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Conserved domains on  [gi|46195711|ref|NP_034277|]
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epsin-1 isoform 1 [Mus musculus]

Protein Classification

ENTH domain-containing protein( domain architecture ID 13016662)

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

CATH:  1.25.40.90
Gene Ontology:  GO:0030276|GO:0005543|GO:0006897|GO:1901981|GO:0072659
PubMed:  10567358|27466364|14657269|12742163|22748146|11911874|29774507
SCOP:  4001355

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 19-142 4.74e-99

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: 296.19  E-value: 4.74e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990   1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 46195711  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 142
Cdd:cd16990  81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 270-437 3.81e-09

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 59.61  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  270 PQASDPWGGPAsvptavpvAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPD 349
Cdd:PRK07764 615 PAAPAAPAAPA--------APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPA 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  350 PWGSSDGGAPVSGPPSSDPWAPAPA--FSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLA 427
Cdd:PRK07764 687 PAAPAAPAGAAPAQPAPAPAATPPAgqADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766

                        170
                 ....*....|
gi 46195711  428 GEVPARSPGA 437
Cdd:PRK07764 767 AAAPAAAPPP 776
 
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 4.74e-99

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: 296.19  E-value: 4.74e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990   1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 46195711  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 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 4.72e-73

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: 228.98  E-value: 4.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711    17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 46195711    97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRL 140
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
18-144 1.22e-52

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 175.51  E-value: 1.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711     18 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 46195711     97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 144
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 270-437 3.81e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 59.61  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  270 PQASDPWGGPAsvptavpvAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPD 349
Cdd:PRK07764 615 PAAPAAPAAPA--------APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPA 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  350 PWGSSDGGAPVSGPPSSDPWAPAPA--FSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLA 427
Cdd:PRK07764 687 PAAPAAPAGAAPAQPAPAPAATPPAgqADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766

                        170
                 ....*....|
gi 46195711  428 GEVPARSPGA 437
Cdd:PRK07764 767 AAAPAAAPPP 776
 
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 4.74e-99

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: 296.19  E-value: 4.74e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990   1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 46195711  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 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 4.72e-73

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: 228.98  E-value: 4.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711    17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 46195711    97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRL 140
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 17-144 2.00e-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: 222.53  E-value: 2.00e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:cd16991   2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWA 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 46195711  97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 144
Cdd:cd16991  82 KENIYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREER 129
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 20-136 2.04e-65

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: 208.91  E-value: 2.04e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  20 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 99
Cdd:cd03571   1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 46195711 100 MYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRD 136
Cdd:cd03571  81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 20-147 2.57e-60

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: 195.97  E-value: 2.57e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  20 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKR-LNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16989   1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRmLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 46195711  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHA 147
Cdd:cd16989  81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKA 129
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
18-144 1.22e-52

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 175.51  E-value: 1.22e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711     18 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 46195711     97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 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 6.08e-46

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: 157.61  E-value: 6.08e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  21 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLND-HGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 99
Cdd:cd16992   2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 46195711 100 MYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDR 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 6.64e-41

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: 143.72  E-value: 6.64e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  20 AEIKVREATSNDPWGPSSSLMSEIADLTYN-VVAFSEIMSMIWKRLNDHgkNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd00197   1 FEKTVEKATSNENMGPDWPLIMEICDLINEtNVGPKEAVDAIKKRINNK--NPHVVLKALTLLEYCVKNCGERFHQEVAS 78

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 46195711  99 NMYAVQTLKdFQYVDRDGKDQGVNVREKAKQLVALLRD 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 1.28e-21

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: 90.43  E-value: 1.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  20 AEIKVREAT-SNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHG-----KNWRHVYKAMTLMEYLIKTGSERVS 93
Cdd:cd16994   1 TELKVKQATdDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSkksshKNCVHILKTLTLISYLINNGSNEFI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 46195711  94 QQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDED 138
Cdd:cd16994  81 AWLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDE 125
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 270-437 3.81e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 59.61  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  270 PQASDPWGGPAsvptavpvAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPD 349
Cdd:PRK07764 615 PAAPAAPAAPA--------APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPA 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  350 PWGSSDGGAPVSGPPSSDPWAPAPA--FSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLA 427
Cdd:PRK07764 687 PAAPAAPAGAAPAQPAPAPAATPPAgqADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766

                        170
                 ....*....|
gi 46195711  428 GEVPARSPGA 437
Cdd:PRK07764 767 AAAPAAAPPP 776
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 21-145 9.52e-09

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: 54.78  E-value: 9.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  21 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFsEIMSMIWKRLNDH-------------------GKNWRHVYKAMTLM 81
Cdd:cd16993   2 QIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLY-LMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKCLIVI 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46195711  82 EYLIKTGS--ERVSQ--QCKENMYAVQTLKDFQY---VDRDGKDQ--GVNVREKAKQLVALLRDEDRLREERA 145
Cdd:cd16993  81 EFLLLNVDtgDELNQvlSCLLNHKHIFTREIAQYkvkFSNDGKMEihERGIQKKCELILQLIEDSDFLRQERA 153
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 267-402 9.36e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.99  E-value: 9.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  267 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPW----GGAAPTPASGDPWRPAAptGPSVDPWGGTPAPAA 342
Cdd:PRK07764 649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaapaGAAPAQPAPAPAATPPA--GQADDPAAQPPQAAQ 726

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  343 GEGPTPdpwGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDE 402
Cdd:PRK07764 727 GASAPS---PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 265-526 9.42e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.10  E-value: 9.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   265 TTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPwggtPAPAAGE 344
Cdd:PHA03307  113 SPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEE----TARAPSS 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   345 GPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELE 424
Cdd:PHA03307  189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   425 LLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPFL 504
Cdd:PHA03307  269 IWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPS 348

                         250       260
                  ....*....|....*....|..
gi 46195711   505 PSGAPPTGPSvtnPFQPAPPAT 526
Cdd:PHA03307  349 RSPSPSRPPP---PADPSSPRK 367
PHA03247 PHA03247
large tegument protein UL36; Provisional
 256-523 1.99e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   256 SLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPT--------PASGDPWRPAAPT 327
Cdd:PHA03247 2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparpPTTAGPPAPAPPA 2773

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   328 GPSVDPWGGTPAPAAGE-----GPTPDPWGSSDGGAPVSG-----PPSSDPWAPAPAFSDPWGGSPAKPS---SNGTAVG 394
Cdd:PHA03247 2774 APAAGPPRRLTRPAVASlsesrESLPSPWDPADPPAAVLApaaalPPAASPAGPLPPPTSAQPTAPPPPPgppPPSLPLG 2853

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   395 GFDTEPDEFSDFDRLRTALPTSGSSTgelellagEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFL 474
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKPAAPA--------RPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 46195711   475 GPnaalvdldslvsRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAP 523
Cdd:PHA03247 2926 PP------------QPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
PHA03247 PHA03247
large tegument protein UL36; Provisional
 310-526 7.44e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 7.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   310 GAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPW---------GSSDGGAPvsgPPSSDPWAPAPAFSDPWG 380
Cdd:PHA03247 2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHPRMLtwirgleelASDDAGDP---PPPLPPAAPPAAPDRSVP 2569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   381 GSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAG---------EVPARSPGAFDMSGVGGSLAESV 451
Cdd:PHA03247 2570 PPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLppdthapdpPPPSPSPAANEPDPHPPPTVPPP 2649

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   452 GSPPPAATPTPTPPTRKTPESFLGPNA--------------ALVDLDSLVSRPGPTPPGSKASNPFLPSGAPPTGPSVTN 517
Cdd:PHA03247 2650 ERPRDDPAPGRVSRPRRARRLGRAAQAssppqrprrraarpTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAAR 2729


                  ....*....
gi 46195711   518 PFQPAPPAT 526
Cdd:PHA03247 2730 QASPALPAA 2738
VHS cd03561
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ...
 24-131 1.21e-05

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: 44.95  E-value: 1.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  24 VREATSNDPWGPSSSLMSEIADLtYNVVAFS--EIMSMIWKRLNDhgKNWRHVYKAMTLMEYLIKTGSERVSQQckenmy 101
Cdd:cd03561   5 VEKATSESLTEPDWALNLEICDL-VNSDPAQakDAVRALRKRLQS--KNPKVQLLALTLLETLVKNCGAPFHSE------ 75

                        90       100       110
                ....*....|....*....|....*....|..
gi 46195711 102 aVQTLKDFQYVDR--DGKDQGVNVREKAKQLV 131
Cdd:cd03561  76 -VASRDFLQELVKlvKKKKTSPEVREKALALI 106
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 266-368 1.37e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  266 TPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK07764 402 AAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPA 481

                         90       100
                 ....*....|....*....|...
gi 46195711  346 PTPDPWGSSDGGAPVSGPPSSDP 368
Cdd:PRK07764 482 PAPPAAPAPAAAPAAPAAPAAPA 504
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 152-439 1.80e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.86  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   152 EKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQ-LALSLSREEHDKEERI 230
Cdd:PHA03307  136 EMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPpAAASPRPPRRSSPISA 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   231 RRGDD--LRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPwgGPAVPPAADPw 308
Cdd:PHA03307  216 SASSPapAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP--GPASSSSSPR- 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   309 gGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDpwGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSS 388
Cdd:PHA03307  293 -ERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSS--SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRP 369

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 46195711   389 NGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFD 439
Cdd:PHA03307  370 RPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAG 420
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 297-402 4.24e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.52  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  297 GGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPW-APAPAF 375
Cdd:PRK07764 595 AGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDgWPAKAG 674

                         90       100
                 ....*....|....*....|....*..
gi 46195711  376 SDPWGGSPAKPSSNGTAVGGFDTEPDE 402
Cdd:PRK07764 675 GAAPAAPPPAPAPAAPAAPAGAAPAQP 701
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
266-434 5.59e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 5.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  266 TPAPPQASdPWGGPASVPTAVPVAAAASdpwggpAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK12323 398 APAAPPAA-PAAAPAAAAAARAVAAAPA------RRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPR 470

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  346 PTPDPwgssDGGAPVSGPPSSDPwAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELEL 425
Cdd:PRK12323 471 PVAAA----AAAAPARAAPAAAP-APADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAP 545


                 ....*....
gi 46195711  426 LAGEVPARS 434
Cdd:PRK12323 546 AAAPAPRAA 554
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 277-395 5.87e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  277 GGPASVPTAVPVAAAASDPWGGPAVPPAADP----WGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPT--PDP 350
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAapaaPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASdgGDG 668

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 46195711  351 WGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGG 395
Cdd:PRK07764 669 WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQ 713
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 269-471 8.94e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 8.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  269 PPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGA-APTPASGDPWRPAAPTGPSVDPWGGTPAPAagegpT 347
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAaAPAEASAAPAPGVAAPEHHPKHVAVPDASD-----G 665

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  348 PDPWGSSDGGAPVSGPPSSDPWAPAPAfsdPWGGSPAKPSSNGTAvggfdTEPDEFSDFDRLRTALPTSGSSTGELELLA 427
Cdd:PRK07764 666 GDGWPAKAGGAAPAAPPPAPAPAAPAA---PAGAAPAQPAPAPAA-----TPPAGQADDPAAQPPQAAQGASAPSPAADD 737

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 46195711  428 GEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPE 471
Cdd:PRK07764 738 PVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 297-392 1.42e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.98  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  297 GGPAVPPAADPwGGAAPTPASGDPWRPAAPTGPsvdpwggTPAPAAGEGPTPDPWGSSDGGAPVS--GPPSSDPWAPAPA 374
Cdd:PRK07764 400 SAAAAAPAAAP-APAAAAPAAAAAPAPAAAPQP-------APAPAPAPAPPSPAGNAPAGGAPSPppAAAPSAQPAPAPA 471

                         90
                 ....*....|....*...
gi 46195711  375 FSDPWGGSPAKPSSNGTA 392
Cdd:PRK07764 472 AAPEPTAAPAPAPPAAPA 489
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 265-374 1.62e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  265 TTPAPPQASDPWGGPASVPTAVPVAAAASDPwgGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPA--PAA 342
Cdd:PRK07764 391 AGAPAAAAPSAAAAAPAAAPAPAAAAPAAAA--APAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSaqPAP 468

                         90       100       110
                 ....*....|....*....|....*....|..
gi 46195711  343 GEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPA 374
Cdd:PRK07764 469 APAAAPEPTAAPAPAPPAAPAPAAAPAAPAAP 500
PHA03247 PHA03247
large tegument protein UL36; Provisional
 268-526 2.04e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   268 APPQASDPWGGP-----ASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPAS---GDPWRPAAPTGPSVDPWGGTPA 339
Cdd:PHA03247 2491 AAGAAPDPGGGGppdpdAPPAPSRLAPAILPDEPVGEPVHPRMLTWIRGLEELASddaGDPPPPLPPAAPPAAPDRSVPP 2570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   340 PAAGEGPtPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVggfdTEPDEFSDFDRlrtalptsGSS 419
Cdd:PHA03247 2571 PRPAPRP-SEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHA----PDPPPPSPSPA--------ANE 2637

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   420 TGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKA 499
Cdd:PHA03247 2638 PDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVS 2717

                         250       260
                  ....*....|....*....|....*..
gi 46195711   500 SNPFLPSGAPPTGPSVTNPFQPAPPAT 526
Cdd:PHA03247 2718 ATPLPPGPAAARQASPALPAAPAPPAV 2744
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 279-526 2.22e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  279 PASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPwgssdGGA 358
Cdd:PRK07764 395 AAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQP-----APA 469

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  359 PVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEfSDFDRLRTALPTSGSSTGELeLLAGEVPARSPG-- 436
Cdd:PRK07764 470 PAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLR-ERWPEILAAVPKRSRKTWAI-LLPEATVLGVRGdt 547

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  437 ---AFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAAlvdldsLVSRPGPTPPGSKASNPFLPSGAPPTGP 513
Cdd:PRK07764 548 lvlGFSTGGLARRFASPGNAEVLVTALAEELGGDWQVEAVVGPAPG------AAGGEGPPAPASSGPPEEAARPAAPAAP 621

                        250
                 ....*....|...
gi 46195711  514 SVTNPFQPAPPAT 526
Cdd:PRK07764 622 AAPAAPAPAGAAA 634
PHA03247 PHA03247
large tegument protein UL36; Provisional
 268-525 2.55e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   268 APPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPT 347
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   348 PDPWGSSDGGAPVSG------------PPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPT 415
Cdd:PHA03247 2680 PQRPRRRAARPTVGSltsladppppppTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   416 SGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPP 495
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839

                         250       260       270
                  ....*....|....*....|....*....|
gi 46195711   496 gSKASNPFLPSGAPPTGPSVTNPFQPAPPA 525
Cdd:PHA03247 2840 -PPPPGPPPPSLPLGGSVAPGGDVRRRPPS 2868
PHA03247 PHA03247
large tegument protein UL36; Provisional
 299-374 2.59e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 2.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46195711   299 PAVPPAADPWGGAAPTPAsgdpwRPAAPTGPSVDPwggtPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPA 374
Cdd:PHA03247  255 PAPPPVVGEGADRAPETA-----RGATGPPPPPEA----AAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPA 321
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 298-394 3.00e-04

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 43.46  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  298 GPAVPPAADpwgGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGP---------PSSDP 368
Cdd:PHA03264 263 GYEPPPAPS---GGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPprpapdadrPEGWP 339

                         90       100
                 ....*....|....*....|....*.
gi 46195711  369 WAPAPAFSDPWGGSPAKPSSNGTAVG 394
Cdd:PHA03264 340 SLEAITFPPPTPATPAVPRARPVIVG 365
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 265-394 3.56e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  265 TTPAPPQASDPWGGPASvptaVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSV--DPWGGTPAPAA 342
Cdd:PRK07764 679 AAPPPAPAPAAPAAPAG----AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLppEPDDPPDPAGA 754

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46195711  343 GEGPTPDPWgSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVG 394
Cdd:PRK07764 755 PAQPPPPPA-PAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVA 805
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
267-432 4.32e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 4.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  267 PAPPQASDPWG-GPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPwRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK12323 415 AARAVAAAPARrSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGP-RPVAAAAAAAPARAAPAAAPAPAD 493

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  346 PTPDPWGSSDGGAPVSGPPSSDPwAPAPA----FSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTG 421
Cdd:PRK12323 494 DDPPPWEELPPEFASPAPAQPDA-APAGWvaesIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASG 572

                        170
                 ....*....|.
gi 46195711  422 ELELLAGEVPA 432
Cdd:PRK12323 573 LPDMFDGDWPA 583
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
261-433 5.18e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  261 ADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGP--AVPPAADPWGG----AAPTPASGDPWRPAAPTGPSVDPW 334
Cdd:PRK12323 420 AAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPaaAARPAAAGPRPvaaaAAAAPARAAPAAAPAPADDDPPPW 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  335 GGTPAPAAGEGP-TPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDfdrlrtal 413
Cdd:PRK12323 500 EELPPEFASPAPaQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASAS-------- 571

                        170       180
                 ....*....|....*....|
gi 46195711  414 PTSGSSTGELELLAGEVPAR 433
Cdd:PRK12323 572 GLPDMFDGDWPALAARLPVR 591
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 266-381 9.91e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.01  E-value: 9.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  266 TPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK14951 380 TPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPET 459

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 46195711  346 PTPDPWGSSDGGAPVSGPPSSDPWAPAP----AFSDPWGG 381
Cdd:PRK14951 460 VAIPVRVAPEPAVASAAPAPAAAPAAARltptEEGDVWHA 499
PHA03247 PHA03247
large tegument protein UL36; Provisional
 269-526 1.10e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   269 PPQASDP---WGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTP---ASGDPWRPAAPTGPSVDPWGGTPAPAA 342
Cdd:PHA03247 2673 AAQASSPpqrPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPpgpAAARQASPALPAAPAPPAVPAGPATPG 2752

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   343 GEGPTPDPWGSSdgGAPVSGPPSSDPWAPAPAFSDPwGGSPAKPSSNgtavggfdtepdefsdfdrlrtALPTSGSSTGE 422
Cdd:PHA03247 2753 GPARPARPPTTA--GPPAPAPPAAPAAGPPRRLTRP-AVASLSESRE----------------------SLPSPWDPADP 2807

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   423 LELLAGEVPARSPGAFDMSGVggslaesvgSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNP 502
Cdd:PHA03247 2808 PAAVLAPAAALPPAASPAGPL---------PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAP 2878

                         250       260       270
                  ....*....|....*....|....*....|..
gi 46195711   503 --------FLPSGAPPTGPSVTNPFQPAPPAT 526
Cdd:PHA03247 2879 arppvrrlARPAVSRSTESFALPPDQPERPPQ 2910
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 272-526 1.92e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   272 ASDPWGGPASVPTAVPVAAAASDPWGGPAV-PPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDP 350
Cdd:PHA03307   44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPgPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   351 wgssDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEV 430
Cdd:PHA03307  124 ----ASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPP 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   431 PARSPGAfdmSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPtPPGSKASNPFLPSGAPP 510
Cdd:PHA03307  200 AAASPRP---PRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLP-RPAPITLPTRIWEASGW 275

                         250
                  ....*....|....*.
gi 46195711   511 TGPSVTnpFQPAPPAT 526
Cdd:PHA03307  276 NGPSSR--PGPASSSS 289
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 265-359 2.86e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.43  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  265 TTPAPPQASDPWGGPASVPTAVPVAAAASDPwggPAVPPAADPWGGAAPTPA-SGDPWRPaAPTGPSVDPWGGTPAPAAG 343
Cdd:PRK14959 396 TIPTPGTQGPQGTAPAAGMTPSSAAPATPAP---SAAPSPRVPWDDAPPAPPrSGIPPRP-APRMPEASPVPGAPDSVAS 471

                         90
                 ....*....|....*.
gi 46195711  344 EGPTPDPWGSSDGGAP 359
Cdd:PRK14959 472 ASDAPPTLGDPSDTAE 487
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 266-375 2.94e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 40.48  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  266 TPAPPQASDPWGGPASVPTAVPvaaaasDPWGGPAVPPAADPWGGAAPTPASGDPWRPA-APTGPSVDPWGGTPAPAAGE 344
Cdd:PHA03269  33 TSAATQKPDPAPAPHQAASRAP------DPAVAPTSAASRKPDLAQAPTPAASEKFDPApAPHQAASRAPDPAVAPQLAA 106

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 46195711  345 GPTPDPW-----GSSDGGAPVSGPPSSDPWAPAPAF 375
Cdd:PHA03269 107 APKPDAAeaftsAAQAHEAPADAGTSAASKKPDPAA 142
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 300-388 3.68e-03

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 40.26  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   300 AVPPA-----ADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPA 374
Cdd:PRK12270   24 SVDPSwreffADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAA 103

                          90
                  ....*....|....
gi 46195711   375 FSDPWGGSPAKPSS 388
Cdd:PRK12270  104 AAAAPAAAAVEDEV 117
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 266-359 4.12e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  266 TPAPPQASDPWGGPASVPTAVPVAaaaSDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK07764 422 APAPAAAPQPAPAPAPAPAPPSPA---GNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPA 498

                         90
                 ....*....|....
gi 46195711  346 PTPDPWGSSDGGAP 359
Cdd:PRK07764 499 APAAPAGADDAATL 512
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
267-524 4.49e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  267 PAPPQASDPWGG-PASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGE- 344
Cdd:PRK07003 360 PAVTGGGAPGGGvPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRg 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  345 -----GPTPDPWGSSDGGAPVSGPPSSD------------PWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFD 407
Cdd:PRK07003 440 ddaadGDAPVPAKANARASADSRCDERDaqppadsgsasaPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASRE 519

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711  408 RLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTptpptrkTPESFLGPNAALVDLDSLV 487
Cdd:PRK07003 520 DAPAAAAPPAPEARPPTPAAAAPAARAGGAAAALDVLRNAGMRVSSDRGARAAA-------AAKPAAAPAAAPKPAAPRV 592

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 46195711  488 SRPGPTPPGSKASNPFLPSGAPPTGPSVTNPfQPAPP 524
Cdd:PRK07003 593 AVQVPTPRARAATGDAPPNGAARAEQAAESR-GAPPP 628
PHA03247 PHA03247
large tegument protein UL36; Provisional
 266-572 8.26e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   266 TPAPPQASDPWGGPASVPTAVPVAAAASDPWGG----PAVPPaaDPWGGAAPTPASGDPWRPAAPTGPSVDPwggTPAPA 341
Cdd:PHA03247 2552 PPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSrarrPDAPP--QSARPRAPVDDRGDPRGPAPPSPLPPDT---HAPDP 2626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   342 AGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPwggsPAKPSSNGTAvggfdTEPDEFSDFDRLRTALPTSGSSTG 421
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR----PRRARRLGRA-----AQASSPPQRPRRRAARPTVGSLTS 2697

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46195711   422 ELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTptpptrkTPESFLGPNAALVDLdslvsrpGPTPPGSKASN 501
Cdd:PHA03247 2698 LADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPA-------APAPPAVPAGPATPG-------GPARPARPPTT 2763

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46195711   502 PFLPSGAPPTGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNP 572
Cdd:PHA03247 2764 AGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSA 2834
 
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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