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Conserved domains on  [gi|755519085|ref|XP_006539594|]
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epsin-1 isoform X1 [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 4.87e-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: 4.87e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990    1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755519085  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLRE 142
Cdd:cd16990   81 NIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 267-393 1.76e-07

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: 54.22  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 267 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPW----GGAAPTPASGDPWRPAAptGPSVDPWGGTPAPAA 342
Cdd:PRK07764 649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaapaGAAPAQPAPAPAATPPA--GQADDPAAQPPQAAQ 726

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755519085 343 GEGPTPdpwGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAA 393
Cdd:PRK07764 727 GASAPS---PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 256-524 1.77e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  256 SLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPT--------PASGDPWRPAAPT 327
Cdd:PHA03247 2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparpPTTAGPPAPAPPA 2773

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  328 GPSVDPWGGTPAPAAGE-----GPTPDPWGSSDGGAPVSG-----PPSSDPWAPAPAFSDPWGGSPAKPS--SNGTAAVG 395
Cdd:PHA03247 2774 APAAGPPRRLTRPAVASlsesrESLPSPWDPADPPAAVLApaaalPPAASPAGPLPPPTSAQPTAPPPPPgpPPPSLPLG 2853

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  396 GFDTEPDEFSDFDRLRTALPTSGSSTgelellagEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFL 475
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKPAAPA--------RPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 755519085  476 GPnaalvdldslvsRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAP 524
Cdd:PHA03247 2926 PP------------QPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
 
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 4.87e-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: 4.87e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990    1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755519085  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 4.83e-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: 4.83e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085   17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 755519085   97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRL 140
Cdd:pfam01417  81 RENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
18-144 1.24e-52

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 175.51  E-value: 1.24e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085    18 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 755519085    97 KENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER 144
Cdd:smart00273  80 LRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 267-393 1.76e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.22  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 267 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPW----GGAAPTPASGDPWRPAAptGPSVDPWGGTPAPAA 342
Cdd:PRK07764 649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaapaGAAPAQPAPAPAATPPA--GQADDPAAQPPQAAQ 726

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755519085 343 GEGPTPdpwGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAA 393
Cdd:PRK07764 727 GASAPS---PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774
PHA03247 PHA03247
large tegument protein UL36; Provisional
 256-524 1.77e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  256 SLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPT--------PASGDPWRPAAPT 327
Cdd:PHA03247 2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparpPTTAGPPAPAPPA 2773

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  328 GPSVDPWGGTPAPAAGE-----GPTPDPWGSSDGGAPVSG-----PPSSDPWAPAPAFSDPWGGSPAKPS--SNGTAAVG 395
Cdd:PHA03247 2774 APAAGPPRRLTRPAVASlsesrESLPSPWDPADPPAAVLApaaalPPAASPAGPLPPPTSAQPTAPPPPPgpPPPSLPLG 2853

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  396 GFDTEPDEFSDFDRLRTALPTSGSSTgelellagEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFL 475
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKPAAPA--------RPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 755519085  476 GPnaalvdldslvsRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAP 524
Cdd:PHA03247 2926 PP------------QPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
 
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 4.87e-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: 4.87e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990    1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 755519085  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 4.83e-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: 4.83e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085   17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 755519085   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 2.04e-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: 2.04e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:cd16991    2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755519085  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 2.09e-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: 2.09e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  20 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 99
Cdd:cd03571    1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755519085 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 2.62e-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: 2.62e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  20 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKR-LNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16989    1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRmLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 755519085  99 NMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHA 147
Cdd:cd16989   81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKA 129
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
18-144 1.24e-52

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 175.51  E-value: 1.24e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085    18 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 755519085    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 6.16e-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: 6.16e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  21 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLND-HGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 99
Cdd:cd16992    2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755519085 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 6.71e-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: 6.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  20 AEIKVREATSNDPWGPSSSLMSEIADLTYN-VVAFSEIMSMIWKRLNDHgkNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd00197    1 FEKTVEKATSNENMGPDWPLIMEICDLINEtNVGPKEAVDAIKKRINNK--NPHVVLKALTLLEYCVKNCGERFHQEVAS 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755519085  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 1.29e-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: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  20 AEIKVREAT-SNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHG-----KNWRHVYKAMTLMEYLIKTGSERVS 93
Cdd:cd16994    1 TELKVKQATdDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSkksshKNCVHILKTLTLISYLINNGSNEFI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 755519085  94 QQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDED 138
Cdd:cd16994   81 AWLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDE 125
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 21-145 9.54e-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: 9.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  21 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFsEIMSMIWKRLNDH-------------------GKNWRHVYKAMTLM 81
Cdd:cd16993    2 QIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLY-LMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKCLIVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755519085  82 EYLIKTGS--ERVSQ--QCKENMYAVQTLKDFQY---VDRDGKDQ--GVNVREKAKQLVALLRDEDRLREERA 145
Cdd:cd16993   81 EFLLLNVDtgDELNQvlSCLLNHKHIFTREIAQYkvkFSNDGKMEihERGIQKKCELILQLIEDSDFLRQERA 153
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 267-393 1.76e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.22  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 267 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPW----GGAAPTPASGDPWRPAAptGPSVDPWGGTPAPAA 342
Cdd:PRK07764 649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaapaGAAPAQPAPAPAATPPA--GQADDPAAQPPQAAQ 726

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755519085 343 GEGPTPdpwGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAA 393
Cdd:PRK07764 727 GASAPS---PAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 270-438 3.53e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 53.45  E-value: 3.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 270 PQASDPWGGPAsvptavpvAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDP-WGGTPAPAAGEGPTP 348
Cdd:PRK07764 615 PAAPAAPAAPA--------APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPaKAGGAAPAAPPPAPA 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 349 DPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLA 428
Cdd:PRK07764 687 PAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766

                        170
                 ....*....|
gi 755519085 429 GEVPARSPGA 438
Cdd:PRK07764 767 AAAPAAAPPP 776
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 269-396 1.18e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.53  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 269 PPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGA-APTPASGDPWRPAAPTGPSVDPWGGTPAPAagegpT 347
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAaAPAEASAAPAPGVAAPEHHPKHVAVPDASD-----G 665

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 755519085 348 PDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGG 396
Cdd:PRK07764 666 GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQA 714
PHA03247 PHA03247
large tegument protein UL36; Provisional
 256-524 1.77e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  256 SLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPT--------PASGDPWRPAAPT 327
Cdd:PHA03247 2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparpPTTAGPPAPAPPA 2773

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  328 GPSVDPWGGTPAPAAGE-----GPTPDPWGSSDGGAPVSG-----PPSSDPWAPAPAFSDPWGGSPAKPS--SNGTAAVG 395
Cdd:PHA03247 2774 APAAGPPRRLTRPAVASlsesrESLPSPWDPADPPAAVLApaaalPPAASPAGPLPPPTSAQPTAPPPPPgpPPPSLPLG 2853

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  396 GFDTEPDEFSDFDRLRTALPTSGSSTgelellagEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFL 475
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKPAAPA--------RPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 755519085  476 GPnaalvdldslvsRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAP 524
Cdd:PHA03247 2926 PP------------QPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQP 2962
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 265-527 3.84e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.17  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  265 TTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPwggtPAPAAGE 344
Cdd:PHA03307  113 SPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEE----TARAPSS 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  345 GPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKpSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGEL 424
Cdd:PHA03307  189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA-DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPT 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  425 ELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPF 504
Cdd:PHA03307  268 RIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSP 347

                         250       260
                  ....*....|....*....|...
gi 755519085  505 LPSGAPPTGPSvtnPFQPAPPAT 527
Cdd:PHA03307  348 SRSPSPSRPPP---PADPSSPRK 367
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 755519085  24 VREATSNDPWGPSSSLMSEIADLtYNVVAFS--EIMSMIWKRLNDhgKNWRHVYKAMTLMEYLIKTGSERVSQQckenmy 101
Cdd:cd03561    5 VEKATSESLTEPDWALNLEICDL-VNSDPAQakDAVRALRKRLQS--KNPKVQLLALTLLETLVKNCGAPFHSE------ 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 755519085 102 aVQTLKDFQYVDR--DGKDQGVNVREKAKQLV 131
Cdd:cd03561   76 -VASRDFLQELVKlvKKKKTSPEVREKALALI 106
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 266-368 1.39e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 266 TPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK07764 402 AAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPA 481

                         90       100
                 ....*....|....*....|...
gi 755519085 346 PTPDPWGSSDGGAPVSGPPSSDP 368
Cdd:PRK07764 482 PAPPAAPAPAAAPAAPAAPAAPA 504
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 152-393 1.88e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.86  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  152 EKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEE--- 228
Cdd:PHA03307  136 EMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPisa 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  229 -----RIRRGDDLRL-------QMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPw 296
Cdd:PHA03307  216 sasspAPAPGRSAADdagasssDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRER- 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  297 gGPAVPPAADPWGGAAPTPASGDPWRP--------AAPTGPSVDPWGGTPAPAAGEGPTPdpwGSSDGGAPVSGPPSSDP 368
Cdd:PHA03307  295 -SPSPSPSSPGSGPAPSSPRASSSSSSsresssssTSSSSESSRGAAVSPGPSPSRSPSP---SRPPPPADPSSPRKRPR 370

                         250       260
                  ....*....|....*....|....*
gi 755519085  369 WAPAPAFSDPWGGSPAKPSSNGTAA 393
Cdd:PHA03307  371 PSRAPSSPAASAGRPTRRRARAAVA 395
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 297-527 2.54e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.29  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 297 GGPAVPPAADPwGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGG-------APVSGPPSSDPW 369
Cdd:PRK07764 400 SAAAAAPAAAP-APAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAaapsaqpAPAPAAAPEPTA 478

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 370 APAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELeLLAGEVPARSPG-----AFDMSGV 444
Cdd:PRK07764 479 APAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAI-LLPEATVLGVRGdtlvlGFSTGGL 557

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 445 GGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAAlvdldsLVSRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAP 524
Cdd:PRK07764 558 ARRFASPGNAEVLVTALAEELGGDWQVEAVVGPAPG------AAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAG 631


                 ...
gi 755519085 525 PAT 527
Cdd:PRK07764 632 AAA 634
PHA03247 PHA03247
large tegument protein UL36; Provisional
 272-573 5.96e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 5.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  272 ASDPWGGPASVPTAVPVAAAA--SDPWGGPAVPPAADPWGGAAPTP-ASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTP 348
Cdd:PHA03247 2544 ASDDAGDPPPPLPPAAPPAAPdrSVPPPRPAPRPSEPAVTSRARRPdAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHA 2623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  349 DPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLA 428
Cdd:PHA03247 2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPP 2703

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  429 GEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTptpptrkTPESFLGPNAALVDLdslvsrpGPTPPGSKASNPFLPSG 508
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPA-------APAPPAVPAGPATPG-------GPARPARPPTTAGPPAP 2769

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755519085  509 APPTGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNP 573
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSA 2834
PHA03247 PHA03247
large tegument protein UL36; Provisional
 299-534 7.44e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  299 PAVPPAADPWGGAAPTPAsgdpwRPAAPTGPSVDPwggtPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAfsdp 378
Cdd:PHA03247  255 PAPPPVVGEGADRAPETA-----RGATGPPPPPEA----AAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPA---- 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  379 wGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARS---PGAFDMSGVGGSLAESVGSP 455
Cdd:PHA03247  322 -GDAEEEDDEDGAMEVVSPLPRPRQHYPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRaslPTRKRRSARHAATPFARGPG 400

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755519085  456 PPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPfLPSGAPPTGPSVTNPFQPAPPATLTLNQLR 534
Cdd:PHA03247  401 GDDQTRPAAPVPASVPTPAPTPVPASAPPPPATPLPSAEPGSDDGPAP-PPERQPPAPATEPAPDDPDDATRKALDALR 478
PHA03247 PHA03247
large tegument protein UL36; Provisional
 310-527 2.19e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  310 GAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPW---------GSSDGGAPvsgPPSSDPWAPAPAFSDPWG 380
Cdd:PHA03247 2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHPRMLtwirgleelASDDAGDP---PPPLPPAAPPAAPDRSVP 2569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  381 GSPAKPSSNGtAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAG---------EVPARSPGAFDMSGVGGSLAES 451
Cdd:PHA03247 2570 PPRPAPRPSE-PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLppdthapdpPPPSPSPAANEPDPHPPPTVPP 2648

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  452 VGSPPPAATPTPTPPTRKTPESFLGPNA--------------ALVDLDSLVSRPGPTPPGSKASNPFLPSGAPPTGPSVT 517
Cdd:PHA03247 2649 PERPRDDPAPGRVSRPRRARRLGRAAQAssppqrprrraarpTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAA 2728

                         250
                  ....*....|
gi 755519085  518 NPFQPAPPAT 527
Cdd:PHA03247 2729 RQASPALPAA 2738
PHA03247 PHA03247
large tegument protein UL36; Provisional
 268-530 3.03e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  268 APPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPT 347
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  348 PDPWGSSDGGAPV-----SGPPSSDPWAPAPAfsdPWGGSPAKPSSNGTAAVGGFDTEPdefsdfdrlrTALPTSGSSTG 422
Cdd:PHA03247 2680 PQRPRRRAARPTVgsltsLADPPPPPPTPEPA---PHALVSATPLPPGPAAARQASPAL----------PAAPAPPAVPA 2746

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  423 ELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAAlVDLDSLVSRPGPTPPGSKASN 502
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP-ADPPAAVLAPAAALPPAASPA 2825

                         250       260
                  ....*....|....*....|....*...
gi 755519085  503 PFLPsgaPPTGPSVTNPFQPAPPATLTL 530
Cdd:PHA03247 2826 GPLP---PPTSAQPTAPPPPPGPPPPSL 2850
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
266-435 3.94e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.33  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 266 TPAPPQASdPWGGPASVPTAVPVAAAASdpwggpAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK12323 398 APAAPPAA-PAAAPAAAAAARAVAAAPA------RRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPR 470

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 346 PTPDPwgssDGGAPVSGPPSSDPwAPAPAFSDPWGGSPAKPSSNGTAAVGGfDTEPDEFSDFDRLRTALPTSGSSTGELE 425
Cdd:PRK12323 471 PVAAA----AAAAPARAAPAAAP-APADDDPPPWEELPPEFASPAPAQPDA-APAGWVAESIPDPATADPDDAFETLAPA 544

                        170
                 ....*....|
gi 755519085 426 LLAGEVPARS 435
Cdd:PRK12323 545 PAAAPAPRAA 554
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 265-378 4.05e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 4.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 265 TTPAPPQASDPWGGPASvptaVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSV--DPWGGTPAPAA 342
Cdd:PRK07764 679 AAPPPAPAPAAPAAPAG----AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLppEPDDPPDPAGA 754

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755519085 343 GEGPTPDPWgSSDGGAPVSGPPSSDPWAPAPAFSDP 378
Cdd:PRK07764 755 PAQPPPPPA-PAPAAAPAAAPPPSPPSEEEEMAEDD 789
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 298-396 4.77e-04

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 42.68  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 298 GPAVPPAADpwgGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPafsD 377
Cdd:PHA03264 263 GYEPPPAPS---GGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDADRP---E 336

                         90
                 ....*....|....*....
gi 755519085 378 PWGGSPAKPSSNGTAAVGG 396
Cdd:PHA03264 337 GWPSLEAITFPPPTPATPA 355
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 297-393 7.35e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 7.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 297 GGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGE-----GPTPDPWGSSDGGAPVSGPPSSDPWAP 371
Cdd:PRK14951 371 EAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPaaappAPVAAPAAAAPAAAPAAAPAAVALAPA 450

                         90       100
                 ....*....|....*....|..
gi 755519085 372 APAFSDPWGGSPAKPSSNGTAA 393
Cdd:PRK14951 451 PPAQAAPETVAIPVRVAPEPAV 472
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
265-404 1.01e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 265 TTPAPPQASDPWGGPASVPTAVPVAAAASDPwggPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGE 344
Cdd:PRK12323 372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAP---PAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAP 448

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 345 GPTPDPWGSSDGGAPVSGPPSSDPwaPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEF 404
Cdd:PRK12323 449 APAPAPAAAPAAAARPAAAGPRPV--AAAAAAAPARAAPAAAPAPADDDPPPWEELPPEF 506
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 266-381 1.02e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.01  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 266 TPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK14951 380 TPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPET 459

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755519085 346 PTPDPWGSSDGGAPVSGPPSSDPWAPAP----AFSDPWGG 381
Cdd:PRK14951 460 VAIPVRVAPEPAVASAAPAPAAAPAAARltptEEGDVWHA 499
PHA03247 PHA03247
large tegument protein UL36; Provisional
 269-527 1.56e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  269 PPQASDP---WGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTP---ASGDPWRPAAPTGPSVDPWGGTPAPAA 342
Cdd:PHA03247 2673 AAQASSPpqrPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPpgpAAARQASPALPAAPAPPAVPAGPATPG 2752

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  343 GEGPTPDPWGSSdgGAPVSGPPSSDPWAPAPAFSDPwGGSPAKPSSNgtaavggfdtepdefsdfdrlrtALPTSGSSTG 422
Cdd:PHA03247 2753 GPARPARPPTTA--GPPAPAPPAAPAAGPPRRLTRP-AVASLSESRE-----------------------SLPSPWDPAD 2806

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  423 ELELLAGEVPARSPGAFDMSGVggslaesvgSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASN 502
Cdd:PHA03247 2807 PPAAVLAPAAALPPAASPAGPL---------PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA 2877

                         250       260       270
                  ....*....|....*....|....*....|...
gi 755519085  503 P--------FLPSGAPPTGPSVTNPFQPAPPAT 527
Cdd:PHA03247 2878 ParppvrrlARPAVSRSTESFALPPDQPERPPQ 2910
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
267-402 1.61e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 267 PAPPQASDPWGG-PASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK07003 360 PAVTGGGAPGGGvPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRG 439

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755519085 346 ptpdpwgssDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPD 402
Cdd:PRK07003 440 ---------DDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPD 487
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
261-394 2.31e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 261 ADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGP--AVPPAADPWGG----AAPTPASGDPWRPAAPTGPSVDPW 334
Cdd:PRK12323 420 AAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPaaAARPAAAGPRPvaaaAAAAPARAAPAAAPAPADDDPPPW 499

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755519085 335 GGTPAPAAGEGP-TPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAV 394
Cdd:PRK12323 500 EELPPEFASPAPaQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPV 560
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 300-393 2.74e-03

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


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 40.64  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  300 AVPPA-----ADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPA 374
Cdd:PRK12270   24 SVDPSwreffADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAA 103

                          90       100
                  ....*....|....*....|..
gi 755519085  375 FSDPWGGSPAKPSSN---GTAA 393
Cdd:PRK12270  104 AAAAPAAAAVEDEVTplrGAAA 125
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 265-359 2.89e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.43  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 265 TTPAPPQASDPWGGPASVPTAVPVAAAASDPwggPAVPPAADPWGGAAPTPA-SGDPWRPaAPTGPSVDPWGGTPAPAAG 343
Cdd:PRK14959 396 TIPTPGTQGPQGTAPAAGMTPSSAAPATPAP---SAAPSPRVPWDDAPPAPPrSGIPPRP-APRMPEASPVPGAPDSVAS 471

                         90
                 ....*....|....*.
gi 755519085 344 EGPTPDPWGSSDGGAP 359
Cdd:PRK14959 472 ASDAPPTLGDPSDTAE 487
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 266-375 2.90e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 40.48  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 266 TPAPPQASDPWGGPASVPTAVPvaaaasDPWGGPAVPPAADPWGGAAPTPASGDPWRPA-APTGPSVDPWGGTPAPAAGE 344
Cdd:PHA03269  33 TSAATQKPDPAPAPHQAASRAP------DPAVAPTSAASRKPDLAQAPTPAASEKFDPApAPHQAASRAPDPAVAPQLAA 106

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 755519085 345 GPTPDPW-----GSSDGGAPVSGPPSSDPWAPAPAF 375
Cdd:PHA03269 107 APKPDAAeaftsAAQAHEAPADAGTSAASKKPDPAA 142
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 266-359 4.13e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 266 TPAPPQASDPWGGPASVPTAVPVAaaaSDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK07764 422 APAPAAAPQPAPAPAPAPAPPSPA---GNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPA 498

                         90
                 ....*....|....
gi 755519085 346 PTPDPWGSSDGGAP 359
Cdd:PRK07764 499 APAAPAGADDAATL 512
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 272-515 6.24e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.77  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  272 ASDPWGGPASVPTAVPVAAAASDPWGGPAV-PPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDP 350
Cdd:PHA03307   44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPgPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  351 wgssDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPD--EFSDFDRLRTALPTSGSSTGELELLA 428
Cdd:PHA03307  124 ----ASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQaaLPLSSPEETARAPSSPPAEPPPSTPP 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  429 GEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPES----FLGPNAALVDLDSLVSRPGPTPPGSKASNPf 504
Cdd:PHA03307  200 AAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESsgcgWGPENECPLPRPAPITLPTRIWEASGWNGP- 278

                         250
                  ....*....|.
gi 755519085  505 lPSGAPPTGPS 515
Cdd:PHA03307  279 -SSRPGPASSS 288
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 326-395 6.94e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 39.28  E-value: 6.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085 326 PTGPSVDPWGGTPAPAAGEG-----PTPDPWG-----SSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVG 395
Cdd:PRK14959 373 PSGGGASAPSGSAAEGPASGgaatiPTPGTQGpqgtaPAAGMTPSSAAPATPAPSAAPSPRVPWDDAPPAPPRSGIPPRP 452
PHA03247 PHA03247
large tegument protein UL36; Provisional
 267-402 9.01e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  267 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAAdpwggaAPTPASGDPWRPAAPTGPSVDPWGGTPApaagEGP 346
Cdd:PHA03247 2889 PAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP------QPQPPPPPPPRPQPPLAPTTDPAGAGEP----SGA 2958

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519085  347 TPDPWGSSDGGAPVSGP----PSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPD 402
Cdd:PHA03247 2959 VPQPWLGALVPGRVAVPrfrvPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETD 3018
 
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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