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Conserved domains on  [gi|157388929|ref|NP_060427|]
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epsin-3 [Homo sapiens]

Protein Classification

ENTH domain-containing protein( domain architecture ID 13016865)

ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to epsin that plays an important role as accessory proteins in clathrin-mediated endocytosis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 19-142 1.04e-95

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: 289.26  E-value: 1.04e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  19 EAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRE 98
Cdd:cd16990    1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 157388929  99 NLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQ 142
Cdd:cd16990   81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 347-630 3.20e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  347 SPIPSG-TVLSRSQPWDLTPMLSSsepwGRTPVLPAGPPTTDPWALNSPHHKLPSTGADPWGASLETSDTPGGASTfdpf 425
Cdd:PHA03247 2574 APRPSEpAVTSRARRPDAPPQSAR----PRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPT---- 2645

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  426 AKPPESTETKEGLEQALPSGKPSSPVEldlfgDPSPSSKQNGTKEPDALD-LGILGEALTQPSKEaracRTPEsflgPSA 504
Cdd:PHA03247 2646 VPPPERPRDDPAPGRVSRPRRARRLGR-----AAQASSPPQRPRRRAARPtVGSLTSLADPPPPP----PTPE----PAP 2712

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  505 SSLVNLDSLVKAPQVAKTRNPFLTGLSAP--SPTNPFGAGEPGRPTLNQMRTGSPALGLAGGPVGAPLGSMTYSASLPL- 581
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPpaVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLs 2792

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157388929  582 ------PLSSVPAGLTLPASVSVFPQAGAFAPQPLLPTPSSAGPRPPPPQTGTNP 630
Cdd:PHA03247 2793 esreslPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847
UIM smart00726
Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated ...
 209-228 2.57e-03

Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated proteins.


:

Pssm-ID: 197845  Cd Length: 20  Bit Score: 35.58  E-value: 2.57e-03
                           10        20
                   ....*....|....*....|
gi 157388929   209 EEELQLQLALAMSREEAEKP 228
Cdd:smart00726   1 DEDEDLQRALELSLQEAEES 20
UIM smart00726
Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated ...
 236-255 8.58e-03

Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated proteins.


:

Pssm-ID: 197845  Cd Length: 20  Bit Score: 34.04  E-value: 8.58e-03
                           10        20
                   ....*....|....*....|
gi 157388929   236 DEDLQLQLALRLSRQEHEKE 255
Cdd:smart00726   1 DEDEDLQRALELSLQEAEES 20
 
Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 19-142 1.04e-95

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: 289.26  E-value: 1.04e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  19 EAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRE 98
Cdd:cd16990    1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 157388929  99 NLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQ 142
Cdd:cd16990   81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 17-140 1.35e-70

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: 223.97  E-value: 1.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929   17 YSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 157388929   97 RENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERL 140
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
18-144 2.49e-51

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 173.20  E-value: 2.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929    18 SEAEIKVREATSNDPWGPPSSLMSEIADLTFNT-VAFTEVMGMLWRRLNDSGkNWRHVYKALTLLDYLLKTGSERVAHQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 157388929    97 RENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQER 144
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PHA03247 PHA03247
large tegument protein UL36; Provisional
 347-630 3.20e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  347 SPIPSG-TVLSRSQPWDLTPMLSSsepwGRTPVLPAGPPTTDPWALNSPHHKLPSTGADPWGASLETSDTPGGASTfdpf 425
Cdd:PHA03247 2574 APRPSEpAVTSRARRPDAPPQSAR----PRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPT---- 2645

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  426 AKPPESTETKEGLEQALPSGKPSSPVEldlfgDPSPSSKQNGTKEPDALD-LGILGEALTQPSKEaracRTPEsflgPSA 504
Cdd:PHA03247 2646 VPPPERPRDDPAPGRVSRPRRARRLGR-----AAQASSPPQRPRRRAARPtVGSLTSLADPPPPP----PTPE----PAP 2712

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  505 SSLVNLDSLVKAPQVAKTRNPFLTGLSAP--SPTNPFGAGEPGRPTLNQMRTGSPALGLAGGPVGAPLGSMTYSASLPL- 581
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPpaVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLs 2792

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157388929  582 ------PLSSVPAGLTLPASVSVFPQAGAFAPQPLLPTPSSAGPRPPPPQTGTNP 630
Cdd:PHA03247 2793 esreslPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847
UIM smart00726
Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated ...
 209-228 2.57e-03

Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated proteins.


Pssm-ID: 197845  Cd Length: 20  Bit Score: 35.58  E-value: 2.57e-03
                           10        20
                   ....*....|....*....|
gi 157388929   209 EEELQLQLALAMSREEAEKP 228
Cdd:smart00726   1 DEDEDLQRALELSLQEAEES 20
UIM smart00726
Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated ...
 236-255 8.58e-03

Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated proteins.


Pssm-ID: 197845  Cd Length: 20  Bit Score: 34.04  E-value: 8.58e-03
                           10        20
                   ....*....|....*....|
gi 157388929   236 DEDLQLQLALRLSRQEHEKE 255
Cdd:smart00726   1 DEDEDLQRALELSLQEAEES 20
 
Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 19-142 1.04e-95

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: 289.26  E-value: 1.04e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  19 EAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRE 98
Cdd:cd16990    1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 157388929  99 NLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQ 142
Cdd:cd16990   81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 17-140 1.35e-70

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: 223.97  E-value: 1.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929   17 YSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 157388929   97 RENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERL 140
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 17-145 3.03e-70

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: 223.30  E-value: 3.03e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  17 YSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQC 96
Cdd:cd16991    2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157388929  97 RENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERT 145
Cdd:cd16991   82 KENIYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREERS 130
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 20-147 1.88e-64

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: 208.30  E-value: 1.88e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  20 AEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRR-LNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRE 98
Cdd:cd16989    1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRmLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157388929  99 NLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQERTHA 147
Cdd:cd16989   81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKA 129
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 20-136 1.70e-63

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: 1.70e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  20 AEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCREN 99
Cdd:cd03571    1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157388929 100 LYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKD 136
Cdd:cd03571   81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
18-144 2.49e-51

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 173.20  E-value: 2.49e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929    18 SEAEIKVREATSNDPWGPPSSLMSEIADLTFNT-VAFTEVMGMLWRRLNDSGkNWRHVYKALTLLDYLLKTGSERVAHQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 157388929    97 RENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQER 144
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 21-139 1.01e-44

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: 155.30  E-value: 1.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  21 EIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLND-SGKNWRHVYKALTLLDYLLKTGSERVAHQCREN 99
Cdd:cd16992    2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 157388929 100 LYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEER 139
Cdd:cd16992   82 LTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK 121
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 20-136 2.99e-31

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: 117.53  E-value: 2.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  20 AEIKVREATSNDPWGPPSSLMSEIADLTFNT-VAFTEVMGMLWRRLNDsgKNWRHVYKALTLLDYLLKTGSERVAHQCRE 98
Cdd:cd00197    1 FEKTVEKATSNENMGPDWPLIMEICDLINETnVGPKEAVDAIKKRINN--KNPHVVLKALTLLEYCVKNCGERFHQEVAS 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 157388929  99 NLYTIQTLKdFQYIDRDGKDQGVNVREKVKQVMALLKD 136
Cdd:cd00197   79 NDFAVELLK-FDKSGLLGDDVSTNVREKAIELVQLWAS 115
ENTH_Ent4 cd16994
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 ...
 20-138 2.78e-18

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: 81.19  E-value: 2.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  20 AEIKVREAT-SNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLN-----DSGKNWRHVYKALTLLDYLLKTGSERVA 93
Cdd:cd16994    1 TELKVKQATdDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSgnskkSSHKNCVHILKTLTLISYLINNGSNEFI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 157388929  94 HQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEE 138
Cdd:cd16994   81 AWLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDE 125
PHA03247 PHA03247
large tegument protein UL36; Provisional
 347-630 3.20e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  347 SPIPSG-TVLSRSQPWDLTPMLSSsepwGRTPVLPAGPPTTDPWALNSPHHKLPSTGADPWGASLETSDTPGGASTfdpf 425
Cdd:PHA03247 2574 APRPSEpAVTSRARRPDAPPQSAR----PRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPT---- 2645

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  426 AKPPESTETKEGLEQALPSGKPSSPVEldlfgDPSPSSKQNGTKEPDALD-LGILGEALTQPSKEaracRTPEsflgPSA 504
Cdd:PHA03247 2646 VPPPERPRDDPAPGRVSRPRRARRLGR-----AAQASSPPQRPRRRAARPtVGSLTSLADPPPPP----PTPE----PAP 2712

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  505 SSLVNLDSLVKAPQVAKTRNPFLTGLSAP--SPTNPFGAGEPGRPTLNQMRTGSPALGLAGGPVGAPLGSMTYSASLPL- 581
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPpaVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLs 2792

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157388929  582 ------PLSSVPAGLTLPASVSVFPQAGAFAPQPLLPTPSSAGPRPPPPQTGTNP 630
Cdd:PHA03247 2793 esreslPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847
PHA03247 PHA03247
large tegument protein UL36; Provisional
 309-630 7.59e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 7.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  309 PALAPPSTHCSADPWDIPGFRPNTEASGSSWG---PSADPWSPIPSGTVLSRSQPWDLTPMLSSSEPWGRTPvlPAGPPT 385
Cdd:PHA03247 2614 PSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTvppPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR--RAARPT 2691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  386 TDPWA-LNSPHHKLPSTGADPWGASLETSDTPGGAS--------TFDPFAKPPESTETKEGLEQ-----ALPSGKPSSPV 451
Cdd:PHA03247 2692 VGSLTsLADPPPPPPTPEPAPHALVSATPLPPGPAAarqaspalPAAPAPPAVPAGPATPGGPArparpPTTAGPPAPAP 2771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  452 ELDLFGDPSPSskqngTKEPDALDLGILGEALTQPSKEA---RACRTPESFLGPSASSlvnlDSLVKAPQVAKTRNPFLT 528
Cdd:PHA03247 2772 PAAPAAGPPRR-----LTRPAVASLSESRESLPSPWDPAdppAAVLAPAAALPPAASP----AGPLPPPTSAQPTAPPPP 2842

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  529 GLSAPSPTNPFGAGEPGRPTLNQMRTGSPALGLAGgPVGAPLGSMTYSA------SLPLPLSSVPAGLTLPASVSVFPQA 602
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA-PARPPVRRLARPAvsrsteSFALPPDQPERPPQPQAPPPPQPQP 2921

                         330       340       350
                  ....*....|....*....|....*....|.
gi 157388929  603 GAFA---PQPLLPTPSSAGPrPPPPQTGTNP 630
Cdd:PHA03247 2922 QPPPppqPQPPPPPPPRPQP-PLAPTTDPAG 2951
PHA03247 PHA03247
large tegument protein UL36; Provisional
 299-623 3.66e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  299 SILDLADifvPALAPPSTHCSADPW--DIPGFRPNTEASGSSWGPSADPWSP-IPSGTVLSRSQPWDLTPMLSSSEPWGR 375
Cdd:PHA03247 2694 SLTSLAD---PPPPPPTPEPAPHALvsATPLPPGPAAARQASPALPAAPAPPaVPAGPATPGGPARPARPPTTAGPPAPA 2770

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  376 TPVLPAG--PPTTDPWALNSPHHKLPSTGAdPWGASLETSDTPGGASTFDPFAKPPESTETKEGLEQALPSgKPSSPVEl 453
Cdd:PHA03247 2771 PPAAPAAgpPRRLTRPAVASLSESRESLPS-PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPP-PPPGPPP- 2847

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  454 dlfgdpsPSSKQNGTKEPDAlDLGILGEALTQPSKEARACRTPESFLGpsasslvnldslvkAPQVAKTRNPFLTGLSAP 533
Cdd:PHA03247 2848 -------PSLPLGGSVAPGG-DVRRRPPSRSPAAKPAAPARPPVRRLA--------------RPAVSRSTESFALPPDQP 2905

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  534 SPTNPFGAGEPGRPTLNQMRTGSPALGLAGGPVGAPlgsmtysaslPLPLSSVPAGLTLPASVSVFPQAGAFAPQ----P 609
Cdd:PHA03247 2906 ERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQP----------PLAPTTDPAGAGEPSGAVPQPWLGALVPGrvavP 2975

                         330
                  ....*....|....
gi 157388929  610 LLPTPSSAGPRPPP 623
Cdd:PHA03247 2976 RFRVPQPAPSREAP 2989
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 21-144 4.21e-05

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: 44.38  E-value: 4.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  21 EIKVREATSNDPWGPPSSLMSEIAdLTFNTVAFTEVMGMLWRRLNDS-------------------GKNWRHVYKALTLL 81
Cdd:cd16993    2 QIDIRRATNTDAWGPTPKHLAKVL-RNRYQVPLYLMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKCLIVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157388929  82 DYLL---KTGSErvAHQ---CRENLYTIQTLKDFQY---IDRDGKDQ--GVNVREKVKQVMALLKDEERLRQER 144
Cdd:cd16993   81 EFLLlnvDTGDE--LNQvlsCLLNHKHIFTREIAQYkvkFSNDGKMEihERGIQKKCELILQLIEDSDFLRQER 152
VHS cd03561
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ...
 24-127 1.07e-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: 42.25  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  24 VREATSNDPWGPPSSLMSEIADLTF-NTVAFTEVMGMLWRRLNDsgKNWRHVYKALTLLDYLLKTGSERVAHQcrenlyt 102
Cdd:cd03561    5 VEKATSESLTEPDWALNLEICDLVNsDPAQAKDAVRALRKRLQS--KNPKVQLLALTLLETLVKNCGAPFHSE------- 75

                         90       100
                 ....*....|....*....|....*..
gi 157388929 103 IQTLKDFQYIDR--DGKDQGVNVREKV 127
Cdd:cd03561   76 VASRDFLQELVKlvKKKKTSPEVREKA 102
PHA03247 PHA03247
large tegument protein UL36; Provisional
 308-630 2.05e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  308 VPALAPPSTHCSADPWDIPGFRPNTEASGS-SWGPSADPWSPIPSGTVLSRSQPwDLTPMLSSSEPWGRTPVLPAGPPTT 386
Cdd:PHA03247 2555 LPPAAPPAAPDRSVPPPRPAPRPSEPAVTSrARRPDAPPQSARPRAPVDDRGDP-RGPAPPSPLPPDTHAPDPPPPSPSP 2633

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  387 DPWALNSPHhklpsTGADPWGASLETSDTPGGASTFDPFAKPPESTETKEGLEQALPSGKPSSPVELDLFGDPSPSSKqn 466
Cdd:PHA03247 2634 AANEPDPHP-----PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPP-- 2706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  467 gtkEPDALDLGILGEALTQPSKEARACRTPESFLGPSASSLVNLDSLVKAPQvAKTRNPFLTGLSAPSPTNPFGAGEPGR 546
Cdd:PHA03247 2707 ---TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA-RPARPPTTAGPPAPAPPAAPAAGPPRR 2782

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  547 PTLNQMRTGSPALGLAGGPVG-APLGSMTYSASLPLPLSSVPAGlTLPASVSVFPQAGAFAPQPLLPTPSSAGP------ 619
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSPWDpADPPAAVLAPAAALPPAASPAG-PLPPPTSAQPTAPPPPPGPPPPSLPLGGSvapggd 2861

                         330
                  ....*....|....
gi 157388929  620 ---RPPPPQTGTNP 630
Cdd:PHA03247 2862 vrrRPPSRSPAAKP 2875
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 302-630 1.89e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  302 DLADIFVPALAPPSThcSADPWDIPGFRPNTEASGSSWGPSAdPWSPIPSGTVLSRSQPWDLTPMLSSSEPWGRTPVlPA 381
Cdd:PHA03307   49 ELAAVTVVAGAAACD--RFEPPTGPPPGPGTEAPANESRSTP-TWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPP-PA 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  382 GPPTTDPWALNSPHHKLPSTGADPWGASLET--------SDTPGGASTFDPFAKPPEStetkeglEQALPSGKPSSPVEL 453
Cdd:PHA03307  125 SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAgaspaavaSDAASSRQAALPLSSPEET-------ARAPSSPPAEPPPST 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  454 DLFGDPSPSSKQNGTKEPDALDLGILGEaltqpskearacRTPESFLGPSASSLVNLDSLVKA--PQVAKTRNPFLTGLS 531
Cdd:PHA03307  198 PPAAASPRPPRRSSPISASASSPAPAPG------------RSAADDAGASSSDSSSSESSGCGwgPENECPLPRPAPITL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157388929  532 APSPTNPFGAGEPG-RPTLNQMRTGSPALGLAGGPVGAPLGSMTYSASLPLPLSSVP-AGLTLPASVSVFPQAGAFAPQP 609
Cdd:PHA03307  266 PTRIWEASGWNGPSsRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSReSSSSSTSSSSESSRGAAVSPGP 345

                         330       340
                  ....*....|....*....|.
gi 157388929  610 LlPTPSSAGPRPPPPQTGTNP 630
Cdd:PHA03307  346 S-PSRSPSPSRPPPPADPSSP 365
UIM smart00726
Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated ...
 209-228 2.57e-03

Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated proteins.


Pssm-ID: 197845  Cd Length: 20  Bit Score: 35.58  E-value: 2.57e-03
                           10        20
                   ....*....|....*....|
gi 157388929   209 EEELQLQLALAMSREEAEKP 228
Cdd:smart00726   1 DEDEDLQRALELSLQEAEES 20
UIM smart00726
Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated ...
 236-255 8.58e-03

Ubiquitin-interacting motif; Present in proteasome subunit S5a and other ubiquitin-associated proteins.


Pssm-ID: 197845  Cd Length: 20  Bit Score: 34.04  E-value: 8.58e-03
                           10        20
                   ....*....|....*....|
gi 157388929   236 DEDLQLQLALRLSRQEHEKE 255
Cdd:smart00726   1 DEDEDLQRALELSLQEAEES 20
 
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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