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Conserved domains on  [gi|338753421|ref|NP_001229722|]
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clathrin coat assembly protein AP180 isoform b [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 ...
 21-282 1.15e-95

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


:

Pssm-ID: 400137  Cd Length: 272  Bit Score: 301.14  E-value: 1.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421   21 AVARAVCKATTHEvMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLAS 99
Cdd:pfam07651   1 DLEVAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  100 RNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMP 169
Cdd:pfam07651  80 ARRRISSLLRIS-SFSLSWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  170 ILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSE 249
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 338753421  250 FLKVAEQVGIDKG-DIPDLTQAPSSLMETLEQHL 282
Cdd:pfam07651 239 FYEVCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 697-867 6.68e-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: 50.32  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  697 PTMAPAGQPAPVSMVPP-SPAMAASKALGSDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWS 775
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPP 2843

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  776 AGVPPSAPLQGAV---------PPTSSVPPVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVM 828
Cdd:PHA03247 2844 GPPPPSLPLGGSVapggdvrrrPPSRSPAAKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQP 2923

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 338753421  829 FAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 867
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 ...
 21-282 1.15e-95

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 301.14  E-value: 1.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421   21 AVARAVCKATTHEvMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLAS 99
Cdd:pfam07651   1 DLEVAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  100 RNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMP 169
Cdd:pfam07651  80 ARRRISSLLRIS-SFSLSWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  170 ILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSE 249
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 338753421  250 FLKVAEQVGIDKG-DIPDLTQAPSSLMETLEQHL 282
Cdd:pfam07651 239 FYEVCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 22-138 1.73e-83

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: 262.74  E-value: 1.73e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  22 VARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRN 101
Cdd:cd16985    1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 338753421 102 TLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSY 138
Cdd:cd16985   81 SLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKAISY 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
20-145 1.28e-43

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 153.94  E-value: 1.28e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421    20 SAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFI-QYL 97
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTkNWRVVYKALILLHYLLRNGSPRVIlEAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 338753421    98 ASRNTLFNLSNFLDKsGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDF 145
Cdd:smart00273  81 RNRNRILNLSDFQDI-DSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PHA03247 PHA03247
large tegument protein UL36; Provisional
 697-867 6.68e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  697 PTMAPAGQPAPVSMVPP-SPAMAASKALGSDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWS 775
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPP 2843

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  776 AGVPPSAPLQGAV---------PPTSSVPPVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVM 828
Cdd:PHA03247 2844 GPPPPSLPLGGSVapggdvrrrPPSRSPAAKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQP 2923

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 338753421  829 FAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 867
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
 691-864 8.94e-04

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: 42.75  E-value: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  691 LGDLLMPTMAPAgQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTT--TKKGDLQWNAGEKKLTGGANWQPK 768
Cdd:TIGR01645 278 VGKCVTPPDALL-QPATVSAIPAAAAVAAAAATAKIMAAEAVAGAAVLGPRAQSpaTPSSSLPTDIGNKAVVSSAKKEAE 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  769 VAPAtwsagVPPSAPLQGAVPPTSSVPPVAgAPSVGQPGagfGMPPAGTGMPMMPqQPVMFAQPmmRPPFGAAAVPGTQL 848
Cdd:TIGR01645 357 EVPP-----LPQAAPAVVKPGPMEIPTPVP-PPGLAIPS---LVAPPGLVAPTEI-NPSFLASP--RKKMKREKLPVTFG 424

                         170
                  ....*....|....*.
gi 338753421  849 SPSPTPASQSPKKPPA 864
Cdd:TIGR01645 425 ALDDTLAWKEPSKEDQ 440
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 763-864 3.26e-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: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  763 ANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM-----MPQQPVMFAQPMMRPP 837
Cdd:pfam09770 205 AQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilqrPQSPQPDPAQPSIQPQ 284

                          90       100
                  ....*....|....*....|....*..
gi 338753421  838 FGAAAVPGTQLSPSPTPASQSPKKPPA 864
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 ...
 21-282 1.15e-95

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 301.14  E-value: 1.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421   21 AVARAVCKATTHEvMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLAS 99
Cdd:pfam07651   1 DLEVAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  100 RNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMP 169
Cdd:pfam07651  80 ARRRISSLLRIS-SFSLSWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  170 ILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSE 249
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 338753421  250 FLKVAEQVGIDKG-DIPDLTQAPSSLMETLEQHL 282
Cdd:pfam07651 239 FYEVCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
ANTH_N_AP180 cd16985
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of adaptor protein 180 (AP180) ...
 22-138 1.73e-83

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: 262.74  E-value: 1.73e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  22 VARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRN 101
Cdd:cd16985    1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 338753421 102 TLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSY 138
Cdd:cd16985   81 SLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKAISY 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
20-145 1.28e-43

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 153.94  E-value: 1.28e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421    20 SAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFI-QYL 97
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTkNWRVVYKALILLHYLLRNGSPRVIlEAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 338753421    98 ASRNTLFNLSNFLDKsGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDF 145
Cdd:smart00273  81 RNRNRILNLSDFQDI-DSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 22-138 1.83e-41

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: 147.42  E-value: 1.83e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  22 VARAVCKATTHEVMGPKKKHLDYLIQATNE--TNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLAS 99
Cdd:cd03564    1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNggGRADVAYIVHALAKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 338753421 100 RN-TLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSY 138
Cdd:cd03564   81 YSgHIFNLSNFKDDSSPEAWDLSAFIRRYARYLEERLECF 120
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 22-137 1.05e-34

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: 128.31  E-value: 1.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  22 VARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRN 101
Cdd:cd00197    1 FEKTVEKATSNENMGPDWPLIMEICDLINETNVGPKEAVDAIKKRINNKNPHVVLKALTLLEYCVKNCGERFHQEVASND 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 338753421 102 TLFNLSNFlDKSGSHGYDMSTFIRRYSRYLNEKAFS 137
Cdd:cd00197   81 FAVELLKF-DKSGLLGDDVSTNVREKAIELVQLWAS 115
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 24-138 6.31e-24

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: 97.25  E-value: 6.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  24 RAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGN-ERFIQYLASRNT 102
Cdd:cd16988    3 KLVKGATKIKLAPPKAKYLDPILLATYSSDASFGEIVRALSRRLRDNSWTVVFKSLIVLHLMIREGEtDDVLLYYLSRPD 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 338753421 103 LFNLSNFLDKSgSHGYDMSTFIRRYSRYLNEKAFSY 138
Cdd:cd16988   83 FLDLRKIRNGS-SAGSGQLQNIQRYAAYLKERVKEY 117
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 19-131 2.17e-19

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: 84.53  E-value: 2.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421   19 GSAVARAVCKATTHEVMGPKKKHLDYLIQATNETnVNIPQMADTLFERA--TNSSWVVVFKALVTTHHLMVHGNERFIQY 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNY-VEFPEIMKMLWKRLndKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 338753421   97 L-ASRNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYL 131
Cdd:pfam01417  80 LrENIYIIRTLTDFHY-IDENGKDQGINVRKKAKEI 114
ANTH_N_AP180_plant cd16987
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of plant Clathrin coat assembly ...
 25-134 8.85e-13

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: 65.72  E-value: 8.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  25 AVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATN-SSWVVVFKALVTTHHLMVHGNERFIQ----YLAS 99
Cdd:cd16987    4 AVVKATSHDDAPPDEKYVREILSLGSSSRAYASACVSALSRRLNRtRDWVVALKCLMLLHRLLRDGSPILEQelslAPSG 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 338753421 100 RNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEK 134
Cdd:cd16987   84 GRNPLNLSDFRDGSSSKSWDFSAFVRAYAAYLDER 118
ANTH_N_Sla2p_HIP1_like cd16986
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p/HIP1/HIP1R subfamily; ...
 25-135 5.15e-08

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: 52.00  E-value: 5.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  25 AVCKATTHEVMGPKKKHLDYLIQATNETNvNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFI---QYLasRN 101
Cdd:cd16986    4 AVNKATNKTDSPPKPKHVRTIIVKSWTHQ-KGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPELSllgGYL--DA 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 338753421 102 TLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKA 135
Cdd:cd16986   81 WLPELVRVKNTQQSLSEFYSQLIKKYVRYLELKV 114
ANTH_N_Sla2p cd17007
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of Sla2p and similar proteins; ...
 24-134 8.95e-07

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: 48.46  E-value: 8.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  24 RAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPqMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFI-QYLASRNT 102
Cdd:cd17007    3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKP-FWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALkEAIRNIEW 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 338753421 103 LFNLSNFLDKSGSHGYdmSTFIRRYSRYLNEK 134
Cdd:cd17007   82 LESLGRQSSGSGAKGY--GRLIKEYVRYLLDK 111
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 29-97 5.39e-06

Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is 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, contributing 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. 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: 340772  Cd Length: 117  Bit Score: 46.36  E-value: 5.39e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338753421  29 ATTHEVMGPKKKHLDYLIQATNETNvNIPQMADTLFER--ATNSSWVVVFKALVTTHHLMVHGNERFIQYL 97
Cdd:cd03571    8 ATSNEPWGPTGSQLAEIAQATFDYD-DYQRIMKVLWKRlnDKGKNWRHVYKALTLLEYLLKNGSERVVDEF 77
PHA03247 PHA03247
large tegument protein UL36; Provisional
 697-867 6.68e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  697 PTMAPAGQPAPVSMVPP-SPAMAASKALGSDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWS 775
Cdd:PHA03247 2771 PPAAPAAGPPRRLTRPAvASLSESRESLPSPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPP 2843

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  776 AGVPPSAPLQGAV---------PPTSSVPPVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVM 828
Cdd:PHA03247 2844 GPPPPSLPLGGSVapggdvrrrPPSRSPAAKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQP 2923

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 338753421  829 FAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 867
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
767-869 1.59e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.25  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 767 PKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPgt 846
Cdd:PRK12323 381 PVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAP-- 458

                         90       100
                 ....*....|....*....|...
gi 338753421 847 qlSPSPTPASQSPKKPPAKDPLA 869
Cdd:PRK12323 459 --AAAARPAAAGPRPVAAAAAAA 479
PHA03247 PHA03247
large tegument protein UL36; Provisional
 767-867 3.51e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  767 PKVAPATWSAGVP------------PSAPLQGAVPPTSSVPPVAGAPS-VGQPGAgfgmpPAGTGMPMMPQQPVMFAQPM 833
Cdd:PHA03247 2708 PEPAPHALVSATPlppgpaaarqasPALPAAPAPPAVPAGPATPGGPArPARPPT-----TAGPPAPAPPAAPAAGPPRR 2782

                          90       100       110
                  ....*....|....*....|....*....|....
gi 338753421  834 MRPPFGAAAVPGTQLSPSPTPASQSPKKPPAKDP 867
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDPADPPAAVLAPAA 2816
PHA03378 PHA03378
EBNA-3B; Provisional
 767-867 4.35e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 767 PKVAPATwsAGVPPSAPLQG---AVPPTSSVPPvAGAPSVGQPGA---GFGMPPAGTGMPMMP-------QQPVMFAQPM 833
Cdd:PHA03378 687 IQWAPGT--MQPPPRAPTPMrppAAPPGRAQRP-AAATGRARPPAaapGRARPPAAAPGRARPpaaapgrARPPAAAPGR 763

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 338753421 834 MRPPFGAAAVPGTQLSPSPTPAS-QSPKKPPAKDP 867
Cdd:PHA03378 764 ARPPAAAPGAPTPQPPPQAPPAPqQRPRGAPTPQP 798
PHA03247 PHA03247
large tegument protein UL36; Provisional
 649-863 8.60e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 8.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  649 APSPSPVTPAQNNLLQPnfEAAFGTTPSTSSSSSFDPSVFDGLGDLLMPTMAPAGQPAPVSMVPPSPAMAASKALGSDLD 728
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRP--AVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  729 SSLaSLVGNLGISGTTTKKGDLQ----WNAGEKKLTGGANWQPKVAPATWSAGVPPsapLQGAVPPTSSVPPVAGAPSVG 804
Cdd:PHA03247 2848 PSL-PLGGSVAPGGDVRRRPPSRspaaKPAAPARPPVRRLARPAVSRSTESFALPP---DQPERPPQPQAPPPPQPQPQP 2923

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  805 QPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRP------PFGAAAVPGT-----QLSPSPTPASQSPKKPP 863
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsgavpqPWLGALVPGRvavprFRVPQPAPSREAPASST 2993
PHA03247 PHA03247
large tegument protein UL36; Provisional
 769-867 8.82e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 8.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  769 VAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAgfgmPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAV----- 843
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP----PRRLTRPAVASLSESRESLPSPWDPADPPAAvlapa 2815

                          90       100       110
                  ....*....|....*....|....*....|..
gi 338753421  844 --------PGTQLSPSPTPASQSPKKPPAKDP 867
Cdd:PHA03247 2816 aalppaasPAGPLPPPTSAQPTAPPPPPGPPP 2847
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
 691-864 8.94e-04

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: 42.75  E-value: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  691 LGDLLMPTMAPAgQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTT--TKKGDLQWNAGEKKLTGGANWQPK 768
Cdd:TIGR01645 278 VGKCVTPPDALL-QPATVSAIPAAAAVAAAAATAKIMAAEAVAGAAVLGPRAQSpaTPSSSLPTDIGNKAVVSSAKKEAE 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  769 VAPAtwsagVPPSAPLQGAVPPTSSVPPVAgAPSVGQPGagfGMPPAGTGMPMMPqQPVMFAQPmmRPPFGAAAVPGTQL 848
Cdd:TIGR01645 357 EVPP-----LPQAAPAVVKPGPMEIPTPVP-PPGLAIPS---LVAPPGLVAPTEI-NPSFLASP--RKKMKREKLPVTFG 424

                         170
                  ....*....|....*.
gi 338753421  849 SPSPTPASQSPKKPPA 864
Cdd:TIGR01645 425 ALDDTLAWKEPSKEDQ 440
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 700-870 1.33e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 700 APAGQPAPVSMVPPSPAMAASKAlgsdldSSLASLVGNLGISGTTTKKGDLQWNAGEkkltGGANWQPKVAPATWSAGVP 779
Cdd:PRK07764 614 RPAAPAAPAAPAAPAPAGAAAAP------AEASAAPAPGVAAPEHHPKHVAVPDASD----GGDGWPAKAGGAAPAAPPP 683

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 780 PSAPlQGAVPPTSSVPPVAGAPSVGQPGAGfgmpPAGTGMPMMPQQPVMFAQPmmrPPFGAAAVPGTQLSPSPTPASQSP 859
Cdd:PRK07764 684 APAP-AAPAAPAGAAPAQPAPAPAATPPAG----QADDPAAQPPQAAQGASAP---SPAADDPVPLPPEPDDPPDPAGAP 755

                        170
                 ....*....|.
gi 338753421 860 KKPPAKDPLAD 870
Cdd:PRK07764 756 AQPPPPPAPAP 766
PHA03247 PHA03247
large tegument protein UL36; Provisional
 697-867 2.14e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  697 PTMAPAGQPAPvSMVPPSPAMAASKALGSDLDSSL-------ASLVGNLGISGTTTKKGDLQWNAGEKKLTGGANWQPKV 769
Cdd:PHA03247 2614 PSPLPPDTHAP-DPPPPSPSPAANEPDPHPPPTVPpperprdDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTV 2692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  770 APATWSAGvPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPgtqls 849
Cdd:PHA03247 2693 GSLTSLAD-PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP----- 2766

                         170
                  ....*....|....*...
gi 338753421  850 PSPTPASQSPKKPPAKDP 867
Cdd:PHA03247 2767 PAPAPPAAPAAGPPRRLT 2784
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 767-869 2.46e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 767 PKVAPATWSAGVPPSAPLQGAVPPtsSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGT 846
Cdd:PRK14951 371 EAAAPAEKKTPARPEAAAPAAAPV--AQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALA 448

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 338753421 847 QLSP--------------SPTPASQSPKKPPAKDPLA 869
Cdd:PRK14951 449 PAPPaqaapetvaipvrvAPEPAVASAAPAPAAAPAA 485
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
744-864 2.70e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.30  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 744 TTKKGDLQWNAGEKKLTGGANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPgagfgmppagtgmpmmp 823
Cdd:PRK14971 363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPP----------------- 425

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 338753421 824 qqpvmfaQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPA 864
Cdd:PRK14971 426 -------TVSVDPPAAVPVNPPSTAPQAVRPAQFKEEKKIP 459
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 770-864 2.70e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.20  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 770 APATWSAGVPPSAPLQGAVPPTSSVPPVAGAP------SVGQPGAGfgmPPAGTGMPMMPQQPVMFAQPMMR-PPFGAAA 842
Cdd:PRK14959 379 SAPSGSAAEGPASGGAATIPTPGTQGPQGTAPaagmtpSSAAPATP---APSAAPSPRVPWDDAPPAPPRSGiPPRPAPR 455

                         90       100
                 ....*....|....*....|...
gi 338753421 843 VPGTQLSP-SPTPASQSPKKPPA 864
Cdd:PRK14959 456 MPEASPVPgAPDSVASASDAPPT 478
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
767-871 2.83e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 767 PKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM---MPQQPVMFAQPmmRPPFGAAAV 843
Cdd:PRK12323 401 APPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAaapAAAARPAAAGP--RPVAAAAAA 478

                         90       100
                 ....*....|....*....|....*...
gi 338753421 844 PGTQLSPSPTPASQSPKKPPAKDPLADL 871
Cdd:PRK12323 479 APARAAPAAAPAPADDDPPPWEELPPEF 506
PHA03247 PHA03247
large tegument protein UL36; Provisional
 700-872 3.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  700 APAGQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGnlgisgtttkKGDLQWNAGekkltgganwQPKVAPATWSagvP 779
Cdd:PHA03247  305 APLALPAPPDPPPPAPAGDAEEEDDEDGAMEVVSPLP----------RPRQHYPLG----------FPKRRRPTWT---P 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  780 PSAP---LQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMmPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPT--- 853
Cdd:PHA03247  362 PSSLedlSAGRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTR-PAAPVPASVPTPAPTPVPASAPPPPATPLPSaep 440

                         170
                  ....*....|....*....
gi 338753421  854 PASQSPKKPPAKDPLADLN 872
Cdd:PHA03247  441 GSDDGPAPPPERQPPAPAT 459
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 763-864 3.26e-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: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  763 ANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM-----MPQQPVMFAQPMMRPP 837
Cdd:pfam09770 205 AQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilqrPQSPQPDPAQPSIQPQ 284

                          90       100
                  ....*....|....*....|....*..
gi 338753421  838 FGAAAVPGTQLSPSPTPASQSPKKPPA 864
Cdd:pfam09770 285 AQQFHQQPPPVPVQPTQILQNPNRLSA 311
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 756-864 3.69e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 756 EKKLTGGANWQPKVAPATWSAGVPPSA---PLQGAVPPTSSVPPVAGAPSVGQPGA-----GFGMPPAGTGMPMMPQQPV 827
Cdd:PRK07764 382 ERRLGVAGGAGAPAAAAPSAAAAAPAAapaPAAAAPAAAAAPAPAAAPQPAPAPAPapappSPAGNAPAGGAPSPPPAAA 461

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 338753421 828 MFAQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPA 864
Cdd:PRK07764 462 PSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPA 498
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 45-133 4.83e-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: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  45 LIQATNETNVNIPQMADTL------FERATNSSWVVVFKALVTTHHLMVHGNERFIQYlaSRNTLFNLSN-----FLDks 113
Cdd:cd16992   20 LMQEIAQGTYNYQQFNEIMpmiykrFTEKAGSEWRQIYKALQLLEYLIKNGSERVVDD--ARGHLTLIKMlrsfhYID-- 95

                         90       100
                 ....*....|....*....|
gi 338753421 114 gSHGYDMSTFIRRYSRYLNE 133
Cdd:cd16992   96 -DKGKDQGINVRNRAKELIE 114
PHA03247 PHA03247
large tegument protein UL36; Provisional
 759-869 5.42e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421  759 LTGGANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPP----VAGAPSVGQPGAGFGMPPAGT----GMPMMPQQPVMFA 830
Cdd:PHA03247 2721 LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPArpptTAGPPAPAPPAAPAAGPPRRLtrpaVASLSESRESLPS 2800

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 338753421  831 QPMMRPPFGAAAVPGTQLSPSPTPASQSPkKPPAKDPLA 869
Cdd:PHA03247 2801 PWDPADPPAAVLAPAAALPPAASPAGPLP-PPTSAQPTA 2838
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 767-875 6.09e-03

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 39.46  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 767 PKVAPATWSAGVPPSAPLQGAVPPTS-SVPPVAGAPSVGQPGAGfgMPPAGTGMPMMPQQPVMFAQPMMRPPFGAaavpg 845
Cdd:PHA02682  96 PACAPAAPAPAVTCPAPAPACPPATApTCPPPAVCPAPARPAPA--CPPSTRQCPPAPPLPTPKPAPAAKPIFLH----- 168

                         90       100       110
                 ....*....|....*....|....*....|..
gi 338753421 846 TQLSPSPTPASQSP--KKPPAKDPLADLNIKD 875
Cdd:PHA02682 169 NQLPPPDYPAASCPtiETAPAASPVLEPRIPD 200
PHA03378 PHA03378
EBNA-3B; Provisional
 767-877 6.10e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 767 PKVAPATWSAGVPPSAPLQGAVPPTSSVP----PVAGAPSVGQPGA---GFGMPPAGT-GMPMMPQQPVMFAQPMMRPPF 838
Cdd:PHA03378 713 RAQRPAAATGRARPPAAAPGRARPPAAAPgrarPPAAAPGRARPPAaapGRARPPAAApGAPTPQPPPQAPPAPQQRPRG 792

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 338753421 839 GAAAVPGTQLSPspTPASQSPKKPPAKDPLADLNIKDFL 877
Cdd:PHA03378 793 APTPQPPPQAGP--TSMQLMPRAAPGQQGPTKQILRQLL 829
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 780-867 7.19e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 39.85  E-value: 7.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 780 PSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPASQSP 859
Cdd:PRK07994 361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKK 440


                 ....*...
gi 338753421 860 KKPPAKDP 867
Cdd:PRK07994 441 SEPAAASR 448
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
697-864 9.57e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.47  E-value: 9.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 697 PTMAPAGQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTTTKKGdlqwnagekklTGGANWQPKVAPATWSA 776
Cdd:PRK12323 392 PAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARG-----------PGGAPAPAPAPAAAPAA 460

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753421 777 GVPPSAPLQGAVPPTSSVPPVAGAPsVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPAS 856
Cdd:PRK12323 461 AARPAAAGPRPVAAAAAAAPARAAP-AAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFE 539


                 ....*...
gi 338753421 857 QSPKKPPA 864
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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