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Conserved domains on  [gi|7657439|ref|NP_055224|]
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TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L isoform a [Homo sapiens]

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];
272-541 2.07e-78

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 253.29  E-value: 2.07e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  272 NTAEISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFL 351
Cdd:COG2319 166 TSVAFSPDGKLLASGSDDGTVRLWDLAT--------------------------------GKLLRTLTGHTGAVRSVAFS 213

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  352 ADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDC 431
Cdd:COG2319 214 PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNS 293

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  432 VKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTD 511
Cdd:COG2319 294 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTG 373

                       250       260       270
                ....*....|....*....|....*....|
gi 7657439  512 NITSLTFSPDSGLIASASMDNSVRVWDIRN 541
Cdd:COG2319 374 AVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
TAF5_NTD2 cd08044
TAF5_NTD2 is the second conserved N-terminal region of TATA Binding Protein (TBP) Associated ...
 67-201 1.21e-44

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: 154.66  E-value: 1.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   67 PQQYEVQFGRLRNFLTDSDSQHSHEVMPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFlqNASQKDVIEQLQTTQTI 146
Cdd:cd08044   1 PNDYEQAYSKLRKWIESSLDIYKYELSQLLYPIFVHSYLDLVASGHLEEAKSFFERFSGDF--EDSHSEDIKKLSSITTP 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7657439  147 QDILSNFKLRAFLDNKYVVRLQEDSYNYLIRYLQSDNNTALCKVLTLHIHLDVQP 201
Cdd:cd08044  79 EHLKENELAKLFRSNKYVIRMSRDAYSLLLRFLESWGGSLLLKILNEHIDIDVRD 133
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
272-541 2.07e-78

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 253.29  E-value: 2.07e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  272 NTAEISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFL 351
Cdd:COG2319 166 TSVAFSPDGKLLASGSDDGTVRLWDLAT--------------------------------GKLLRTLTGHTGAVRSVAFS 213

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  352 ADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDC 431
Cdd:COG2319 214 PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNS 293

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  432 VKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTD 511
Cdd:COG2319 294 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTG 373

                       250       260       270
                ....*....|....*....|....*....|
gi 7657439  512 NITSLTFSPDSGLIASASMDNSVRVWDIRN 541
Cdd:COG2319 374 AVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 276-581 2.96e-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: 233.38  E-value: 2.96e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  276 ISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFLADSS 355
Cdd:cd00200  17 FSPDGKLLATGSGDGTIKVWDLET--------------------------------GELLRTLKGHTGPVRDVAASADGT 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  356 GLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFH 435
Cdd:cd00200  65 YLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  436 PNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTDNITS 515
Cdd:cd00200 145 PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS 224

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7657439  516 LTFSPDSGLIASASMDNSVRVWDIRNTYCSAPADGSSSElvgvytgqmsnVLSVQFMACNLLLVTG 581
Cdd:cd00200 225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNS-----------VTSLAWSPDGKRLASG 279
TAF5_NTD2 cd08044
TAF5_NTD2 is the second conserved N-terminal region of TATA Binding Protein (TBP) Associated ...
 67-201 1.21e-44

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: 154.66  E-value: 1.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   67 PQQYEVQFGRLRNFLTDSDSQHSHEVMPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFlqNASQKDVIEQLQTTQTI 146
Cdd:cd08044   1 PNDYEQAYSKLRKWIESSLDIYKYELSQLLYPIFVHSYLDLVASGHLEEAKSFFERFSGDF--EDSHSEDIKKLSSITTP 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7657439  147 QDILSNFKLRAFLDNKYVVRLQEDSYNYLIRYLQSDNNTALCKVLTLHIHLDVQP 201
Cdd:cd08044  79 EHLKENELAKLFRSNKYVIRMSRDAYSLLLRFLESWGGSLLLKILNEHIDIDVRD 133
TFIID_NTD2 pfam04494
WD40 associated region in TFIID subunit, NTD2 domain; This region is an all-alpha domain ...
 64-195 3.68e-42

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: 148.03  E-value: 3.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439     64 QAEPQQYEVQFGRLRNFLTDSDSQHSHEVMPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFLqnASQKDVIEQLQTT 143
Cdd:pfam04494   1 EGDPQKYERAYSLLRNWIESSLDIYKPELRRLLYPVFVHSYLDLVAKGHIEEAKEFFEKFRGDHE--ALHGDDLRKLAGI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7657439    144 QTIQDILSNFKLRAFLDNKYVVRLQEDSYNYLIRYLQSDNNTALCKVLTLHI 195
Cdd:pfam04494  79 TLPEHLEENELAKLFRSNKYRIRLSRYSFDLLLRFLQENESSVILRIINEHL 130
PTZ00421 PTZ00421
coronin; Provisional
 421-554 1.12e-11

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 67.23  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   421 IYAGHLADVDCVKFHP-NSNYLATGSTDKTVRLWSA-----QQGNSVRL--FTGHRGPVLSLAFSPNGK-YLASAGEDQR 491
Cdd:PTZ00421  70 ILLGQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIpeeglTQNISDPIvhLQGHTKKVGIVSFHPSAMnVLASAGADMV 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657439   492 LKLWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRNtyCSAPADGSSSE 554
Cdd:PTZ00421 150 VNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRD--GTIVSSVEAHA 210
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 499-538 3.89e-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: 58.09  E-value: 3.89e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 7657439     499 SGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWD 538
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
500-538 2.58e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.43  E-value: 2.58e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 7657439    500 GTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWD 538
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
272-541 2.07e-78

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 253.29  E-value: 2.07e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  272 NTAEISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFL 351
Cdd:COG2319 166 TSVAFSPDGKLLASGSDDGTVRLWDLAT--------------------------------GKLLRTLTGHTGAVRSVAFS 213

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  352 ADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDC 431
Cdd:COG2319 214 PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNS 293

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  432 VKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTD 511
Cdd:COG2319 294 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTG 373

                       250       260       270
                ....*....|....*....|....*....|
gi 7657439  512 NITSLTFSPDSGLIASASMDNSVRVWDIRN 541
Cdd:COG2319 374 AVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
272-581 1.98e-77

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 250.98  E-value: 1.98e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  272 NTAEISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFL 351
Cdd:COG2319 124 RSVAFSPDGKTLASGSADGTVRLWDLAT--------------------------------GKLLRTLTGHSGAVTSVAFS 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  352 ADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDC 431
Cdd:COG2319 172 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS 251

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  432 VKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTD 511
Cdd:COG2319 252 VAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTG 331

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  512 NITSLTFSPDSGLIASASMDNSVRVWDIrntycsapadgSSSELVGVYTGQMSNVLSVQFMACNLLLVTG 581
Cdd:COG2319 332 AVRSVAFSPDGKTLASGSDDGTVRLWDL-----------ATGELLRTLTGHTGAVTSVAFSPDGRTLASG 390
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 276-581 2.96e-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: 233.38  E-value: 2.96e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  276 ISPDSKLLAAGFDNSCIKLWSLRSkklksephqvdvsrihlacdileeeddeddnaGTEMKILRGHCGPVYSTRFLADSS 355
Cdd:cd00200  17 FSPDGKLLATGSGDGTIKVWDLET--------------------------------GELLRTLKGHTGPVRDVAASADGT 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  356 GLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFH 435
Cdd:cd00200  65 YLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  436 PNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTDNITS 515
Cdd:cd00200 145 PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNS 224

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7657439  516 LTFSPDSGLIASASMDNSVRVWDIRNTYCSAPADGSSSElvgvytgqmsnVLSVQFMACNLLLVTG 581
Cdd:cd00200 225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNS-----------VTSLAWSPDGKRLASG 279
WD40 COG2319
WD40 repeat [General function prediction only];
331-571 4.17e-69

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 229.03  E-value: 4.17e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  331 AGTEMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARL 410
Cdd:COG2319  67 AGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRL 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  411 WSFDRTYPLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQ 490
Cdd:COG2319 147 WDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADG 226

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  491 RLKLWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIrntycsapadgSSSELVGVYTGQMSNVLSVQ 570
Cdd:COG2319 227 TVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-----------ATGELLRTLTGHSGGVNSVA 295


                .
gi 7657439  571 F 571
Cdd:COG2319 296 F 296
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 334-581 4.84e-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: 219.90  E-value: 4.84e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  334 EMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSF 413
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  414 DRTYPLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLK 493
Cdd:cd00200  81 ETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  494 LWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRntycsapadgsSSELVGVYTGQMSNVLSVQFMA 573
Cdd:cd00200 161 LWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS-----------TGKCLGTLRGHENGVNSVAFSP 229


                ....*...
gi 7657439  574 CNLLLVTG 581
Cdd:cd00200 230 DGYLLASG 237
WD40 COG2319
WD40 repeat [General function prediction only];
338-581 5.84e-66

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 220.55  E-value: 5.84e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  338 LRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTY 417
Cdd:COG2319  32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGL 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  418 PLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDL 497
Cdd:COG2319 112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDL 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  498 ASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRntycsapadgsSSELVGVYTGQMSNVLSVQFMACNLL 577
Cdd:COG2319 192 ATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA-----------TGKLLRTLTGHSGSVRSVAFSPDGRL 260


                ....
gi 7657439  578 LVTG 581
Cdd:COG2319 261 LASG 264
WD40 COG2319
WD40 repeat [General function prediction only];
349-581 4.52e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 180.88  E-value: 4.52e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  349 RFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLAD 428
Cdd:COG2319   1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  429 VDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRG 508
Cdd:COG2319  81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657439  509 HTDNITSLTFSPDSGLIASASMDNSVRVWDIRntycsapadgsSSELVGVYTGQMSNVLSVQFMACNLLLVTG 581
Cdd:COG2319 161 HSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA-----------TGKLLRTLTGHTGAVRSVAFSPDGKLLASG 222
TAF5_NTD2 cd08044
TAF5_NTD2 is the second conserved N-terminal region of TATA Binding Protein (TBP) Associated ...
 67-201 1.21e-44

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: 154.66  E-value: 1.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   67 PQQYEVQFGRLRNFLTDSDSQHSHEVMPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFlqNASQKDVIEQLQTTQTI 146
Cdd:cd08044   1 PNDYEQAYSKLRKWIESSLDIYKYELSQLLYPIFVHSYLDLVASGHLEEAKSFFERFSGDF--EDSHSEDIKKLSSITTP 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 7657439  147 QDILSNFKLRAFLDNKYVVRLQEDSYNYLIRYLQSDNNTALCKVLTLHIHLDVQP 201
Cdd:cd08044  79 EHLKENELAKLFRSNKYVIRMSRDAYSLLLRFLESWGGSLLLKILNEHIDIDVRD 133
TFIID_NTD2 pfam04494
WD40 associated region in TFIID subunit, NTD2 domain; This region is an all-alpha domain ...
 64-195 3.68e-42

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: 148.03  E-value: 3.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439     64 QAEPQQYEVQFGRLRNFLTDSDSQHSHEVMPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFLqnASQKDVIEQLQTT 143
Cdd:pfam04494   1 EGDPQKYERAYSLLRNWIESSLDIYKPELRRLLYPVFVHSYLDLVAKGHIEEAKEFFEKFRGDHE--ALHGDDLRKLAGI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7657439    144 QTIQDILSNFKLRAFLDNKYVVRLQEDSYNYLIRYLQSDNNTALCKVLTLHI 195
Cdd:pfam04494  79 TLPEHLEENELAKLFRSNKYRIRLSRYSFDLLLRFLQENESSVILRIINEHL 130
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 276-454 3.64e-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: 134.00  E-value: 3.64e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  276 ISPDSKLLAAGFDNSCIKLWSLRSKKLksephqvdvsrihlacdileeeddeddnagteMKILRGHCGPVYSTRFLADSS 355
Cdd:cd00200 143 FSPDGTFVASSSQDGTIKLWDLRTGKC--------------------------------VATLTGHTGEVNSVAFSPDGE 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  356 GLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFH 435
Cdd:cd00200 191 KLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWS 270

                       170
                ....*....|....*....
gi 7657439  436 PNSNYLATGSTDKTVRLWS 454
Cdd:cd00200 271 PDGKRLASGSADGTIRIWD 289
PTZ00421 PTZ00421
coronin; Provisional
 421-554 1.12e-11

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 67.23  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   421 IYAGHLADVDCVKFHP-NSNYLATGSTDKTVRLWSA-----QQGNSVRL--FTGHRGPVLSLAFSPNGK-YLASAGEDQR 491
Cdd:PTZ00421  70 ILLGQEGPIIDVAFNPfDPQKLFTASEDGTIMGWGIpeeglTQNISDPIvhLQGHTKKVGIVSFHPSAMnVLASAGADMV 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657439   492 LKLWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRNtyCSAPADGSSSE 554
Cdd:PTZ00421 150 VNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRD--GTIVSSVEAHA 210
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 499-538 3.89e-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: 58.09  E-value: 3.89e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 7657439     499 SGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWD 538
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 457-496 1.40e-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: 56.55  E-value: 1.40e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 7657439     457 QGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWD 496
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
500-538 2.58e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.43  E-value: 2.58e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 7657439    500 GTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWD 538
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
458-496 5.75e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 5.75e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 7657439    458 GNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWD 496
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 355-537 1.11e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 61.26  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   355 SGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYS-LYFASGSHDRTARLWSFDRTYPLRIYAGHlADVDCVK 433
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADpTLLASGSDDGSVKLWSINQGVSIGTIKTK-ANICCVQ 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   434 FHPNSNY-LATGSTDKTVRLWSAQQgNSVRLFT--GHRGPVLSLAFSpNGKYLASAGEDQRLKLWDL---ASG---TLYK 504
Cdd:PLN00181 625 FPSESGRsLAFGSADHKVYYYDLRN-PKLPLCTmiGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDLsmsISGineTPLH 702

                        170       180       190
                 ....*....|....*....|....*....|...
gi 7657439   505 ELRGHTDNITSLTFSPDSGLIASASMDNSVRVW 537
Cdd:PLN00181 703 SFMGHTNVKNFVGLSVSDGYIATGSETNEVFVY 735
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 418-454 2.06e-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: 53.09  E-value: 2.06e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 7657439     418 PLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWS 454
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
418-454 3.31e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 52.35  E-value: 3.31e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 7657439    418 PLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWS 454
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 471-541 5.54e-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: 5.54e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7657439   471 VLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRG-HTDNITSLTFSPDSGLIA-SASMDN---SVRVWDIRN 541
Cdd:COG4946  391 VFNPVWSPDGKKIAFTDNRGRLWVVDLASGKVRKVDTDgYGDGISDLAWSPDSKWLAySKPGPNqlsQIFLYDVET 466
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 400-539 3.25e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 53.55  E-value: 3.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   400 ASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFHP-NSNYLATGSTDKTVRLWSAQQGNSVRLFTGhRGPVLSLAF-S 477
Cdd:PLN00181 549 ASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKT-KANICCVQFpS 627

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657439   478 PNGKYLASAGEDQRLKLWDLASGTL-YKELRGHTDNITSLTFSpDSGLIASASMDNSVRVWDI 539
Cdd:PLN00181 628 ESGRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 380-412 1.71e-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: 45.00  E-value: 1.71e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 7657439     380 YQGHAYPVWDLDISPYSLYFASGSHDRTARLWS 412
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 332-370 4.25e-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: 43.84  E-value: 4.25e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 7657439     332 GTEMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWD 370
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
380-412 4.71e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.49  E-value: 4.71e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 7657439    380 YQGHAYPVWDLDISPYSLYFASGSHDRTARLWS 412
Cdd:pfam00400   7 LEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 432-519 6.70e-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: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439    432 VKFHPNSNYLATGSTDKTVRLwsaQQGNSVRLFTG----HRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELR 507
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLL---HRLNWQRVWTLspdkEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFS 77

                          90
                  ....*....|..
gi 7657439    508 GHTDNITSLTFS 519
Cdd:pfam12894  78 AGSDLITCLGWG 89
PTZ00420 PTZ00420
coronin; Provisional
 450-541 9.20e-06

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 48.41  E-value: 9.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   450 VRLWSAQQGNSVRLFTGHRGPVLSLAFSP-NGKYLASAGEDQRLKLWDLA-SGTLYKE-------LRGHTDNITSLTFSP 520
Cdd:PTZ00420  56 IRLENQMRKPPVIKLKGHTSSILDLQFNPcFSEILASGSEDLTIRVWEIPhNDESVKEikdpqciLKGHKKKISIIDWNP 135

                         90       100
                 ....*....|....*....|..
gi 7657439   521 DSGLI-ASASMDNSVRVWDIRN 541
Cdd:PTZ00420 136 MNYYImCSSGFDSFVNIWDIEN 157
WD40 pfam00400
WD domain, G-beta repeat;
332-370 1.15e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 1.15e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 7657439    332 GTEMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWD 370
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
397-541 3.44e-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: 3.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  397 LYFASGSHDRTARLWSFDRTYPLRIYAGhlADVDCVKFHPNSNYL-ATGSTDKTVRLWSAQQGNSVRLFTGHRGPVlSLA 475
Cdd:COG3391  82 LYVANSGSGRVSVIDLATGKVVATIPVG--GGPRGLAVDPDGGRLyVADSGNGRVSVIDTATGKVVATIPVGAGPH-GIA 158

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7657439  476 FSPNGKYL--ASAGEDQRLKL---WDLASGTLYKELRGHtDNITSLTFSPDSGLI--------ASASMDNSVRVWDIRN 541
Cdd:COG3391 159 VDPDGKRLyvANSGSNTVSVIvsvIDTATGKVVATIPVG-GGPVGVAVSPDGRRLyvanrgsnTSNGGSNTVSVIDLAT 236
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 444-556 3.60e-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: 41.20  E-value: 3.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  444 GSTDktVRLWSAQQGNSVRLfTGHRGPVLSLAFSPNGKYLA-SAGEDQRLKLW--DLASGTLYKELRGHTDNiTSLTFSP 520
Cdd:COG0823   9 GNSD--IYVVDLDGGEPRRL-TNSPGIDTSPAWSPDGRRIAfTSDRGGGPQIYvvDADGGEPRRLTFGGGYN-ASPSWSP 84

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 7657439  521 DSGLIASASMDNSvrVWDIRntycSAPADGSSSELV 556
Cdd:COG0823  85 DGKRLAFVSRSDG--RFDIY----VLDLDGGAPRRL 114
PTZ00420 PTZ00420
coronin; Provisional
 338-501 8.97e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 42.24  E-value: 8.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   338 LRGHCGPVYSTRFLADSSGLL-SCSEDMSIRYWDLGSFTNTV--------LYQGHAYPVWDLDISPYSLY-FASGSHDRT 407
Cdd:PTZ00420  70 LKGHTSSILDLQFNPCFSEILaSGSEDLTIRVWEIPHNDESVkeikdpqcILKGHKKKISIIDWNPMNYYiMCSSGFDSF 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   408 ARLW-------SFDRTYPLRIYA------GHLADVDCVKFHPN----------SNYLATGSTDKTVRLWsaqqgnsVRLF 464
Cdd:PTZ00420 150 VNIWdienekrAFQINMPKKLSSlkwnikGNLLSGTCVGKHMHiidprkqeiaSSFHIHDGGKNTKNIW-------IDGL 222

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 7657439   465 TGHRGPVLSLAFSPNGKylasagedQRLKLWDLASGT 501
Cdd:PTZ00420 223 GGDDNYILSTGFSKNNM--------REMKLWDLKNTT 251
COG4946 COG4946
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ...
 436-521 9.03e-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: 9.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   436 PNSNYLATgsTDKTVRLW-----SaqqGNSVRLFTG-HRGPVLSLAFSPNGKYLA----SAGEDQRLKLWDLASGTLYKE 505
Cdd:COG4946  398 PDGKKIAF--TDNRGRLWvvdlaS---GKVRKVDTDgYGDGISDLAWSPDSKWLAyskpGPNQLSQIFLYDVETGKTVQL 472

                         90
                 ....*....|....*.
gi 7657439   506 LRGHTDNiTSLTFSPD 521
Cdd:COG4946  473 TDGRYDD-GSPAFSPD 487
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 483-571 1.42e-03

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 41.61  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439   483 LASAGEDQRLKLWDLASGTLYKELRGHTDNITSLTF-SPDSGLIASASMDNSVRVWDIRNtycsapadgssselvGVYTG 561
Cdd:PLN00181 548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGSVKLWSINQ---------------GVSIG 612

                         90
                 ....*....|...
gi 7657439   562 QM---SNVLSVQF 571
Cdd:PLN00181 613 TIktkANICCVQF 625
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 386-495 1.85e-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: 39.27  E-value: 1.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  386 PVWdldiSPY--SLYFASgSHDRTARLWSFDR--TYPLRIYAGHLADVDCVkFHPNSNYLA-TGSTDKTVRLW--SAQQG 458
Cdd:COG0823  36 PAW----SPDgrRIAFTS-DRGGGPQIYVVDAdgGEPRRLTFGGGYNASPS-WSPDGKRLAfVSRSDGRFDIYvlDLDGG 109

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 7657439  459 NSVRLFTGHRGPvlslAFSPNGKYLA-SAGEDQRLKLW 495
Cdd:COG0823 110 APRRLTDGPGSP----SWSPDGRRIVfSSDRGGRPDLY 143
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 434-529 2.03e-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: 39.27  E-value: 2.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657439  434 FHPNSNYLA-TGSTDKTVRLW--SAQQGNSVRLfTGHRGPVLSLAFSPNGKYLA-SAGEDQRLKLW--DLASGtlykELR 507
Cdd:COG0823  38 WSPDGRRIAfTSDRGGGPQIYvvDADGGEPRRL-TFGGGYNASPSWSPDGKRLAfVSRSDGRFDIYvlDLDGG----APR 112

                        90       100
                ....*....|....*....|..
gi 7657439  508 GHTDNITSLTFSPDSGLIASAS 529
Cdd:COG0823 113 RLTDGPGSPSWSPDGRRIVFSS 134
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 477-539 7.39e-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: 7.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7657439    477 SPNGKYLASAGE-DQRLKLWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDI 539
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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