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Conserved domains on  [gi|966923833|ref|XP_014981213|]
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TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L isoform X2 [Macaca mulatta]

Protein Classification

TAF5 family protein( domain architecture ID 10169025)

TATA binding protein (TBP) associated factor 5 (TAF5) family protein, similar to TAF5 which is one of several TAFs that bind TBP and are involved in forming the transcription factor IID (TFIID) complex

Gene Ontology:  GO:0006357

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
180-449 5.87e-78

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 249.44  E-value: 5.87e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 180 NTAEISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFL 259
Cdd:COG2319  166 TSVAFSPDGKLLASGSDDGTVRLWDLAT--------------------------------GKLLRTLTGHTGAVRSVAFS 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 260 ADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDC 339
Cdd:COG2319  214 PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNS 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 340 VKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTD 419
Cdd:COG2319  294 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTG 373

                        250       260       270
                 ....*....|....*....|....*....|
gi 966923833 420 NITSLTFSPDSGLIASASMDNSVRVWDIRN 449
Cdd:COG2319  374 AVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
TAF5_NTD2 cd08044
TAF5_NTD2 is the second conserved N-terminal region of TATA Binding Protein (TBP) Associated ...
 2-109 7.76e-34

TAF5_NTD2 is the second conserved N-terminal region of TATA Binding Protein (TBP) Associated Factor 5 (TAF5), involved in forming Transcription Factor IID (TFIID); The TATA Binding Protein (TBP) Associated Factor 5 (TAF5) is one of several TAFs that bind TBP and are involved in forming Transcription Factor IID (TFIID) complex. TAF5 contains three domains, two conserved sequence motifs at the N-terminal and one at the C-terminal region. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and assembly of the preinitiation complex. TFIID complex is composed of the TBP and at least 13 TAFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. TAF5 may play a major role in forming TFIID and its related complexes. TAFs from various species were originally named by their predicted molecular weight or their electrophoretic mobility in polyacrylamide gels. A new, unified nomenclature for the pol II TAFs has been suggested to show the relationship between TAF orthologs and paralogs. TAF5 has a paralog gene (TAF5L) which has a redundant function. Several hypotheses are proposed for TAFs functions such as serving as activator-binding sites, core-promoter recognition or a role in essential catalytic activity. C-terminus of TAF5 contains six WD40 repeats that likely form a closed beta propeller structure and may be involved in protein-protein interaction. The first part of the TAF5 N-terminal (TAF5_NTD1) homodimerizes in the absence of other TAFs. The second conserved N-terminal part of TAF5 (TAF5_NTD2) has an alpha-helical domain. One study has shown that TAF5_NTD2 homodimerizes only at high concentration of calcium but not any other metals. No dimerization was observed in other structural studies of TAF_NTD2. Several TAFs interact via histone-fold (HFD) motifs; HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamer. However, TAF5 does not have a HFD motif.


:

Pssm-ID: 176269  Cd Length: 133  Bit Score: 124.23  E-value: 7.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833   2 PLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFlqNASQKDVIEQLQTTQTIQDILSNFKLRAFLDNKYVVRLQEDSYN 81
Cdd:cd08044   28 QLLYPIFVHSYLDLVASGHLEEAKSFFERFSGDF--EDSHSEDIKKLSSITTPEHLKENELAKLFRSNKYVIRMSRDAYS 105

                         90       100
                 ....*....|....*....|....*...
gi 966923833  82 YLIRYLQSDNNTALCKVLTLHIHLDVQP 109
Cdd:cd08044  106 LLLRFLESWGGSLLLKILNEHIDIDVRD 133
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
180-449 5.87e-78

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 249.44  E-value: 5.87e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 180 NTAEISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFL 259
Cdd:COG2319  166 TSVAFSPDGKLLASGSDDGTVRLWDLAT--------------------------------GKLLRTLTGHTGAVRSVAFS 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 260 ADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDC 339
Cdd:COG2319  214 PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNS 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 340 VKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTD 419
Cdd:COG2319  294 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTG 373

                        250       260       270
                 ....*....|....*....|....*....|
gi 966923833 420 NITSLTFSPDSGLIASASMDNSVRVWDIRN 449
Cdd:COG2319  374 AVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 184-489 8.39e-72

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 229.53  E-value: 8.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 184 ISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFLADSS 263
Cdd:cd00200   17 FSPDGKLLATGSGDGTIKVWDLET--------------------------------GELLRTLKGHTGPVRDVAASADGT 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 264 GLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFH 343
Cdd:cd00200   65 YLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 344 PNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTDNITS 423
Cdd:cd00200  145 PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966923833 424 LTFSPDSGLIASASMDNSVRVWDIRNTygsapadgsssELVGVYTGQMSNVLSVQFMACNLLLVTG 489
Cdd:cd00200  225 VAFSPDGYLLASGSEDGTIRVWDLRTG-----------ECVQTLSGHTNSVTSLAWSPDGKRLASG 279
TAF5_NTD2 cd08044
TAF5_NTD2 is the second conserved N-terminal region of TATA Binding Protein (TBP) Associated ...
 2-109 7.76e-34

TAF5_NTD2 is the second conserved N-terminal region of TATA Binding Protein (TBP) Associated Factor 5 (TAF5), involved in forming Transcription Factor IID (TFIID); The TATA Binding Protein (TBP) Associated Factor 5 (TAF5) is one of several TAFs that bind TBP and are involved in forming Transcription Factor IID (TFIID) complex. TAF5 contains three domains, two conserved sequence motifs at the N-terminal and one at the C-terminal region. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and assembly of the preinitiation complex. TFIID complex is composed of the TBP and at least 13 TAFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. TAF5 may play a major role in forming TFIID and its related complexes. TAFs from various species were originally named by their predicted molecular weight or their electrophoretic mobility in polyacrylamide gels. A new, unified nomenclature for the pol II TAFs has been suggested to show the relationship between TAF orthologs and paralogs. TAF5 has a paralog gene (TAF5L) which has a redundant function. Several hypotheses are proposed for TAFs functions such as serving as activator-binding sites, core-promoter recognition or a role in essential catalytic activity. C-terminus of TAF5 contains six WD40 repeats that likely form a closed beta propeller structure and may be involved in protein-protein interaction. The first part of the TAF5 N-terminal (TAF5_NTD1) homodimerizes in the absence of other TAFs. The second conserved N-terminal part of TAF5 (TAF5_NTD2) has an alpha-helical domain. One study has shown that TAF5_NTD2 homodimerizes only at high concentration of calcium but not any other metals. No dimerization was observed in other structural studies of TAF_NTD2. Several TAFs interact via histone-fold (HFD) motifs; HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamer. However, TAF5 does not have a HFD motif.


Pssm-ID: 176269  Cd Length: 133  Bit Score: 124.23  E-value: 7.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833   2 PLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFlqNASQKDVIEQLQTTQTIQDILSNFKLRAFLDNKYVVRLQEDSYN 81
Cdd:cd08044   28 QLLYPIFVHSYLDLVASGHLEEAKSFFERFSGDF--EDSHSEDIKKLSSITTPEHLKENELAKLFRSNKYVIRMSRDAYS 105

                         90       100
                 ....*....|....*....|....*...
gi 966923833  82 YLIRYLQSDNNTALCKVLTLHIHLDVQP 109
Cdd:cd08044  106 LLLRFLESWGGSLLLKILNEHIDIDVRD 133
TFIID_NTD2 pfam04494
WD40 associated region in TFIID subunit, NTD2 domain; This region is an all-alpha domain ...
 1-103 9.38e-31

WD40 associated region in TFIID subunit, NTD2 domain; This region is an all-alpha domain associated with the WD40 helical bundle of the TAF5 subunit of transcription factor TFIID. The domain has distant structural similarity to RNA polymerase II CTD interacting factors. It contains several conserved clefts that are likely to be critical for TFIID complex assembly. The TAF5 subunit is present twice in the TFIID complex and is critical for the function and assembly of the complex, and the NTD2 and N-terminal domain is crucial for homodimerization.


Pssm-ID: 461330  Cd Length: 130  Bit Score: 115.67  E-value: 9.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833    1 MPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFLqnASQKDVIEQLQTTQTIQDILSNFKLRAFLDNKYVVRLQEDSY 80
Cdd:pfam04494  30 RRLLYPVFVHSYLDLVAKGHIEEAKEFFEKFRGDHE--ALHGDDLRKLAGITLPEHLEENELAKLFRSNKYRIRLSRYSF 107

                          90       100
                  ....*....|....*....|...
gi 966923833   81 NYLIRYLQSDNNTALCKVLTLHI 103
Cdd:pfam04494 108 DLLLRFLQENESSVILRIINEHL 130
PTZ00421 PTZ00421
coronin; Provisional
 329-462 1.44e-11

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 66.45  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 329 IYAGHLADVDCVKFHP-NSNYLATGSTDKTVRLWSA-----QQGNSVRL--FTGHRGPVLSLAFSPNGK-YLASAGEDQR 399
Cdd:PTZ00421  70 ILLGQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIpeeglTQNISDPIvhLQGHTKKVGIVSFHPSAMnVLASAGADMV 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966923833 400 LKLWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRNtyGSAPADGSSSE 462
Cdd:PTZ00421 150 VNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRD--GTIVSSVEAHA 210
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 407-446 6.51e-11

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 56.94  E-value: 6.51e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 966923833   407 SGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWD 446
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
408-446 4.00e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 4.00e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 966923833  408 GTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWD 446
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
180-449 5.87e-78

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 249.44  E-value: 5.87e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 180 NTAEISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFL 259
Cdd:COG2319  166 TSVAFSPDGKLLASGSDDGTVRLWDLAT--------------------------------GKLLRTLTGHTGAVRSVAFS 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 260 ADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDC 339
Cdd:COG2319  214 PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNS 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 340 VKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTD 419
Cdd:COG2319  294 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTG 373

                        250       260       270
                 ....*....|....*....|....*....|
gi 966923833 420 NITSLTFSPDSGLIASASMDNSVRVWDIRN 449
Cdd:COG2319  374 AVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
179-489 7.24e-73

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 236.35  E-value: 7.24e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 179 LNTAEISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRF 258
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLAT--------------------------------GLLLRTLTGHTGAVRSVAF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 259 LADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVD 338
Cdd:COG2319  129 SPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVR 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 339 CVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHT 418
Cdd:COG2319  209 SVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHS 288

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966923833 419 DNITSLTFSPDSGLIASASMDNSVRVWDIrntygsapadgSSSELVGVYTGQMSNVLSVQFMACNLLLVTG 489
Cdd:COG2319  289 GGVNSVAFSPDGKLLASGSDDGTVRLWDL-----------ATGKLLRTLTGHTGAVRSVAFSPDGKTLASG 348
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 184-489 8.39e-72

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 229.53  E-value: 8.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 184 ISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFLADSS 263
Cdd:cd00200   17 FSPDGKLLATGSGDGTIKVWDLET--------------------------------GELLRTLKGHTGPVRDVAASADGT 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 264 GLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFH 343
Cdd:cd00200   65 YLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 344 PNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTDNITS 423
Cdd:cd00200  145 PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966923833 424 LTFSPDSGLIASASMDNSVRVWDIRNTygsapadgsssELVGVYTGQMSNVLSVQFMACNLLLVTG 489
Cdd:cd00200  225 VAFSPDGYLLASGSEDGTIRVWDLRTG-----------ECVQTLSGHTNSVTSLAWSPDGKRLASG 279
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 242-489 5.58e-67

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 217.20  E-value: 5.58e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 242 EMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSF 321
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 322 DRTYPLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLK 401
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 402 LWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRntygsapadgsSSELVGVYTGQMSNVLSVQFMA 481
Cdd:cd00200  161 LWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS-----------TGKCLGTLRGHENGVNSVAFSP 229


                 ....*...
gi 966923833 482 CNLLLVTG 489
Cdd:cd00200  230 DGYLLASG 237
WD40 COG2319
WD40 repeat [General function prediction only];
246-489 1.16e-65

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 217.47  E-value: 1.16e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 246 LRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTY 325
Cdd:COG2319   32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 326 PLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDL 405
Cdd:COG2319  112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDL 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 406 ASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRntygsapadgsSSELVGVYTGQMSNVLSVQFMACNLL 485
Cdd:COG2319  192 ATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA-----------TGKLLRTLTGHSGSVRSVAFSPDGRL 260


                 ....
gi 966923833 486 LVTG 489
Cdd:COG2319  261 LASG 264
WD40 COG2319
WD40 repeat [General function prediction only];
257-489 7.75e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.18  E-value: 7.75e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 257 RFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLAD 336
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 337 VDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRG 416
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966923833 417 HTDNITSLTFSPDSGLIASASMDNSVRVWDIRntygsapadgsSSELVGVYTGQMSNVLSVQFMACNLLLVTG 489
Cdd:COG2319  161 HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA-----------TGKLLRTLTGHTGAVRSVAFSPDGKLLASG 222
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 184-362 5.65e-35

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 132.46  E-value: 5.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 184 ISPDSKLLAAGFDNSCIKLWSLRSKKLksephqvdvsrihlacdileeeddeddnagteMKILRGHCGPVYSTRFLADSS 263
Cdd:cd00200  143 FSPDGTFVASSSQDGTIKLWDLRTGKC--------------------------------VATLTGHTGEVNSVAFSPDGE 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 264 GLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFH 343
Cdd:cd00200  191 KLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWS 270

                        170
                 ....*....|....*....
gi 966923833 344 PNSNYLATGSTDKTVRLWS 362
Cdd:cd00200  271 PDGKRLASGSADGTIRIWD 289
TAF5_NTD2 cd08044
TAF5_NTD2 is the second conserved N-terminal region of TATA Binding Protein (TBP) Associated ...
 2-109 7.76e-34

TAF5_NTD2 is the second conserved N-terminal region of TATA Binding Protein (TBP) Associated Factor 5 (TAF5), involved in forming Transcription Factor IID (TFIID); The TATA Binding Protein (TBP) Associated Factor 5 (TAF5) is one of several TAFs that bind TBP and are involved in forming Transcription Factor IID (TFIID) complex. TAF5 contains three domains, two conserved sequence motifs at the N-terminal and one at the C-terminal region. TFIID is one of seven General Transcription Factors (GTF) (TFIIA, TFIIB, TFIID, TFIIE, TFIIF, and TFIID) involved in accurate initiation of transcription by RNA polymerase II in eukaryotes. TFIID plays an important role in the recognition of promoter DNA and assembly of the preinitiation complex. TFIID complex is composed of the TBP and at least 13 TAFs. In yeast and human cells, TAFs have been found as components of other complexes besides TFIID. TAF5 may play a major role in forming TFIID and its related complexes. TAFs from various species were originally named by their predicted molecular weight or their electrophoretic mobility in polyacrylamide gels. A new, unified nomenclature for the pol II TAFs has been suggested to show the relationship between TAF orthologs and paralogs. TAF5 has a paralog gene (TAF5L) which has a redundant function. Several hypotheses are proposed for TAFs functions such as serving as activator-binding sites, core-promoter recognition or a role in essential catalytic activity. C-terminus of TAF5 contains six WD40 repeats that likely form a closed beta propeller structure and may be involved in protein-protein interaction. The first part of the TAF5 N-terminal (TAF5_NTD1) homodimerizes in the absence of other TAFs. The second conserved N-terminal part of TAF5 (TAF5_NTD2) has an alpha-helical domain. One study has shown that TAF5_NTD2 homodimerizes only at high concentration of calcium but not any other metals. No dimerization was observed in other structural studies of TAF_NTD2. Several TAFs interact via histone-fold (HFD) motifs; HFD is the interaction motif involved in heterodimerization of the core histones and their assembly into nucleosome octamer. However, TAF5 does not have a HFD motif.


Pssm-ID: 176269  Cd Length: 133  Bit Score: 124.23  E-value: 7.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833   2 PLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFlqNASQKDVIEQLQTTQTIQDILSNFKLRAFLDNKYVVRLQEDSYN 81
Cdd:cd08044   28 QLLYPIFVHSYLDLVASGHLEEAKSFFERFSGDF--EDSHSEDIKKLSSITTPEHLKENELAKLFRSNKYVIRMSRDAYS 105

                         90       100
                 ....*....|....*....|....*...
gi 966923833  82 YLIRYLQSDNNTALCKVLTLHIHLDVQP 109
Cdd:cd08044  106 LLLRFLESWGGSLLLKILNEHIDIDVRD 133
TFIID_NTD2 pfam04494
WD40 associated region in TFIID subunit, NTD2 domain; This region is an all-alpha domain ...
 1-103 9.38e-31

WD40 associated region in TFIID subunit, NTD2 domain; This region is an all-alpha domain associated with the WD40 helical bundle of the TAF5 subunit of transcription factor TFIID. The domain has distant structural similarity to RNA polymerase II CTD interacting factors. It contains several conserved clefts that are likely to be critical for TFIID complex assembly. The TAF5 subunit is present twice in the TFIID complex and is critical for the function and assembly of the complex, and the NTD2 and N-terminal domain is crucial for homodimerization.


Pssm-ID: 461330  Cd Length: 130  Bit Score: 115.67  E-value: 9.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833    1 MPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFLqnASQKDVIEQLQTTQTIQDILSNFKLRAFLDNKYVVRLQEDSY 80
Cdd:pfam04494  30 RRLLYPVFVHSYLDLVAKGHIEEAKEFFEKFRGDHE--ALHGDDLRKLAGITLPEHLEENELAKLFRSNKYRIRLSRYSF 107

                          90       100
                  ....*....|....*....|...
gi 966923833   81 NYLIRYLQSDNNTALCKVLTLHI 103
Cdd:pfam04494 108 DLLLRFLQENESSVILRIINEHL 130
PTZ00421 PTZ00421
coronin; Provisional
 329-462 1.44e-11

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 66.45  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 329 IYAGHLADVDCVKFHP-NSNYLATGSTDKTVRLWSA-----QQGNSVRL--FTGHRGPVLSLAFSPNGK-YLASAGEDQR 399
Cdd:PTZ00421  70 ILLGQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIpeeglTQNISDPIvhLQGHTKKVGIVSFHPSAMnVLASAGADMV 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966923833 400 LKLWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRNtyGSAPADGSSSE 462
Cdd:PTZ00421 150 VNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRD--GTIVSSVEAHA 210
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 407-446 6.51e-11

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 56.94  E-value: 6.51e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 966923833   407 SGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWD 446
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 365-404 2.17e-10

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 55.78  E-value: 2.17e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 966923833   365 QGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWD 404
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
408-446 4.00e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 4.00e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 966923833  408 GTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWD 446
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 263-445 8.13e-10

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 61.26  E-value: 8.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 263 SGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYS-LYFASGSHDRTARLWSFDRTYPLRIYAGHlADVDCVK 341
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADpTLLASGSDDGSVKLWSINQGVSIGTIKTK-ANICCVQ 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 342 FHPNSNY-LATGSTDKTVRLWSAQQgNSVRLFT--GHRGPVLSLAFSpNGKYLASAGEDQRLKLWDL---ASG---TLYK 412
Cdd:PLN00181 625 FPSESGRsLAFGSADHKVYYYDLRN-PKLPLCTmiGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDLsmsISGineTPLH 702

                        170       180       190
                 ....*....|....*....|....*....|...
gi 966923833 413 ELRGHTDNITSLTFSPDSGLIASASMDNSVRVW 445
Cdd:PLN00181 703 SFMGHTNVKNFVGLSVSDGYIATGSETNEVFVY 735
WD40 pfam00400
WD domain, G-beta repeat;
366-404 9.09e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.89  E-value: 9.09e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 966923833  366 GNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWD 404
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 326-362 3.13e-09

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 52.31  E-value: 3.13e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 966923833   326 PLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWS 362
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 379-449 4.08e-09

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 59.28  E-value: 4.08e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966923833  379 VLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRG-HTDNITSLTFSPDSGLIA-SASMDN---SVRVWDIRN 449
Cdd:COG4946   391 VFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDgYGDGISDLAWSPDSKWLAySKPGPNqlsQIFLYDVET 466
WD40 pfam00400
WD domain, G-beta repeat;
326-362 5.14e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 51.58  E-value: 5.14e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 966923833  326 PLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWS 362
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 308-447 2.48e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 53.55  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 308 ASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFHP-NSNYLATGSTDKTVRLWSAQQGNSVRLFTGhRGPVLSLAF-S 385
Cdd:PLN00181 549 ASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKT-KANICCVQFpS 627

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966923833 386 PNGKYLASAGEDQRLKLWDLASGTL-YKELRGHTDNITSLTFSpDSGLIASASMDNSVRVWDI 447
Cdd:PLN00181 628 ESGRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 288-320 2.26e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 44.23  E-value: 2.26e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 966923833   288 YQGHAYPVWDLDISPYSLYFASGSHDRTARLWS 320
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 240-278 5.92e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.07  E-value: 5.92e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 966923833   240 GTEMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWD 278
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
288-320 6.25e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.10  E-value: 6.25e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 966923833  288 YQGHAYPVWDLDISPYSLYFASGSHDRTARLWS 320
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 340-427 6.92e-06

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 44.58  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833  340 VKFHPNSNYLATGSTDKTVRLwsaQQGNSVRLFTG----HRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELR 415
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLL---HRLNWQRVWTLspdkEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFS 77

                          90
                  ....*....|..
gi 966923833  416 GHTDNITSLTFS 427
Cdd:pfam12894  78 AGSDLITCLGWG 89
PTZ00420 PTZ00420
coronin; Provisional
 358-449 7.12e-06

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 48.41  E-value: 7.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 358 VRLWSAQQGNSVRLFTGHRGPVLSLAFSP-NGKYLASAGEDQRLKLWDLA-SGTLYKE-------LRGHTDNITSLTFSP 428
Cdd:PTZ00420  56 IRLENQMRKPPVIKLKGHTSSILDLQFNPcFSEILASGSEDLTIRVWEIPhNDESVKEikdpqciLKGHKKKISIIDWNP 135

                         90       100
                 ....*....|....*....|..
gi 966923833 429 DSGLI-ASASMDNSVRVWDIRN 449
Cdd:PTZ00420 136 MNYYImCSSGFDSFVNIWDIEN 157
WD40 pfam00400
WD domain, G-beta repeat;
240-278 1.53e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.95  E-value: 1.53e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 966923833  240 GTEMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWD 278
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
305-449 2.76e-04

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 42.37  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 305 LYFASGSHDRTARLWSFDRTYPLRIYAGhlADVDCVKFHPNSNYL-ATGSTDKTVRLWSAQQGNSVRLFTGHRGPVlSLA 383
Cdd:COG3391   82 LYVANSGSGRVSVIDLATGKVVATIPVG--GGPRGLAVDPDGGRLyVADSGNGRVSVIDTATGKVVATIPVGAGPH-GIA 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966923833 384 FSPNGKYL--ASAGEDQRLKL---WDLASGTLYKELRGHtDNITSLTFSPDSGLI--------ASASMDNSVRVWDIRN 449
Cdd:COG3391  159 VDPDGKRLyvANSGSNTVSVIvsvIDTATGKVVATIPVG-GGPVGVAVSPDGRRLyvanrgsnTSNGGSNTVSVIDLAT 236
PTZ00420 PTZ00420
coronin; Provisional
 246-409 7.08e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 42.24  E-value: 7.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 246 LRGHCGPVYSTRFLADSSGLL-SCSEDMSIRYWDLGSFTNTV--------LYQGHAYPVWDLDISPYSLY-FASGSHDRT 315
Cdd:PTZ00420  70 LKGHTSSILDLQFNPCFSEILaSGSEDLTIRVWEIPHNDESVkeikdpqcILKGHKKKISIIDWNPMNYYiMCSSGFDSF 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 316 ARLW-------SFDRTYPLRIYA------GHLADVDCVKFHPN----------SNYLATGSTDKTVRLWsaqqgnsVRLF 372
Cdd:PTZ00420 150 VNIWdienekrAFQINMPKKLSSlkwnikGNLLSGTCVGKHMHiidprkqeiaSSFHIHDGGKNTKNIW-------IDGL 222

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 966923833 373 TGHRGPVLSLAFSPNGKylasagedQRLKLWDLASGT 409
Cdd:PTZ00420 223 GGDDNYILSTGFSKNNM--------REMKLWDLKNTT 251
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 344-429 7.09e-04

Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];


Pssm-ID: 443973 [Multi-domain]  Cd Length: 1072  Bit Score: 42.33  E-value: 7.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833  344 PNSNYLATgsTDKTVRLW-----SaqqGNSVRLFTG-HRGPVLSLAFSPNGKYLA----SAGEDQRLKLWDLASGTLYKE 413
Cdd:COG4946   398 PDGKKIAF--TDNRGRLWvvdlaS---GKVRKVDTDgYGDGISDLAWSPDSKWLAyskpGPNQLSQIFLYDVETGKTVQL 472

                          90
                  ....*....|....*.
gi 966923833  414 LRGHTDNiTSLTFSPD 429
Cdd:COG4946   473 TDGRYDD-GSPAFSPD 487
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 352-464 7.31e-04

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 40.04  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 352 GSTDktVRLWSAQQGNSVRLfTGHRGPVLSLAFSPNGKYLA-SAGEDQRLKLW--DLASGTLYKELRGHTDNiTSLTFSP 428
Cdd:COG0823    9 GNSD--IYVVDLDGGEPRRL-TNSPGIDTSPAWSPDGRRIAfTSDRGGGPQIYvvDADGGEPRRLTFGGGYN-ASPSWSP 84

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 966923833 429 DSGLIASASMDNSvrVWDIRntygSAPADGSSSELV 464
Cdd:COG0823   85 DGKRLAFVSRSDG--RFDIY----VLDLDGGAPRRL 114
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 391-479 1.13e-03

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 41.61  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 391 LASAGEDQRLKLWDLASGTLYKELRGHTDNITSLTF-SPDSGLIASASMDNSVRVWDIRNtygsapadgssselvGVYTG 469
Cdd:PLN00181 548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQ---------------GVSIG 612

                         90
                 ....*....|...
gi 966923833 470 QM---SNVLSVQF 479
Cdd:PLN00181 613 TIktkANICCVQF 625
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 342-437 3.67e-03

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 38.11  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 342 FHPNSNYLA-TGSTDKTVRLW--SAQQGNSVRLfTGHRGPVLSLAFSPNGKYLA-SAGEDQRLKLW--DLASGtlykELR 415
Cdd:COG0823   38 WSPDGRRIAfTSDRGGGPQIYvvDADGGEPRRL-TFGGGYNASPSWSPDGKRLAfVSRSDGRFDIYvlDLDGG----APR 112

                         90       100
                 ....*....|....*....|..
gi 966923833 416 GHTDNITSLTFSPDSGLIASAS 437
Cdd:COG0823  113 RLTDGPGSPSWSPDGRRIVFSS 134
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 294-403 4.07e-03

Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440585 [Multi-domain]  Cd Length: 158  Bit Score: 38.11  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923833 294 PVWdldiSPY--SLYFASgSHDRTARLWSFDR--TYPLRIYAGHLADVDCVkFHPNSNYLA-TGSTDKTVRLW--SAQQG 366
Cdd:COG0823   36 PAW----SPDgrRIAFTS-DRGGGPQIYVVDAdgGEPRRLTFGGGYNASPS-WSPDGKRLAfVSRSDGRFDIYvlDLDGG 109

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966923833 367 NSVRLFTGHRGPvlslAFSPNGKYLA-SAGEDQRLKLW 403
Cdd:COG0823  110 APRRLTDGPGSP----SWSPDGRRIVfSSDRGGRPDLY 143
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 385-447 6.06e-03

Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.


Pssm-ID: 466575 [Multi-domain]  Cd Length: 350  Bit Score: 38.90  E-value: 6.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966923833  385 SPNGKYLASAGE-DQRLKLWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDI 447
Cdd:pfam20426  90 TPSENFLISCGNwENSFQVISLNDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVWEV 153
 
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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