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Conserved domains on  [gi|1911217435|ref|XP_036163740|]
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transcription initiation factor TFIID subunit 6 isoform X1 [Myotis myotis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TAF6C cd08050
C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model ...
261-477 2.78e-114

C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model characterizes the carboxy (C)-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6), which is one of several TAFs that bind TBP and are involved in forming the Transcription Factor IID (TFIID) complex. This C-terminal HEAT repeat domain of TAF6 (TAF6C) is proposed to form a homodimer that effectively bridges the downstream promoter-interacting TAFs (TAF1, -2, and -7) with lobe B of TFIID. This domain influences the TAF6-TAF9 complex, is thus important for TFIID assembly, and may trigger signals from transcriptional effectors. The HEAT domain motif is generally involved in protein/protein interactions, and in A. locustae, the conserved TAF6C domain is formed by five HEAT repeats, tightly packed against each other, defining a single structural domain. TFIID is one of several General Transcription Factors (GTFs), which also include TFIIA, TFIIB, TFIIE, TFIIF and TFIIH, that are involved in the accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays a key role in the recognition of promoter DNA and assembly of the pre-initiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions such as serving as activator-binding sites, core-promoter recognition, or a role in essential catalytic activity. These TAFs, with the help of specific activators, are required only for expression of a subset of genes and are not universally involved for transcription, as are GTFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold domain (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFs and many other transcription factors. TFIID has a histone octamer-like substructure. TAF6 is a shared subunit of histone acetyltransferase complex SAGA and TFIID complexes. The N-terminal HFD of TAF6, interacts with the HFD of TAF9 and makes a novel histone-like heterodimer that is structurally related to histones H4 and H3. TAF6 may also interact with the downstream core promoter element (DPE).


:

Pssm-ID: 381749  Cd Length: 216  Bit Score: 343.47  E-value: 2.78e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 261 HELSVEQQLYYKEITEACVGSCEAKRAEALQSIATDPGLYQMLPRFSTFISEGVRVNVVqnNLALLIYLMRMVKALMDNP 340
Cdd:cd08050     2 HVLSKELQLYFEKITEALLGDDEELRKAALASLRTDPGLQPLLPYFVQFIAEGVTKNLR--NLALLIYLLRMVRALLDNP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 341 TLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTR 420
Cdd:cd08050    80 HLFLEPYLHQLLPSVLTCLLAKQLGSRPPTDNHWALRDFAASLLAQICKKYSTSYPTLQPRITKTLLKALLDPSKPLTTH 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1911217435 421 YGSIAGLAELGHDVIKTLILPRLQQEGERIRSVLDGPVLSNIDRIGADHVQSLLLKH 477
Cdd:cd08050   160 YGAIVGLAALGPEAVRALLLPNLKAYLERLESELEDSSSNALKRIEAEKVYGALLKA 216
TAF6 super family cl34898
Transcription initiation factor TFIID, subunit TAF6 (also component of histone ...
56-455 1.15e-95

Transcription initiation factor TFIID, subunit TAF6 (also component of histone acetyltransferase SAGA) [Transcription];


The actual alignment was detected with superfamily member COG5095:

Pssm-ID: 227426 [Multi-domain]  Cd Length: 450  Bit Score: 303.82  E-value: 1.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  56 LSNTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYGFHA 135
Cdd:COG5095     1 MSLTLWSKETLKDVAESLGISNIDDDALRALAMDLEYRIKEVCQEASKFMVHSKRTVLTIDDISYALRSLNVEPLYGYDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 136 QEFIPF-RFASGGGRELYFYEEKEVDLSDIINTPLPRVPLDVCLKAHWLSIEGCQPAIPENPPPAPKEQQKAEATEPLks 214
Cdd:COG5095    81 SRPLQFsLVFRGLGQSVYYLDDEEVDFEEYINRPLPKVPRRVSIQSHWLAIEGVQPAIPQNPILLDKPVAKWASKDTL-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 215 akpgqeedgplkskgqGAAPADGKGKEKKAPPLLEGGPFRLKPRSIHELSVEQQLYYKEITEACVG-SCEAKRAEALQSI 293
Cdd:COG5095   159 ----------------GVMPGASTAAYQARNGVTSMENAELKPLVKHVLSKELQMYFDKVISALLDeSDEQTRDAALESL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 294 ATDPGLYQMLPRFSTFISEGVRVNVvqNNLALLIYLMRMVKALMDNPTLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNH 373
Cdd:COG5095   223 RNDSGLHQLVPYFIHFFNEQITKNL--KNLEKLTTVVMMYSSLLKNKYIFVDPYLHQLMPSILTCLIAKKLGNVPDDHEH 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 374 WALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDVIKTLILPRLQQEGERIRSV 453
Cdd:COG5095   301 YALRDVAADLLKYVFSNFSSSYKTLKPRVTRTLLKAFLDREKTESTQYGALKGLSILSKEVIRTVIKPNADYYVRLVNKT 380

                  ..
gi 1911217435 454 LD 455
Cdd:COG5095   381 LE 382
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
604-726 1.36e-04

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: 45.36  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 604 STSAPGSGSTTTSPVTTTVPSVQPIVKLVSTATAAPPSTAPSGPGSVQkyivvslPPTGDGKGGPPTSHPSPVPPQSSAP 683
Cdd:PRK07764  592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEA-------SAAPAPGVAAPEHHPKHVAVPDASD 664
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1911217435 684 SPLGGSALCGGKQEAGDSPPPAPGTPKANGSQPPGSGSPQPAP 726
Cdd:PRK07764  665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA 707
PHA03247 super family cl33720
large tegument protein UL36; Provisional
480-726 1.14e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  480 PVLAKLRPPPDNQDAYRAEFGSLGPLLCSHVVKARAQAALQAQQVNRTTLTITQP---------------RPT---LTLS 541
Cdd:PHA03247  2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAaqassppqrprrraaRPTvgsLTSL 2698
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  542 QAPQPGPRTPGLLKVPGSIALPVQTLVSARAAAPPQPSPPPTKFIVMSSSSSASSTQQVLSLSTSA--PGSGSTTTSPVT 619
Cdd:PHA03247  2699 ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgpPAPAPPAAPAAG 2778
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  620 TTVPSVQPIVKLVSTATAAPPS-TAPSGPGSVQKYIVVSLPPTGDGKGG-PPTSHPSPVPPQSSAPSPLGGSALCGGKQE 697
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSpWDPADPPAAVLAPAAALPPAASPAGPlPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1911217435  698 AGD----SPPPAPGTPKANGSQPPGSGSPQPAP 726
Cdd:PHA03247  2859 GGDvrrrPPSRSPAAKPAAPARPPVRRLARPAV 2891
 
Name Accession Description Interval E-value
TAF6C cd08050
C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model ...
261-477 2.78e-114

C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model characterizes the carboxy (C)-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6), which is one of several TAFs that bind TBP and are involved in forming the Transcription Factor IID (TFIID) complex. This C-terminal HEAT repeat domain of TAF6 (TAF6C) is proposed to form a homodimer that effectively bridges the downstream promoter-interacting TAFs (TAF1, -2, and -7) with lobe B of TFIID. This domain influences the TAF6-TAF9 complex, is thus important for TFIID assembly, and may trigger signals from transcriptional effectors. The HEAT domain motif is generally involved in protein/protein interactions, and in A. locustae, the conserved TAF6C domain is formed by five HEAT repeats, tightly packed against each other, defining a single structural domain. TFIID is one of several General Transcription Factors (GTFs), which also include TFIIA, TFIIB, TFIIE, TFIIF and TFIIH, that are involved in the accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays a key role in the recognition of promoter DNA and assembly of the pre-initiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions such as serving as activator-binding sites, core-promoter recognition, or a role in essential catalytic activity. These TAFs, with the help of specific activators, are required only for expression of a subset of genes and are not universally involved for transcription, as are GTFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold domain (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFs and many other transcription factors. TFIID has a histone octamer-like substructure. TAF6 is a shared subunit of histone acetyltransferase complex SAGA and TFIID complexes. The N-terminal HFD of TAF6, interacts with the HFD of TAF9 and makes a novel histone-like heterodimer that is structurally related to histones H4 and H3. TAF6 may also interact with the downstream core promoter element (DPE).


Pssm-ID: 381749  Cd Length: 216  Bit Score: 343.47  E-value: 2.78e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 261 HELSVEQQLYYKEITEACVGSCEAKRAEALQSIATDPGLYQMLPRFSTFISEGVRVNVVqnNLALLIYLMRMVKALMDNP 340
Cdd:cd08050     2 HVLSKELQLYFEKITEALLGDDEELRKAALASLRTDPGLQPLLPYFVQFIAEGVTKNLR--NLALLIYLLRMVRALLDNP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 341 TLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTR 420
Cdd:cd08050    80 HLFLEPYLHQLLPSVLTCLLAKQLGSRPPTDNHWALRDFAASLLAQICKKYSTSYPTLQPRITKTLLKALLDPSKPLTTH 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1911217435 421 YGSIAGLAELGHDVIKTLILPRLQQEGERIRSVLDGPVLSNIDRIGADHVQSLLLKH 477
Cdd:cd08050   160 YGAIVGLAALGPEAVRALLLPNLKAYLERLESELEDSSSNALKRIEAEKVYGALLKA 216
TAF6 COG5095
Transcription initiation factor TFIID, subunit TAF6 (also component of histone ...
56-455 1.15e-95

Transcription initiation factor TFIID, subunit TAF6 (also component of histone acetyltransferase SAGA) [Transcription];


Pssm-ID: 227426 [Multi-domain]  Cd Length: 450  Bit Score: 303.82  E-value: 1.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  56 LSNTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYGFHA 135
Cdd:COG5095     1 MSLTLWSKETLKDVAESLGISNIDDDALRALAMDLEYRIKEVCQEASKFMVHSKRTVLTIDDISYALRSLNVEPLYGYDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 136 QEFIPF-RFASGGGRELYFYEEKEVDLSDIINTPLPRVPLDVCLKAHWLSIEGCQPAIPENPPPAPKEQQKAEATEPLks 214
Cdd:COG5095    81 SRPLQFsLVFRGLGQSVYYLDDEEVDFEEYINRPLPKVPRRVSIQSHWLAIEGVQPAIPQNPILLDKPVAKWASKDTL-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 215 akpgqeedgplkskgqGAAPADGKGKEKKAPPLLEGGPFRLKPRSIHELSVEQQLYYKEITEACVG-SCEAKRAEALQSI 293
Cdd:COG5095   159 ----------------GVMPGASTAAYQARNGVTSMENAELKPLVKHVLSKELQMYFDKVISALLDeSDEQTRDAALESL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 294 ATDPGLYQMLPRFSTFISEGVRVNVvqNNLALLIYLMRMVKALMDNPTLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNH 373
Cdd:COG5095   223 RNDSGLHQLVPYFIHFFNEQITKNL--KNLEKLTTVVMMYSSLLKNKYIFVDPYLHQLMPSILTCLIAKKLGNVPDDHEH 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 374 WALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDVIKTLILPRLQQEGERIRSV 453
Cdd:COG5095   301 YALRDVAADLLKYVFSNFSSSYKTLKPRVTRTLLKAFLDREKTESTQYGALKGLSILSKEVIRTVIKPNADYYVRLVNKT 380

                  ..
gi 1911217435 454 LD 455
Cdd:COG5095   381 LE 382
TAF6_C pfam07571
TAF6 C-terminal HEAT repeat domain; TAF6_C is the C-terminal domain of the TAF6 subunit of the ...
355-444 1.65e-42

TAF6 C-terminal HEAT repeat domain; TAF6_C is the C-terminal domain of the TAF6 subunit of the general transcription factor TFIID. The crystal structure reveals the presence of five conserved HEAT repeats. This region is necessary for the complexing together of the subunits TAF5, TAF6 and TAF9.


Pssm-ID: 462212  Cd Length: 90  Bit Score: 148.78  E-value: 1.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 355 VMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDV 434
Cdd:pfam07571   1 ILTCLVAKKLGARPPLDDHWALRDFAASLLAQICRKYSSSYPTLKPRITRTLLKALLDPKKPLGTHYGALIGLAALGPEA 80
                          90
                  ....*....|
gi 1911217435 435 IKTLILPRLQ 444
Cdd:pfam07571  81 IRALILPNLK 90
HFD_TAF6 cd22931
histone-fold domain found in transcription initiation factor TFIID subunit 6 (TAF6) and ...
59-124 5.57e-31

histone-fold domain found in transcription initiation factor TFIID subunit 6 (TAF6) and similar proteins; TAF6, also called TATA Binding Protein (TBP) associated factor 6, RNA polymerase II TBP-associated factor subunit E, transcription initiation factor TFIID 70 kDa subunit (TAF(II)70, TAFII-70, TAFII70), or transcription initiation factor TFIID 80 kDa subunit (TAF(II)80, TAFII-80, TAFII80), is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC.


Pssm-ID: 467055  Cd Length: 66  Bit Score: 115.29  E-value: 5.57e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911217435  59 TVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKL 124
Cdd:cd22931     1 SVLPPESVKVIAESVGISNLSDEAARALADDVEYRLREIIQDALKFMRHSKRTKLTTDDIDNALRL 66
TAF pfam02969
TATA box binding protein associated factor (TAF); TAF proteins adopt a histone-like fold.
58-123 6.44e-30

TATA box binding protein associated factor (TAF); TAF proteins adopt a histone-like fold.


Pssm-ID: 427084  Cd Length: 66  Bit Score: 112.53  E-value: 6.44e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911217435  58 NTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALK 123
Cdd:pfam02969   1 TSIIPQESVKVVAESLGITNLNDEAAALLAEDVEYRLKEIVQEAAKFMRHSKRTKLTVADVDSALR 66
TAF smart00803
TATA box binding protein associated factor; TAFs (TATA box binding protein associated factors) ...
59-123 7.48e-30

TATA box binding protein associated factor; TAFs (TATA box binding protein associated factors) are part of the transcription initiation factor TFIID multimeric protein complex. TFIID is composed of the TATA box binding protein (TBP) and a number of TAFs. The TAFs provide binding sites for many different transcriptional activators and co-activators that modulate transcription initiation by Pol II. TAF proteins adopt a histone-like fold.


Pssm-ID: 129039  Cd Length: 65  Bit Score: 112.33  E-value: 7.48e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911217435   59 TVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALK 123
Cdd:smart00803   1 SWLPKETIKDVAESLGIGNLSDEAAKLLAEDVEYRIKEIVQEALKFMRHSKRTTLTTSDIDSALR 65
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
604-726 1.36e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 604 STSAPGSGSTTTSPVTTTVPSVQPIVKLVSTATAAPPSTAPSGPGSVQkyivvslPPTGDGKGGPPTSHPSPVPPQSSAP 683
Cdd:PRK07764  592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEA-------SAAPAPGVAAPEHHPKHVAVPDASD 664
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1911217435 684 SPLGGSALCGGKQEAGDSPPPAPGTPKANGSQPPGSGSPQPAP 726
Cdd:PRK07764  665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA 707
PHA03247 PHA03247
large tegument protein UL36; Provisional
480-726 1.14e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  480 PVLAKLRPPPDNQDAYRAEFGSLGPLLCSHVVKARAQAALQAQQVNRTTLTITQP---------------RPT---LTLS 541
Cdd:PHA03247  2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAaqassppqrprrraaRPTvgsLTSL 2698
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  542 QAPQPGPRTPGLLKVPGSIALPVQTLVSARAAAPPQPSPPPTKFIVMSSSSSASSTQQVLSLSTSA--PGSGSTTTSPVT 619
Cdd:PHA03247  2699 ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgpPAPAPPAAPAAG 2778
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  620 TTVPSVQPIVKLVSTATAAPPS-TAPSGPGSVQKYIVVSLPPTGDGKGG-PPTSHPSPVPPQSSAPSPLGGSALCGGKQE 697
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSpWDPADPPAAVLAPAAALPPAASPAGPlPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1911217435  698 AGD----SPPPAPGTPKANGSQPPGSGSPQPAP 726
Cdd:PHA03247  2859 GGDvrrrPPSRSPAAKPAAPARPPVRRLARPAV 2891
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
632-725 1.56e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 41.83  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 632 VSTATAAPPSTAPSgpgsVQKYIVVSLPPTGDGKGGPPTShPSPVP----PQSSAPSPLGGSALCGGKQEAGDSPPPAPG 707
Cdd:pfam05109 454 VPTNLTAPASTGPT----VSTADVTSPTPAGTTSGASPVT-PSPSPrdngTESKAPDMTSPTSAVTTPTPNATSPTPAVT 528
                          90
                  ....*....|....*....
gi 1911217435 708 TPKANGSQPP-GSGSPQPA 725
Cdd:pfam05109 529 TPTPNATSPTlGKTSPTSA 547
 
Name Accession Description Interval E-value
TAF6C cd08050
C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model ...
261-477 2.78e-114

C-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6); This model characterizes the carboxy (C)-terminal domain of TATA Binding Protein (TBP) Associated Factor 6 (TAF6), which is one of several TAFs that bind TBP and are involved in forming the Transcription Factor IID (TFIID) complex. This C-terminal HEAT repeat domain of TAF6 (TAF6C) is proposed to form a homodimer that effectively bridges the downstream promoter-interacting TAFs (TAF1, -2, and -7) with lobe B of TFIID. This domain influences the TAF6-TAF9 complex, is thus important for TFIID assembly, and may trigger signals from transcriptional effectors. The HEAT domain motif is generally involved in protein/protein interactions, and in A. locustae, the conserved TAF6C domain is formed by five HEAT repeats, tightly packed against each other, defining a single structural domain. TFIID is one of several General Transcription Factors (GTFs), which also include TFIIA, TFIIB, TFIIE, TFIIF and TFIIH, that are involved in the accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays a key role in the recognition of promoter DNA and assembly of the pre-initiation complex. The TFIID complex is composed of the TBP and at least 13 TAFs. TAFs are named after their electrophoretic mobility in polyacrylamide gels in different species. A new, unified nomenclature has been suggested for the pol II TAFs to show the relationship between TAF orthologs and paralogs. Several hypotheses are proposed for TAFs' functions such as serving as activator-binding sites, core-promoter recognition, or a role in essential catalytic activity. These TAFs, with the help of specific activators, are required only for expression of a subset of genes and are not universally involved for transcription, as are GTFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. Several TAFs interact via histone-fold domain (HFD) motifs; the HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamers. The minimal HFD contains three alpha-helices linked by two loops and is found in core histones, TAFs and many other transcription factors. TFIID has a histone octamer-like substructure. TAF6 is a shared subunit of histone acetyltransferase complex SAGA and TFIID complexes. The N-terminal HFD of TAF6, interacts with the HFD of TAF9 and makes a novel histone-like heterodimer that is structurally related to histones H4 and H3. TAF6 may also interact with the downstream core promoter element (DPE).


Pssm-ID: 381749  Cd Length: 216  Bit Score: 343.47  E-value: 2.78e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 261 HELSVEQQLYYKEITEACVGSCEAKRAEALQSIATDPGLYQMLPRFSTFISEGVRVNVVqnNLALLIYLMRMVKALMDNP 340
Cdd:cd08050     2 HVLSKELQLYFEKITEALLGDDEELRKAALASLRTDPGLQPLLPYFVQFIAEGVTKNLR--NLALLIYLLRMVRALLDNP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 341 TLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTR 420
Cdd:cd08050    80 HLFLEPYLHQLLPSVLTCLLAKQLGSRPPTDNHWALRDFAASLLAQICKKYSTSYPTLQPRITKTLLKALLDPSKPLTTH 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1911217435 421 YGSIAGLAELGHDVIKTLILPRLQQEGERIRSVLDGPVLSNIDRIGADHVQSLLLKH 477
Cdd:cd08050   160 YGAIVGLAALGPEAVRALLLPNLKAYLERLESELEDSSSNALKRIEAEKVYGALLKA 216
TAF6 COG5095
Transcription initiation factor TFIID, subunit TAF6 (also component of histone ...
56-455 1.15e-95

Transcription initiation factor TFIID, subunit TAF6 (also component of histone acetyltransferase SAGA) [Transcription];


Pssm-ID: 227426 [Multi-domain]  Cd Length: 450  Bit Score: 303.82  E-value: 1.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  56 LSNTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYGFHA 135
Cdd:COG5095     1 MSLTLWSKETLKDVAESLGISNIDDDALRALAMDLEYRIKEVCQEASKFMVHSKRTVLTIDDISYALRSLNVEPLYGYDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 136 QEFIPF-RFASGGGRELYFYEEKEVDLSDIINTPLPRVPLDVCLKAHWLSIEGCQPAIPENPPPAPKEQQKAEATEPLks 214
Cdd:COG5095    81 SRPLQFsLVFRGLGQSVYYLDDEEVDFEEYINRPLPKVPRRVSIQSHWLAIEGVQPAIPQNPILLDKPVAKWASKDTL-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 215 akpgqeedgplkskgqGAAPADGKGKEKKAPPLLEGGPFRLKPRSIHELSVEQQLYYKEITEACVG-SCEAKRAEALQSI 293
Cdd:COG5095   159 ----------------GVMPGASTAAYQARNGVTSMENAELKPLVKHVLSKELQMYFDKVISALLDeSDEQTRDAALESL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 294 ATDPGLYQMLPRFSTFISEGVRVNVvqNNLALLIYLMRMVKALMDNPTLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNH 373
Cdd:COG5095   223 RNDSGLHQLVPYFIHFFNEQITKNL--KNLEKLTTVVMMYSSLLKNKYIFVDPYLHQLMPSILTCLIAKKLGNVPDDHEH 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 374 WALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDVIKTLILPRLQQEGERIRSV 453
Cdd:COG5095   301 YALRDVAADLLKYVFSNFSSSYKTLKPRVTRTLLKAFLDREKTESTQYGALKGLSILSKEVIRTVIKPNADYYVRLVNKT 380

                  ..
gi 1911217435 454 LD 455
Cdd:COG5095   381 LE 382
TAF6_C pfam07571
TAF6 C-terminal HEAT repeat domain; TAF6_C is the C-terminal domain of the TAF6 subunit of the ...
355-444 1.65e-42

TAF6 C-terminal HEAT repeat domain; TAF6_C is the C-terminal domain of the TAF6 subunit of the general transcription factor TFIID. The crystal structure reveals the presence of five conserved HEAT repeats. This region is necessary for the complexing together of the subunits TAF5, TAF6 and TAF9.


Pssm-ID: 462212  Cd Length: 90  Bit Score: 148.78  E-value: 1.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 355 VMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDV 434
Cdd:pfam07571   1 ILTCLVAKKLGARPPLDDHWALRDFAASLLAQICRKYSSSYPTLKPRITRTLLKALLDPKKPLGTHYGALIGLAALGPEA 80
                          90
                  ....*....|
gi 1911217435 435 IKTLILPRLQ 444
Cdd:pfam07571  81 IRALILPNLK 90
HFD_TAF6 cd22931
histone-fold domain found in transcription initiation factor TFIID subunit 6 (TAF6) and ...
59-124 5.57e-31

histone-fold domain found in transcription initiation factor TFIID subunit 6 (TAF6) and similar proteins; TAF6, also called TATA Binding Protein (TBP) associated factor 6, RNA polymerase II TBP-associated factor subunit E, transcription initiation factor TFIID 70 kDa subunit (TAF(II)70, TAFII-70, TAFII70), or transcription initiation factor TFIID 80 kDa subunit (TAF(II)80, TAFII-80, TAFII80), is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC.


Pssm-ID: 467055  Cd Length: 66  Bit Score: 115.29  E-value: 5.57e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911217435  59 TVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKL 124
Cdd:cd22931     1 SVLPPESVKVIAESVGISNLSDEAARALADDVEYRLREIIQDALKFMRHSKRTKLTTDDIDNALRL 66
TAF pfam02969
TATA box binding protein associated factor (TAF); TAF proteins adopt a histone-like fold.
58-123 6.44e-30

TATA box binding protein associated factor (TAF); TAF proteins adopt a histone-like fold.


Pssm-ID: 427084  Cd Length: 66  Bit Score: 112.53  E-value: 6.44e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1911217435  58 NTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALK 123
Cdd:pfam02969   1 TSIIPQESVKVVAESLGITNLNDEAAALLAEDVEYRLKEIVQEAAKFMRHSKRTKLTVADVDSALR 66
TAF smart00803
TATA box binding protein associated factor; TAFs (TATA box binding protein associated factors) ...
59-123 7.48e-30

TATA box binding protein associated factor; TAFs (TATA box binding protein associated factors) are part of the transcription initiation factor TFIID multimeric protein complex. TFIID is composed of the TATA box binding protein (TBP) and a number of TAFs. The TAFs provide binding sites for many different transcriptional activators and co-activators that modulate transcription initiation by Pol II. TAF proteins adopt a histone-like fold.


Pssm-ID: 129039  Cd Length: 65  Bit Score: 112.33  E-value: 7.48e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1911217435   59 TVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALK 123
Cdd:smart00803   1 SWLPKETIKDVAESLGIGNLSDEAAKLLAEDVEYRIKEIVQEALKFMRHSKRTTLTTSDIDSALR 65
HFD_TAF6-like cd22917
histone-fold domain found in transcription initiation factor TFIID subunit 6 (TAF6) and ...
61-124 5.04e-24

histone-fold domain found in transcription initiation factor TFIID subunit 6 (TAF6) and similar proteins; This subfamily includes TAF6 and TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L (TAF6L). TAF6, also called TATA Binding Protein (TBP) associated factor 6, RNA polymerase II TBP-associated factor subunit E, transcription initiation factor TFIID 70 kDa subunit (TAF(II)70, TAFII-70, TAFII70), or transcription initiation factor TFIID 80 kDa subunit, (TAF(II)80, TAFII-80, TAFII80), is a TBP-associated factor (TAF). TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex, and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. TFIID and PCAF are composed of TATA binding protein (TBP) and several TAFs. TBP is not part of TFTC. TAF6L, also called PCAF-associated factor 65-alpha (PAF65-alpha), is a component of the PCAF complex, which can efficiently acetylate histones in a nucleosomal context. The PCAF complex is composed of several TAFs and PCAF-associated factors (PAFs). It might be the human version of the yeast SAGA complex. With TAF5L, TAF6L acts as an epigenetic regulator essential for somatic reprogramming. It also regulates target genes through H3K9ac deposition and MYC recruitment, which trigger the MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state.


Pssm-ID: 467042  Cd Length: 64  Bit Score: 95.74  E-value: 5.04e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1911217435  61 LPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKL 124
Cdd:cd22917     1 FPNDTVKLIAESLGIVNLSEEVAQLLAEDAEYRILEVIQNAKKFAHHSKRKKLTADDINNALRL 64
HFD_TAF6L cd22932
histone-fold domain found in TAF6-like RNA polymerase II p300/CBP-associated factor-associated ...
61-132 1.71e-22

histone-fold domain found in TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L (TAF6L) and similar proteins; TAF6L, also called PCAF-associated factor 65-alpha (PAF65-alpha), is a component of the PCAF complex, which can efficiently acetylate histones in a nucleosomal context. The PCAF complex is composed of several TBP-associated factors (TAFs) and PCAF-associated factors (PAFs). It might be the human version of the yeast SAGA complex. With TAF5L, TAF6L acts as an epigenetic regulator essential for somatic reprogramming. It also regulates target genes through H3K9ac deposition and MYC recruitment, which trigger the MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state.


Pssm-ID: 467056  Cd Length: 72  Bit Score: 91.49  E-value: 1.71e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1911217435  61 LPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYG 132
Cdd:cd22932     1 LSTESIRLMAESLGISELSEDVAKLLAEDVSYRLREVIQNASQFMRHSKRRKLTTEDVNRALKWSDVEPVYG 72
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
61-123 1.09e-07

histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


Pssm-ID: 467021  Cd Length: 63  Bit Score: 49.14  E-value: 1.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911217435  61 LPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALK 123
Cdd:cd00076     1 LLRSAVARILKSAGFDSVSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
604-726 1.36e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 604 STSAPGSGSTTTSPVTTTVPSVQPIVKLVSTATAAPPSTAPSGPGSVQkyivvslPPTGDGKGGPPTSHPSPVPPQSSAP 683
Cdd:PRK07764  592 PGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEA-------SAAPAPGVAAPEHHPKHVAVPDASD 664
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1911217435 684 SPLGGSALCGGKQEAGDSPPPAPGTPKANGSQPPGSGSPQPAP 726
Cdd:PRK07764  665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA 707
PHA03247 PHA03247
large tegument protein UL36; Provisional
480-726 1.14e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  480 PVLAKLRPPPDNQDAYRAEFGSLGPLLCSHVVKARAQAALQAQQVNRTTLTITQP---------------RPT---LTLS 541
Cdd:PHA03247  2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAaqassppqrprrraaRPTvgsLTSL 2698
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  542 QAPQPGPRTPGLLKVPGSIALPVQTLVSARAAAPPQPSPPPTKFIVMSSSSSASSTQQVLSLSTSA--PGSGSTTTSPVT 619
Cdd:PHA03247  2699 ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgpPAPAPPAAPAAG 2778
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  620 TTVPSVQPIVKLVSTATAAPPS-TAPSGPGSVQKYIVVSLPPTGDGKGG-PPTSHPSPVPPQSSAPSPLGGSALCGGKQE 697
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSpWDPADPPAAVLAPAAALPPAASPAGPlPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1911217435  698 AGD----SPPPAPGTPKANGSQPPGSGSPQPAP 726
Cdd:PHA03247  2859 GGDvrrrPPSRSPAAKPAAPARPPVRRLARPAV 2891
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
606-726 1.28e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 606 SAPGSGSTTTSPVTTTVPSVQPIVKLVSTATAAPPSTAPSGPGSVQKYIVVSLPPTGDGKGGPPTSHPSPVPPQSSAPSP 685
Cdd:PRK07003  379 AVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARAS 458
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1911217435 686 LGGSALCGGKQE----------AGDSPPPAPGTPKANGSQPPGSGSPQPAP 726
Cdd:PRK07003  459 ADSRCDERDAQPpadsgsasapASDAPPDAAFEPAPRAAAPSAATPAAVPD 509
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
632-725 1.56e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 41.83  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 632 VSTATAAPPSTAPSgpgsVQKYIVVSLPPTGDGKGGPPTShPSPVP----PQSSAPSPLGGSALCGGKQEAGDSPPPAPG 707
Cdd:pfam05109 454 VPTNLTAPASTGPT----VSTADVTSPTPAGTTSGASPVT-PSPSPrdngTESKAPDMTSPTSAVTTPTPNATSPTPAVT 528
                          90
                  ....*....|....*....
gi 1911217435 708 TPKANGSQPP-GSGSPQPA 725
Cdd:pfam05109 529 TPTPNATSPTlGKTSPTSA 547
HFD_archaea_histone-like cd22909
histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription ...
61-123 1.82e-03

histone-fold domain mainly found in archaeal histone-fold proteins, histone-like transcription regulators and similar proteins; The family includes many archaeal histone-fold proteins and histone-like transcription regulators, which may bind and compact DNA (95 to 150 base pairs) to form nucleosome-like structures that contain positive DNA supercoils. They can increase the resistance of DNA to thermal denaturation.


Pssm-ID: 467034  Cd Length: 64  Bit Score: 37.14  E-value: 1.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1911217435  61 LPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALK 123
Cdd:cd22909     2 LPKAPVKRIIKKAGAERVSEDAAEELAKLLEEIAEEIAEEAVKLAKHAGRKTVKAEDIELAVK 64
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
632-726 2.15e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 632 VSTATAAPPSTAPSGPGSvqkyIVVSLPPTGDGKGGPPTSHPSPVPPQSSAPSPLGGSALCGGKQEAGDSPPPAPGTPKA 711
Cdd:PRK07764  398 APSAAAAAPAAAPAPAAA----APAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAA 473
                          90
                  ....*....|....*
gi 1911217435 712 NGSQPPGSGSPQPAP 726
Cdd:PRK07764  474 PEPTAAPAPAPPAAP 488
PHA03264 PHA03264
envelope glycoprotein D; Provisional
638-720 3.65e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 40.37  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435 638 APPSTAPSGPGSVQKYIVVSLP-PTGDGKGGPPTSHPSPVPPQSSAPS--PLGGSALcggkqEAGDSPPPAPGTPKANGS 714
Cdd:PHA03264  285 AKPEPGPVEDGAPGRETGGEGEgPEPAGRDGAAGGEPKPGPPRPAPDAdrPEGWPSL-----EAITFPPPTPATPAVPRA 359

                  ....*.
gi 1911217435 715 QPPGSG 720
Cdd:PHA03264  360 RPVIVG 365
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
635-724 5.28e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1911217435  635 ATAAPPSTAPSGPGSVQKYIVVSLPPTGDGKGGPPTSHPSPVPPQSSAPSPLGGSALCGGKQEAGDSPPPAPGTPKANGS 714
Cdd:PHA03307   119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTP 198
                           90
                   ....*....|
gi 1911217435  715 QPPGSGSPQP 724
Cdd:PHA03307   199 PAAASPRPPR 208
 
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.
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