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Conserved domains on  [gi|568938216|ref|XP_006504542|]
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carbohydrate-responsive element-binding protein isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NES2-NLS_ChREBP cd21771
nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in ...
81-196 5.27e-87

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in carbohydrate-responsive element-binding protein (ChREBP), and similar proteins; ChREBP, also called class D basic helix-loop-helix protein 14 (bHLHd14), Max-like protein (MLX) interactor or MIO, MLX-interacting protein-like (MLXIPL), WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a large transcription factor that functions at two levels, nuclear localization and DNA binding. It binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. It also binds DNA as a heterodimer with TCFL4/MLX. ChREBP contains functional domains, including two nuclear export signals, NES1 and NES2, and a nuclear import signal (NLS) in the N-terminal region. This model corresponds to NES2 and NLS domains.


:

Pssm-ID: 439287  Cd Length: 116  Bit Score: 272.61  E-value: 5.27e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  81 SIDPTLTHLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVQRRKSPVCGFVTPLQGSEADEHRKP 160
Cdd:cd21771    1 SIDPTLTRLFECMSLAYSGKLVSPKWKNFKGLRLLWRDKIRLNNAIWRAWYIQYVEKRKNPVCGFVTPLEGSEADEHRKP 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568938216 161 EAVILEGNYWKRRIEVVMREYHKWRIYYKKRLRKSS 196
Cdd:cd21771   81 EAVVLEGNYWKRRIEVVMKEYHKWRIYYKKRLRKSS 116
bHLH_SF super family cl00081
basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators ...
657-772 5.01e-40

basic Helix Loop Helix (bHLH) domain superfamily; bHLH proteins are transcriptional regulators that are found in organisms from yeast to humans. Members of the bHLH superfamily have two highly conserved and functionally distinct regions. The basic part is at the amino end of the bHLH that may bind DNA to a consensus hexanucleotide sequence known as the E box (CANNTG). Different families of bHLH proteins recognize different E-box consensus sequences. At the carboxyl-terminal end of the region is the HLH region that interacts with other proteins to form homo- and heterodimers. bHLH proteins function as a diverse set of regulatory factors because they recognize different DNA sequences and dimerize with different proteins. The bHLH proteins can be divided to cell-type specific and widely expressed proteins. The cell-type specific members of bHLH superfamily are involved in cell-fate determination and act in neurogenesis, cardiogenesis, myogenesis, and hematopoiesis.


The actual alignment was detected with superfamily member cd19689:

Pssm-ID: 469605  Cd Length: 76  Bit Score: 142.03  E-value: 5.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 657 KMENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLKvspqpamhtpleswnpsldqhptpapracqhrgphwwrs 736
Cdd:cd19689    1 KTETRRITHISAEQKRRFNIKLGFDTLHSLVTTLSSQPSIK--------------------------------------- 41
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568938216 737 qVSKATTLQKTAEYILMLQQERAAMQEEAQQLRDEI 772
Cdd:cd19689   42 -ISKATTLQKTAEYISKLQQERAQLQEEAQRLRDQI 76
PHA03247 super family cl33720
large tegument protein UL36; Provisional
308-648 1.06e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  308 PPQTPTSSNYIESPSF-GPMADSLFSSGILAPEMPSPASSSSSSGMTPhSGNTRLQARNSCSGPLDPNPflssefllPED 386
Cdd:PHA03247 2704 PPPTPEPAPHALVSATpLPPGPAAARQASPALPAAPAPPAVPAGPATP-GGPARPARPPTTAGPPAPAP--------PAA 2774
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  387 PKTkiPPAPGPTPLLPFPTPVKVHGL-EPCTPSPFPTMAPPPSllpeesllsARFPFTSAPPAPgvstLPAPTTFVPTPQ 465
Cdd:PHA03247 2775 PAA--GPPRRLTRPAVASLSESRESLpSPWDPADPPAAVLAPA---------AALPPAASPAGP----LPPPTSAQPTAP 2839
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  466 PGPgPVPFSVDHLPHGYLEPvFGPHFTVPQGMQPRCKPSSPS-PGGQKASPPTLASATASPTATATARDNNPcLTQLLRA 544
Cdd:PHA03247 2840 PPP-PGPPPPSLPLGGSVAP-GGDVRRRPPSRSPAAKPAAPArPPVRRLARPAVSRSTESFALPPDQPERPP-QPQAPPP 2916
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  545 AKPEQALEPPTMPGTLLRPPESPDT--VSEIPRARAFFPPIPAPTPPRPPPGPATLAPPRSLVVPKAERLSPPASSGSER 622
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPPPRPQPplAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
                         330       340
                  ....*....|....*....|....*...
gi 568938216  623 RLSGD--LNSIQPSGALSVHLSPPQTVL 648
Cdd:PHA03247 2997 TGHSLsrVSSWASSLALHEETDPPPVSL 3024
 
Name Accession Description Interval E-value
NES2-NLS_ChREBP cd21771
nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in ...
81-196 5.27e-87

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in carbohydrate-responsive element-binding protein (ChREBP), and similar proteins; ChREBP, also called class D basic helix-loop-helix protein 14 (bHLHd14), Max-like protein (MLX) interactor or MIO, MLX-interacting protein-like (MLXIPL), WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a large transcription factor that functions at two levels, nuclear localization and DNA binding. It binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. It also binds DNA as a heterodimer with TCFL4/MLX. ChREBP contains functional domains, including two nuclear export signals, NES1 and NES2, and a nuclear import signal (NLS) in the N-terminal region. This model corresponds to NES2 and NLS domains.


Pssm-ID: 439287  Cd Length: 116  Bit Score: 272.61  E-value: 5.27e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  81 SIDPTLTHLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVQRRKSPVCGFVTPLQGSEADEHRKP 160
Cdd:cd21771    1 SIDPTLTRLFECMSLAYSGKLVSPKWKNFKGLRLLWRDKIRLNNAIWRAWYIQYVEKRKNPVCGFVTPLEGSEADEHRKP 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568938216 161 EAVILEGNYWKRRIEVVMREYHKWRIYYKKRLRKSS 196
Cdd:cd21771   81 EAVVLEGNYWKRRIEVVMKEYHKWRIYYKKRLRKSS 116
bHLHzip_MLXIPL cd19689
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein-like (MLXIPL) ...
657-772 5.01e-40

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein-like (MLXIPL) and similar proteins; MLXIPL, also termed carbohydrate-responsive element-binding protein (ChREBP), or Class D basic helix-loop-helix protein 14 (bHLHd14), or MLX interactor, or WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a bHLHZip transcriptional factor integral to the regulation of glycolysis and lipogenesis in the liver. It forms heterodimers with the bHLHZip protein Mlx to bind the DNA sequence 5'-CACGTG-3'.


Pssm-ID: 381532  Cd Length: 76  Bit Score: 142.03  E-value: 5.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 657 KMENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLKvspqpamhtpleswnpsldqhptpapracqhrgphwwrs 736
Cdd:cd19689    1 KTETRRITHISAEQKRRFNIKLGFDTLHSLVTTLSSQPSIK--------------------------------------- 41
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568938216 737 qVSKATTLQKTAEYILMLQQERAAMQEEAQQLRDEI 772
Cdd:cd19689   42 -ISKATTLQKTAEYISKLQQERAQLQEEAQRLRDQI 76
PHA03247 PHA03247
large tegument protein UL36; Provisional
308-648 1.06e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  308 PPQTPTSSNYIESPSF-GPMADSLFSSGILAPEMPSPASSSSSSGMTPhSGNTRLQARNSCSGPLDPNPflssefllPED 386
Cdd:PHA03247 2704 PPPTPEPAPHALVSATpLPPGPAAARQASPALPAAPAPPAVPAGPATP-GGPARPARPPTTAGPPAPAP--------PAA 2774
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  387 PKTkiPPAPGPTPLLPFPTPVKVHGL-EPCTPSPFPTMAPPPSllpeesllsARFPFTSAPPAPgvstLPAPTTFVPTPQ 465
Cdd:PHA03247 2775 PAA--GPPRRLTRPAVASLSESRESLpSPWDPADPPAAVLAPA---------AALPPAASPAGP----LPPPTSAQPTAP 2839
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  466 PGPgPVPFSVDHLPHGYLEPvFGPHFTVPQGMQPRCKPSSPS-PGGQKASPPTLASATASPTATATARDNNPcLTQLLRA 544
Cdd:PHA03247 2840 PPP-PGPPPPSLPLGGSVAP-GGDVRRRPPSRSPAAKPAAPArPPVRRLARPAVSRSTESFALPPDQPERPP-QPQAPPP 2916
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  545 AKPEQALEPPTMPGTLLRPPESPDT--VSEIPRARAFFPPIPAPTPPRPPPGPATLAPPRSLVVPKAERLSPPASSGSER 622
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPPPRPQPplAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
                         330       340
                  ....*....|....*....|....*...
gi 568938216  623 RLSGD--LNSIQPSGALSVHLSPPQTVL 648
Cdd:PHA03247 2997 TGHSLsrVSSWASSLALHEETDPPPVSL 3024
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
370-574 6.28e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  370 PLDPNPFLSSEFLLPedPKTKIPPAPGPTPLLpfptpvkvHGLEPCTPSPF--PTMAPPPSLLPEESLLSARFPFTSAPP 447
Cdd:pfam03154 344 PLPPAPLSMPHIKPP--PTTPIPQLPNPQSHK--------HPPHLSGPSPFqmNSNLPPPPALKPLSSLSTHHPPSAHPP 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  448 A----PGVSTLPAPTTFVPTPQPGPGPVPFSVDHLPHGYLEPV-----FGPHFTVPQG----MQPRCKPSSPSPGGQKAS 514
Cdd:pfam03154 414 PlqlmPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVpsqspFPQHPFVPGGpppiTPPSGPPTSTSSAMPGIQ 493
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  515 PPTLASATASPTATATARDNNPCLTqlLRAAKPEQALEPPTMPGTlLRPPESPDTVSEIP 574
Cdd:pfam03154 494 PPSSASVSSSGPVPAAVSCPLPPVQ--IKEEALDEAEEPESPPPP-PRSPSPEPTVVNTP 550
 
Name Accession Description Interval E-value
NES2-NLS_ChREBP cd21771
nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in ...
81-196 5.27e-87

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in carbohydrate-responsive element-binding protein (ChREBP), and similar proteins; ChREBP, also called class D basic helix-loop-helix protein 14 (bHLHd14), Max-like protein (MLX) interactor or MIO, MLX-interacting protein-like (MLXIPL), WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a large transcription factor that functions at two levels, nuclear localization and DNA binding. It binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. It also binds DNA as a heterodimer with TCFL4/MLX. ChREBP contains functional domains, including two nuclear export signals, NES1 and NES2, and a nuclear import signal (NLS) in the N-terminal region. This model corresponds to NES2 and NLS domains.


Pssm-ID: 439287  Cd Length: 116  Bit Score: 272.61  E-value: 5.27e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  81 SIDPTLTHLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVQRRKSPVCGFVTPLQGSEADEHRKP 160
Cdd:cd21771    1 SIDPTLTRLFECMSLAYSGKLVSPKWKNFKGLRLLWRDKIRLNNAIWRAWYIQYVEKRKNPVCGFVTPLEGSEADEHRKP 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568938216 161 EAVILEGNYWKRRIEVVMREYHKWRIYYKKRLRKSS 196
Cdd:cd21771   81 EAVVLEGNYWKRRIEVVMKEYHKWRIYYKKRLRKSS 116
NES2-NLS_MLXIP cd21772
nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in ...
81-194 1.90e-68

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in MLX-interacting protein (MLXIP), and similar proteins; MLXIP, also called class E basic helix-loop-helix protein 36 (bHLHe36), transcriptional activator MondoA, or MIR, is a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like network. It binds DNA by forming a heterodimer with Max-like protein (MLX) and activates transcription. It binds to the canonical E box sequence 5'-CACGTG-3'. MLXIP plays a role in transcriptional activation of glycolytic target genes and is involved in glucose-responsive gene regulation. MLXIP may contain functional domains, including two nuclear export signals, NES1 and NES2, and a nuclear import signal (NLS) in the N-terminal region. This model corresponds to NES2 and NLS domains.


Pssm-ID: 439288  Cd Length: 117  Bit Score: 223.01  E-value: 1.90e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  81 SIDPTLTHLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVQRRKSPVCGFVTPLQGS-EADEHRK 159
Cdd:cd21772    1 SIDASLTKLFECMTLAYSGKLVSPKWKNFKGLKLQWRDKIRLNNAIWRAWYMQYLEKRKNPVCHFVTPLDGSvDVDEHRR 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 568938216 160 PEAVILEGNYWKRRIEVVMREYHKWRIYYKKRLRK 194
Cdd:cd21772   81 PEAIATEGKYWKRRIEIVIREYHKWRTYFKKRLQK 115
NES2-NLS_ChREBP-like cd21739
nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in ...
81-196 1.08e-64

nuclear export signal 2 (NES2) and nuclear import signal (NLS) domains found in carbohydrate-responsive element-binding protein (ChREBP), MLX-interacting protein (MLXIP), and similar proteins; This family includes two transcription factors: ChREBP and MLXIP. ChREBP, also called class D basic helix-loop-helix protein 14 (bHLHd14), Max-like protein (MLX) interactor or MIO, MLX-interacting protein-like (MLXIPL), WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), functions at two levels; nuclear localization and DNA binding. ChREBP binds to the canonical and non-canonical E box sequences 5'-CACGTG-3'. It also binds DNA as a heterodimer with TCFL4/MLX. MLXIP, also called class E basic helix-loop-helix protein 36 (bHLHe36), transcriptional activator MondoA, or MIR, is a novel basic helix-loop-helix-leucine zipper transcriptional activator that constitutes a positive branch of a max-like network. MLXIP binds DNA by forming a heterodimer with Max-like protein (MLX), and activates transcription. It binds to the canonical E box sequence 5'-CACGTG-3'. MLXIP plays a role in transcriptional activation of glycolytic target genes and is involved in glucose-responsive gene regulation. Members in this family may contain functional domains, including two nuclear export signals, NES1 and NES2, and a nuclear import signal (NLS) in the N-terminal region. This model corresponds to NES2 and NLS domains.


Pssm-ID: 439286  Cd Length: 113  Bit Score: 212.51  E-value: 1.08e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  81 SIDPTLTHLFECLSLAYSGKLVSPKWKNFKGLKLLCRDKIRLNNAIWRAWYIQYVQRRKSPVCGFVTPLqgsEADEHRKP 160
Cdd:cd21739    1 AIDESLTKLFKCLTLAYSGKLTSPKWKNFKGLKLRWKDKIRLNNAIWREWHMQFVKKKKPPVCQFAVPL---DDDTHKKP 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568938216 161 EAVILEGNYWKRRIEVVMREYHKWRIYYKKRLRKSS 196
Cdd:cd21739   78 EAVVLEGKYWKRRLETVVREYKKWRLFYKDKLAGKT 113
bHLHzip_MLXIPL cd19689
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein-like (MLXIPL) ...
657-772 5.01e-40

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein-like (MLXIPL) and similar proteins; MLXIPL, also termed carbohydrate-responsive element-binding protein (ChREBP), or Class D basic helix-loop-helix protein 14 (bHLHd14), or MLX interactor, or WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a bHLHZip transcriptional factor integral to the regulation of glycolysis and lipogenesis in the liver. It forms heterodimers with the bHLHZip protein Mlx to bind the DNA sequence 5'-CACGTG-3'.


Pssm-ID: 381532  Cd Length: 76  Bit Score: 142.03  E-value: 5.01e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 657 KMENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLKvspqpamhtpleswnpsldqhptpapracqhrgphwwrs 736
Cdd:cd19689    1 KTETRRITHISAEQKRRFNIKLGFDTLHSLVTTLSSQPSIK--------------------------------------- 41
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568938216 737 qVSKATTLQKTAEYILMLQQERAAMQEEAQQLRDEI 772
Cdd:cd19689   42 -ISKATTLQKTAEYISKLQQERAQLQEEAQRLRDQI 76
bHLHzip_MLXIP_like cd11405
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), ...
659-772 2.00e-31

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP), MLX-interacting protein-like (MLXIPL) and similar proteins; The family includes MLXIP and MLXIPL. MLXIP, also termed Class E basic helix-loop-helix protein 36 (bHLHe36), or transcriptional activator MondoA, is a bHLHZip transcriptional activator that binds DNA as a heterodimer with Mlx. It binds to the canonical E box sequence 5'-CACGTG-3' and plays a role in transcriptional activation of glycolytic target genes. MLXIP is most highly expressed in skeletal muscle and functions as an indirect glucose sensor, by sensing glucose 6-phosphate and shuttling between the nucleus and the cytoplasm. MLXIPL, also termed carbohydrate-responsive element-binding protein (ChREBP), or Class D basic helix-loop-helix protein 14 (bHLHd14), or MLX interactor, or WS basic-helix-loop-helix leucine zipper protein (WS-bHLH), or Williams-Beuren syndrome chromosomal region 14 protein (WBSCR14), is a bHLHZip transcriptional factor integral to the regulation of glycolysis and lipogenesis in the liver. It forms heterodimers with the bHLHZip protein Mlx to bind the DNA sequence 5'-CACGTG-3'.


Pssm-ID: 381411 [Multi-domain]  Cd Length: 74  Bit Score: 117.38  E-value: 2.00e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 659 ENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLKVSpqpamhtpleswnpsldqhptpapracqhrgphwwrsqv 738
Cdd:cd11405    1 EQRRLSHISAEQKRRFNIKSGFDTLQSLIPSLGQNPNQKVS--------------------------------------- 41
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568938216 739 sKATTLQKTAEYILMLQQERAAMQEEAQQLRDEI 772
Cdd:cd11405   42 -KAAMLQKAAEYIKSLKRERQQMQEEAEQLRQEI 74
bHLHzip_MLXIP cd19688
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP) and ...
659-772 3.03e-26

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in MLX-interacting protein (MLXIP) and similar proteins; MLXIP, also termed Class E basic helix-loop-helix protein 36 (bHLHe36), or transcriptional activator MondoA, is a bHLHZip transcriptional activator that binds DNA as a heterodimer with Mlx. It binds to the canonical E box sequence 5'-CACGTG-3' and plays a role in transcriptional activation of glycolytic target genes. MLXIP is most highly expressed in skeletal muscle and functions as an indirect glucose sensor, by sensing glucose 6-phosphate and shuttling between the nucleus and the cytoplasm.


Pssm-ID: 381531  Cd Length: 72  Bit Score: 102.33  E-value: 3.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 659 ENRRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQpslkvspqpamhtpleswnpsldqhptpapracqhrgphwwrSQV 738
Cdd:cd19688    1 KNRRMKHISAEQKRRFNIKICFDTLNSLVSTLKNS------------------------------------------KPI 38
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568938216 739 SKATTLQKTAEYILMLQQERAAMQEEAQQLRDEI 772
Cdd:cd19688   39 SNAITLQKTVEYIAKLQQERTQMQEETKRLREEI 72
bHLHzip_Mlx cd19687
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) and similar ...
660-772 1.04e-12

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) and similar proteins; Mlx, also termed Class D basic helix-loop-helix protein 13 (bHLHd13), or Max-like bHLHZip protein, or protein BigMax, or transcription factor-like protein 4, is a Max-like bHLHZip transcription regulator that interacts with the Max network of transcription factors. It forms a sequence-specific DNA-binding protein complex with some member of Mad family (Mad1 and Mad4) and Mondo family but not the Myc family and bind the E-box DNA to control transcription.


Pssm-ID: 381530 [Multi-domain]  Cd Length: 76  Bit Score: 63.98  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 660 NRRITHISAEQKRRFNIKLGFDTLHGLVSTLsaQPSLKVSPQpamhtpleswnpsldqhptpapracqhrgphwwrsQVS 739
Cdd:cd19687    1 RRREAHTQAEQKRRDAIKKGYDDLQDIVPTC--QQQDDIGSQ-----------------------------------KLS 43
                         90       100       110
                 ....*....|....*....|....*....|...
gi 568938216 740 KATTLQKTAEYILMLQQERAAMQEEAQQLRDEI 772
Cdd:cd19687   44 KATILQRSIDYIQFLHQQKKKQEEELSALRKEV 76
bHLHzip_SREBP_like cd11395
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding ...
659-772 1.46e-10

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in sterol regulatory element-binding protein (SREBP) family and similar proteins; The SREBP family includes SREBP1 and SREBP2, which are bHLHzip transcriptional activator of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. SREBP1 and SREBP2 are principally found in the liver and in adipocytes and made up of an N-terminal transcription factor portion (composed of an activation domain, a bHLHzip domain, and a nuclear localization signal), a hydrophobic region containing two membrane spanning regions, and a C-terminal regulatory segment. They recognize a symmetric sterol regulatory element (TCACNCCAC) instead of E-box. The family also includes Saccharomyces cerevisiae transcription factor HMS1 (also termed high-copy MEP suppressor protein 1) and serine-rich protein TYE7. HMS1 is a putative bHLHzip transcription factor involved in exit from mitosis and pseudohyphal differentiation. TYE7, also termed basic-helix-loop-helix protein SGC1, is a putative bHLHzip transcription activator required for Ty1-mediated glycolytic gene expression. TYE7 N-terminal is extremely rich in serine residues. It binds DNA on E-box motifs, 5'-CANNTG-3'. TYE7 is not essential for growth.


Pssm-ID: 381401 [Multi-domain]  Cd Length: 87  Bit Score: 58.50  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 659 ENRRITHISAEQKRRFNIKLGFDTLHGLVstlsaqPSLKVSPQPamhtplesWNPSLDQHPTPAPRacqhrgphwwrsqV 738
Cdd:cd11395    1 PRKRLPHNAIEKRYRSNLNTKIERLRDAI------PSLRSPEGK--------SDDGGLGGLAPTTK-------------L 53
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568938216 739 SKATTLQKTAEYILMLQQERAAMQEEAQQLRDEI 772
Cdd:cd11395   54 SKATILTKAIEYIRHLEQENERLEEENEELRQQV 87
bHLHzip_Mlx_like cd11404
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, ...
661-779 1.82e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in Max-like protein X (Mlx) family; Mlx, also termed Class D basic helix-loop-helix protein 13 (bHLHd13), or Max-like bHLHZip protein, or protein BigMax, or transcription factor-like protein 4, is a Max-like bHLHZip transcription regulator that interacts with the Max network of transcription factors. It forms a sequence-specific DNA-binding protein complex with some member of Mad family (Mad1 and Mad4) and Mondo family but not the Myc family and bind the E-box DNA to control transcription. The family also includes Saccharomyces cerevisiae INO4, which is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast.


Pssm-ID: 381410 [Multi-domain]  Cd Length: 70  Bit Score: 46.14  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 661 RRITHISAEQKRRFNIKLGFDTLHGLVstlsaqpslkvspqpamhtpleswnPSLDQhptpapracqhrgphwwrSQVSK 740
Cdd:cd11404    2 RRLNHVRSEKKRRELIKKGYDELCALV-------------------------PGLDP------------------QKRTK 38
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568938216 741 ATTLQKTAEYIlmlqqerAAMQEEAQQLRDEIEELNAAI 779
Cdd:cd11404   39 ADILQKAADWI-------QELKEENEKLEEQLDELKEAA 70
bHLHzip_Myc cd11400
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a ...
661-777 2.92e-06

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in the Myc family; The Myc family is a member of the bHLHzip family of transcription factors that play important roles in the control of normal cell proliferation, growth, survival and differentiation. All Myc isoforms contain two independently functioning polypeptide chain regions: N-terminal transactivating residues and a C-terminal bHLHzip segment. The bHLHzip family of bHLH transcription factors are characterized by a highly conserved N-terminal basic region that may bind DNA at a consensus hexanucleotide sequence known as the E-box (CANNTG) followed by HLH and leucine zipper motifs that may interact with other proteins to form homo- and heterodimers. Myc heterodimerizes with Max enabling specific binding to E-box DNA sequences in the promoters of target genes. The Myc proto-oncoprotein family includes at least five different functional members: c-, N-, L-, S- and B-Myc (which is lacking the bHLH domain).


Pssm-ID: 381406 [Multi-domain]  Cd Length: 80  Bit Score: 46.00  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 661 RRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPslkvspqpamhtpleswnpsldqhptpapRAcqhrgphwwrsqvSK 740
Cdd:cd11400    1 KRRLHNVLERQRRNDLKNSFEKLRDLVPELADNE-----------------------------KA-------------SK 38
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568938216 741 ATTLQKTAEYILMLQQERAAMQEEAQQLRDEIEELNA 777
Cdd:cd11400   39 VVILKKATEYIKQLQQEEKKLEKEKDKLKARNEQLRK 75
PHA03247 PHA03247
large tegument protein UL36; Provisional
308-648 1.06e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  308 PPQTPTSSNYIESPSF-GPMADSLFSSGILAPEMPSPASSSSSSGMTPhSGNTRLQARNSCSGPLDPNPflssefllPED 386
Cdd:PHA03247 2704 PPPTPEPAPHALVSATpLPPGPAAARQASPALPAAPAPPAVPAGPATP-GGPARPARPPTTAGPPAPAP--------PAA 2774
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  387 PKTkiPPAPGPTPLLPFPTPVKVHGL-EPCTPSPFPTMAPPPSllpeesllsARFPFTSAPPAPgvstLPAPTTFVPTPQ 465
Cdd:PHA03247 2775 PAA--GPPRRLTRPAVASLSESRESLpSPWDPADPPAAVLAPA---------AALPPAASPAGP----LPPPTSAQPTAP 2839
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  466 PGPgPVPFSVDHLPHGYLEPvFGPHFTVPQGMQPRCKPSSPS-PGGQKASPPTLASATASPTATATARDNNPcLTQLLRA 544
Cdd:PHA03247 2840 PPP-PGPPPPSLPLGGSVAP-GGDVRRRPPSRSPAAKPAAPArPPVRRLARPAVSRSTESFALPPDQPERPP-QPQAPPP 2916
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  545 AKPEQALEPPTMPGTLLRPPESPDT--VSEIPRARAFFPPIPAPTPPRPPPGPATLAPPRSLVVPKAERLSPPASSGSER 622
Cdd:PHA03247 2917 PQPQPQPPPPPQPQPPPPPPPRPQPplAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
                         330       340
                  ....*....|....*....|....*...
gi 568938216  623 RLSGD--LNSIQPSGALSVHLSPPQTVL 648
Cdd:PHA03247 2997 TGHSLsrVSSWASSLALHEETDPPPVSL 3024
PHA03247 PHA03247
large tegument protein UL36; Provisional
411-622 4.28e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 4.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  411 GLEPCTPSPFPTMAPPPSLLPEESLLSARFPFT-----------------SAPPAPGVSTLPAPTTFVPTPQPGP---GP 470
Cdd:PHA03247 2501 GGPPDPDAPPAPSRLAPAILPDEPVGEPVHPRMltwirgleelasddagdPPPPLPPAAPPAAPDRSVPPPRPAPrpsEP 2580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  471 VPFSVDHLPHGYLEPVFGPHFTVPQGMQPRCKPSSPSP----------------------GGQKASPPTLASATASPTAT 528
Cdd:PHA03247 2581 AVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPpdthapdppppspspaanepdpHPPPTVPPPERPRDDPAPGR 2660
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  529 ATARDNNPCLTQLLRAAKPEQALEPPTMPGT------LLRPPESPDTVSEIPRARA------FFPPIPAPTPPRPPPGPA 596
Cdd:PHA03247 2661 VSRPRRARRLGRAAQASSPPQRPRRRAARPTvgsltsLADPPPPPPTPEPAPHALVsatplpPGPAAARQASPALPAAPA 2740
                         250       260
                  ....*....|....*....|....*...
gi 568938216  597 TLAPPRSLVVPKAER--LSPPASSGSER 622
Cdd:PHA03247 2741 PPAVPAGPATPGGPArpARPPTTAGPPA 2768
PHA03378 PHA03378
EBNA-3B; Provisional
415-650 6.02e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.90  E-value: 6.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 415 CTPSPFPTmaPPPSLLPEESLLSARFPFTSAPpapgvSTLPAPTTFVPTPQPGPGPVPFSVDHLPHGYLEPVFGPHFTVP 494
Cdd:PHA03378 592 YAQTPWPV--PHPSQTPEPPTTQSHIPETSAP-----RQWPMPLRPIPMRPLRMQPITFNVLVFPTPHQPPQVEITPYKP 664
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 495 QGMQPRCKPSSPSPGGQKASpptlasatasptatatardnnpcltqLLRAAKPEQALEPPTMPGTlLRPPESPDTVSEIP 574
Cdd:PHA03378 665 TWTQIGHIPYQPSPTGANTM--------------------------LPIQWAPGTMQPPPRAPTP-MRPPAAPPGRAQRP 717
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568938216 575 RAraffppipaptpprpppgPATLAPPRSLVVPKAERlsPPASSGSERRLSGDLNSIQPSGALSVHLSPPQTVLSR 650
Cdd:PHA03378 718 AA------------------ATGRARPPAAAPGRARP--PAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGA 773
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
370-574 6.28e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  370 PLDPNPFLSSEFLLPedPKTKIPPAPGPTPLLpfptpvkvHGLEPCTPSPF--PTMAPPPSLLPEESLLSARFPFTSAPP 447
Cdd:pfam03154 344 PLPPAPLSMPHIKPP--PTTPIPQLPNPQSHK--------HPPHLSGPSPFqmNSNLPPPPALKPLSSLSTHHPPSAHPP 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  448 A----PGVSTLPAPTTFVPTPQPGPGPVPFSVDHLPHGYLEPV-----FGPHFTVPQG----MQPRCKPSSPSPGGQKAS 514
Cdd:pfam03154 414 PlqlmPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVpsqspFPQHPFVPGGpppiTPPSGPPTSTSSAMPGIQ 493
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  515 PPTLASATASPTATATARDNNPCLTqlLRAAKPEQALEPPTMPGTlLRPPESPDTVSEIP 574
Cdd:pfam03154 494 PPSSASVSSSGPVPAAVSCPLPPVQ--IKEEALDEAEEPESPPPP-PRSPSPEPTVVNTP 550
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
409-655 1.20e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  409 VHGLEPCTPSPFPTMAPP-------------PSLLPEESLLSARFPFTSAPPAPGVSTLPAPTTFVPTPQPGPGPVPFSV 475
Cdd:PHA03307   56 VAGAAACDRFEPPTGPPPgpgteapanesrsTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLS 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  476 DHLPHGYLEPVFGPHFTVPQGMQPRCKPSSPSPGGQKASPptLASATASPTATATARDNNPCLTQLLRAAKPEQALEPPT 555
Cdd:PHA03307  136 EMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALP--LSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPI 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  556 MPGTLLRPPESPDTVSEIPRARAFFPPIPAPTPPRPPPGPATLAPPRSLVV------------PKAERLSPPASSGSERR 623
Cdd:PHA03307  214 SASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITlptriweasgwnGPSSRPGPASSSSSPRE 293
                         250       260       270
                  ....*....|....*....|....*....|..
gi 568938216  624 LSGDLNSIQPSGALSVhlSPPQTVLSRGRVDN 655
Cdd:PHA03307  294 RSPSPSPSSPGSGPAP--SSPRASSSSSSSRE 323
bHLH_scINO4_like cd11403
basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar ...
661-695 1.27e-03

basic Helix-Loop-Helix (bHLH) domain found in Saccharomyces cerevisiae INO4 and similar proteins; INO4 is a bHLH transcriptional activator of phospholipid synthetic genes (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.). It is required for de-repression of phospholipid biosynthetic gene expression in response to inositol deprivation in yeast. INO4 dimerizes with INO2 and binds to an UAS DNA element to control expression of the genes whose expression is inositol-responsive.


Pssm-ID: 381409  Cd Length: 71  Bit Score: 38.21  E-value: 1.27e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568938216 661 RRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPS 695
Cdd:cd11403    2 KKENHISSEHKRREAIREGFDRLCAIVPALSSSQS 36
PHA03247 PHA03247
large tegument protein UL36; Provisional
417-648 1.42e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  417 PSPFPTMAPPPSLLPEESLLSARFPFTSAPPAPGvsTLPAPTTFVPTPQPGPGPVPFSVDHLPHGYLEPVFGPhftvPQG 496
Cdd:PHA03247 2609 RGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHP--PPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSP----PQR 2682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  497 MQPRCKPSSPSPGGQKASPPTLASATASPTATATARDNNPCLTQLLRAAKPEQALEP--------PTMPGTLLRPPeSPD 568
Cdd:PHA03247 2683 PRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPappavpagPATPGGPARPA-RPP 2761
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  569 TVSEIPRARAffppipAPTPPRPPPGPATLAPPRSLVVPKAERLSPPASSGSERRLSGDLNSIQPSGALSVHLSPPQTVL 648
Cdd:PHA03247 2762 TTAGPPAPAP------PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ 2835
PHA03247 PHA03247
large tegument protein UL36; Provisional
384-653 2.15e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  384 PEDPKTKIPPAPGPTPLLPFPTPVKVHGLEPCTP-SPFPTMAPPPSLLPEESLLSARFPFTSAPPAPGVSTLPAPTTFVP 462
Cdd:PHA03247 2703 PPPPTPEPAPHALVSATPLPPGPAAARQASPALPaAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR 2782
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  463 TPQPGPGPVPFSVDHLPH-----GYLEPVFGPHFTVPQGMQPRCKPSSPSPGGQKASPPTLASATASPTATATARDNNPc 537
Cdd:PHA03247 2783 LTRPAVASLSESRESLPSpwdpaDPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD- 2861
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  538 ltqlLRAAKPEQAlePPTMPGTLLRPPESPDTVSEIPRARAFFPPIPAPTPPRPPPGPATLA-PPRSLVVPKAERLSPPA 616
Cdd:PHA03247 2862 ----VRRRPPSRS--PAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPqPQPQPPPPPQPQPPPPP 2935
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 568938216  617 SSGSERRLSGDLNSIQPSGALSVHLSPPQTVLSRGRV 653
Cdd:PHA03247 2936 PPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRV 2972
bHLH_ScINO2_like cd11388
basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and ...
661-699 2.34e-03

basic helix-loop-helix (bHLH) domain found in Saccharomyces cerevisiae protein INO2 and similar proteins; INO2 is a positive regulatory factor required for depression of the co-regulated phospholipid biosynthetic enzymes in Saccharomyces cerevisiae. It is also involved in the expression of ITR1.


Pssm-ID: 381394  Cd Length: 68  Bit Score: 37.33  E-value: 2.34e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 568938216 661 RRITHISAEQKRRFNIKLGFDTLHGLVSTLSAQPSLKVS 699
Cdd:cd11388    3 KKWKHVEAEKKRRNQIKKGFEDLINLINYPRNNNEKRIS 41
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
387-568 2.55e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 387 PKTKIPPAPGPTPLLPFPTPVKVHGLEPCTPSPFPtMAPPPSLLPEESLLSARFPFTSAPPAPGVSTLPAPTTFVPTPQP 466
Cdd:PRK12323 391 APAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPAR-RSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGP 469
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216 467 GPGPVPFSVDHLPHGYLEPVFGPHFTVPQGMQPRCKPSSPSPGGQKASPPTLASATASPTATATARDNNPCLTqllrAAK 546
Cdd:PRK12323 470 RPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLA----PAP 545
                        170       180
                 ....*....|....*....|..
gi 568938216 547 PEQALEPPTMPGTLLRPPESPD 568
Cdd:PRK12323 546 AAAPAPRAAAATEPVVAPRPPR 567
bHLHzip_TFAP4 cd11419
basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor AP-4 (TFAP4) and ...
731-761 4.52e-03

basic Helix-Loop-Helix-zipper (bHLHzip) domain found in transcription factor AP-4 (TFAP4) and similar proteins; TFAP4, also termed activating enhancer-binding protein 4, or Class C basic helix-loop-helix protein 41 (bHLHc41), is a bHLHzip transcription factor that activates both viral and cellular genes involved in the regulation of cellular proliferation, stemness, and epithelial-mesenchymal transition by binding to the symmetrical DNA sequence 5'-CAGCTG-3'.


Pssm-ID: 381425  Cd Length: 61  Bit Score: 36.14  E-value: 4.52e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568938216 731 PHWWRSQVSKATTLQKTAEYILMLQQERAAM 761
Cdd:cd11419   31 PHCDGEKLSKAAILQQTAEYIFSLEQEKTRL 61
PHA03247 PHA03247
large tegument protein UL36; Provisional
354-731 8.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 8.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  354 PHSGNTRLQARNSCSGPLDPNPflsseflLPEDPKTKIPPAPGPTPLLPFPTPVKVHGlEPCTPSPFPTMAPPPSLLPEE 433
Cdd:PHA03247 2595 SARPRAPVDDRGDPRGPAPPSP-------LPPDTHAPDPPPPSPSPAANEPDPHPPPT-VPPPERPRDDPAPGRVSRPRR 2666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  434 SLLSARFPFTSAPP-APGVSTLPAP----TTFVPTPQPGPGPVPFSVDHLPHGYLEPvfGPHFTVPQGMQPRCKPSSPSP 508
Cdd:PHA03247 2667 ARRLGRAAQASSPPqRPRRRAARPTvgslTSLADPPPPPPTPEPAPHALVSATPLPP--GPAAARQASPALPAAPAPPAV 2744
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  509 GGQKASPPTLASATASPTATATARDNNPCLtqllRAAKPEQALEPPTMPGTLLRPPESPDTVSEIPRARAffpPIPAPTP 588
Cdd:PHA03247 2745 PAGPATPGGPARPARPPTTAGPPAPAPPAA----PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA---VLAPAAA 2817
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938216  589 PRPPPGPATLAPPRSLVVPKAERLSPPASSGSERrLSGdlnSIQPSGALSVH---LSPPQTVLSRGRVDNNKMenrrith 665
Cdd:PHA03247 2818 LPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP-LGG---SVAPGGDVRRRppsRSPAAKPAAPARPPVRRL------- 2886
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568938216  666 isaeqkrrfniklgfdtlhglvstlsAQPSLKVSPQPAMHTPLESW---NPSLDQHPTPAPRACQHRGP 731
Cdd:PHA03247 2887 --------------------------ARPAVSRSTESFALPPDQPErppQPQAPPPPQPQPQPPPPPQP 2929
 
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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