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Conserved domains on  [gi|18411135|ref|NP_567079|]
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ENTH/VHS family protein [Arabidopsis thaliana]

Protein Classification

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 1.01e-61

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: 205.06  E-value: 1.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   26 IEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQITMGVLWKRLSDSGKNWRHVYKALTVLEYMVGHGSERVIEEVKEH 105
Cdd:cd03571    1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18411135  106 AYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVND 142
Cdd:cd03571   81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
285-397 3.27e-06

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 51.03  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   285 SEQNIGAAPPSYEEA-VSESRSPVYSERDGGETPQVAPPGAAASPLAENISVDNKAADFVNESSPQQVEAFDEFDPRGSV 363
Cdd:PRK12323  366 GQSGGGAGPATAAAApVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPG 445

                          90       100       110
                  ....*....|....*....|....*....|....
gi 18411135   364 SAACAPTAGASVPAPIPPTVVSTPAPPASINAEM 397
Cdd:PRK12323  446 GAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 771-1017 3.92e-06

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.78  E-value: 3.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    771 QSGPVAAHGNSNNVVGDMFSPAGLSSLETSASQPSLTPLTGAIEIVPQ----NQKKFEPKSTIWADTLSRGLVNFNISGp 846
Cdd:pfam09606   60 QQQPQGGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGgpmgQQMGGPGTASNLLASLGRPQMPMGGAG- 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    847 ktNPLADIGVDFEAINRKEKRLEKPTITQQQVTSTINMGKAMGSGTGL-----GRAGAGAMRPPTNSMVGSSMPtGMNVG 921
Cdd:pfam09606  139 --FPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQaggmnGGQQGPMGGQMPPQMGVPGMP-GPADA 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    922 GYGGMNQHQPIG---------------MNQNHPMGMNQNLSMGMNQNYPMGMNQNYPmgmgmnmnmGGYGQGYPMQPQQG 986
Cdd:pfam09606  216 GAQMGQQAQANGgmnpqqmggapnqvaMQQQQPQQQGQQSQLGMGINQMQQMPQGVG---------GGAGQGGPGQPMGP 286

                          250       260       270
                   ....*....|....*....|....*....|.
gi 18411135    987 MGMAPPGAPQGMTGAYNPMMGQGGYNPQQQQ 1017
Cdd:pfam09606  287 PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQ 317
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 252-705 5.66e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   252 RPIEDDGQSSSRDSGAPADDHSQDGRGGLERKFSEQNIGAAPPSYEEAV---SESRSPVYSERDGGETPQVAPP-----G 323
Cdd:PHA03247 2576 RPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPdppPPSPSPAANEPDPHPPPTVPPPerprdD 2655

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   324 AAASPLAENISVDNKAADFVNESSPQQVEAFDEFDPRGSVSAACAPTAGASVPAPIP-PTVVSTPAPPASINAemdllgs 402
Cdd:PHA03247 2656 PAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPhALVSATPLPPGPAAA------- 2728

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   403 lSDVFSPNPLAIVTSDS-TSVETNGQANTGLAPSFSTSQSSTQPFDDPFGDSPFKAITSADTETSQH-QSFGVPFQPTPP 480
Cdd:PHA03247 2729 -RQASPALPAAPAPPAVpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESrESLPSPWDPADP 2807

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   481 TSnpnnehnfgfgeafsAVTDSEPGVQNMQAPPNLSVFPQEQFDTSQSeidilagilPPSGPPVSLSPQPDSTMPTSQFH 560
Cdd:PHA03247 2808 PA---------------AVLAPAAALPPAASPAGPLPPPTSAQPTAPP---------PPPGPPPPSLPLGGSVAPGGDVR 2863

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   561 PNGNSYESYHHQAAPTDLNMQ--GQTPFGQASQQFNMvshsqnhhegmqfnnggftQQPGYAGPATSQPPQyTPGVSSHP 638
Cdd:PHA03247 2864 RRPPSRSPAAKPAAPARPPVRrlARPAVSRSTESFAL-------------------PPDQPERPPQPQAPP-PPQPQPQP 2923

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411135   639 PSESFPhQPGSATSASSQTPYATTPNVS-AGQFDGGSFMTQQPYGVTQQVHVVPSHIPQRTQSGPVAA 705
Cdd:PHA03247 2924 PPPPQP-QPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPA 2990
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
 176-252 1.26e-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: 42.07  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    176 DYEGRYGDRDEGRSSYGKEREYGYRDDD------RNSRDGDRYSRDSEDRYGRDGNTDDEYRGRSRSVDNYNGSRGRSSD 249
Cdd:pfam12871   11 DEEEEEDEEEDEEASDESERASLSRKRRsrsrrrSSTRDRSRSRSRSRSRDRRSRGTRDRRRDRDRDRYRSLRSRSRDRS 90


                   ...
gi 18411135    250 RER 252
Cdd:pfam12871   91 RDR 93
 
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 1.01e-61

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: 205.06  E-value: 1.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   26 IEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQITMGVLWKRLSDSGKNWRHVYKALTVLEYMVGHGSERVIEEVKEH 105
Cdd:cd03571    1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18411135  106 AYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVND 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 2.48e-57

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: 193.16  E-value: 2.48e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135     26 IEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQITMGVLWKRLSDSGKNWRHVYKALTVLEYMVGHGSERVIEEVKEH 105
Cdd:pfam01417    4 TELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDLREN 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 18411135    106 AYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVNDKERI 146
Cdd:pfam01417   84 IYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
24-150 3.96e-41

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 147.01  E-value: 3.96e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135      24 PGIEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQIT-MGVLWKRLSDSGkNWRHVYKALTVLEYMVGHGSERVIEEV 102
Cdd:smart00273    1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEiMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 18411135     103 KEHAYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVNDKERITEVR 150
Cdd:smart00273   80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
285-397 3.27e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 51.03  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   285 SEQNIGAAPPSYEEA-VSESRSPVYSERDGGETPQVAPPGAAASPLAENISVDNKAADFVNESSPQQVEAFDEFDPRGSV 363
Cdd:PRK12323  366 GQSGGGAGPATAAAApVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPG 445

                          90       100       110
                  ....*....|....*....|....*....|....
gi 18411135   364 SAACAPTAGASVPAPIPPTVVSTPAPPASINAEM 397
Cdd:PRK12323  446 GAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 771-1017 3.92e-06

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.78  E-value: 3.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    771 QSGPVAAHGNSNNVVGDMFSPAGLSSLETSASQPSLTPLTGAIEIVPQ----NQKKFEPKSTIWADTLSRGLVNFNISGp 846
Cdd:pfam09606   60 QQQPQGGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGgpmgQQMGGPGTASNLLASLGRPQMPMGGAG- 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    847 ktNPLADIGVDFEAINRKEKRLEKPTITQQQVTSTINMGKAMGSGTGL-----GRAGAGAMRPPTNSMVGSSMPtGMNVG 921
Cdd:pfam09606  139 --FPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQaggmnGGQQGPMGGQMPPQMGVPGMP-GPADA 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    922 GYGGMNQHQPIG---------------MNQNHPMGMNQNLSMGMNQNYPMGMNQNYPmgmgmnmnmGGYGQGYPMQPQQG 986
Cdd:pfam09606  216 GAQMGQQAQANGgmnpqqmggapnqvaMQQQQPQQQGQQSQLGMGINQMQQMPQGVG---------GGAGQGGPGQPMGP 286

                          250       260       270
                   ....*....|....*....|....*....|.
gi 18411135    987 MGMAPPGAPQGMTGAYNPMMGQGGYNPQQQQ 1017
Cdd:pfam09606  287 PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQ 317
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-705 5.66e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   252 RPIEDDGQSSSRDSGAPADDHSQDGRGGLERKFSEQNIGAAPPSYEEAV---SESRSPVYSERDGGETPQVAPP-----G 323
Cdd:PHA03247 2576 RPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPdppPPSPSPAANEPDPHPPPTVPPPerprdD 2655

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   324 AAASPLAENISVDNKAADFVNESSPQQVEAFDEFDPRGSVSAACAPTAGASVPAPIP-PTVVSTPAPPASINAemdllgs 402
Cdd:PHA03247 2656 PAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPhALVSATPLPPGPAAA------- 2728

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   403 lSDVFSPNPLAIVTSDS-TSVETNGQANTGLAPSFSTSQSSTQPFDDPFGDSPFKAITSADTETSQH-QSFGVPFQPTPP 480
Cdd:PHA03247 2729 -RQASPALPAAPAPPAVpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESrESLPSPWDPADP 2807

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   481 TSnpnnehnfgfgeafsAVTDSEPGVQNMQAPPNLSVFPQEQFDTSQSeidilagilPPSGPPVSLSPQPDSTMPTSQFH 560
Cdd:PHA03247 2808 PA---------------AVLAPAAALPPAASPAGPLPPPTSAQPTAPP---------PPPGPPPPSLPLGGSVAPGGDVR 2863

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   561 PNGNSYESYHHQAAPTDLNMQ--GQTPFGQASQQFNMvshsqnhhegmqfnnggftQQPGYAGPATSQPPQyTPGVSSHP 638
Cdd:PHA03247 2864 RRPPSRSPAAKPAAPARPPVRrlARPAVSRSTESFAL-------------------PPDQPERPPQPQAPP-PPQPQPQP 2923

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411135   639 PSESFPhQPGSATSASSQTPYATTPNVS-AGQFDGGSFMTQQPYGVTQQVHVVPSHIPQRTQSGPVAA 705
Cdd:PHA03247 2924 PPPPQP-QPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPA 2990
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 250-668 1.12e-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: 49.77  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    250 RERPIEDDGQSSSRDSGAPADDHSQDGRGGLERKFSEQNIGAAPP-------SYEEAVSESRSPVYSERDGGETPQVAPP 322
Cdd:pfam03154   31 RASPTNEDLRSSGRNSPSAASTSSNDSKAESMKKSSKKIKEEAPSplksakrQREKGASDTEEPERATAKKSKTQEISRP 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    323 GAAAS---------PLAENISVDNKAADFVNES------SPQQVEAFDEFDPRGSVSAACAPTAGASVPAPIPP------ 381
Cdd:pfam03154  111 NSPSEgegessdgrSVNDEGSSDPKDIDQDNRStspsipSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPsppppg 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    382 -TVVSTPAPPASINAeMDLLGSLSDVFSPNPLAIVTSDSTSVETNGQAN-----------TGLAPSFSTSQSSTQPFDDP 449
Cdd:pfam03154  191 tTQAATAGPTPSAPS-VPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHpqrlpsphpplQPMTQPPPPSQVSPQPLPQP 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    450 FGDSPFKAITSADTETSQHQSFGVPFQPTPPTSNPNNehnfGFGEAFSAVTDSEPGVQNMQAPPNLSVFPQEQFDTSQSe 529
Cdd:pfam03154  270 SLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQ----SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP- 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    530 idilagiLPPSgpPVSLSP-QPDSTMPTSQFhPNGNSYESYHHQAAPTDLNMQGQTPFGQASQQFNMVShsqNHHEGMQ- 607
Cdd:pfam03154  345 -------LPPA--PLSMPHiKPPPTTPIPQL-PNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLS---THHPPSAh 411

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18411135    608 ------FNNGGFTQQPGYAGPATSQPPQYTPGVSSHPPsesfphqPGSATSASSQTPYATTPNVSAG 668
Cdd:pfam03154  412 ppplqlMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPP-------TSGLHQVPSQSPFPQHPFVPGG 471
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
 176-252 1.26e-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: 42.07  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    176 DYEGRYGDRDEGRSSYGKEREYGYRDDD------RNSRDGDRYSRDSEDRYGRDGNTDDEYRGRSRSVDNYNGSRGRSSD 249
Cdd:pfam12871   11 DEEEEEDEEEDEEASDESERASLSRKRRsrsrrrSSTRDRSRSRSRSRSRDRRSRGTRDRRRDRDRDRYRSLRSRSRDRS 90


                   ...
gi 18411135    250 RER 252
Cdd:pfam12871   91 RDR 93
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 144-283 2.81e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   144 ERITEVREKAAANRDKyhnsMHRPSGGYGDKYDYEGRYGDRDEGRSSYGKEREYGYRDDDRNSRDGDRYSRDSEDRYGRD 223
Cdd:PRK12678  125 AQARERRERGEAARRG----AARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDG 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411135   224 GNTDDEYRGRSRSVDNYNGSRGRSSDRERPIEDDGQSSSRDSG--APADDHSQDGRGGLERK 283
Cdd:PRK12678  201 DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNreDRGDRDGDDGEGRGGRR 262
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 173-263 4.79e-04

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: 44.11  E-value: 4.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    173 DKYDYEGRYGDRDEGRSSYGKEREYGYRDDDRNSRDGDRY--SRD----SEDRYGRDgNTDDEYRGRSRSVDNyngSRGR 246
Cdd:TIGR01642    8 EREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYRedSRPrdrrRYDSRSPR-SLRYSSVRRSRDRPR---RRSR 83

                           90
                   ....*....|....*..
gi 18411135    247 SSDRERPIEDDGQSSSR 263
Cdd:TIGR01642   84 SVRSIEQHRRRLRDRSP 100
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 200-391 9.37e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 39.83  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135  200 RDDDRNSRDGDRYSRDSEDRYGRDGNTDDEYRGRSRSVDNYNGSRGRSSDRERPIEDDGQSSSRDSGAPADDHSQDGRGG 279
Cdd:COG3266  165 LALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLLLLLASALGEAVAAAAELAALALLAAGAAEVLTARL 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135  280 LERKFSEQNIGAAPPSYEEAVSESRSPVYSERDGGETPQVAP-PGAAASPLAENISVDNKAADFVNESSPQQVEAfdefd 358
Cdd:COG3266  245 VLLLLIIGSALKAPSQASSASAPATTSLGEQQEVSLPPAVAAqPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAA----- 319

                        170       180       190
                 ....*....|....*....|....*....|....
gi 18411135  359 PRGSVSA-ACAPTAGASVPAPIPPTVVSTPAPPA 391
Cdd:COG3266  320 PQPTAAKpVVTETAAPAAPAPEAAAAAAAPAAPA 353
 
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 1.01e-61

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: 205.06  E-value: 1.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   26 IEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQITMGVLWKRLSDSGKNWRHVYKALTVLEYMVGHGSERVIEEVKEH 105
Cdd:cd03571    1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18411135  106 AYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVND 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 2.48e-57

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: 193.16  E-value: 2.48e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135     26 IEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQITMGVLWKRLSDSGKNWRHVYKALTVLEYMVGHGSERVIEEVKEH 105
Cdd:pfam01417    4 TELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDLREN 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 18411135    106 AYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVNDKERI 146
Cdd:pfam01417   84 IYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 26-148 5.61e-51

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: 175.24  E-value: 5.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   26 IEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQITMGVLWKRLSDSGKNWRHVYKALTVLEYMVGHGSERVIEEVKEH 105
Cdd:cd16990    2 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKEN 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18411135  106 AYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVNDKERITE 148
Cdd:cd16990   82 IFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 26-150 1.94e-50

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: 174.00  E-value: 1.94e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   26 IEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQITMGVLWKRLSDSGKNWRHVYKALTVLEYMVGHGSERVIEEVKEH 105
Cdd:cd16991    5 TQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWAKEN 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 18411135  106 AYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVNDKERITEVR 150
Cdd:cd16991   85 IYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREER 129
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 26-153 2.45e-50

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: 173.63  E-value: 2.45e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   26 IEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQITMGVLWKR-LSDSGKNWRHVYKALTVLEYMVGHGSERVIEEVKE 104
Cdd:cd16989    1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRmLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 18411135  105 HAYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVNDKERITEVREKA 153
Cdd:cd16989   81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKA 129
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
24-150 3.96e-41

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 147.01  E-value: 3.96e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135      24 PGIEQKVLDATSNESWGPHGSLLADIAHASRNYHEYQIT-MGVLWKRLSDSGkNWRHVYKALTVLEYMVGHGSERVIEEV 102
Cdd:smart00273    1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSSFAEiMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 18411135     103 KEHAYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVNDKERITEVR 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 2.32e-39

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: 141.82  E-value: 2.32e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   27 EQKVLDATSNESWGPHGSLLADIAHASRNYHEYQITMGVLWKRLSD-SGKNWRHVYKALTVLEYMVGHGSERVIEEVKEH 105
Cdd:cd16992    2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 18411135  106 AYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVNDKER 145
Cdd:cd16992   82 LTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK 121
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 27-139 3.36e-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: 3.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   27 EQKVLDATSNESWGPHGSLLADIAHASRNYHE-YQITMGVLWKRLSDsgKNWRHVYKALTVLEYMVGHGSERVIEEVKEH 105
Cdd:cd00197    2 EKTVEKATSNENMGPDWPLIMEICDLINETNVgPKEAVDAIKKRINN--KNPHVVLKALTLLEYCVKNCGERFHQEVASN 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 18411135  106 AYqITTLSGFQYIDSSGKDQGSNVRKKAQSLVAL 139
Cdd:cd00197   80 DF-AVELLKFDKSGLLGDDVSTNVREKAIELVQL 112
ENTH_Ent4 cd16994
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 ...
 27-144 2.84e-11

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: 61.93  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   27 EQKVLDAT-SNESWGPHGSLLADIA---HASRNYHEyqITmGVLWKRLS-----DSGKNWRHVYKALTVLEYMVGHGSER 97
Cdd:cd16994    2 ELKVKQATdDNETSGATGTLMNEISvltYSPKTLKE--IT-QVLKKRLSgnskkSSHKNCVHILKTLTLISYLINNGSNE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 18411135   98 VIEEVKEHAYQITTLSGFQYIDSSGKDQGSNVRKKAQSLVALVNDKE 144
Cdd:cd16994   79 FIAWLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDE 125
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
285-397 3.27e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 51.03  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   285 SEQNIGAAPPSYEEA-VSESRSPVYSERDGGETPQVAPPGAAASPLAENISVDNKAADFVNESSPQQVEAFDEFDPRGSV 363
Cdd:PRK12323  366 GQSGGGAGPATAAAApVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPG 445

                          90       100       110
                  ....*....|....*....|....*....|....
gi 18411135   364 SAACAPTAGASVPAPIPPTVVSTPAPPASINAEM 397
Cdd:PRK12323  446 GAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAA 479
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 771-1017 3.92e-06

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 50.78  E-value: 3.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    771 QSGPVAAHGNSNNVVGDMFSPAGLSSLETSASQPSLTPLTGAIEIVPQ----NQKKFEPKSTIWADTLSRGLVNFNISGp 846
Cdd:pfam09606   60 QQQPQGGQGNGGMGGGQQGMPDPINALQNLAGQGTRPQMMGPMGPGPGgpmgQQMGGPGTASNLLASLGRPQMPMGGAG- 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    847 ktNPLADIGVDFEAINRKEKRLEKPTITQQQVTSTINMGKAMGSGTGL-----GRAGAGAMRPPTNSMVGSSMPtGMNVG 921
Cdd:pfam09606  139 --FPSQMSRVGRMQPGGQAGGMMQPSSGQPGSGTPNQMGPNGGPGQGQaggmnGGQQGPMGGQMPPQMGVPGMP-GPADA 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    922 GYGGMNQHQPIG---------------MNQNHPMGMNQNLSMGMNQNYPMGMNQNYPmgmgmnmnmGGYGQGYPMQPQQG 986
Cdd:pfam09606  216 GAQMGQQAQANGgmnpqqmggapnqvaMQQQQPQQQGQQSQLGMGINQMQQMPQGVG---------GGAGQGGPGQPMGP 286

                          250       260       270
                   ....*....|....*....|....*....|.
gi 18411135    987 MGMAPPGAPQGMTGAYNPMMGQGGYNPQQQQ 1017
Cdd:pfam09606  287 PGQQPGAMPNVMSIGDQNNYQQQQTRQQQQQ 317
PHA03247 PHA03247
large tegument protein UL36; Provisional
 252-705 5.66e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   252 RPIEDDGQSSSRDSGAPADDHSQDGRGGLERKFSEQNIGAAPPSYEEAV---SESRSPVYSERDGGETPQVAPP-----G 323
Cdd:PHA03247 2576 RPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPdppPPSPSPAANEPDPHPPPTVPPPerprdD 2655

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   324 AAASPLAENISVDNKAADFVNESSPQQVEAFDEFDPRGSVSAACAPTAGASVPAPIP-PTVVSTPAPPASINAemdllgs 402
Cdd:PHA03247 2656 PAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPhALVSATPLPPGPAAA------- 2728

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   403 lSDVFSPNPLAIVTSDS-TSVETNGQANTGLAPSFSTSQSSTQPFDDPFGDSPFKAITSADTETSQH-QSFGVPFQPTPP 480
Cdd:PHA03247 2729 -RQASPALPAAPAPPAVpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESrESLPSPWDPADP 2807

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   481 TSnpnnehnfgfgeafsAVTDSEPGVQNMQAPPNLSVFPQEQFDTSQSeidilagilPPSGPPVSLSPQPDSTMPTSQFH 560
Cdd:PHA03247 2808 PA---------------AVLAPAAALPPAASPAGPLPPPTSAQPTAPP---------PPPGPPPPSLPLGGSVAPGGDVR 2863

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   561 PNGNSYESYHHQAAPTDLNMQ--GQTPFGQASQQFNMvshsqnhhegmqfnnggftQQPGYAGPATSQPPQyTPGVSSHP 638
Cdd:PHA03247 2864 RRPPSRSPAAKPAAPARPPVRrlARPAVSRSTESFAL-------------------PPDQPERPPQPQAPP-PPQPQPQP 2923

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411135   639 PSESFPhQPGSATSASSQTPYATTPNVS-AGQFDGGSFMTQQPYGVTQQVHVVPSHIPQRTQSGPVAA 705
Cdd:PHA03247 2924 PPPPQP-QPPPPPPPRPQPPLAPTTDPAgAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPA 2990
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 250-668 1.12e-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: 49.77  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    250 RERPIEDDGQSSSRDSGAPADDHSQDGRGGLERKFSEQNIGAAPP-------SYEEAVSESRSPVYSERDGGETPQVAPP 322
Cdd:pfam03154   31 RASPTNEDLRSSGRNSPSAASTSSNDSKAESMKKSSKKIKEEAPSplksakrQREKGASDTEEPERATAKKSKTQEISRP 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    323 GAAAS---------PLAENISVDNKAADFVNES------SPQQVEAFDEFDPRGSVSAACAPTAGASVPAPIPP------ 381
Cdd:pfam03154  111 NSPSEgegessdgrSVNDEGSSDPKDIDQDNRStspsipSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPsppppg 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    382 -TVVSTPAPPASINAeMDLLGSLSDVFSPNPLAIVTSDSTSVETNGQAN-----------TGLAPSFSTSQSSTQPFDDP 449
Cdd:pfam03154  191 tTQAATAGPTPSAPS-VPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHpqrlpsphpplQPMTQPPPPSQVSPQPLPQP 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    450 FGDSPFKAITSADTETSQHQSFGVPFQPTPPTSNPNNehnfGFGEAFSAVTDSEPGVQNMQAPPNLSVFPQEQFDTSQSe 529
Cdd:pfam03154  270 SLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQ----SQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP- 344

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    530 idilagiLPPSgpPVSLSP-QPDSTMPTSQFhPNGNSYESYHHQAAPTDLNMQGQTPFGQASQQFNMVShsqNHHEGMQ- 607
Cdd:pfam03154  345 -------LPPA--PLSMPHiKPPPTTPIPQL-PNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLS---THHPPSAh 411

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18411135    608 ------FNNGGFTQQPGYAGPATSQPPQYTPGVSSHPPsesfphqPGSATSASSQTPYATTPNVSAG 668
Cdd:pfam03154  412 ppplqlMPQSQQLPPPPAQPPVLTQSQSLPPPAASHPP-------TSGLHQVPSQSPFPQHPFVPGG 471
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 33-156 1.25e-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: 43.60  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   33 ATSNESWGPHGSLLADIAHasrnyHEYQITMGVL----WKRLSDS-------------------GKNWRHVYKALTVLEY 89
Cdd:cd16993    8 ATNTDAWGPTPKHLAKVLR-----NRYQVPLYLMteytLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKCLIVIEF 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18411135   90 M---VGHGSE--RVIEEVKEHaYQITTLSGFQY---IDSSGKDQ--GSNVRKKAQSLVALVNDKERITEVREKAAAN 156
Cdd:cd16993   83 LllnVDTGDElnQVLSCLLNH-KHIFTREIAQYkvkFSNDGKMEihERGIQKKCELILQLIEDSDFLRQERAKNKKN 158
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
 176-252 1.26e-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: 42.07  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    176 DYEGRYGDRDEGRSSYGKEREYGYRDDD------RNSRDGDRYSRDSEDRYGRDGNTDDEYRGRSRSVDNYNGSRGRSSD 249
Cdd:pfam12871   11 DEEEEEDEEEDEEASDESERASLSRKRRsrsrrrSSTRDRSRSRSRSRSRDRRSRGTRDRRRDRDRDRYRSLRSRSRDRS 90


                   ...
gi 18411135    250 RER 252
Cdd:pfam12871   91 RDR 93
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 144-283 2.81e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   144 ERITEVREKAAANRDKyhnsMHRPSGGYGDKYDYEGRYGDRDEGRSSYGKEREYGYRDDDRNSRDGDRYSRDSEDRYGRD 223
Cdd:PRK12678  125 AQARERRERGEAARRG----AARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDG 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18411135   224 GNTDDEYRGRSRSVDNYNGSRGRSSDRERPIEDDGQSSSRDSG--APADDHSQDGRGGLERK 283
Cdd:PRK12678  201 DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNreDRGDRDGDDGEGRGGRR 262
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 141-266 2.88e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   141 NDKERITEVREKAAANRDKYHNSMHRPSGGYGDKYDYEGRYGDRDEGRSSYGKEREYGYRDDDRNSRDGDRYSRDSEDRY 220
Cdd:PRK12678  157 RADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRR 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 18411135   221 GRDGNTDDEYRGRSRSvDNYNGSRGRSSDRERPIEDDGQSSSRDSG 266
Cdd:PRK12678  237 DARGDDNREDRGDRDG-DDGEGRGGRRGRRFRDRDRRGRRGGDGGN 281
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 178-283 3.66e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.51  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   178 EGRYGDRDEGRSSYGKEREYGYRDDDRNSRDGDRYSRDSEDRYGRDGNTDDEYRGRSRSVDNYNGS-RGRSSDRERPIED 256
Cdd:PRK12678  162 ERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRgRRRRRDRRDARGD 241

                          90       100
                  ....*....|....*....|....*..
gi 18411135   257 DGQSSSRDSGAPADDHSQDGRGGLERK 283
Cdd:PRK12678  242 DNREDRGDRDGDDGEGRGGRRGRRFRD 268
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 179-259 3.76e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.51  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   179 GRYGDRDEGRSSYGKEREYGYRDDDRNSRDGDRYSRDSEDRYGRDGNTDDEYRGRSRSVDNYNGSRGRSSDRERPIEDDG 258
Cdd:PRK12678  206 RDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGNEREP 285


                  .
gi 18411135   259 Q 259
Cdd:PRK12678  286 E 286
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
 182-264 3.82e-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: 40.53  E-value: 3.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    182 GDRDEGRSSYGKEREYGYRDDDRNSRDGDRYSRDSEDRYGRDGntdDEYRGRSRS-VDNYNGSRGRSSDRERPIEDDGQS 260
Cdd:pfam12871    8 DDLDEEEEEDEEEDEEASDESERASLSRKRRSRSRRRSSTRDR---SRSRSRSRSrDRRSRGTRDRRRDRDRDRYRSLRS 84


                   ....
gi 18411135    261 SSRD 264
Cdd:pfam12871   85 RSRD 88
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 173-263 4.79e-04

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: 44.11  E-value: 4.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    173 DKYDYEGRYGDRDEGRSSYGKEREYGYRDDDRNSRDGDRY--SRD----SEDRYGRDgNTDDEYRGRSRSVDNyngSRGR 246
Cdd:TIGR01642    8 EREKSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYRedSRPrdrrRYDSRSPR-SLRYSSVRRSRDRPR---RRSR 83

                           90
                   ....*....|....*..
gi 18411135    247 SSDRERPIEDDGQSSSR 263
Cdd:TIGR01642   84 SVRSIEQHRRRLRDRSP 100
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 28-124 8.36e-04

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: 40.33  E-value: 8.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   28 QKVLDATSNESWGPHgslLADIAHAsrnyheyqitmgvLWKRLSDsgKNWRHVYKALTVLEYMVGHGSERVIEEVKEHAY 107
Cdd:cd03564   22 RKLLLATSNGGGRAD---VAYIVHA-------------LAKRLHK--KNWIVVLKTLIVIHRLLREGSPSFLEELLRYSG 83

                         90
                 ....*....|....*..
gi 18411135  108 QITTLSGFqyIDSSGKD 124
Cdd:cd03564   84 HIFNLSNF--KDDSSPE 98
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
 227-395 1.16e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 42.24  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   227 DDEYRGRSRSVDnyngSRGRSSDRERPIEDDGQSSSRDSGAPADDHSQDGRGGLERKFSEQNIGAAPPSYEEAVSESRSP 306
Cdd:PTZ00436  166 DEQHRHKARKQE----LRKREKDRERARREDAAAAAAAKQKAAAKKAAAPSGKKSAKAAAPAKAAAAPAKAAAPPAKAAA 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   307 VYSERDGGETPQVAPPGAAASPLAENISVDNKAAdfvneSSPQQVEAFDEFDPRGSVSAACAPTAGASVPAPIPPTVVST 386
Cdd:PTZ00436  242 APAKAAAAPAKAAAPPAKAAAPPAKAAAPPAKAA-----APPAKAAAPPAKAAAPPAKAAAAPAKAAAAPAKAAAAPAKA 316


                  ....*....
gi 18411135   387 PAPPASINA 395
Cdd:PTZ00436  317 AAPPAKAAA 325
PRP38_assoc pfam12871
Pre-mRNA-splicing factor 38-associated hydrophilic C-term; This domain is a hydrophilic region ...
 178-252 1.41e-03

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: 38.99  E-value: 1.41e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18411135    178 EGRYGDRDEGRSSY---GKEREYGYRDDDRNSRDGDRYSRDSEDRYgrdgntdDEYRGRSRSvdnyngsRGRSSDRER 252
Cdd:pfam12871   34 SRKRRSRSRRRSSTrdrSRSRSRSRSRDRRSRGTRDRRRDRDRDRY-------RSLRSRSRD-------RSRDRDRDR 97
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 178-279 1.61e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.20  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   178 EGRYGDRDEGRSSYGKE-REYGYRDDDRNSRDGDRYSRDSEDRYGRDGNTDDEYRGRSRSVDNYNGSRGRSSDRERPIED 256
Cdd:PRK12678  175 RGDREDRQAEAERGERGrREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDD 254

                          90       100
                  ....*....|....*....|....*
gi 18411135   257 DGQSSSRDS--GAPADDHSQDGRGG 279
Cdd:PRK12678  255 GEGRGGRRGrrFRDRDRRGRRGGDG 279
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
 180-256 2.58e-03

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: 41.44  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    180 RYGDRDEGRSSygKEREYGYRDDDRN-SRDGDRySRDSEDRYGRDGNTDdeyRGRSRsvDNYNGSRGRS-----SDRERP 253
Cdd:TIGR01622    1 RYRDRERERLR--DSSSAGDRDRRRDkGRERSR-DRSRDRERSRSRRRD---RHRDR--DYYRGRERRSrsrrpNRRYRP 72


                   ...
gi 18411135    254 IED 256
Cdd:TIGR01622   73 REK 75
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 550-663 2.89e-03

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 41.98  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   550 PDSTMPTSQFHPNGNSYESYH-HQAAPTDLNMQGQTPFGQASQQ---FNMVSHSQNHHEGMQFNNGGFTQqPGYAGPATS 625
Cdd:PTZ00395  347 PNAASAGAPFNGLGNQADGGHiNQVHPDARGAWAGGPHSNASYNcaaYSNAAQSNAAQSNAGFSNAGYSN-PGNSNPGYN 425

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 18411135   626 QPPqYTPGVSSHPPSESFPH-QPGSATSASSQTPYATTP 663
Cdd:PTZ00395  426 NAP-NSNTPYNNPPNSNTPYsNPPNSNPPYSNLPYSNTP 463
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 509-699 4.85e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   509 MQAPPnlsvFPQEQFDTSQSEIDILAGILPPSGPPVsLSPQPDSTMPTSQFHPNGNSYESYHHQAAPTDLNMQGQTPFGQ 588
Cdd:PRK10263  341 TQTPP----VASVDVPPAQPTVAWQPVPGPQTGEPV-IAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQP 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   589 ASQQFNMVSHSQNhhegmqfnnggfTQQPGYAgPATSQPPQYTPGVSShPPSESFPHQPGSATSASSQTPYATTPnvsag 668
Cdd:PRK10263  416 AQQPYYAPAPEQP------------AQQPYYA-PAPEQPVAGNAWQAE-EQQSTFAPQSTYQTEQTYQQPAAQEP----- 476

                         170       180       190
                  ....*....|....*....|....*....|.
gi 18411135   669 qfdggsfMTQQPYGVTQQVHVVPSHIPQRTQ 699
Cdd:PRK10263  477 -------LYQQPQPVEQQPVVEPEPVVEETK 500
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 44-148 5.84e-03

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: 37.55  E-value: 5.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   44 SLLADIAHASRNYHEyqiTMGVLWKRLSDSgkNWRHVYKALTVLEYMVGHG-SERVIEEVKEHAyQITTLSGFQYIDSSG 122
Cdd:cd16988   23 PILLATYSSDASFGE---IVRALSRRLRDN--SWTVVFKSLIVLHLMIREGeTDDVLLYYLSRP-DFLDLRKIRNGSSAG 96

                         90       100
                 ....*....|....*....|....*.
gi 18411135  123 KDQGSNVRKKAQSLvalvndKERITE 148
Cdd:cd16988   97 SGQLQNIQRYAAYL------KERVKE 116
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 246-561 6.08e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 40.33  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    246 RSSDRERPIEDDGQSSSRDSGAPADDHSQDGRGGLErkfSEQNIGAAPPSYEEAVSES---RSPVYSERDGGETPQVAPP 322
Cdd:pfam17823   93 HGTDLSEPATREGAADGAASRALAAAASSSPSSAAQ---SLPAAIAALPSEAFSAPRAaacRANASAAPRAAIAAASAPH 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    323 GAAASPLAENISVDNKAADFVNESSPQQ--VEAFDEFDP-RGSVSAACA---PTAG---ASVP--APIPPTVVS-----T 386
Cdd:pfam17823  170 AASPAPRTAASSTTAASSTTAASSAPTTaaSSAPATLTPaRGISTAATAtghPAAGtalAAVGnsSPAAGTVTAavgtvT 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    387 PAPPASINAEMDLLGSLSDVFS-PNPLAIVTSDSTSVETNGQANTGLAPSFSTSQSStqpfddpfgdspfkaITSADTET 465
Cdd:pfam17823  250 PAALATLAAAAGTVASAAGTINmGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGP---------------IIQVSTDQ 314

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135    466 SQHQSFGvpfQPTPPTSNpnnehnfgfgeafsavTDSEPGVQNMQAPPNLSVFPQEQFDTSQSEidilAGILPPsgPPVS 545
Cdd:pfam17823  315 PVHNTAG---EPTPSPSN----------------TTLEPNTPKSVASTNLAVVTTTKAQAKEPS----ASPVPV--LHTS 369

                          330
                   ....*....|....*.
gi 18411135    546 LSPQPDSTMPTSQFHP 561
Cdd:pfam17823  370 MIPEVEATSPTTQPSP 385
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 182-284 9.03e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 39.89  E-value: 9.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135   182 GDRDEGRSSYGKEREYGYRDDDRNSRDGDRYSRDSEDRYGRDGNTDDEYRGRSRSVDNYNGSRGRSSDRERPIEDDGQSS 261
Cdd:PRK12678  164 TEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDN 243

                          90       100
                  ....*....|....*....|...
gi 18411135   262 SRDSGAPADDHSQDGRGGLERKF 284
Cdd:PRK12678  244 REDRGDRDGDDGEGRGGRRGRRF 266
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 200-391 9.37e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 39.83  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135  200 RDDDRNSRDGDRYSRDSEDRYGRDGNTDDEYRGRSRSVDNYNGSRGRSSDRERPIEDDGQSSSRDSGAPADDHSQDGRGG 279
Cdd:COG3266  165 LALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLLLLLASALGEAVAAAAELAALALLAAGAAEVLTARL 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18411135  280 LERKFSEQNIGAAPPSYEEAVSESRSPVYSERDGGETPQVAP-PGAAASPLAENISVDNKAADFVNESSPQQVEAfdefd 358
Cdd:COG3266  245 VLLLLIIGSALKAPSQASSASAPATTSLGEQQEVSLPPAVAAqPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAA----- 319

                        170       180       190
                 ....*....|....*....|....*....|....
gi 18411135  359 PRGSVSA-ACAPTAGASVPAPIPPTVVSTPAPPA 391
Cdd:COG3266  320 PQPTAAKpVVTETAAPAAPAPEAAAAAAAPAAPA 353
 
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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