|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00104 |
PLN00104 |
MYST -like histone acetyltransferase; Provisional |
15-449 |
0e+00 |
|
MYST -like histone acetyltransferase; Provisional
Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 566.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 15 SGVAGEGEPGPGENAAAEGTAPSPGRVSPPTPARGEPEVTVEIGETYLCR-RPDSTWHSAEVIQSRVNDQEGRE--EFYV 91
Cdd:PLN00104 14 AAPAASDDAAATDGAGANAAAPAAPAESDPSKKRPGVMLPLEVGTRVMCRwRFDGKYHPVKVIERRRGGSGGPNdyEYYV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 92 HYVGFNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSelaeqpeRKITRNQKRKHDEINHVQKtYAEMDPttaALEKEHE 171
Cdd:PLN00104 94 HYTEFNRRLDEWVKLEQLDLDTVETVGDEKVEDKVAS-------LKMTRHQKRKIDETHVEEG-HEELDA---ASLREHE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 172 AITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRK----SNIS 247
Cdd:PLN00104 163 EFTKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRHptrqEGLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 248 VYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRG 327
Cdd:PLN00104 243 MFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 328 YGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVK 407
Cdd:PLN00104 323 YGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKGNISIKELSDMTAIKAEDIVSTLQSLNLIQ 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 226371636 408 YWKGQHVICVTPKLVEEHLKSAqyKKPPITVDSVCLKWAPPK 449
Cdd:PLN00104 403 YRKGQHVICADPKVLEEHLKAA--GRGGLEVDPSKLIWTPYK 442
|
|
| MOZ_SAS |
pfam01853 |
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
235-412 |
7.96e-138 |
|
MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases.
Pssm-ID: 460362 [Multi-domain] Cd Length: 179 Bit Score: 392.95 E-value: 7.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 235 PPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNV 314
Cdd:pfam01853 1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 315 ACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFR-GTLSIKDLSQMTSITQ 393
Cdd:pfam01853 81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRkEGISIEDISKATGITP 160
|
170
....*....|....*....
gi 226371636 394 NDIISTLQSLNMVKYWKGQ 412
Cdd:pfam01853 161 EDIISTLQSLNMLKYYKGQ 179
|
|
| SAS2 |
COG5027 |
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
65-445 |
1.42e-132 |
|
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 387.98 E-value: 1.42e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 65 RPDSTWHSAEVIQSRVNdqEGREEFYVHYVGFNRRLDEWVDKNRLALT--------KTVKDAVQKNSEKYLSELAEQPER 136
Cdd:COG5027 15 EKDGEARKAEILEINTR--KSRIKFYVHYVELNRRLDEWITADLINLGaaisipkrKKQTEKGKKEKKPKVSDRMDLDNE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 137 KItrnQKRKHDEINHVQKTYAEMDPTTAALEKEHEAitKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKY 216
Cdd:COG5027 93 NV---QLEMLYSISNEREIRQLRFGGSKVQNPHEGA--RVKNINEIKLGNYEIEPWYFSPYPEEFSDLDIVYICEFCLKY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 217 MKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGA 296
Cdd:COG5027 168 YGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 297 HIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDF 376
Cdd:COG5027 248 HLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLLKM 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 377 RG-TLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSvcLKW 445
Cdd:COG5027 328 DKeITDINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNSDKLHNYLRLWSKKRRRINPDL--LLW 395
|
|
| CBD_MOF_like |
cd18984 |
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
58-124 |
1.90e-31 |
|
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar proteins; This subgroup includes the chromo barrel domain of Drosophila melanogaster males-absent on the first (MOF) protein. The histone H4 lysine 16 (H4K16)-specific acetyltransferase MOF is part of two distinct complexes involved in X chromosome dosage compensation and autosomal transcription regulation. Its chromobarrel domain is essential for H4K16 acetylation throughout the Drosophila genome and controls spreading of the male-specific lethal (MSL) complex on the X chromosome. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. The MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.
Pssm-ID: 350847 [Multi-domain] Cd Length: 70 Bit Score: 114.96 E-value: 1.90e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 58 GETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALT---KTVKDAVQKNSE 124
Cdd:cd18984 1 GSTYYCRRSDDTVHRAEVIQSRTTKQAGREEYYVHYVGLNRRLDEWVDKSRLSLNdlgKIVKTPAPPNAE 70
|
|
| CHROMO |
smart00298 |
Chromatin organization modifier domain; |
71-111 |
5.14e-05 |
|
Chromatin organization modifier domain;
Pssm-ID: 214605 [Multi-domain] Cd Length: 55 Bit Score: 40.66 E-value: 5.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 226371636 71 HSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLAL 111
Cdd:smart00298 2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLN 42
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00104 |
PLN00104 |
MYST -like histone acetyltransferase; Provisional |
15-449 |
0e+00 |
|
MYST -like histone acetyltransferase; Provisional
Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 566.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 15 SGVAGEGEPGPGENAAAEGTAPSPGRVSPPTPARGEPEVTVEIGETYLCR-RPDSTWHSAEVIQSRVNDQEGRE--EFYV 91
Cdd:PLN00104 14 AAPAASDDAAATDGAGANAAAPAAPAESDPSKKRPGVMLPLEVGTRVMCRwRFDGKYHPVKVIERRRGGSGGPNdyEYYV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 92 HYVGFNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSelaeqpeRKITRNQKRKHDEINHVQKtYAEMDPttaALEKEHE 171
Cdd:PLN00104 94 HYTEFNRRLDEWVKLEQLDLDTVETVGDEKVEDKVAS-------LKMTRHQKRKIDETHVEEG-HEELDA---ASLREHE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 172 AITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRK----SNIS 247
Cdd:PLN00104 163 EFTKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRHptrqEGLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 248 VYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRG 327
Cdd:PLN00104 243 MFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 328 YGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVK 407
Cdd:PLN00104 323 YGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKGNISIKELSDMTAIKAEDIVSTLQSLNLIQ 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 226371636 408 YWKGQHVICVTPKLVEEHLKSAqyKKPPITVDSVCLKWAPPK 449
Cdd:PLN00104 403 YRKGQHVICADPKVLEEHLKAA--GRGGLEVDPSKLIWTPYK 442
|
|
| PLN03238 |
PLN03238 |
probable histone acetyltransferase MYST; Provisional |
160-427 |
2.55e-149 |
|
probable histone acetyltransferase MYST; Provisional
Pssm-ID: 215642 [Multi-domain] Cd Length: 290 Bit Score: 426.58 E-value: 2.55e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 160 DPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKE 239
Cdd:PLN03238 1 DPVLAELEREHEETTKVKNIEMIELGKYEMDTWYYSPYPEPYASCTKLYICEYCLKYMRKKKSLLRHLAKCDIRQPPGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 240 IYR---KSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVAC 316
Cdd:PLN03238 81 IYGavtEGPLSVFEVDGKKAKVYCQNLCLLAKLFLDHKTLYYDVDPFLFYVMTEVDDHGSHIVGYFSKEKVSAEDYNLAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 317 ILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDI 396
Cdd:PLN03238 161 ILTLPPYQRKGYGKFLISFAYELSKREGKVGTPERPLSDLGKVSFRSYWTRVLLEQLRDVKGDVSIKDLSLATGIRGEDI 240
|
250 260 270
....*....|....*....|....*....|.
gi 226371636 397 ISTLQSLNMVKYWKGQHVICVTPKLVEEHLK 427
Cdd:PLN03238 241 VSTLQSLNLIKYWKGQHVIHVDQRVLDEHWA 271
|
|
| MOZ_SAS |
pfam01853 |
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
235-412 |
7.96e-138 |
|
MOZ/SAS family; This region of these proteins has been suggested to be homologous to acetyltransferases.
Pssm-ID: 460362 [Multi-domain] Cd Length: 179 Bit Score: 392.95 E-value: 7.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 235 PPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNV 314
Cdd:pfam01853 1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 315 ACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFR-GTLSIKDLSQMTSITQ 393
Cdd:pfam01853 81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRkEGISIEDISKATGITP 160
|
170
....*....|....*....
gi 226371636 394 NDIISTLQSLNMVKYWKGQ 412
Cdd:pfam01853 161 EDIISTLQSLNMLKYYKGQ 179
|
|
| SAS2 |
COG5027 |
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
65-445 |
1.42e-132 |
|
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 387.98 E-value: 1.42e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 65 RPDSTWHSAEVIQSRVNdqEGREEFYVHYVGFNRRLDEWVDKNRLALT--------KTVKDAVQKNSEKYLSELAEQPER 136
Cdd:COG5027 15 EKDGEARKAEILEINTR--KSRIKFYVHYVELNRRLDEWITADLINLGaaisipkrKKQTEKGKKEKKPKVSDRMDLDNE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 137 KItrnQKRKHDEINHVQKTYAEMDPTTAALEKEHEAitKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKY 216
Cdd:COG5027 93 NV---QLEMLYSISNEREIRQLRFGGSKVQNPHEGA--RVKNINEIKLGNYEIEPWYFSPYPEEFSDLDIVYICEFCLKY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 217 MKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGA 296
Cdd:COG5027 168 YGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 297 HIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDF 376
Cdd:COG5027 248 HLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEKPLSDLGLLSYRAYWSEIVAKLLLKM 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 377 RG-TLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSvcLKW 445
Cdd:COG5027 328 DKeITDINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNSDKLHNYLRLWSKKRRRINPDL--LLW 395
|
|
| PLN03239 |
PLN03239 |
histone acetyltransferase; Provisional |
89-447 |
4.68e-110 |
|
histone acetyltransferase; Provisional
Pssm-ID: 178777 [Multi-domain] Cd Length: 351 Bit Score: 328.92 E-value: 4.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 89 FYVHYVGFNRRLDEWVDKnrlaltktvkdavqknsEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEK 168
Cdd:PLN03239 1 YYVHYKDFNRRMDEWISK-----------------DKSNEEILALPSDHLATHTVGEDVVATIAAPELDEHEGLDDAALK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 169 EHEAITKVKYVDKIHIGNYEIDAWYFSPFPE----DYGKQPKLWLCEYCLK-YMKYEKSYRFHLGQC--QWRQPPGKEIY 241
Cdd:PLN03239 64 EHEEVTKVKNVAFLELGPYQMDTWYFSPLPKelfkAGGFIDVLYVCEFSFGfFARKSELLRFQAKELpkERRHPPGNEIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 242 RKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLP 321
Cdd:PLN03239 144 RCGDLAMFEVDGFEERIYCQNLCYIAKLFLDHKTLYFDVDPFLFYVLCEVDERGFHPVGYYSKEKYSDVGYNLACILTFP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 322 PYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRG---TLSIKDLSQMTSITQNDIIS 398
Cdd:PLN03239 224 AHQRKGYGRFLIAFSYELSKKEEKVGSPEKPMSDLGQQAYIPYWGSTIVDFLLNHSGndsSLSIMDIAKKTSIMAEDIVF 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 226371636 399 TLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPpiTVDSVCLKWAP 447
Cdd:PLN03239 304 ALNQLGILKFINGIYFIAAEKGLLEELAEKHPVKEP--RVDPSKLHWTP 350
|
|
| PTZ00064 |
PTZ00064 |
histone acetyltransferase; Provisional |
76-447 |
1.38e-102 |
|
histone acetyltransferase; Provisional
Pssm-ID: 173359 [Multi-domain] Cd Length: 552 Bit Score: 316.57 E-value: 1.38e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 76 IQSRVNDQEGRE--EFYVHYVGFNRRLDEWVDKNRLALTKTVKD--------AVQKNSEKYLSEL--AEQPERKITRNQK 143
Cdd:PTZ00064 136 VSSSSNESQIKEdyEFYVHFRGLNRRLDRWVKGKDIKLSFDVEElndpnlieRFQKQGIKFISSLsvSNSANKSGNKSKK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 144 RKhdeINHVQKTYAEmDPTT------AALEkEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYM 217
Cdd:PTZ00064 216 RN---VGVLDISDGE-DPDEhegmdhSAIL-DHEETTRLRTIGRVRIGKFILDTWYFSPLPDEYQNVDTLHFCEYCLDFF 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 218 KYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAH 297
Cdd:PTZ00064 291 CFEDELIRHLSRCQLRHPPGNEIYRKDNISVFEIDGALTRGYAENLCYLAKLFLDHKTLQYDVEPFLFYIVTEVDEEGCH 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 298 IVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYW----SWVLLEIL 373
Cdd:PTZ00064 371 IVGYFSKEKVSLLHYNLACILTLPCYQRKGYGKLLVDLSYKLSLKEGKWGHPERPLSDLGRAIYNNWWahriSEYLLEYF 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 374 RD----FRG-----------TLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAqyKKPPITV 438
Cdd:PTZ00064 451 KQnkicERGgskqplqvsnyWKFIDNVVRSTGIRREDVIRILEENGIMRNIKDQHYIFCNQEFLKGIVKRS--GRPGITL 528
|
....*....
gi 226371636 439 DSVCLKWAP 447
Cdd:PTZ00064 529 IDKYFNWVP 537
|
|
| CBD_MOF_like |
cd18984 |
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
58-124 |
1.90e-31 |
|
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar proteins; This subgroup includes the chromo barrel domain of Drosophila melanogaster males-absent on the first (MOF) protein. The histone H4 lysine 16 (H4K16)-specific acetyltransferase MOF is part of two distinct complexes involved in X chromosome dosage compensation and autosomal transcription regulation. Its chromobarrel domain is essential for H4K16 acetylation throughout the Drosophila genome and controls spreading of the male-specific lethal (MSL) complex on the X chromosome. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. The MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.
Pssm-ID: 350847 [Multi-domain] Cd Length: 70 Bit Score: 114.96 E-value: 1.90e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226371636 58 GETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALT---KTVKDAVQKNSE 124
Cdd:cd18984 1 GSTYYCRRSDDTVHRAEVIQSRTTKQAGREEYYVHYVGLNRRLDEWVDKSRLSLNdlgKIVKTPAPPNAE 70
|
|
| zf-MYST |
pfam17772 |
MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone ... |
176-230 |
4.67e-26 |
|
MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone acetyltransferases.
Pssm-ID: 407644 [Multi-domain] Cd Length: 55 Bit Score: 100.00 E-value: 4.67e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 226371636 176 VKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQC 230
Cdd:pfam17772 1 VKNIEKIQFGRYEIDTWYFSPYPEEYTNVDKLYVCEFCLKYMKSRKSYKRHRKKC 55
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|
| Tudor-knot |
pfam11717 |
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ... |
55-111 |
7.60e-20 |
|
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is required for binding to RNA. The know influences the loop conformation of the helical turn Ht2 - residues 61-6 3- that is located at the side opposite the knot in the tudor domain-chromodomain; stabilization of Ht2 is essential for RNA binding.
Pssm-ID: 432022 [Multi-domain] Cd Length: 55 Bit Score: 82.64 E-value: 7.60e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 226371636 55 VEIGETYLCRRPDSTWHSAEVIQSRvnDQEGREEFYVHYVGFNRRLDEWVDKNRLAL 111
Cdd:pfam11717 1 IEIGCKVLVRKRDGEWRLAEILSIR--PKKGKYEYYVHYVGFNKRLDEWVPEDRIDL 55
|
|
| CBD_MOF_like |
cd18642 |
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
62-111 |
3.19e-14 |
|
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar proteins; This subgroup includes the chromo barrel domains found in human Tat-interactive protein 60 (TIP60, (also known as KAT5 or HTATIP), Drosophila melanogaster males-absent on the first (MOF) protein, and Saccharomyces ESA1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. The MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.
Pssm-ID: 350844 [Multi-domain] Cd Length: 67 Bit Score: 67.07 E-value: 3.19e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 226371636 62 LCRRPDSTWHSAEVIQSRVNdQEGREEFYVHYVGFNRRLDEWVDKNRLAL 111
Cdd:cd18642 5 CWVQRNDEEHLAEVLSRRTR-KHAPPEFYVHYVELNRRLDEWITTDRIDL 53
|
|
| CBD_TIP60_like |
cd18985 |
chromo barrel domain of human tat-interactive protein 60, and similar proteins; ... |
63-113 |
4.62e-10 |
|
chromo barrel domain of human tat-interactive protein 60, and similar proteins; Tat-interactive protein 60 (also known as KAT5 or HTATIP) catalyzes the acetylation of lysine side chains in various histone and nonhistone proteins, and in itself. It plays roles in multiple cellular processes including remodeling, transcription, DNA double-strand break repair, apoptosis, embryonic stem cell identity, and embryonic development. The TIP60 chromo barrel domain recognizes trimethylated lysine at site 9 of histone H3 (H3K9me3) which triggers TIP60 to acetylate and activate ataxia telangiectasia-mutated kinase, thereby promoting the DSB repair pathway. In a different study, the TIP60 chromo barrel domain was shown to bind H3K4me1, which stabilizes TIP60 recruitment to a subset of estrogen receptor alpha target genes, facilitating regulation of the associated gene transcription. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. This subgroup belongs to the MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.
Pssm-ID: 350848 [Multi-domain] Cd Length: 64 Bit Score: 55.28 E-value: 4.62e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 226371636 63 CRRP---DSTWHSAEVIQsrVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTK 113
Cdd:cd18985 3 LRVRmhkTDEWPLAEILS--VKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKK 54
|
|
| CBD |
cd18643 |
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ... |
59-109 |
1.25e-08 |
|
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the chromo barrel domains found in human Tat-interactive protein 60 (TIP60, (also known as KAT5 or HTATIP), Drosophila melanogaster males-absent on the first (MOF) protein, human male-specific lethal (MSL) complex subunit 3 (MSL3), and retinoblastoma binding protein 1. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain. The chromobarrel domains include a MOF-like subgroup which may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.
Pssm-ID: 350845 [Multi-domain] Cd Length: 61 Bit Score: 51.02 E-value: 1.25e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 226371636 59 ETYLCRRPDS---TWHSAEVIQSRVNDQEGRE-EFYVHYVGFNRRLDEWVDKNRL 109
Cdd:cd18643 1 EKVLVFEPDPkarVLYDAKILSVITGKDGRAPpEYLVHYVGWNRRLDEWVAEDRV 55
|
|
| CBD_ESA1_like |
cd18986 |
chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, ... |
73-115 |
1.37e-07 |
|
chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, and similar proteins; The subgroup includes the chromo barrel domain of NuA4 histone acetyltransferase (HAT) complex catalytic subunit Esa1 (also known as Tas1 and Kat5). Yeast Esa1p acetylates specific histones nonrandomly in H4, H3, and H2A. Esa1 also plays roles in cell cycle progression. In addition, its chromo barrel domain plays a role in the yeast Piccolo NuA4 complex's ability to distinguish between histones and nucleosomes; however, the chromodomain is not required for the Piccolo to bind to nucleosomes. SH3-fold-beta-barrel domains of the chromo-like superfamily include chromodomains, chromo shadow domains, and chromo barrel domains, and are implicated in the recognition of lysine-methylated histone tails and nucleic acids. The chromodomain differs, in that it lacks the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromodomain. This subgroup belongs to the MOF-like chromo barrels may be may be auto-inhibited, i.e. they seem to have occluded peptide binding sites.
Pssm-ID: 350849 [Multi-domain] Cd Length: 65 Bit Score: 48.36 E-value: 1.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 226371636 73 AEVIQsrVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTKTV 115
Cdd:cd18986 16 AEILS--INTRKAPPKFYVHYEDFNKRLDEWITADRINLSKEV 56
|
|
| MBT_PHF20L1-like |
cd20104 |
malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and ... |
55-114 |
5.26e-06 |
|
malignant brain tumor (MBT) repeat found in PHD finger protein 20-like protein 1 (PHF20L1) and similar domains; PHF20L1 associates with SOX2, antagonizes SOX2 ubiquitination and the sequential degradation induced by MLL1/WDR5 complexes. It binds both monomethylated Lys-42 and Lys-117 in SOX2 and thereby prevents SOX2 proteolysis. PHF20L1 also reads and controls enzyme levels of methylated DNMT1 in cells, thus representing a novel antagonist of DNMT1 degradation. PHF20L1 contains one MBT (malignant brain tumor) repeat. The MBT repeat is a protein module that recognizes methylated lysine residues on histones. MBT repeats contain a semi-aromatic cage to accommodate methyllysine and show specificity towards the lower methylation states of lysine. This model corresponds to the MBT repeat of PHF20L1 and similar domains that contains the semi-aromatic cage that may bind methylated lysine residues.
Pssm-ID: 439094 [Multi-domain] Cd Length: 60 Bit Score: 43.77 E-value: 5.26e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226371636 55 VEIGETYLCRRPDSTWHSAEVIQSRVNDQEgreeFYVHYVGFNRRLDEWVDKN--RLALTKT 114
Cdd:cd20104 1 FKVGDRVDALDGEGKWYEAKIVEVDEEENK----VLVHYDGWSSRYDEWIDRDseRLRPLHT 58
|
|
| CHROMO |
smart00298 |
Chromatin organization modifier domain; |
71-111 |
5.14e-05 |
|
Chromatin organization modifier domain;
Pssm-ID: 214605 [Multi-domain] Cd Length: 55 Bit Score: 40.66 E-value: 5.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 226371636 71 HSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLAL 111
Cdd:smart00298 2 YEVEKILDHRWKKKGELEYLVKWKGYSYSEDTWEPEENLLN 42
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