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Conserved domains on  [gi|1733573764|ref|NP_001359429|]
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epsin-1 isoform 2 [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 family proteins that play an important role as accessory proteins in clathrin-mediated endocytosis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 19-142 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 1733573764  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1733573764  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 1733573764 267 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPW----GGAAPTPASGDPWRPAAptGPSVDPWGGTPAPAA 342
Cdd:PRK07764  649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaapaGAAPAQPAPAPAATPPA--GQADDPAAQPPQAAQ 726

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1733573764 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 1733573764  256 SLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPT--------PASGDPWRPAAPT 327
Cdd:PHA03247  2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparpPTTAGPPAPAPPA 2773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  328 GPSVDPWGGTPAPAAGE-----GPTPDPWGSSDGGAPVSG-----PPSSDPWAPAPAFSDPWGGSPAKPS--SNGTAAVG 395
Cdd:PHA03247  2774 APAAGPPRRLTRPAVASlsesrESLPSPWDPADPPAAVLApaaalPPAASPAGPLPPPTSAQPTAPPPPPgpPPPSLPLG 2853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  396 GFDTEPDEFSDFDRLRTALPTSGSSTgelellagEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFL 475
Cdd:PHA03247  2854 GSVAPGGDVRRRPPSRSPAAKPAAPA--------RPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1733573764  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 1733573764  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1733573764  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 1733573764  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1733573764  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 1733573764   18 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1733573764   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 1733573764 267 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPW----GGAAPTPASGDPWRPAAptGPSVDPWGGTPAPAA 342
Cdd:PRK07764  649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaapaGAAPAQPAPAPAATPPA--GQADDPAAQPPQAAQ 726

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1733573764 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 1733573764  256 SLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPT--------PASGDPWRPAAPT 327
Cdd:PHA03247  2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparpPTTAGPPAPAPPA 2773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  328 GPSVDPWGGTPAPAAGE-----GPTPDPWGSSDGGAPVSG-----PPSSDPWAPAPAFSDPWGGSPAKPS--SNGTAAVG 395
Cdd:PHA03247  2774 APAAGPPRRLTRPAVASlsesrESLPSPWDPADPPAAVLApaaalPPAASPAGPLPPPTSAQPTAPPPPPgpPPPSLPLG 2853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  396 GFDTEPDEFSDFDRLRTALPTSGSSTgelellagEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFL 475
Cdd:PHA03247  2854 GSVAPGGDVRRRPPSRSPAAKPAAPA--------RPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1733573764  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 1733573764  19 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCKE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1733573764  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 1733573764  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLNDKGKNWRHIYKALTLLEYLLKNGSERVVDDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1733573764  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 1733573764  17 YSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:cd16991     2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLWA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1733573764  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 1733573764  20 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 99
Cdd:cd03571     1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1733573764 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 1733573764  20 AEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKR-LNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd16989     1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRmLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1733573764  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 1733573764   18 SEAEIKVREATSNDPWGPSSSLMSEIADLTYNV-VAFSEIMSMIWKRLNDHGkNWRHVYKAMTLMEYLIKTGSERVSQQC 96
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLNDTK-NWRVVYKALILLHYLLRNGSPRVILEA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1733573764   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 1733573764  21 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLND-HGKNWRHVYKAMTLMEYLIKTGSERVSQQCKEN 99
Cdd:cd16992     2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEkAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1733573764 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 1733573764  20 AEIKVREATSNDPWGPSSSLMSEIADLTYN-VVAFSEIMSMIWKRLNDHgkNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98
Cdd:cd00197     1 FEKTVEKATSNENMGPDWPLIMEICDLINEtNVGPKEAVDAIKKRINNK--NPHVVLKALTLLEYCVKNCGERFHQEVAS 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1733573764  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 1733573764  20 AEIKVREAT-SNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHG-----KNWRHVYKAMTLMEYLIKTGSERVS 93
Cdd:cd16994     1 TELKVKQATdDNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSkksshKNCVHILKTLTLISYLINNGSNEFI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1733573764  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 1733573764  21 EIKVREATSNDPWGPSSSLMSEIADLTYNVVAFsEIMSMIWKRLNDH-------------------GKNWRHVYKAMTLM 81
Cdd:cd16993     2 QIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLY-LMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKCLIVI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733573764  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 1733573764 267 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPW----GGAAPTPASGDPWRPAAptGPSVDPWGGTPAPAA 342
Cdd:PRK07764  649 APEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPaapaGAAPAQPAPAPAATPPA--GQADDPAAQPPQAAQ 726

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1733573764 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 1733573764 270 PQASDPWGGPAsvptavpvAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDP-WGGTPAPAAGEGPTP 348
Cdd:PRK07764  615 PAAPAAPAAPA--------APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPaKAGGAAPAAPPPAPA 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764 349 DPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLA 428
Cdd:PRK07764  687 PAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAP 766

                         170
                  ....*....|
gi 1733573764 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 1733573764 269 PPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGA-APTPASGDPWRPAAPTGPSVDPWGGTPAPAagegpT 347
Cdd:PRK07764  591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAaAPAEASAAPAPGVAAPEHHPKHVAVPDASD-----G 665

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1733573764 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 1733573764  256 SLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPT--------PASGDPWRPAAPT 327
Cdd:PHA03247  2694 SLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGgparparpPTTAGPPAPAPPA 2773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  328 GPSVDPWGGTPAPAAGE-----GPTPDPWGSSDGGAPVSG-----PPSSDPWAPAPAFSDPWGGSPAKPS--SNGTAAVG 395
Cdd:PHA03247  2774 APAAGPPRRLTRPAVASlsesrESLPSPWDPADPPAAVLApaaalPPAASPAGPLPPPTSAQPTAPPPPPgpPPPSLPLG 2853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  396 GFDTEPDEFSDFDRLRTALPTSGSSTgelellagEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFL 475
Cdd:PHA03247  2854 GSVAPGGDVRRRPPSRSPAAKPAAPA--------RPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1733573764  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 1733573764  265 TTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPwggtPAPAAGE 344
Cdd:PHA03307   113 SPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEE----TARAPSS 188

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  345 GPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKpSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGEL 424
Cdd:PHA03307   189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA-DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPT 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  425 ELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPF 504
Cdd:PHA03307   268 RIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSP 347

                          250       260
                   ....*....|....*....|...
gi 1733573764  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 1733573764  24 VREATSNDPWGPSSSLMSEIADLtYNVVAFS--EIMSMIWKRLNDhgKNWRHVYKAMTLMEYLIKTGSERVSQQckenmy 101
Cdd:cd03561     5 VEKATSESLTEPDWALNLEICDL-VNSDPAQakDAVRALRKRLQS--KNPKVQLLALTLLETLVKNCGAPFHSE------ 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1733573764 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 1733573764 266 TPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK07764  402 AAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPA 481

                          90       100
                  ....*....|....*....|...
gi 1733573764 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 1733573764  152 EKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEE--- 228
Cdd:PHA03307   136 EMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPisa 215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  229 -----RIRRGDDLRL-------QMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPw 296
Cdd:PHA03307   216 sasspAPAPGRSAADdagasssDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRER- 294

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  297 gGPAVPPAADPWGGAAPTPASGDPWRP--------AAPTGPSVDPWGGTPAPAAGEGPTPdpwGSSDGGAPVSGPPSSDP 368
Cdd:PHA03307   295 -SPSPSPSSPGSGPAPSSPRASSSSSSsresssssTSSSSESSRGAAVSPGPSPSRSPSP---SRPPPPADPSSPRKRPR 370

                          250       260
                   ....*....|....*....|....*
gi 1733573764  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 1733573764 297 GGPAVPPAADPwGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGG-------APVSGPPSSDPW 369
Cdd:PRK07764  400 SAAAAAPAAAP-APAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAaapsaqpAPAPAAAPEPTA 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764 370 APAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELeLLAGEVPARSPG-----AFDMSGV 444
Cdd:PRK07764  479 APAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAI-LLPEATVLGVRGdtlvlGFSTGGL 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764 445 GGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAAlvdldsLVSRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAP 524
Cdd:PRK07764  558 ARRFASPGNAEVLVTALAEELGGDWQVEAVVGPAPG------AAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAG 631


                  ...
gi 1733573764 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 1733573764  272 ASDPWGGPASVPTAVPVAAAA--SDPWGGPAVPPAADPWGGAAPTP-ASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTP 348
Cdd:PHA03247  2544 ASDDAGDPPPPLPPAAPPAAPdrSVPPPRPAPRPSEPAVTSRARRPdAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  349 DPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLA 428
Cdd:PHA03247  2624 PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPP 2703

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  429 GEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTptpptrkTPESFLGPNAALVDLdslvsrpGPTPPGSKASNPFLPSG 508
Cdd:PHA03247  2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPA-------APAPPAVPAGPATPG-------GPARPARPPTTAGPPAP 2769

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733573764  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 1733573764  299 PAVPPAADPWGGAAPTPAsgdpwRPAAPTGPSVDPwggtPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAfsdp 378
Cdd:PHA03247   255 PAPPPVVGEGADRAPETA-----RGATGPPPPPEA----AAPNGAAAPPDGVWGAALAGAPLALPAPPDPPPPAPA---- 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  379 wGGSPAKPSSNGTAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARS---PGAFDMSGVGGSLAESVGSP 455
Cdd:PHA03247   322 -GDAEEEDDEDGAMEVVSPLPRPRQHYPLGFPKRRRPTWTPPSSLEDLSAGRHHPKRaslPTRKRRSARHAATPFARGPG 400

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1733573764  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 1733573764  310 GAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPW---------GSSDGGAPvsgPPSSDPWAPAPAFSDPWG 380
Cdd:PHA03247  2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVHPRMLtwirgleelASDDAGDP---PPPLPPAAPPAAPDRSVP 2569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  381 GSPAKPSSNGtAAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAG---------EVPARSPGAFDMSGVGGSLAES 451
Cdd:PHA03247  2570 PPRPAPRPSE-PAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLppdthapdpPPPSPSPAANEPDPHPPPTVPP 2648

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  452 VGSPPPAATPTPTPPTRKTPESFLGPNA--------------ALVDLDSLVSRPGPTPPGSKASNPFLPSGAPPTGPSVT 517
Cdd:PHA03247  2649 PERPRDDPAPGRVSRPRRARRLGRAAQAssppqrprrraarpTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAA 2728

                          250
                   ....*....|
gi 1733573764  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 1733573764  268 APPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPT 347
Cdd:PHA03247  2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP 2679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  348 PDPWGSSDGGAPV-----SGPPSSDPWAPAPAfsdPWGGSPAKPSSNGTAAVGGFDTEPdefsdfdrlrTALPTSGSSTG 422
Cdd:PHA03247  2680 PQRPRRRAARPTVgsltsLADPPPPPPTPEPA---PHALVSATPLPPGPAAARQASPAL----------PAAPAPPAVPA 2746

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  423 ELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAAlVDLDSLVSRPGPTPPGSKASN 502
Cdd:PHA03247  2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP-ADPPAAVLAPAAALPPAASPA 2825

                          250       260
                   ....*....|....*....|....*...
gi 1733573764  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 1733573764 266 TPAPPQASdPWGGPASVPTAVPVAAAASdpwggpAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK12323  398 APAAPPAA-PAAAPAAAAAARAVAAAPA------RRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPR 470

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764 346 PTPDPwgssDGGAPVSGPPSSDPwAPAPAFSDPWGGSPAKPSSNGTAAVGGfDTEPDEFSDFDRLRTALPTSGSSTGELE 425
Cdd:PRK12323  471 PVAAA----AAAAPARAAPAAAP-APADDDPPPWEELPPEFASPAPAQPDA-APAGWVAESIPDPATADPDDAFETLAPA 544

                         170
                  ....*....|
gi 1733573764 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 1733573764 265 TTPAPPQASDPWGGPASvptaVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSV--DPWGGTPAPAA 342
Cdd:PRK07764  679 AAPPPAPAPAAPAAPAG----AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLppEPDDPPDPAGA 754

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1733573764 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 1733573764 298 GPAVPPAADpwgGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPafsD 377
Cdd:PHA03264  263 GYEPPPAPS---GGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDADRP---E 336

                          90
                  ....*....|....*....
gi 1733573764 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 1733573764 297 GGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGE-----GPTPDPWGSSDGGAPVSGPPSSDPWAP 371
Cdd:PRK14951  371 EAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPaaappAPVAAPAAAAPAAAPAAAPAAVALAPA 450

                          90       100
                  ....*....|....*....|..
gi 1733573764 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 1733573764 265 TTPAPPQASDPWGGPASVPTAVPVAAAASDPwggPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGE 344
Cdd:PRK12323  372 AGPATAAAAPVAQPAPAAAAPAAAAPAPAAP---PAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAP 448

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764 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 1733573764 266 TPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK14951  380 TPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPET 459

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1733573764 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 1733573764  269 PPQASDP---WGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTP---ASGDPWRPAAPTGPSVDPWGGTPAPAA 342
Cdd:PHA03247  2673 AAQASSPpqrPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPpgpAAARQASPALPAAPAPPAVPAGPATPG 2752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  343 GEGPTPDPWGSSdgGAPVSGPPSSDPWAPAPAFSDPwGGSPAKPSSNgtaavggfdtepdefsdfdrlrtALPTSGSSTG 422
Cdd:PHA03247  2753 GPARPARPPTTA--GPPAPAPPAAPAAGPPRRLTRP-AVASLSESRE-----------------------SLPSPWDPAD 2806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  423 ELELLAGEVPARSPGAFDMSGVggslaesvgSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASN 502
Cdd:PHA03247  2807 PPAAVLAPAAALPPAASPAGPL---------PPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA 2877

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1733573764  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 1733573764 267 PAPPQASDPWGG-PASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK07003  360 PAVTGGGAPGGGvPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRG 439

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1733573764 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 1733573764 261 ADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGP--AVPPAADPWGG----AAPTPASGDPWRPAAPTGPSVDPW 334
Cdd:PRK12323  420 AAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPaaAARPAAAGPRPvaaaAAAAPARAAPAAAPAPADDDPPPW 499

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733573764 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 1733573764  300 AVPPA-----ADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPA 374
Cdd:PRK12270    24 SVDPSwreffADYGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPAAA 103

                           90       100
                   ....*....|....*....|..
gi 1733573764  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 1733573764 265 TTPAPPQASDPWGGPASVPTAVPVAAAASDPwggPAVPPAADPWGGAAPTPA-SGDPWRPaAPTGPSVDPWGGTPAPAAG 343
Cdd:PRK14959  396 TIPTPGTQGPQGTAPAAGMTPSSAAPATPAP---SAAPSPRVPWDDAPPAPPrSGIPPRP-APRMPEASPVPGAPDSVAS 471

                          90
                  ....*....|....*.
gi 1733573764 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 1733573764 266 TPAPPQASDPWGGPASVPTAVPvaaaasDPWGGPAVPPAADPWGGAAPTPASGDPWRPA-APTGPSVDPWGGTPAPAAGE 344
Cdd:PHA03269   33 TSAATQKPDPAPAPHQAASRAP------DPAVAPTSAASRKPDLAQAPTPAASEKFDPApAPHQAASRAPDPAVAPQLAA 106

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1733573764 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 1733573764 266 TPAPPQASDPWGGPASVPTAVPVAaaaSDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEG 345
Cdd:PRK07764  422 APAPAAAPQPAPAPAPAPAPPSPA---GNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPA 498

                          90
                  ....*....|....
gi 1733573764 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 1733573764  272 ASDPWGGPASVPTAVPVAAAASDPWGGPAV-PPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDP 350
Cdd:PHA03307    44 VSDSAELAAVTVVAGAAACDRFEPPTGPPPgPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPP 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  351 wgssDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAAVGGFDTEPD--EFSDFDRLRTALPTSGSSTGELELLA 428
Cdd:PHA03307   124 ----ASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQaaLPLSSPEETARAPSSPPAEPPPSTPP 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  429 GEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPES----FLGPNAALVDLDSLVSRPGPTPPGSKASNPf 504
Cdd:PHA03307   200 AAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESsgcgWGPENECPLPRPAPITLPTRIWEASGWNGP- 278

                          250
                   ....*....|.
gi 1733573764  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 1733573764 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 1733573764  267 PAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAAdpwggaAPTPASGDPWRPAAPTGPSVDPWGGTPApaagEGP 346
Cdd:PHA03247  2889 PAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP------QPQPPPPPPPRPQPPLAPTTDPAGAGEP----SGA 2958

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733573764  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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