ...
 10-247 1.73e-84

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: 270.32  E-value: 1.73e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604   10 LIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDkSGSHGYDMSTF 88
Cdd:pfam07651  24 EILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRARRRISSLLRIS-SFSLSWDYGAF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604   89 IRRYSRYLNEKAFSYRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMPILQGQIDALLEFDVHPNELTNGVI 158
Cdd:pfam07651 103 IRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  159 NAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKG-DIPDLTQAPS 237
Cdd:pfam07651 183 IAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKEFYEVCKNLGYFRSlEIPKLPHIPP 262

                         250
                  ....*....|
gi 375493604  238 SLMETLEQHL 247
Cdd:pfam07651 263 NLLEALEEYL 272
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 636-806 7.26e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  636 PTMAPAGQPAPVSMVPP-SPAMAASKALGSDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWS 714
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPP 2843

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  715 AGVPPSAPLQGAV---------PPTSSVPPVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVM 767
Cdd:PHA03247 2844 GPPPPSLPLGGSVapggdvrrrPPSRSPAAKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQP 2923

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 375493604  768 FAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 806
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 ...
 10-247 1.73e-84

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: 270.32  E-value: 1.73e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604   10 LIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDkSGSHGYDMSTF 88
Cdd:pfam07651  24 EILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRARRRISSLLRIS-SFSLSWDYGAF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604   89 IRRYSRYLNEKAFSYRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMPILQGQIDALLEFDVHPNELTNGVI 158
Cdd:pfam07651 103 IRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  159 NAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKG-DIPDLTQAPS 237
Cdd:pfam07651 183 IAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKEFYEVCKNLGYFRSlEIPKLPHIPP 262

                         250
                  ....*....|
gi 375493604  238 SLMETLEQHL 247
Cdd:pfam07651 263 NLLEALEEYL 272
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 10-103 6.24e-63

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: 206.89  E-value: 6.24e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  10 LIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFI 89
Cdd:cd16985   24 LVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRNSLFNLSNFLDKSGSQGYDMSTFI 103

                         90
                 ....*....|....
gi 375493604  90 RRYSRYLNEKAFSY 103
Cdd:cd16985  104 RRYAKYLNEKAISY 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
10-110 1.29e-30

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 116.96  E-value: 1.29e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604    10 LIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFI-QYLASRNTLFNLSNFLDKsGSHGYDMST 87
Cdd:smart00273  26 IIQGTHNEKSSFAEIMAVLWRRLNDTkNWRVVYKALILLHYLLRNGSPRVIlEALRNRNRILNLSDFQDI-DSRGKDQGA 104

                           90       100
                   ....*....|....*....|...
gi 375493604    88 FIRRYSRYLNEKAFSYRQMAFDF 110
Cdd:smart00273 105 NIRTYAKYLLERLEDDRRLKEER 127
PHA03247 PHA03247
large tegument protein UL36; Provisional
 636-806 7.26e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  636 PTMAPAGQPAPVSMVPP-SPAMAASKALGSDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWS 714
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPP 2843

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  715 AGVPPSAPLQGAV---------PPTSSVPPVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVM 767
Cdd:PHA03247 2844 GPPPPSLPLGGSVapggdvrrrPPSRSPAAKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQP 2923

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 375493604  768 FAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 806
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 702-803 3.34e-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: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  702 ANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM-----MPQQPVMFAQPMMRPP 776
Cdd:pfam09770 205 AQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilqrPQSPQPDPAQPSIQPQ 284

                          90       100
                  ....*....|....*....|....*..
gi 375493604  777 FGAAAVPGTQLSPSPTPASQSPKKPPA 803
Cdd:pfam09770 285 AQQFHQQPPPVPVQPTQILQNPNRLSA 311
 
Name Accession Description Interval E-value
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 10-247 1.73e-84

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: 270.32  E-value: 1.73e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604   10 LIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDkSGSHGYDMSTF 88
Cdd:pfam07651  24 EILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLRARRRISSLLRIS-SFSLSWDYGAF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604   89 IRRYSRYLNEKAFSYRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMPILQGQIDALLEFDVHPNELTNGVI 158
Cdd:pfam07651 103 IRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIPKLQKLLFRLLKCRPTGNALSNECI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  159 NAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKG-DIPDLTQAPS 237
Cdd:pfam07651 183 IAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKEFYEVCKNLGYFRSlEIPKLPHIPP 262

                         250
                  ....*....|
gi 375493604  238 SLMETLEQHL 247
Cdd:pfam07651 263 NLLEALEEYL 272
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 10-103 6.24e-63

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: 206.89  E-value: 6.24e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  10 LIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFI 89
Cdd:cd16985   24 LVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRNSLFNLSNFLDKSGSQGYDMSTFI 103

                         90
                 ....*....|....
gi 375493604  90 RRYSRYLNEKAFSY 103
Cdd:cd16985  104 RRYAKYLNEKAISY 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
10-110 1.29e-30

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 116.96  E-value: 1.29e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604    10 LIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFI-QYLASRNTLFNLSNFLDKsGSHGYDMST 87
Cdd:smart00273  26 IIQGTHNEKSSFAEIMAVLWRRLNDTkNWRVVYKALILLHYLLRNGSPRVIlEALRNRNRILNLSDFQDI-DSRGKDQGA 104

                           90       100
                   ....*....|....*....|...
gi 375493604    88 FIRRYSRYLNEKAFSYRQMAFDF 110
Cdd:smart00273 105 NIRTYAKYLLERLEDDRRLKEER 127
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 10-103 1.46e-29

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: 113.52  E-value: 1.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  10 LIQATNE--TNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRN-TLFNLSNFLDKSGSHGYDMS 86
Cdd:cd03564   24 LLLATSNggGRADVAYIVHALAKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYSgHIFNLSNFKDDSSPEAWDLS 103

                         90
                 ....*....|....*..
gi 375493604  87 TFIRRYSRYLNEKAFSY 103
Cdd:cd03564  104 AFIRRYARYLEERLECF 120
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 10-102 4.28e-25

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: 100.58  E-value: 4.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  10 LIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFlDKSGSHGYDMSTFI 89
Cdd:cd00197   24 ICDLINETNVGPKEAVDAIKKRINNKNPHVVLKALTLLEYCVKNCGERFHQEVASNDFAVELLKF-DKSGLLGDDVSTNV 102

                         90
                 ....*....|...
gi 375493604  90 RRYSRYLNEKAFS 102
Cdd:cd00197  103 REKAIELVQLWAS 115
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 10-103 5.95e-17

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: 77.22  E-value: 5.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  10 LIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGN-ERFIQYLASRNTLFNLSNFLDKSgSHGYDMSTF 88
Cdd:cd16988   24 ILLATYSSDASFGEIVRALSRRLRDNSWTVVFKSLIVLHLMIREGEtDDVLLYYLSRPDFLDLRKIRNGS-SAGSGQLQN 102

                         90
                 ....*....|....*
gi 375493604  89 IRRYSRYLNEKAFSY 103
Cdd:cd16988  103 IQRYAAYLKERVKEY 117
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 8-96 7.61e-12

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: 62.96  E-value: 7.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604    8 NNLIQATNETnVNIPQMADTLFERA--TNSSWVVVFKALVTTHHLMVHGNERFIQYL-ASRNTLFNLSNFLDkSGSHGYD 84
Cdd:pfam01417  25 DEIARLTYNY-VEFPEIMKMLWKRLndKGKNWRHIYKALTLLEYLLKNGSERVVDDLrENIYIIRTLTDFHY-IDENGKD 102

                          90
                  ....*....|..
gi 375493604   85 MSTFIRRYSRYL 96
Cdd:pfam01417 103 QGINVRKKAKEI 114
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 36-99 8.24e-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: 8.24e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375493604  36 SWVVVFKALVTTHHLMVHGNERFIQ----YLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEK 99
Cdd:cd16987   51 DWVVALKCLMLLHRLLRDGSPILEQelslAPSGGRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDER 118
PHA03247 PHA03247
large tegument protein UL36; Provisional
 636-806 7.26e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.94  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  636 PTMAPAGQPAPVSMVPP-SPAMAASKALGSDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWS 714
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPP 2843

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  715 AGVPPSAPLQGAV---------PPTSSVPPVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVM 767
Cdd:PHA03247 2844 GPPPPSLPLGGSVapggdvrrrPPSRSPAAKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQP 2923

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 375493604  768 FAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 806
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
706-808 1.48e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.25  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 706 PKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPgt 785
Cdd:PRK12323 381 PVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAP-- 458

                         90       100
                 ....*....|....*....|...
gi 375493604 786 qlSPSPTPASQSPKKPPAKDPLA 808
Cdd:PRK12323 459 --AAAARPAAAGPRPVAAAAAAA 479
PHA03247 PHA03247
large tegument protein UL36; Provisional
 706-806 3.77e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  706 PKVAPATWSAGVP------------PSAPLQGAVPPTSSVPPVAGAPS-VGQPGAgfgmpPAGTGMPMMPQQPVMFAQPM 772
Cdd:PHA03247 2708 PEPAPHALVSATPlppgpaaarqasPALPAAPAPPAVPAGPATPGGPArPARPPT-----TAGPPAPAPPAAPAAGPPRR 2782

                          90       100       110
                  ....*....|....*....|....*....|....
gi 375493604  773 MRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 806
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816
PHA03378 PHA03378
EBNA-3B; Provisional
 706-806 5.73e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 706 PKVAPATwsAGVPPSAPLQG---AVPPTSSVPPvAGAPSVGQPGA---GFGMPPAGTGMPMMP-------QQPVMFAQPM 772
Cdd:PHA03378 687 IQWAPGT--MQPPPRAPTPMrppAAPPGRAQRP-AAATGRARPPAaapGRARPPAAAPGRARPpaaapgrARPPAAAPGR 763

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 375493604 773 MRPPFGAAAVPGTQLSPSPTPAS-QSPKKPPAKDP 806
Cdd:PHA03378 764 ARPPAAAPGAPTPQPPPQAPPAPqQRPRGAPTPQP 798
PHA03247 PHA03247
large tegument protein UL36; Provisional
 588-802 9.31e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 9.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  588 APSPSPVTPAQNNLLQPnfEAAFGTTPSTSSSSSFDPSVFDGLGDLLMPTMAPAGQPAPVSMVPPSPAMAASKALGSDLD 667
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRP--AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  668 SSLaSLVGNLGISGTTTKKGDLQ----WNAGEKKLTGGANWQPKVAPATWSAGVPPsapLQGAVPPTSSVPPVAGAPSVG 743
Cdd:PHA03247 2848 PSL-PLGGSVAPGGDVRRRPPSRspaaKPAAPARPPVRRLARPAVSRSTESFALPP---DQPERPPQPQAPPPPQPQPQP 2923

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  744 QPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRP------PFGAAAVPGT-----QLSPSPTPASQSPKKPP 802
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsgavpqPWLGALVPGRvavprFRVPQPAPSREAPASST 2993
PHA03247 PHA03247
large tegument protein UL36; Provisional
 708-806 9.80e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 9.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  708 VAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAgfgmPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAV----- 782
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP----PRRLTRPAVASLSESRESLPSPWDPADPPAAvlapa 2815

                          90       100       110
                  ....*....|....*....|....*....|..
gi 375493604  783 --------PGTQLSPSPTPASQSPKKPPAKDP 806
Cdd:PHA03247 2816 aalppaasPAGPLPPPTSAQPTAPPPPPGPPP 2847
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 639-809 1.24e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 639 APAGQPAPVSMVPPSPAMAASKAlgsdldSSLASLVGNLGISGTTTKKGDLQWNAGEkkltGGANWQPKVAPATWSAGVP 718
Cdd:PRK07764 614 RPAAPAAPAAPAAPAPAGAAAAP------AEASAAPAPGVAAPEHHPKHVAVPDASD----GGDGWPAKAGGAAPAAPPP 683

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 719 PSAPlQGAVPPTSSVPPVAGAPSVGQPGAGfgmpPAGTGMPMMPQQPVMFAQPmmrPPFGAAAVPGTQLSPSPTPASQSP 798
Cdd:PRK07764 684 APAP-AAPAAPAGAAPAQPAPAPAATPPAG----QADDPAAQPPQAAQGASAP---SPAADDPVPLPPEPDDPPDPAGAP 755

                        170
                 ....*....|.
gi 375493604 799 KKPPAKDPLAD 809
Cdd:PRK07764 756 AQPPPPPAPAP 766
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
 21-100 1.42e-03

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; Members of the Sla2p/HIP1/HIP1R subfamily share a common domain architecture, containing an N-terminal ANTH, a central clathrin-binding colied-coil, and a C-terminal actin-binding talin-like (also called I/LWEQ) domains. HIP1 was identified in 1997 as an interactor of huntingtin; when mutated, it is involved in the neurodegenerative disorder Huntington's disease. Both HIP1 and HIP1R promote clathrin assembly in vitro. Yeast Sla2p, is a regulator of membrane cytoskeleton assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. While the ANTH domain of Sla2p preferentially binds PtdIns(4,5)P2, which is considered to be an interaction hub in the clathrin interactome, mammalian HIP1 and HIP1R were found to preferentially bind PtdIns(3,4)P2 and PtdIns(3,5)P2, respectively. This model describes the N-terminal region of ANTH domains of the Sla2p/HIP1/HIP1R subfamily.


Pssm-ID: 340783  Cd Length: 117  Bit Score: 39.28  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  21 IPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFI---QYLasRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLN 97
Cdd:cd16986   34 GPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPELSllgGYL--DAWLPELVRVKNTQQSLSEFYSQLIKKYVRYLE 111


                 ...
gi 375493604  98 EKA 100
Cdd:cd16986  112 LKV 114
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 706-808 2.19e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 706 PKVAPATWSAGVPPSAPLQGAVPPtsSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGT 785
Cdd:PRK14951 371 EAAAPAEKKTPARPEAAAPAAAPV--AQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALA 448

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 375493604 786 QLSP--------------SPTPASQSPKKPPAKDPLA 808
Cdd:PRK14951 449 PAPPaqaapetvaipvrvAPEPAVASAAPAPAAAPAA 485
PHA03247 PHA03247
large tegument protein UL36; Provisional
 636-806 2.22e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  636 PTMAPAGQPAPvSMVPPSPAMAASKALGSDLDSSL-------ASLVGNLGISGTTTKKGDLQWNAGEKKLTGGANWQPKV 708
Cdd:PHA03247 2614 PSPLPPDTHAP-DPPPPSPSPAANEPDPHPPPTVPpperprdDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV 2692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  709 APATWSAGvPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPgtqls 788
Cdd:PHA03247 2693 GSLTSLAD-PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP----- 2766

                         170
                  ....*....|....*...
gi 375493604  789 PSPTPASQSPKKPPAKDP 806
Cdd:PHA03247 2767 PAPAPPAAPAAGPPRRLT 2784
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 714-803 2.58e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.20  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 714 SAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGfgmPPAGTGMPMMPQQPVMFAQPMMR-PPFGAAAVPGTQLSP-SP 791
Cdd:PRK14959 390 ASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATP---APSAAPSPRVPWDDAPPAPPRSGiPPRPAPRMPEASPVPgAP 466

                         90
                 ....*....|..
gi 375493604 792 TPASQSPKKPPA 803
Cdd:PRK14959 467 DSVASASDAPPT 478
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
706-810 2.66e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 706 PKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM---MPQQPVMFAQPmmRPPFGAAAV 782
Cdd:PRK12323 401 APPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAaapAAAARPAAAGP--RPVAAAAAA 478

                         90       100
                 ....*....|....*....|....*...
gi 375493604 783 PGTQLSPSPTPASQSPKKPPAKDPLADL 810
Cdd:PRK12323 479 APARAAPAAAPAPADDDPPPWEELPPEF 506
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
683-803 2.67e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.30  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 683 TTKKGDLQWNAGEKKLTGGANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPgagfgmppagtgmpmmp 762
Cdd:PRK14971 363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPP----------------- 425

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 375493604 763 qqpvmfaQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPA 803
Cdd:PRK14971 426 -------TVSVDPPAAVPVNPPSTAPQAVRPAQFKEEKKIP 459
PHA03247 PHA03247
large tegument protein UL36; Provisional
 639-811 3.07e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  639 APAGQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGnlgisgtttkKGDLQWNAGekkltgganwQPKVAPATWSagvP 718
Cdd:PHA03247  305 APLALPAPPDPPPPAPAGDAEEEDDEDGAMEVVSPLP----------RPRQHYPLG----------FPKRRRPTWT---P 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  719 PSAP---LQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMmPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPT--- 792
Cdd:PHA03247  362 PSSLedlSAGRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTR-PAAPVPASVPTPAPTPVPASAPPPPATPLPSaep 440

                         170
                  ....*....|....*....
gi 375493604  793 PASQSPKKPPAKDPLADLN 811
Cdd:PHA03247  441 GSDDGPAPPPERQPPAPAT 459
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 702-803 3.34e-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: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  702 ANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM-----MPQQPVMFAQPMMRPP 776
Cdd:pfam09770 205 AQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilqrPQSPQPDPAQPSIQPQ 284

                          90       100
                  ....*....|....*....|....*..
gi 375493604  777 FGAAAVPGTQLSPSPTPASQSPKKPPA 803
Cdd:pfam09770 285 AQQFHQQPPPVPVQPTQILQNPNRLSA 311
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 10-98 4.47e-03

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-3 (Ent3 or Ent3p), and similar proteins. Ent3 is an adaptor proteins at the Trans-Golgi Network (TGN); it cooperates with yeast SNARE Vti1p to regulate transport from the TGN to the prevacuolar endosome. Ent3 facilitates the interaction between Gga2p with both the endosomal syntaxin Pep12p and clathrin in the GGA-dependent transport to the late endosome. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, 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. Similar to mammalian epsinR, The ENTH domain of Ent3 binds to the yeast SNARE Vti1p; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. ENTH and ANTH (E/ANTH)-containing 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: 340789  Cd Length: 121  Bit Score: 37.82  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  10 LIQATNETNVNIPQMADTL------FERATNSSWVVVFKALVTTHHLMVHGNERFIQYlaSRNTLFNLSN-----FLDks 78
Cdd:cd16992   20 LMQEIAQGTYNYQQFNEIMpmiykrFTEKAGSEWRQIYKALQLLEYLIKNGSERVVDD--ARGHLTLIKMlrsfhYID-- 95

                         90       100
                 ....*....|....*....|
gi 375493604  79 gSHGYDMSTFIRRYSRYLNE 98
Cdd:cd16992   96 -DKGKDQGINVRNRAKELIE 114
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
 38-99 5.06e-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: 5.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 375493604  38 VVVFKALVTTHHLMVHGNERFI-QYLASRNTLFNLSNFLDKSGSHGYdmSTFIRRYSRYLNEK 99
Cdd:cd17007   51 VQCFKALITIHKVLQEGHPSALkEAIRNIEWLESLGRQSSGSGAKGY--GRLIKEYVRYLLDK 111
PHA03247 PHA03247
large tegument protein UL36; Provisional
 698-808 5.73e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604  698 LTGGANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPP----VAGAPSVGQPGAGFGMPPAGT----GMPMMPQQPVMFA 769
Cdd:PHA03247 2721 LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPArpptTAGPPAPAPPAAPAAGPPRRLtrpaVASLSESRESLPS 2800

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 375493604  770 QPMMRPPFGAAAVPGTQLSPSPTPASQSPkKPPAKDPLA 808
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAALPPAASPAGPLP-PPTSAQPTA 2838
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 706-814 6.23e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.46  E-value: 6.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 706 PKVAPATWSAGVPPSAPLQGAVPPTS-SVPPVAGAPSVGQPGAGfgMPPAGTGMPMMPQQPVMFAQPMMRPPFGAaavpg 784
Cdd:PHA02682  96 PACAPAAPAPAVTCPAPAPACPPATApTCPPPAVCPAPARPAPA--CPPSTRQCPPAPPLPTPKPAPAAKPIFLH----- 168

                         90       100       110
                 ....*....|....*....|....*....|..
gi 375493604 785 TQLSPSPTPASQSP--KKPPAKDPLADLNIKD 814
Cdd:PHA02682 169 NQLPPPDYPAASCPtiETAPAASPVLEPRIPD 200
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 719-806 6.48e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 39.85  E-value: 6.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 719 PSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPASQSP 798
Cdd:PRK07994 361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKK 440


                 ....*...
gi 375493604 799 KKPPAKDP 806
Cdd:PRK07994 441 SEPAAASR 448
PHA03378 PHA03378
EBNA-3B; Provisional
 706-816 7.41e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.05  E-value: 7.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 706 PKVAPATWSAGVPPSAPLQGAVPPTSSVP----PVAGAPSVGQPGA---GFGMPPAGT-GMPMMPQQPVMFAQPMMRPPF 777
Cdd:PHA03378 713 RAQRPAAATGRARPPAAAPGRARPPAAAPgrarPPAAAPGRARPPAaapGRARPPAAApGAPTPQPPPQAPPAPQQRPRG 792

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 375493604 778 GAAAVPGTQLSPspTPASQSPKKPPAKDPLADLNIKDFL 816
Cdd:PHA03378 793 APTPQPPPQAGP--TSMQLMPRAAPGQQGPTKQILRQLL 829
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
636-803 8.85e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.47  E-value: 8.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 636 PTMAPAGQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTTTKKGdlqwnagekklTGGANWQPKVAPATWSA 715
Cdd:PRK12323 392 PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARG-----------PGGAPAPAPAPAAAPAA 460

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375493604 716 GVPPSAPLQGAVPPTSSVPPVAGAPsVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPAS 795
Cdd:PRK12323 461 AARPAAAGPRPVAAAAAAAPARAAP-AAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFE 539


                 ....*...
gi 375493604 796 QSPKKPPA 803
Cdd:PRK12323 540 TLAPAPAA 547
 
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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