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Conserved domains on  [gi|1907189795|ref|XP_036009995|]
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centromere protein T isoform X5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CENP-T_N super family cl24676
Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral ...
 1-270 4.81e-128

Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This family represents the N-terminus of CENP-T.


The actual alignment was detected with superfamily member pfam16171:

Pssm-ID: 465039  Cd Length: 378  Bit Score: 374.20  E-value: 4.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795   1 MPDPVVKPAQVPEVARSSRRESSRGSLELHLPELEPPSTLAPGLTAPGKRKQKLRLSVFQQEVDQGLPLSQEPRRSrsAD 80
Cdd:pfam16171 105 MPESVVKPVPVPQVVQPSRRESSRGSLELQLPELEPPTTLAPGLLAPGRRKQRLRLSVFQQGVDQGLPLSQEPRGN--AD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795  81 VSSLASSFNLTFVLPGQPETVERPGLARRRPIRQLVNAGALLQDLEDNSLASALPGDSHRTPVAALPMDVGLEDTQPFSQ 160
Cdd:pfam16171 183 ASSLTSSLNLTFATPLQPQSVQRPGLARRPPTRRAVDVGAFLQDLRDTSLALAPPGDSHRTPVATLPTDTVLEDTQPFSQ 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795 161 SLAAFSLSGKHSLPSPSRPGVEDVERVMGP--PSSGTRLQSRMSRS--GPAASPSPFLEPQPPP-AEPREAVGSNEAAEP 235
Cdd:pfam16171 263 PLVGCSPSVHHSLPCPSHTGAEDAERAVGRrtQSSGPGLQNNSPGKpaEVDALALPFPNTQPEGhTEVTEAEGSQEAVEA 342

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907189795 236 KDQEGSSGYEETSARPASGELSSSTHDSLPAEQPP 270
Cdd:pfam16171 343 KEPEGSSGDEDTSGRPASPELASSTPEFLQARRPH 377
HFD_SF super family cl45933
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 307-402 2.53e-34

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


The actual alignment was detected with superfamily member pfam15511:

Pssm-ID: 480273  Cd Length: 108  Bit Score: 123.31  E-value: 2.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795 307 KAGLSPYVKFFSF--CTKMPVEKTALEIVEKCLDKYFQHLCNDLEVFASHAGRKIVKPEDLLLLMRRQGLVTDQVSQHVL 384
Cdd:pfam15511  10 TAVVKRLAQRFARtsGSKGKLSKEALAALEQASDWFFEQMGEDLAAYAKHAGRKTIDESDVILLMKRQRQITSQTTLFSL 89

                          90
                  ....*....|....*...
gi 1907189795 385 VERYLPLEYRQQLIPCAF 402
Cdd:pfam15511  90 AQRYLPRELLQELRMPPP 107
 
Name Accession Description Interval E-value
CENP-T_N pfam16171
Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral ...
 1-270 4.81e-128

Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This family represents the N-terminus of CENP-T.


Pssm-ID: 465039  Cd Length: 378  Bit Score: 374.20  E-value: 4.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795   1 MPDPVVKPAQVPEVARSSRRESSRGSLELHLPELEPPSTLAPGLTAPGKRKQKLRLSVFQQEVDQGLPLSQEPRRSrsAD 80
Cdd:pfam16171 105 MPESVVKPVPVPQVVQPSRRESSRGSLELQLPELEPPTTLAPGLLAPGRRKQRLRLSVFQQGVDQGLPLSQEPRGN--AD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795  81 VSSLASSFNLTFVLPGQPETVERPGLARRRPIRQLVNAGALLQDLEDNSLASALPGDSHRTPVAALPMDVGLEDTQPFSQ 160
Cdd:pfam16171 183 ASSLTSSLNLTFATPLQPQSVQRPGLARRPPTRRAVDVGAFLQDLRDTSLALAPPGDSHRTPVATLPTDTVLEDTQPFSQ 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795 161 SLAAFSLSGKHSLPSPSRPGVEDVERVMGP--PSSGTRLQSRMSRS--GPAASPSPFLEPQPPP-AEPREAVGSNEAAEP 235
Cdd:pfam16171 263 PLVGCSPSVHHSLPCPSHTGAEDAERAVGRrtQSSGPGLQNNSPGKpaEVDALALPFPNTQPEGhTEVTEAEGSQEAVEA 342

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907189795 236 KDQEGSSGYEETSARPASGELSSSTHDSLPAEQPP 270
Cdd:pfam16171 343 KEPEGSSGDEDTSGRPASPELASSTPEFLQARRPH 377
CENP-T_C pfam15511
Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral ...
 307-402 2.53e-34

Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This domain is the C-terminal histone fold domain of CENP-T, which associates with chromatin.


Pssm-ID: 434768  Cd Length: 108  Bit Score: 123.31  E-value: 2.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795 307 KAGLSPYVKFFSF--CTKMPVEKTALEIVEKCLDKYFQHLCNDLEVFASHAGRKIVKPEDLLLLMRRQGLVTDQVSQHVL 384
Cdd:pfam15511  10 TAVVKRLAQRFARtsGSKGKLSKEALAALEQASDWFFEQMGEDLAAYAKHAGRKTIDESDVILLMKRQRQITSQTTLFSL 89

                          90
                  ....*....|....*...
gi 1907189795 385 VERYLPLEYRQQLIPCAF 402
Cdd:pfam15511  90 AQRYLPRELLQELRMPPP 107
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 315-399 3.03e-32

histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also called interphase centromere complex protein 22 (ICEN22), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression, and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENP-T is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Moreover, CENP-T is a component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENP-T has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


Pssm-ID: 467045  Cd Length: 94  Bit Score: 117.27  E-value: 3.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795 315 KFFSFCTKMPVEKTALEIVEKCLDKYFQHLCNDLEVFASHAGRKIVKPEDLLLLMRRQGLVTDQVSQHVLVERYLPLEYR 394
Cdd:cd22920    10 KLFKHFLKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVELLMKRQRLVTDKQSLESLARKYLPLELL 89


                  ....*
gi 1907189795 395 QQLIP 399
Cdd:cd22920    90 DELIP 94
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
174-309 2.16e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795 174 PSPSRPGVEDVERVMGPPSSGTRLQSRMSRSGPAASPSPFLEPQPPPAEPREAVGSNEAAEPKDQEGSSGyEETSARPAS 253
Cdd:PRK07003  410 LAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASA-PASDAPPDA 488

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189795 254 GELSSSTHDSLPAEQPPPSPGVAVLSSEPLESV---TAKCPSRTQTAGPRRRQDPHKAG 309
Cdd:PRK07003  489 AFEPAPRAAAPSAATPAAVPDARAPAAASREDApaaAAPPAPEARPPTPAAAAPAARAG 547
 
Name Accession Description Interval E-value
CENP-T_N pfam16171
Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral ...
 1-270 4.81e-128

Centromere kinetochore component CENP-T N-terminus; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This family represents the N-terminus of CENP-T.


Pssm-ID: 465039  Cd Length: 378  Bit Score: 374.20  E-value: 4.81e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795   1 MPDPVVKPAQVPEVARSSRRESSRGSLELHLPELEPPSTLAPGLTAPGKRKQKLRLSVFQQEVDQGLPLSQEPRRSrsAD 80
Cdd:pfam16171 105 MPESVVKPVPVPQVVQPSRRESSRGSLELQLPELEPPTTLAPGLLAPGRRKQRLRLSVFQQGVDQGLPLSQEPRGN--AD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795  81 VSSLASSFNLTFVLPGQPETVERPGLARRRPIRQLVNAGALLQDLEDNSLASALPGDSHRTPVAALPMDVGLEDTQPFSQ 160
Cdd:pfam16171 183 ASSLTSSLNLTFATPLQPQSVQRPGLARRPPTRRAVDVGAFLQDLRDTSLALAPPGDSHRTPVATLPTDTVLEDTQPFSQ 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795 161 SLAAFSLSGKHSLPSPSRPGVEDVERVMGP--PSSGTRLQSRMSRS--GPAASPSPFLEPQPPP-AEPREAVGSNEAAEP 235
Cdd:pfam16171 263 PLVGCSPSVHHSLPCPSHTGAEDAERAVGRrtQSSGPGLQNNSPGKpaEVDALALPFPNTQPEGhTEVTEAEGSQEAVEA 342

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1907189795 236 KDQEGSSGYEETSARPASGELSSSTHDSLPAEQPP 270
Cdd:pfam16171 343 KEPEGSSGDEDTSGRPASPELASSTPEFLQARRPH 377
CENP-T_C pfam15511
Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral ...
 307-402 2.53e-34

Centromere kinetochore component CENP-T histone fold; CENP-T is a family of vertebral kinetochore proteins that associates directly with CENP-W. The N-terminus of CENP-T proteins interacts directly with the Ndc80 complex in the outer kinetochore. Importantly, the CENP-T-W complex does not directly associate with CENP-A, but with histone H3 in the centromere region. CENP-T and -W form a hetero-tetramer with CENP-S and -X and bind to a ~100 bp region of nucleosome-free DNA forming a nucleosome-like structure. The DNA-CENP-T-W-S-X complex is likely to be associated with histone H3-containing nucleosomes rather than with CENP-nucleosomes. This domain is the C-terminal histone fold domain of CENP-T, which associates with chromatin.


Pssm-ID: 434768  Cd Length: 108  Bit Score: 123.31  E-value: 2.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795 307 KAGLSPYVKFFSF--CTKMPVEKTALEIVEKCLDKYFQHLCNDLEVFASHAGRKIVKPEDLLLLMRRQGLVTDQVSQHVL 384
Cdd:pfam15511  10 TAVVKRLAQRFARtsGSKGKLSKEALAALEQASDWFFEQMGEDLAAYAKHAGRKTIDESDVILLMKRQRQITSQTTLFSL 89

                          90
                  ....*....|....*...
gi 1907189795 385 VERYLPLEYRQQLIPCAF 402
Cdd:pfam15511  90 AQRYLPRELLQELRMPPP 107
HFD_CENP-T cd22920
histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also ...
 315-399 3.03e-32

histone-fold domain found in centromere protein T (CENP-T) and similar proteins; CENP-T, also called interphase centromere complex protein 22 (ICEN22), is a component of the CENPA-NAC (nucleosome-associated) complex, which plays a central role in the assembly of kinetochore proteins, mitotic progression, and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENP-T is also part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Moreover, CENP-T is a component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENP-T has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. It is required for normal chromosome organization and normal progress through mitosis.


Pssm-ID: 467045  Cd Length: 94  Bit Score: 117.27  E-value: 3.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795 315 KFFSFCTKMPVEKTALEIVEKCLDKYFQHLCNDLEVFASHAGRKIVKPEDLLLLMRRQGLVTDQVSQHVLVERYLPLEYR 394
Cdd:cd22920    10 KLFKHFLKRRVSKEALEALEEISEEFFEQLSDDLEAYADHAGRKTINEKDVELLMKRQRLVTDKQSLESLARKYLPLELL 89


                  ....*
gi 1907189795 395 QQLIP 399
Cdd:cd22920    90 DELIP 94
HFD_CENP-S cd22919
histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also ...
 322-371 2.24e-10

histone-fold domain found in centromere protein S (CENP-S) and similar proteins; CENP-S, also called MHF1, apoptosis-inducing TAF9-like domain-containing protein 1 (APITD1), FANCM-associated histone fold protein 1, FANCM-interacting histone fold protein 1, or Fanconi anemia-associated polypeptide of 16 kDa (FAAP16), is a DNA-binding component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. CENP-S, together with CENP-X, forms the MHF heterodimer, which can further assemble to form tetrameric structures. CENP-S acts as a crucial cofactor for FANCM, in both binding and ATP-dependent remodeling of DNA. It can stabilize FANCM. CENP-S also forms a discrete complex with FANCM and CENP-X, called FANCM-MHF. This interaction leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling. In complex with CENP-T, CENP-W and CENP-X (CENP-T-W-S-X heterotetramer), CENP-S is involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, CENP-S binds DNA and bends it to form a nucleosome-like structure. Its DNA-binding function is fulfilled in the presence of CENP-X. It does not bind DNA on its own.


Pssm-ID: 467044  Cd Length: 77  Bit Score: 56.42  E-value: 2.24e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907189795 322 KMPVEKTALEIVEKCLDKYFQHLCNDLEVFASHAGRKIVKPEDLLLLMRR 371
Cdd:cd22919    21 GVTVSPQFVAALAELVYKQLESLARDLEAFARHAKRKTITVDDVKLLARR 70
CENP-S pfam15630
CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. ...
 347-371 2.58e-07

CENP-S protein; CENP-S is a family of vertebral and fungal kinetochore component proteins. CENP-S complexes with CENP-X to form a stable CENP-T-W-S-X heterotetramer.


Pssm-ID: 464782  Cd Length: 76  Bit Score: 47.57  E-value: 2.58e-07
                          10        20
                  ....*....|....*....|....*
gi 1907189795 347 DLEVFASHAGRKIVKPEDLLLLMRR 371
Cdd:pfam15630  48 DLEAFAKHAGRSTITTDDVKLLARR 72
HFD_SF cd00076
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
 325-370 3.17e-06

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


Pssm-ID: 467021  Cd Length: 63  Bit Score: 44.13  E-value: 3.17e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907189795 325 VEKTALEIVEKCLDKYFQHLCNDLEVFASHAGRKIVKPEDLLLLMR 370
Cdd:cd00076    18 VSKSALELLSDLLERYLEELARAAKAYAELAGRTTPNAEDVELALE 63
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
174-309 2.16e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.68  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795 174 PSPSRPGVEDVERVMGPPSSGTRLQSRMSRSGPAASPSPFLEPQPPPAEPREAVGSNEAAEPKDQEGSSGyEETSARPAS 253
Cdd:PRK07003  410 LAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASA-PASDAPPDA 488

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907189795 254 GELSSSTHDSLPAEQPPPSPGVAVLSSEPLESV---TAKCPSRTQTAGPRRRQDPHKAG 309
Cdd:PRK07003  489 AFEPAPRAAAPSAATPAAVPDARAPAAASREDApaaAAPPAPEARPPTPAAAAPAARAG 547
PHA03247 PHA03247
large tegument protein UL36; Provisional
 135-305 3.32e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795  135 PGDSHRT-PVAALPMDVGLEDTQPFSQSLAAFSLSGKHSLPSPSRPGVEDvervmGPPSSGTRLQSRMSRSGPAASPS-P 212
Cdd:PHA03247  2605 RGDPRGPaPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRD-----DPAPGRVSRPRRARRLGRAAQASsP 2679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795  213 FLEPQPPPAEPreAVGS-NEAAEPKDQE--------GSSGYEETSARPASGELSSSTHDSLPAeqPPPSPGVAVLSSEPl 283
Cdd:PHA03247  2680 PQRPRRRAARP--TVGSlTSLADPPPPPptpepaphALVSATPLPPGPAAARQASPALPAAPA--PPAVPAGPATPGGP- 2754

                          170       180
                   ....*....|....*....|..
gi 1907189795  284 esvtAKCPSRTQTAGPRRRQDP 305
Cdd:PHA03247  2755 ----ARPARPPTTAGPPAPAPP 2772
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 32-312 3.47e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795   32 PELEPPSTLAPGLTAPGKRKQKLRLSVFQQEVDQGLPLSQEPRRSRSADVSSLASSfnltfvLPGQPETVERPGLARRRP 111
Cdd:PHA03307   122 PPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLS------SPEETARAPSSPPAEPPP 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795  112 IRQLVNAGALLQDLEDNSLASALPGDSHRTPVAALPMDVGLEDTQPFSQSLAAFSLSGKHSLPSPSRpgvedvERVMGPP 191
Cdd:PHA03307   196 STPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAP------ITLPTRI 269

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795  192 SSGTRLQSRMSRSGPAASPSPFLEPQPPPAEPREAVGSNEAAEPKDQEGSSGYEETSARPASGELSSSThdslPAEQPPP 271
Cdd:PHA03307   270 WEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRG----AAVSPGP 345

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907189795  272 SPGVAVLSSEPlesvtakcPSRTQTAGPRRRQDPHKAGLSP 312
Cdd:PHA03307   346 SPSRSPSPSRP--------PPPADPSSPRKRPRPSRAPSSP 378
PHA03247 PHA03247
large tegument protein UL36; Provisional
 36-308 4.08e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 4.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795   36 PPSTLAPGLTAPGKRKQKLRLSVFQQEVDQGLPLSQEPRRSRSADVSSLASSfnltfvlpgqpeTVERPglaRRRPIRQL 115
Cdd:PHA03247  2627 PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASS------------PPQRP---RRRAARPT 2691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795  116 VNAGAllqdlednslASALPGDSHRTPVAALPMDVGLEDTQPFSQSlaafslSGKHSLPSPSRPGVEDVERVMGPPSSGT 195
Cdd:PHA03247  2692 VGSLT----------SLADPPPPPPTPEPAPHALVSATPLPPGPAA------ARQASPALPAAPAPPAVPAGPATPGGPA 2755

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189795  196 RLQSRMSRSGPAASPSPFLEPQ-PPPAEPREAVGSNEAAEPKDQEGSSGYEETSARPASGELSSSTHDSLPAEQPPPS-- 272
Cdd:PHA03247  2756 RPARPPTTAGPPAPAPPAAPAAgPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSaq 2835

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907189795  273 PGVAVLSSEPLESVTAKCPSrTQTAGPRRRQDPHKA 308
Cdd:PHA03247  2836 PTAPPPPPGPPPPSLPLGGS-VAPGGDVRRRPPSRS 2870
 
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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