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Conserved domains on  [gi|30689274|ref|NP_850387|]
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ENTH/VHS family protein [Arabidopsis thaliana]

Protein Classification

ENTH domain-containing protein( domain architecture ID 10132260)

ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to Arabidopsis thaliana clathrin interactor EPSIN 1 that may have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes

CATH:  1.25.40.90
Gene Ontology:  GO:0030276|GO:0072659|GO:1901981|GO:0006897|GO:0005543
PubMed:  27466364|14657269|12742163|22748146|11911874|29774507
SCOP:  4001355

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 26-142 2.25e-62

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: 206.21  E-value: 2.25e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  26 VEQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSDTGKNWRHVYKALTVLEYMVGHGSERVIDEIRER 105
Cdd:cd03571   1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 30689274 106 AYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVND 142
Cdd:cd03571  81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
 142-280 2.33e-07

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 54.52  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  142 DKERIAEVRQKAAANRDKYRSSAPGGMYKPSGGYGDKYDYGSRDE--ERSSYGREREYGYRDDDRNSRDGDRHSRDSEDR 219
Cdd:PRK12678 124 AAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEErdERRRRGDREDRQAEAERGERGRREERGRDGDDR 203

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30689274  220 YGRDGNRDDDYRGRSRSVDNYGSRGRSSEREREDDGHSSSRGSGARADDNSQDGRGGLQRK 280
Cdd:PRK12678 204 DRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGR 264
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 366-707 1.07e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   366 PRSAFSAGPPAYASTDGVTAPPTVTSMSAPTTSNSVEMDLLGSLADVFSSNALAIVPADSiyvETNGQANAGPAPSFSTS 445
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA---LPPAASPAGPLPPPTSA 2834

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   446 QPSTQsfddPFGDSPFKAFTSTDTDSTPQQNFGASFQP-PPPAFTSEVSHPDTAhnfgfgdSFSAVANPDPASQNVQPPS 524
Cdd:PHA03247 2835 QPTAP----PPPPGPPPPSLPLGGSVAPGGDVRRRPPSrSPAAKPAAPARPPVR-------RLARPAVSRSTESFALPPD 2903

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   525 NSPGFPQEQFATsqsgidilagilPPSGPPVQSGPSIPTSQFPPsgnnmyegfhsqPPVSTAPNLPGQTPFGQAvQPYNM 604
Cdd:PHA03247 2904 QPERPPQPQAPP------------PPQPQPQPPPPPQPQPPPPP------------PPRPQPPLAPTTDPAGAG-EPSGA 2958

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   605 VPHSQNmtGAMpfnSGGFMHQPGSQTPYSTPSGPAGQFMAHQGHGMPPSHGP---------QRTQSGPVTLQGNNNVMGD 675
Cdd:PHA03247 2959 VPQPWL--GAL---VPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSswasslalhEETDPPPVSLKQTLWPPDD 3033

                         330       340       350
                  ....*....|....*....|....*....|..
gi 30689274   676 MFSQATPNSLTSSSSHPDLtpltGAIEIVPPP 707
Cdd:PHA03247 3034 TEDSDADSLFDSDSERSDL----EALDPLPPE 3061
 
Name Accession Description Interval E-value
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 26-142 2.25e-62

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: 206.21  E-value: 2.25e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  26 VEQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSDTGKNWRHVYKALTVLEYMVGHGSERVIDEIRER 105
Cdd:cd03571   1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 30689274 106 AYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVND 142
Cdd:cd03571  81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 26-146 3.67e-60

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: 200.09  E-value: 3.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274    26 VEQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSDTGKNWRHVYKALTVLEYMVGHGSERVIDEIRER 105
Cdd:pfam01417   4 TELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDLREN 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 30689274   106 AYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKERI 146
Cdd:pfam01417  84 IYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
24-150 1.43e-45

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 159.72  E-value: 1.43e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274     24 PGVEQKVLDATSNEPWGPHGSLLADLAQASRNY-HEYQLIMVVIWKRLSDTGkNWRHVYKALTVLEYMVGHGSERVIDEI 102
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 30689274    103 RERAYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKERIAEVR 150
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 142-280 2.33e-07

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 54.52  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  142 DKERIAEVRQKAAANRDKYRSSAPGGMYKPSGGYGDKYDYGSRDE--ERSSYGREREYGYRDDDRNSRDGDRHSRDSEDR 219
Cdd:PRK12678 124 AAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEErdERRRRGDREDRQAEAERGERGRREERGRDGDDR 203

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30689274  220 YGRDGNRDDDYRGRSRSVDNYGSRGRSSEREREDDGHSSSRGSGARADDNSQDGRGGLQRK 280
Cdd:PRK12678 204 DRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGR 264
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 170-298 1.27e-06

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 52.20  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   170 KPSGGYGDKYDYGSRDEERS---SYGREREYGYRDDDRNSRDGDRHSRDSEDRygrdGNRDDDYRGRSRSVDNYGSRGRS 246
Cdd:TIGR01642  11 KSRGRDRDRSSERPRRRSRDrsrFRDRHRRSRERSYREDSRPRDRRRYDSRSP----RSLRYSSVRRSRDRPRRRSRSVR 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30689274   247 SEREREDDGHSSSRGSGARADDNSqdgRGGLQRKfseqnigaPPSYEEAVSD 298
Cdd:TIGR01642  87 SIEQHRRRLRDRSPSNQWRKDDKK---RSLWDIK--------PPGYELVTAD 127
PHA03247 PHA03247
large tegument protein UL36; Provisional
 366-707 1.07e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   366 PRSAFSAGPPAYASTDGVTAPPTVTSMSAPTTSNSVEMDLLGSLADVFSSNALAIVPADSiyvETNGQANAGPAPSFSTS 445
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA---LPPAASPAGPLPPPTSA 2834

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   446 QPSTQsfddPFGDSPFKAFTSTDTDSTPQQNFGASFQP-PPPAFTSEVSHPDTAhnfgfgdSFSAVANPDPASQNVQPPS 524
Cdd:PHA03247 2835 QPTAP----PPPPGPPPPSLPLGGSVAPGGDVRRRPPSrSPAAKPAAPARPPVR-------RLARPAVSRSTESFALPPD 2903

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   525 NSPGFPQEQFATsqsgidilagilPPSGPPVQSGPSIPTSQFPPsgnnmyegfhsqPPVSTAPNLPGQTPFGQAvQPYNM 604
Cdd:PHA03247 2904 QPERPPQPQAPP------------PPQPQPQPPPPPQPQPPPPP------------PPRPQPPLAPTTDPAGAG-EPSGA 2958

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   605 VPHSQNmtGAMpfnSGGFMHQPGSQTPYSTPSGPAGQFMAHQGHGMPPSHGP---------QRTQSGPVTLQGNNNVMGD 675
Cdd:PHA03247 2959 VPQPWL--GAL---VPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSswasslalhEETDPPPVSLKQTLWPPDD 3033

                         330       340       350
                  ....*....|....*....|....*....|..
gi 30689274   676 MFSQATPNSLTSSSSHPDLtpltGAIEIVPPP 707
Cdd:PHA03247 3034 TEDSDADSLFDSDSERSDL----EALDPLPPE 3061
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 428-716 4.82e-05

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.45  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   428 VETNGQANAGPAPSFSTSQPSTQSFDDPfgdSPFKAFTSTDTDS-----TPQQNFGASFQPPPPAFTSEVSHPDTAHNfg 502
Cdd:pfam03154 198 GPTPSAPSVPPQGSPATSQPPNQTQSTA---APHTLIQQTPTLHpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLH-- 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   503 fgdsfsAVANPDPASQNVQPPS-NSPGFPQEQFATSQSGidilAGILPPSGPPVQSGPSIPTSQFPPSGNNMYEGfhsQP 581
Cdd:pfam03154 273 ------GQMPPMPHSLQTGPSHmQHPVPPQPFPLTPQSS----QSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQ---QP 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   582 P----VSTAP------NLPGQTPFGQAVQPYNMvPHSQNMTGAMPFnsggfmhqpgsQTPYSTPSGPAGQFMAHQGHGMP 651
Cdd:pfam03154 340 PreqpLPPAPlsmphiKPPPTTPIPQLPNPQSH-KHPPHLSGPSPF-----------QMNSNLPPPPALKPLSSLSTHHP 407

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30689274   652 PSHGPQRTQSGPVTLQGNNNVMGDMFSQATPNSLTSSSSHPDLTPLTGAIEIVPPPQKKFEPKSS 716
Cdd:pfam03154 408 PSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGP 472
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
 180-256 1.58e-04

Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region found at the C-terminus of plant and metazoan pre-mRNA-splicing factor 38 proteins. The function is not known.


Pssm-ID: 463734 [Multi-domain]  Cd Length: 98  Bit Score: 41.69  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   180 DYGSRDEERSSYGREREYGYRDDD------RNSRDGDRHSRDSEDRYGRDGNRDDDYRGRSRSV-DNYGSRGRSSERERE 252
Cdd:pfam12871  15 EEDEEEDEEASDESERASLSRKRRsrsrrrSSTRDRSRSRSRSRSRDRRSRGTRDRRRDRDRDRyRSLRSRSRDRSRDRD 94


                  ....
gi 30689274   253 DDGH 256
Cdd:pfam12871  95 RDRR 98
 
Name Accession Description Interval E-value
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 26-142 2.25e-62

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: 206.21  E-value: 2.25e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  26 VEQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSDTGKNWRHVYKALTVLEYMVGHGSERVIDEIRER 105
Cdd:cd03571   1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 30689274 106 AYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVND 142
Cdd:cd03571  81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 26-146 3.67e-60

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: 200.09  E-value: 3.67e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274    26 VEQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSDTGKNWRHVYKALTVLEYMVGHGSERVIDEIRER 105
Cdd:pfam01417   4 TELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDLREN 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 30689274   106 AYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKERI 146
Cdd:pfam01417  84 IYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 26-150 4.53e-52

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This subfamily is composed of the two orthologs of epsin in Saccharomyces cerevisiae, Epsin-1 (Ent1 or Ent1p) and Epsin-2 (Ent2 or Ent2p), and similar proteins. Yeast single epsin knockouts, either Ent1 and Ent2, are viable while the double knockout is not. Yeast epsins are required for endocytosis and localization of actin. Ent2 also plays a signaling role during cell division. The ENTH domain of Ent2 interacts with the septin organizing, Cdc42 GTPase activating protein, Bem3, leading to increased cytokinesis failure when overexpressed. 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. 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: 340788  Cd Length: 132  Bit Score: 178.24  E-value: 4.53e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  26 VEQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSDTGKNWRHVYKALTVLEYMVGHGSERVIDEIRER 105
Cdd:cd16991   5 TQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWAKEN 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 30689274 106 AYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKERIAEVR 150
Cdd:cd16991  85 IYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREER 129
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 26-148 8.65e-52

Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The 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 CCVs. 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: 340787  Cd Length: 124  Bit Score: 177.16  E-value: 8.65e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  26 VEQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSDTGKNWRHVYKALTVLEYMVGHGSERVIDEIRER 105
Cdd:cd16990   2 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKEN 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 30689274 106 AYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKERIAE 148
Cdd:cd16990  82 IFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 26-153 1.35e-49

Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein (EpsinR) is also called clathrin interactor 1 (Clint), enthoprotin, or epsin-4. It is a clathrin-coated vesicle (CCV) protein that binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). It contains an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The 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. The ENTH domain of human epsinR binds directly to the helical bundle domain of the mouse SNARE Vti1b; 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: 340786  Cd Length: 130  Bit Score: 170.93  E-value: 1.35e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  26 VEQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKR-LSDTGKNWRHVYKALTVLEYMVGHGSERVIDEIRE 104
Cdd:cd16989   1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRmLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 30689274 105 RAYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKERIAEVRQKA 153
Cdd:cd16989  81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKA 129
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
24-150 1.43e-45

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 159.72  E-value: 1.43e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274     24 PGVEQKVLDATSNEPWGPHGSLLADLAQASRNY-HEYQLIMVVIWKRLSDTGkNWRHVYKALTVLEYMVGHGSERVIDEI 102
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 30689274    103 RERAYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKERIAEVR 150
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 27-145 3.34e-41

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: 146.83  E-value: 3.34e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  27 EQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSD-TGKNWRHVYKALTVLEYMVGHGSERVIDEIRER 105
Cdd:cd16992   2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30689274 106 AYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKER 145
Cdd:cd16992  82 LTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK 121
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 26-139 2.37e-18

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: 81.32  E-value: 2.37e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  26 VEQKVLDATSNEPWGPHGSLLADLAQASRNYHE-YQLIMVVIWKRLsdTGKNWRHVYKALTVLEYMVGHGSERVIDEIRE 104
Cdd:cd00197   1 FEKTVEKATSNENMGPDWPLIMEICDLINETNVgPKEAVDAIKKRI--NNKNPHVVLKALTLLEYCVKNCGERFHQEVAS 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 30689274 105 RAYQISTLSdFQYIDSGGRDQGSNVRKKSQSLVAL 139
Cdd:cd00197  79 NDFAVELLK-FDKSGLLGDDVSTNVREKAIELVQL 112
ENTH_Ent4 cd16994
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 ...
 27-144 1.98e-09

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 (Ent4 or Ent4p) has been reported to be involved in the Trans-Golgi Network (TGN)-to-vacuole sorting of Arn1p, a transporter for the uptake of ferrichrome, an important nutritional source of iron. 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. 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: 340791  Cd Length: 126  Bit Score: 56.53  E-value: 1.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  27 EQKVLDAT-SNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSDTG-----KNWRHVYKALTVLEYMVGHGSERVID 100
Cdd:cd16994   2 ELKVKQATdDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSkksshKNCVHILKTLTLISYLINNGSNEFIA 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 30689274 101 EIRERAYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKE 144
Cdd:cd16994  82 WLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDE 125
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 142-280 2.33e-07

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 54.52  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  142 DKERIAEVRQKAAANRDKYRSSAPGGMYKPSGGYGDKYDYGSRDE--ERSSYGREREYGYRDDDRNSRDGDRHSRDSEDR 219
Cdd:PRK12678 124 AAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEErdERRRRGDREDRQAEAERGERGRREERGRDGDDR 203

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30689274  220 YGRDGNRDDDYRGRSRSVDNYGSRGRSSEREREDDGHSSSRGSGARADDNSQDGRGGLQRK 280
Cdd:PRK12678 204 DRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGR 264
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 170-298 1.27e-06

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 52.20  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   170 KPSGGYGDKYDYGSRDEERS---SYGREREYGYRDDDRNSRDGDRHSRDSEDRygrdGNRDDDYRGRSRSVDNYGSRGRS 246
Cdd:TIGR01642  11 KSRGRDRDRSSERPRRRSRDrsrFRDRHRRSRERSYREDSRPRDRRRYDSRSP----RSLRYSSVRRSRDRPRRRSRSVR 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30689274   247 SEREREDDGHSSSRGSGARADDNSqdgRGGLQRKfseqnigaPPSYEEAVSD 298
Cdd:TIGR01642  87 SIEQHRRRLRDRSPSNQWRKDDKK---RSLWDIK--------PPGYELVTAD 127
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 142-276 1.28e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 52.21  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  142 DKERIAEVRQKAAANRDKYRSSAPGGMYKPSGGyGDKYDYGSRDEERSSYGREREYGYRDDDRNSRDGDRHSRDSEDRYG 221
Cdd:PRK12678 143 RKAGEGGEQPATEARADAAERTEEEERDERRRR-GDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRR 221

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30689274  222 RDGNRDDDYRGRSRSVDNYGSRGRSSEREREDDGHSSSRGSGARADDNSQDGRGG 276
Cdd:PRK12678 222 DGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRG 276
PHA03247 PHA03247
large tegument protein UL36; Provisional
 366-707 1.07e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   366 PRSAFSAGPPAYASTDGVTAPPTVTSMSAPTTSNSVEMDLLGSLADVFSSNALAIVPADSiyvETNGQANAGPAPSFSTS 445
Cdd:PHA03247 2758 ARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA---LPPAASPAGPLPPPTSA 2834

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   446 QPSTQsfddPFGDSPFKAFTSTDTDSTPQQNFGASFQP-PPPAFTSEVSHPDTAhnfgfgdSFSAVANPDPASQNVQPPS 524
Cdd:PHA03247 2835 QPTAP----PPPPGPPPPSLPLGGSVAPGGDVRRRPPSrSPAAKPAAPARPPVR-------RLARPAVSRSTESFALPPD 2903

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   525 NSPGFPQEQFATsqsgidilagilPPSGPPVQSGPSIPTSQFPPsgnnmyegfhsqPPVSTAPNLPGQTPFGQAvQPYNM 604
Cdd:PHA03247 2904 QPERPPQPQAPP------------PPQPQPQPPPPPQPQPPPPP------------PPRPQPPLAPTTDPAGAG-EPSGA 2958

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   605 VPHSQNmtGAMpfnSGGFMHQPGSQTPYSTPSGPAGQFMAHQGHGMPPSHGP---------QRTQSGPVTLQGNNNVMGD 675
Cdd:PHA03247 2959 VPQPWL--GAL---VPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSswasslalhEETDPPPVSLKQTLWPPDD 3033

                         330       340       350
                  ....*....|....*....|....*....|..
gi 30689274   676 MFSQATPNSLTSSSSHPDLtpltGAIEIVPPP 707
Cdd:PHA03247 3034 TEDSDADSLFDSDSERSDL----EALDPLPPE 3061
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 182-274 2.76e-05

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 47.61  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   182 GSRDEERSSYGREREYGYRDDDRN-SRDGDRhSRDSEDRYGRDGNRD-----DDYRGRSRSVDNYGSRGRSSEREREDDG 255
Cdd:TIGR01622   1 RYRDRERERLRDSSSAGDRDRRRDkGRERSR-DRSRDRERSRSRRRDrhrdrDYYRGRERRSRSRRPNRRYRPREKRRRR 79

                          90
                  ....*....|....*....
gi 30689274   256 HSSSRgsgaRADDNSQDGR 274
Cdd:TIGR01622  80 GDSYR----RRRDDRRSRR 94
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 428-716 4.82e-05

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.45  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   428 VETNGQANAGPAPSFSTSQPSTQSFDDPfgdSPFKAFTSTDTDS-----TPQQNFGASFQPPPPAFTSEVSHPDTAHNfg 502
Cdd:pfam03154 198 GPTPSAPSVPPQGSPATSQPPNQTQSTA---APHTLIQQTPTLHpqrlpSPHPPLQPMTQPPPPSQVSPQPLPQPSLH-- 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   503 fgdsfsAVANPDPASQNVQPPS-NSPGFPQEQFATSQSGidilAGILPPSGPPVQSGPSIPTSQFPPSGNNMYEGfhsQP 581
Cdd:pfam03154 273 ------GQMPPMPHSLQTGPSHmQHPVPPQPFPLTPQSS----QSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQ---QP 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   582 P----VSTAP------NLPGQTPFGQAVQPYNMvPHSQNMTGAMPFnsggfmhqpgsQTPYSTPSGPAGQFMAHQGHGMP 651
Cdd:pfam03154 340 PreqpLPPAPlsmphiKPPPTTPIPQLPNPQSH-KHPPHLSGPSPF-----------QMNSNLPPPPALKPLSSLSTHHP 407

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30689274   652 PSHGPQRTQSGPVTLQGNNNVMGDMFSQATPNSLTSSSSHPDLTPLTGAIEIVPPPQKKFEPKSS 716
Cdd:pfam03154 408 PSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGP 472
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 176-255 5.63e-05

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 46.82  E-value: 5.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  176 GDKYDYGSRDEERSSYGREREYGYRDDDRNSRDGDRHSRDSEDRYGRDGNRDDDYRGRSRSVDNYGSRGRSSERE-REDD 254
Cdd:PRK12678 212 GDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGNEREPElREDD 291


                 .
gi 30689274  255 G 255
Cdd:PRK12678 292 V 292
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 180-256 1.31e-04

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 45.68  E-value: 1.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30689274   180 DYGSRDEERSSYGREREYGYRDDDRNSRDGDRHSRDSEDRY-GRDGN-RDDDYRGRSRSVDNYGSRGRSSEREREDDGH 256
Cdd:TIGR01622  14 SSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYrGRERRsRSRRPNRRYRPREKRRRRGDSYRRRRDDRRS 92
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
 180-256 1.58e-04

Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region found at the C-terminus of plant and metazoan pre-mRNA-splicing factor 38 proteins. The function is not known.


Pssm-ID: 463734 [Multi-domain]  Cd Length: 98  Bit Score: 41.69  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   180 DYGSRDEERSSYGREREYGYRDDD------RNSRDGDRHSRDSEDRYGRDGNRDDDYRGRSRSV-DNYGSRGRSSERERE 252
Cdd:pfam12871  15 EEDEEEDEEASDESERASLSRKRRsrsrrrSSTRDRSRSRSRSRSRDRRSRGTRDRRRDRDRDRyRSLRSRSRDRSRDRD 94


                  ....
gi 30689274   253 DDGH 256
Cdd:pfam12871  95 RDRR 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
 288-723 2.57e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   288 APPSYEEAVS--DSRSPVYSERDGGETPQVTAPGAASPPPPQVAAPEAASPPTGTNTANTTATFVNESPSQKVETFDEFD 365
Cdd:PHA03247 2574 APRPSEPAVTsrARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPR 2653

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   366 ----------PRSAFSAGPPAYASTDGV-----TAPPTVTSM--------------SAPTTSNSVEMDLLGSLADVFSSN 416
Cdd:PHA03247 2654 ddpapgrvsrPRRARRLGRAAQASSPPQrprrrAARPTVGSLtsladpppppptpePAPHALVSATPLPPGPAAARQASP 2733

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   417 ALAIVPADSIYVE---TNGQANAGPAPSFSTSQPSTQSFDDPFGDSPfKAFTSTDTDSTPQQNFGASFQPPPPAFTSEVS 493
Cdd:PHA03247 2734 ALPAAPAPPAVPAgpaTPGGPARPARPPTTAGPPAPAPPAAPAAGPP-RRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   494 HPDTAHNfgfGDSFSAVANPDPASQNVQPPSNSPGFPQEQFAtsqsgidiLAGILPPSGPPVQSGPSIPTSQFPPSGNNM 573
Cdd:PHA03247 2813 APAAALP---PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP--------LGGSVAPGGDVRRRPPSRSPAAKPAAPARP 2881

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   574 YEGFHSQPPVSTAPNLPGQTPFGQAVQPynmVPHSQNMTGAMPFNSGGFMHQPGSQTPySTPSGPAGQFMAHQGHGMPPS 653
Cdd:PHA03247 2882 PVRRLARPAVSRSTESFALPPDQPERPP---QPQAPPPPQPQPQPPPPPQPQPPPPPP-PRPQPPLAPTTDPAGAGEPSG 2957

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   654 HGPQRTQSGPVTlqGNNNVMGDMFSQATPNSLTSSSShpdltpltgaieiVPPPQKKFEPKSSVWADTLS 723
Cdd:PHA03247 2958 AVPQPWLGALVP--GRVAVPRFRVPQPAPSREAPASS-------------TPPLTGHSLSRVSSWASSLA 3012
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 183-274 4.61e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.74  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  183 SRDEERSSYGREREYGYRDDDRNSRDGDRHSRDSEDRYGRDGNRDD--DYRGRSRSVDNYGSRGRSSEREREDDghssSR 260
Cdd:PRK12678 197 GRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDnrEDRGDRDGDDGEGRGGRRGRRFRDRD----RR 272

                         90
                 ....*....|....
gi 30689274  261 GSGARADDNSQDGR 274
Cdd:PRK12678 273 GRRGGDGGNEREPE 286
VHS cd03561
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ...
 26-155 5.30e-04

VHS (Vps27/Hrs/STAM) domain family; 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 has a superhelical structure similar to that of the ARM (Armadillo) repeats and is present at the N-termini of proteins involved in intracellular membrane trafficking. There are four general groups of VHS domain containing proteins based on their association with other domains. The first group consists of proteins of the STAM/EAST/Hbp family, which has the domain composition of VHS-SH3-ITAM. The second consists of proteins with a FYVE domain C-terminal to VHS. The third consists of GGA proteins with a domain composition of VHS-GAT (GGA and TOM)-GAE (Gamma-Adaptin Ear) domain. The fourth consists of proteins with a VHS domain alone or with domains other than those mentioned above. In GGA proteins, VHS domains are involved in cargo recognition in trans-Golgi, thereby having a general membrane targeting/cargo recognition role in vesicular trafficking.


Pssm-ID: 340765  Cd Length: 131  Bit Score: 40.71  E-value: 5.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  26 VEQKVLDATS----NEPWgPHGSLLADLAQASRNYHEYqlIMVVIWKRLSDtgKNWRHVYKALTVLEYMVGHGSERVIDE 101
Cdd:cd03561   1 VEELVEKATSesltEPDW-ALNLEICDLVNSDPAQAKD--AVRALRKRLQS--KNPKVQLLALTLLETLVKNCGAPFHSE 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30689274 102 IRERayqistlsDFQyidsggrdqgsnvrkksQSLVALVNDKERIAEVRQKAAA 155
Cdd:cd03561  76 VASR--------DFL-----------------QELVKLVKKKKTSPEVREKALA 104
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 119-272 5.37e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.74  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  119 DSGGRDQGSNVRKKSQSlvalVNDKERIAEVRQKAAANRDKYRSSAPGGMYKPSGGYGDKYDYGSRDEERSSYGREREYG 198
Cdd:PRK12678 144 KAGEGGEQPATEARADA----AERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERG 219

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30689274  199 YRDDDRNSRDGDRHSRDSEDRygrDGNRDDDYRGRSRSVDNYGSRGRSSEREREDDGHSSSRGSGARADDNSQD 272
Cdd:PRK12678 220 RRDGGDRRGRRRRRDRRDARG---DDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGNEREPELRED 290
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 33-156 9.91e-04

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-5 (Ent5 or Ent5p), and similar proteins. Ent5 is required, together with Ent3 and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. It is also required for protein transport from the Trans-Golgi Network (TGN) to the vacuole. 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. 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: 340790  Cd Length: 158  Bit Score: 40.52  E-value: 9.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274  33 ATSNEPWGPhgsLLADLAQASRNYHEYQLIMVV--IWKRLSD-------------------TGKNWRHVYKALTVLEYM- 90
Cdd:cd16993   8 ATNTDAWGP---TPKHLAKVLRNRYQVPLYLMTeyTLKRLVDhiatrpknlyekarkdyvnYGSEWRVVLKCLIVIEFLl 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30689274  91 --VGHGSErvIDEIRE---RAYQI--STLSDFQYIDSG-GRDQ--GSNVRKKSQSLVALVNDKERIAEVRQKAAAN 156
Cdd:cd16993  85 lnVDTGDE--LNQVLScllNHKHIftREIAQYKVKFSNdGKMEihERGIQKKCELILQLIEDSDFLRQERAKNKKN 158
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 478-593 1.52e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   478 GASFQPPP---PAFTSEVSHPDTAhnfgfgdsfsavANPDPASQNVQPPSNSPgFPQEQFATSQSgidilAGILPPSGPP 554
Cdd:pfam03154 421 SQQLPPPPaqpPVLTQSQSLPPPA------------ASHPPTSGLHQVPSQSP-FPQHPFVPGGP-----PPITPPSGPP 482

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 30689274   555 VQSGPSIPTSQFPPSGnnmyegfhsqpPVSTAPNLPGQT 593
Cdd:pfam03154 483 TSTSSAMPGIQPPSSA-----------SVSSSGPVPAAV 510
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 184-301 2.18e-03

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 41.42  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689274   184 RDEER-----SSYGREREYGYRDDDRNSRDGDRhSRDsEDRYGRDGNRDDDYRGRSRSvdNYGSRGRSSEREreddghSS 258
Cdd:TIGR01642   1 RDEEPdrereKSRGRDRDRSSERPRRRSRDRSR-FRD-RHRRSRERSYREDSRPRDRR--RYDSRSPRSLRY------SS 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 30689274   259 SRGSGARADDNSQDGRGGLQRKfsEQNIGAPPSYEEAVSDSRS 301
Cdd:TIGR01642  71 VRRSRDRPRRRSRSVRSIEQHR--RRLRDRSPSNQWRKDDKKR 111
 
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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