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Conserved domains on  [gi|1776842908|ref|NP_001363642|]
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clathrin coat assembly protein AP180 isoform p [Homo sapiens]

Protein Classification

ANTH domain-containing protein( domain architecture ID 10541692)

ANTH (AP180 N-Terminal Homology) domain-containing protein may act as clathrin coat assembly protein; similar to Homo sapiens phosphatidylinositol-binding clathrin assembly protein and clathrin coat assembly protein AP180

CATH:  1.20.58.150|1.25.40.90
Gene Ontology:  GO:0030276|GO:0048268|GO:0072583
PubMed:  12740367|12742163|22748146|14657269
SCOP:  4000571|4000581

Graphical summary

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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 1.08e-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: 1.08e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  21 AVARAVCKATTHEvMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLAS 99
Cdd:pfam07651   1 DLEVAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 100 RNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMP 169
Cdd:pfam07651  80 ARRRISSLLRIS-SFSLSWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 170 ILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSE 249
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1776842908 250 FLKVAEQVGIDKG-DIPDLTQAPSSLMETLEQHL 282
Cdd:pfam07651 239 FYEVCKNLGYFRSlEIPKLPHIPPNLLEALEEYL 272
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 643-864 3.59e-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: 51.09  E-value: 3.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  643 AGFGGSFMAPSPSPVTPAQNNllqpnfEAAFGTTPSTSSSSSFDPSGDLLMPTMAPAGQPAPVSMVPP-SPAMAASKALG 721
Cdd:PHA03247  2726 AAARQASPALPAAPAPPAVPA------GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAvASLSESRESLP 2799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  722 SDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWSAGVPPSAPLQGAV---------PPTSSVP 792
Cdd:PHA03247  2800 SPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPPGPPPPSLPLGGSVapggdvrrrPPSRSPA 2872

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  793 PVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVMFAQPMMRPPFGAAAVPGTQLSPSPTPASQ 854
Cdd:PHA03247  2873 AKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952

                          250
                   ....*....|
gi 1776842908  855 SPKKPPAKDP 864
Cdd:PHA03247  2953 GEPSGAVPQP 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 1.08e-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: 1.08e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  21 AVARAVCKATTHEvMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLAS 99
Cdd:pfam07651   1 DLEVAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 100 RNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMP 169
Cdd:pfam07651  80 ARRRISSLLRIS-SFSLSWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 170 ILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSE 249
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1776842908 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 1.65e-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: 1.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  22 VARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRN 101
Cdd:cd16985     1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1776842908 102 TLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSY 138
Cdd:cd16985    81 SLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKAISY 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
20-145 1.27e-43

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 153.94  E-value: 1.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908   20 SAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFI-QYL 97
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTkNWRVVYKALILLHYLLRNGSPRVIlEAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1776842908   98 ASRNTLFNLSNFLDKsGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDF 145
Cdd:smart00273  81 RNRNRILNLSDFQDI-DSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PHA03247 PHA03247
large tegument protein UL36; Provisional
 643-864 3.59e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 3.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  643 AGFGGSFMAPSPSPVTPAQNNllqpnfEAAFGTTPSTSSSSSFDPSGDLLMPTMAPAGQPAPVSMVPP-SPAMAASKALG 721
Cdd:PHA03247  2726 AAARQASPALPAAPAPPAVPA------GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAvASLSESRESLP 2799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  722 SDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWSAGVPPSAPLQGAV---------PPTSSVP 792
Cdd:PHA03247  2800 SPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPPGPPPPSLPLGGSVapggdvrrrPPSRSPA 2872

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  793 PVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVMFAQPMMRPPFGAAAVPGTQLSPSPTPASQ 854
Cdd:PHA03247  2873 AKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952

                          250
                   ....*....|
gi 1776842908  855 SPKKPPAKDP 864
Cdd:PHA03247  2953 GEPSGAVPQP 2962
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
 694-861 2.66e-03

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


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 41.21  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 694 PTMAPAgQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTT--TKKGDLQWNAGEKKLTGGANWQPKVAPAtw 771
Cdd:TIGR01645 284 PPDALL-QPATVSAIPAAAAVAAAAATAKIMAAEAVAGAAVLGPRAQSpaTPSSSLPTDIGNKAVVSSAKKEAEEVPP-- 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 772 sagVPPSAPLQGAVPPTSSVPPVAgAPSVGQPGagfGMPPAGTGMPMMPqQPVMFAQPmmRPPFGAAAVPGTQLSPSPTP 851
Cdd:TIGR01645 361 ---LPQAAPAVVKPGPMEIPTPVP-PPGLAIPS---LVAPPGLVAPTEI-NPSFLASP--RKKMKREKLPVTFGALDDTL 430

                         170
                  ....*....|
gi 1776842908 852 ASQSPKKPPA 861
Cdd:TIGR01645 431 AWKEPSKEDQ 440
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 760-861 3.63e-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: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 760 ANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM-----MPQQPVMFAQPMMRPP 834
Cdd:pfam09770 205 AQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilqrPQSPQPDPAQPSIQPQ 284

                          90       100
                  ....*....|....*....|....*..
gi 1776842908 835 FGAAAVPGTQLSPSPTPASQSPKKPPA 861
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 1.08e-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: 1.08e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  21 AVARAVCKATTHEvMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFIQYLAS 99
Cdd:pfam07651   1 DLEVAVVKATSHD-EAPPKEKHVREILVGTSSSAKLAALFWALSRRLPLTrSWVVAFKALILVHKLLREGHPSVLQELLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 100 RNTLFNLSNFLDkSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFD---FARVKKGA-----DGVMR--TMAPEKLLKSMP 169
Cdd:pfam07651  80 ARRRISSLLRIS-SFSLSWDYGAFIRAYAKYLDERLDFHRKLPRDpgtFERVEYGSlvavgDPNERylTMSMEDLLDSIP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 170 ILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSE 249
Cdd:pfam07651 159 KLQKLLFRLLKCRPTGNALSNECIIAALILLVKESFGLYRAINEGIINLLEKFFELSKPDADRALGIYKRFVKQFERLKE 238

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1776842908 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 1.65e-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: 1.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  22 VARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRN 101
Cdd:cd16985     1 LAKAVCKATTHEVMGPKKKHLDYLVQCTNEPNVNIPQLADLLFERTQNSSWVVVFKALITTHHLMVYGNERFIQYLASRN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1776842908 102 TLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSY 138
Cdd:cd16985    81 SLFNLSNFLDKSGSQGYDMSTFIRRYAKYLNEKAISY 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
20-145 1.27e-43

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 153.94  E-value: 1.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908   20 SAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNS-SWVVVFKALVTTHHLMVHGNERFI-QYL 97
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEIMAVLWRRLNDTkNWRVVYKALILLHYLLRNGSPRVIlEAL 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1776842908   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 1.82e-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: 1.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  22 VARAVCKATTHEVMGPKKKHLDYLIQATNE--TNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLAS 99
Cdd:cd03564     1 LDVAVVKATNHDEVPPKEKHVRKLLLATSNggGRADVAYIVHALAKRLHKKNWIVVLKTLIVIHRLLREGSPSFLEELLR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1776842908 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 1.04e-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: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  22 VARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRN 101
Cdd:cd00197     1 FEKTVEKATSNENMGPDWPLIMEICDLINETNVGPKEAVDAIKKRINNKNPHVVLKALTLLEYCVKNCGERFHQEVASND 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1776842908 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 6.29e-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: 6.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  24 RAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGN-ERFIQYLASRNT 102
Cdd:cd16988     3 KLVKGATKIKLAPPKAKYLDPILLATYSSDASFGEIVRALSRRLRDNSWTVVFKSLIVLHLMIREGEtDDVLLYYLSRPD 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1776842908 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 2.16e-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: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  19 GSAVARAVCKATTHEVMGPKKKHLDYLIQATNETnVNIPQMADTLFERA--TNSSWVVVFKALVTTHHLMVHGNERFIQY 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNY-VEFPEIMKMLWKRLndKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1776842908  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 8.81e-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: 8.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  25 AVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATN-SSWVVVFKALVTTHHLMVHGNERFIQ----YLAS 99
Cdd:cd16987     4 AVVKATSHDDAPPDEKYVREILSLGSSSRAYASACVSALSRRLNRtRDWVVALKCLMLLHRLLRDGSPILEQelslAPSG 83

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1776842908 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 5.13e-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: 5.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  25 AVCKATTHEVMGPKKKHLDYLIQATNETNvNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFI---QYLasRN 101
Cdd:cd16986     4 AVNKATNKTDSPPKPKHVRTIIVKSWTHQ-KGPQFYEELSKRLLLNNPVVQFKALVTLHKVLRDGPPELSllgGYL--DA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1776842908 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 8.92e-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: 8.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  24 RAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPqMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFI-QYLASRNT 102
Cdd:cd17007     3 VAIKKACSSDETAPKRKHVRACIVYTWDHKSSKP-FWNALKTQPLLSDEVQCFKALITIHKVLQEGHPSALkEAIRNIEW 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1776842908 103 LFNLSNFLDKSGSHGYdmSTFIRRYSRYLNEK 134
Cdd:cd17007    82 LESLGRQSSGSGAKGY--GRLIKEYVRYLLDK 111
PHA03247 PHA03247
large tegument protein UL36; Provisional
 643-864 3.59e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 3.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  643 AGFGGSFMAPSPSPVTPAQNNllqpnfEAAFGTTPSTSSSSSFDPSGDLLMPTMAPAGQPAPVSMVPP-SPAMAASKALG 721
Cdd:PHA03247  2726 AAARQASPALPAAPAPPAVPA------GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAvASLSESRESLP 2799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  722 SDLDSSLASLVgnlgISGTTTKKGDLQWNAGEKKLTGGAnwQPkVAPATWSAGVPPSAPLQGAV---------PPTSSVP 792
Cdd:PHA03247  2800 SPWDPADPPAA----VLAPAAALPPAASPAGPLPPPTSA--QP-TAPPPPPGPPPPSLPLGGSVapggdvrrrPPSRSPA 2872

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  793 PVAGAPS-----------VGQPGAGFGMPPAGTGMPMMPQ-------QPVMFAQPMMRPPFGAAAVPGTQLSPSPTPASQ 854
Cdd:PHA03247  2873 AKPAAPArppvrrlarpaVSRSTESFALPPDQPERPPQPQappppqpQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGA 2952

                          250
                   ....*....|
gi 1776842908  855 SPKKPPAKDP 864
Cdd:PHA03247  2953 GEPSGAVPQP 2962
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 29-97 5.37e-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: 5.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776842908  29 ATTHEVMGPKKKHLDYLIQATNETNvNIPQMADTLFER--ATNSSWVVVFKALVTTHHLMVHGNERFIQYL 97
Cdd:cd03571     8 ATSNEPWGPTGSQLAEIAQATFDYD-DYQRIMKVLWKRlnDKGKNWRHVYKALTLLEYLLKNGSERVVDEF 77
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
764-866 2.58e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 764 PKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPgt 843
Cdd:PRK12323  381 PVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAP-- 458

                          90       100
                  ....*....|....*....|...
gi 1776842908 844 qlSPSPTPASQSPKKPPAKDPLA 866
Cdd:PRK12323  459 --AAAARPAAAGPRPVAAAAAAA 479
PHA03247 PHA03247
large tegument protein UL36; Provisional
 567-860 5.25e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  567 SSPPQGASPvpeSSLTADLLSVDAFAAPSP--ATTASPAKVDSSGVIDLFGDAFGSSASEPQPASQAASSSSASADLLAG 644
Cdd:PHA03247  2677 SSPPQRPRR---RAARPTVGSLTSLADPPPppPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  645 ----------FGGSFMAPSPSPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLM---PTMAPAGQPAPVSMVPPS 711
Cdd:PHA03247  2754 parparppttAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLapaAALPPAASPAGPLPPPTS 2833

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  712 PAMAASKALGSDLDSSLaSLVGNLGISGTTTKKGDLQ----WNAGEKKLTGGANWQPKVAPATWSAGVPPsapLQGAVPP 787
Cdd:PHA03247  2834 AQPTAPPPPPGPPPPSL-PLGGSVAPGGDVRRRPPSRspaaKPAAPARPPVRRLARPAVSRSTESFALPP---DQPERPP 2909

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  788 TSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRP------PFGAAAVPGT-----QLSPSPTPASQSP 856
Cdd:PHA03247  2910 QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPsgavpqPWLGALVPGRvavprFRVPQPAPSREAP 2989


                   ....
gi 1776842908  857 KKPP 860
Cdd:PHA03247  2990 ASST 2993
PHA03378 PHA03378
EBNA-3B; Provisional
 764-864 7.52e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 7.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 764 PKVAPATwsAGVPPSAPLQG---AVPPTSSVPPvAGAPSVGQPGA---GFGMPPAGTGMPMMP-------QQPVMFAQPM 830
Cdd:PHA03378  687 IQWAPGT--MQPPPRAPTPMrppAAPPGRAQRP-AAATGRARPPAaapGRARPPAAAPGRARPpaaapgrARPPAAAPGR 763

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1776842908 831 MRPPFGAAAVPGTQLSPSPTPAS-QSPKKPPAKDP 864
Cdd:PHA03378  764 ARPPAAAPGAPTPQPPPQAPPAPqQRPRGAPTPQP 798
PHA03247 PHA03247
large tegument protein UL36; Provisional
 764-864 8.28e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 8.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  764 PKVAPATWSAGVP-PSAPLQG-----AVPPTSSVPPVAGAPSVGQPGAGFGMPP--AGTGMPMMPQQPVMFAQPMMRPPF 835
Cdd:PHA03247  2708 PEPAPHALVSATPlPPGPAAArqaspALPAAPAPPAVPAGPATPGGPARPARPPttAGPPAPAPPAAPAAGPPRRLTRPA 2787

                           90       100
                   ....*....|....*....|....*....
gi 1776842908  836 GAAAVPGTQLSPSPTPASQSPKKPPAKDP 864
Cdd:PHA03247  2788 VASLSESRESLPSPWDPADPPAAVLAPAA 2816
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 697-867 2.17e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 697 APAGQPAPVSMVPPSPAMAASKAlgsdldSSLASLVGNLGISGTTTKKGDLQWNAGEkkltGGANWQPKVAPATWSAGVP 776
Cdd:PRK07764  614 RPAAPAAPAAPAAPAPAGAAAAP------AEASAAPAPGVAAPEHHPKHVAVPDASD----GGDGWPAKAGGAAPAAPPP 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 777 PSAPlQGAVPPTSSVPPVAGAPSVGQPGAGfgmpPAGTGMPMMPQQPVMFAQPmmrPPFGAAAVPGTQLSPSPTPASQSP 856
Cdd:PRK07764  684 APAP-AAPAAPAGAAPAQPAPAPAATPPAG----QADDPAAQPPQAAQGASAP---SPAADDPVPLPPEPDDPPDPAGAP 755

                         170
                  ....*....|.
gi 1776842908 857 KKPPAKDPLAD 867
Cdd:PRK07764  756 AQPPPPPAPAP 766
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
 694-861 2.66e-03

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


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 41.21  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 694 PTMAPAgQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGNLGISGTT--TKKGDLQWNAGEKKLTGGANWQPKVAPAtw 771
Cdd:TIGR01645 284 PPDALL-QPATVSAIPAAAAVAAAAATAKIMAAEAVAGAAVLGPRAQSpaTPSSSLPTDIGNKAVVSSAKKEAEEVPP-- 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 772 sagVPPSAPLQGAVPPTSSVPPVAgAPSVGQPGagfGMPPAGTGMPMMPqQPVMFAQPmmRPPFGAAAVPGTQLSPSPTP 851
Cdd:TIGR01645 361 ---LPQAAPAVVKPGPMEIPTPVP-PPGLAIPS---LVAPPGLVAPTEI-NPSFLASP--RKKMKREKLPVTFGALDDTL 430

                         170
                  ....*....|
gi 1776842908 852 ASQSPKKPPA 861
Cdd:TIGR01645 431 AWKEPSKEDQ 440
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
741-861 3.10e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 41.30  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 741 TTKKGDLQWNAGEKKLTGGANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPgagfgmppagtgmpmmp 820
Cdd:PRK14971  363 TQKGDDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPP----------------- 425

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1776842908 821 qqpvmfaQPMMRPPFGAAAVPGTQLSPSPTPASQSPKKPPA 861
Cdd:PRK14971  426 -------TVSVDPPAAVPVNPPSTAPQAVRPAQFKEEKKIP 459
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 767-861 3.44e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 41.20  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 767 APATWSAGVPPSAPLQGAVPPTSSVPPVAGAP------SVGQPGAGfgmPPAGTGMPMMPQQPVMFAQPMMR-PPFGAAA 839
Cdd:PRK14959  379 SAPSGSAAEGPASGGAATIPTPGTQGPQGTAPaagmtpSSAAPATP---APSAAPSPRVPWDDAPPAPPRSGiPPRPAPR 455

                          90       100
                  ....*....|....*....|...
gi 1776842908 840 VPGTQLSP-SPTPASQSPKKPPA 861
Cdd:PRK14959  456 MPEASPVPgAPDSVASASDAPPT 478
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 760-861 3.63e-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: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 760 ANWQPKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM-----MPQQPVMFAQPMMRPP 834
Cdd:pfam09770 205 AQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVtilqrPQSPQPDPAQPSIQPQ 284

                          90       100
                  ....*....|....*....|....*..
gi 1776842908 835 FGAAAVPGTQLSPSPTPASQSPKKPPA 861
Cdd:pfam09770 285 AQQFHQQPPPVPVQPTQILQNPNRLSA 311
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 764-866 3.69e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.85  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 764 PKVAPATWSAGVPPSAPLQGAVPPtsSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGT 843
Cdd:PRK14951  371 EAAAPAEKKTPARPEAAAPAAAPV--AQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALA 448

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1776842908 844 QLSP--------------SPTPASQSPKKPPAKDPLA 866
Cdd:PRK14951  449 PAPPaqaapetvaipvrvAPEPAVASAAPAPAAAPAA 485
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
764-868 4.35e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.63  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 764 PKVAPATWSAGVPPSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPM---MPQQPVMFAQPmmRPPFGAAAV 840
Cdd:PRK12323  401 APPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAaapAAAARPAAAGP--RPVAAAAAA 478

                          90       100
                  ....*....|....*....|....*...
gi 1776842908 841 PGTQLSPSPTPASQSPKKPPAKDPLADL 868
Cdd:PRK12323  479 APARAAPAAAPAPADDDPPPWEELPPEF 506
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 45-133 4.82e-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: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  45 LIQATNETNVNIPQMADTL------FERATNSSWVVVFKALVTTHHLMVHGNERFIQYlaSRNTLFNLSN-----FLDks 113
Cdd:cd16992    20 LMQEIAQGTYNYQQFNEIMpmiykrFTEKAGSEWRQIYKALQLLEYLIKNGSERVVDD--ARGHLTLIKMlrsfhYID-- 95

                          90       100
                  ....*....|....*....|
gi 1776842908 114 gSHGYDMSTFIRRYSRYLNE 133
Cdd:cd16992    96 -DKGKDQGINVRNRAKELIE 114
PHA03247 PHA03247
large tegument protein UL36; Provisional
 697-869 5.68e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 5.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  697 APAGQPAPVSMVPPSPAMAASKALGSDLDSSLASLVGnlgisgtttkKGDLQWNAGekkltgganwQPKVAPATWSagvP 776
Cdd:PHA03247   305 APLALPAPPDPPPPAPAGDAEEEDDEDGAMEVVSPLP----------RPRQHYPLG----------FPKRRRPTWT---P 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908  777 PSAP---LQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMmPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPT--- 850
Cdd:PHA03247   362 PSSLedlSAGRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTR-PAAPVPASVPTPAPTPVPASAPPPPATPLPSaep 440

                          170
                   ....*....|....*....
gi 1776842908  851 PASQSPKKPPAKDPLADLN 869
Cdd:PHA03247   441 GSDDGPAPPPERQPPAPAT 459
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 777-864 7.94e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 39.85  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 777 PSAPLQGAVPPTSSVPPVAGAPSVGQPGAGFGMPPAGTGMPMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPASQSP 856
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKK 440


                  ....*...
gi 1776842908 857 KKPPAKDP 864
Cdd:PRK07994  441 SEPAAASR 448
PHA03378 PHA03378
EBNA-3B; Provisional
 764-874 8.91e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776842908 764 PKVAPATWSAGVPPSAPLQGAVPPTSSVP----PVAGAPSVGQPGA---GFGMPPAGT-GMPMMPQQPVMFAQPMMRPPF 835
Cdd:PHA03378  713 RAQRPAAATGRARPPAAAPGRARPPAAAPgrarPPAAAPGRARPPAaapGRARPPAAApGAPTPQPPPQAPPAPQQRPRG 792

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1776842908 836 GAAAVPGTQLSPspTPASQSPKKPPAKDPLADLNIKDFL 874
Cdd:PHA03378  793 APTPQPPPQAGP--TSMQLMPRAAPGQQGPTKQILRQLL 829
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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