|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00104 |
PLN00104 |
MYST -like histone acetyltransferase; Provisional |
21-475 |
0e+00 |
|
MYST -like histone acetyltransferase; Provisional
Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 550.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 21 GEPGPGENAAAEGTAPSPGRVSPPTPARGEPEVTVEIGETYLCR-RPDSTWHSAEVIQSRVNDQEGRE--EFYVHYVGce 97
Cdd:PLN00104 20 DDAAATDGAGANAAAPAAPAESDPSKKRPGVMLPLEVGTRVMCRwRFDGKYHPVKVIERRRGGSGGPNdyEYYVHYTE-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 98 wlgasgpgcgelgalaalswpiltVNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSelaeqpeRKITRNQKRKHDEINH 177
Cdd:PLN00104 98 ------------------------FNRRLDEWVKLEQLDLDTVETVGDEKVEDKVAS-------LKMTRHQKRKIDETHV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 178 VQKtYAEMDPttaALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQ 257
Cdd:PLN00104 147 EEG-HEELDA---ASLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 258 WRQPPGKEIYRK----SNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKE 333
Cdd:PLN00104 223 LKHPPGDEIYRHptrqEGLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 334 SPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQ 413
Cdd:PLN00104 303 SEEDYNLACILTLPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKGNISIKELSD 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622912030 414 MTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAqyKKPPITVDSVCLKWAPPK 475
Cdd:PLN00104 383 MTAIKAEDIVSTLQSLNLIQYRKGQHVICADPKVLEEHLKAA--GRGGLEVDPSKLIWTPYK 442
|
|
| MOZ_SAS |
pfam01853 |
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
261-438 |
8.14e-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: 393.72 E-value: 8.14e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 261 PPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNV 340
Cdd:pfam01853 1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 341 ACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFR-GTLSIKDLSQMTSITQ 419
Cdd:pfam01853 81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRkEGISIEDISKATGITP 160
|
170
....*....|....*....
gi 1622912030 420 NDIISTLQSLNMVKYWKGQ 438
Cdd:pfam01853 161 EDIISTLQSLNMLKYYKGQ 179
|
|
| SAS2 |
COG5027 |
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
65-471 |
3.66e-127 |
|
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 375.26 E-value: 3.66e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 65 RPDSTWHSAEVIQSRVNdqEGREEFYVHYVgcewlgasgpgcgelgalaalswpilTVNRRLDEWVDKNRLAL------- 137
Cdd:COG5027 15 EKDGEARKAEILEINTR--KSRIKFYVHYV--------------------------ELNRRLDEWITADLINLgaaisip 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 138 TKTVKDAVQKNSEKylSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTtAALEKEHEaITKVKYVDKIHIGNYEIDA 217
Cdd:COG5027 67 KRKKQTEKGKKEKK--PKVSDRMDLDNENVQLEMLYSISNEREIRQLRFGG-SKVQNPHE-GARVKNINEIKLGNYEIEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 218 WYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFL 297
Cdd:COG5027 143 WYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 298 DHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEK 377
Cdd:COG5027 223 DHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 378 PLSDLGKLSYRSYWSWVLLEILRDFRG-TLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQ 456
Cdd:COG5027 303 PLSDLGLLSYRAYWSEIVAKLLLKMDKeITDINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNSDKLHNYLRLWS 382
|
410
....*....|....*
gi 1622912030 457 YKKPPITVDSvcLKW 471
Cdd:COG5027 383 KKRRRINPDL--LLW 395
|
|
| CBD_MOF_like |
cd18984 |
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
58-150 |
5.33e-26 |
|
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: 100.71 E-value: 5.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 58 GETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGcewlgasgpgcgelgalaalswpiltVNRRLDEWVDKNRLAL 137
Cdd:cd18984 1 GSTYYCRRSDDTVHRAEVIQSRTTKQAGREEYYVHYVG--------------------------LNRRLDEWVDKSRLSL 54
|
90
....*....|....*.
gi 1622912030 138 T---KTVKDAVQKNSE 150
Cdd:cd18984 55 NdlgKIVKTPAPPNAE 70
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00104 |
PLN00104 |
MYST -like histone acetyltransferase; Provisional |
21-475 |
0e+00 |
|
MYST -like histone acetyltransferase; Provisional
Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 550.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 21 GEPGPGENAAAEGTAPSPGRVSPPTPARGEPEVTVEIGETYLCR-RPDSTWHSAEVIQSRVNDQEGRE--EFYVHYVGce 97
Cdd:PLN00104 20 DDAAATDGAGANAAAPAAPAESDPSKKRPGVMLPLEVGTRVMCRwRFDGKYHPVKVIERRRGGSGGPNdyEYYVHYTE-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 98 wlgasgpgcgelgalaalswpiltVNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSelaeqpeRKITRNQKRKHDEINH 177
Cdd:PLN00104 98 ------------------------FNRRLDEWVKLEQLDLDTVETVGDEKVEDKVAS-------LKMTRHQKRKIDETHV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 178 VQKtYAEMDPttaALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQ 257
Cdd:PLN00104 147 EEG-HEELDA---ASLREHEEFTKVKNIATIELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 258 WRQPPGKEIYRK----SNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKE 333
Cdd:PLN00104 223 LKHPPGDEIYRHptrqEGLSMFEVDGKKNKVYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 334 SPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQ 413
Cdd:PLN00104 303 SEEDYNLACILTLPPYQRKGYGKFLIAFSYELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKKHKGNISIKELSD 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622912030 414 MTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAqyKKPPITVDSVCLKWAPPK 475
Cdd:PLN00104 383 MTAIKAEDIVSTLQSLNLIQYRKGQHVICADPKVLEEHLKAA--GRGGLEVDPSKLIWTPYK 442
|
|
| PLN03238 |
PLN03238 |
probable histone acetyltransferase MYST; Provisional |
186-453 |
7.94e-150 |
|
probable histone acetyltransferase MYST; Provisional
Pssm-ID: 215642 [Multi-domain] Cd Length: 290 Bit Score: 428.89 E-value: 7.94e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 186 DPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKE 265
Cdd:PLN03238 1 DPVLAELEREHEETTKVKNIEMIELGKYEMDTWYYSPYPEPYASCTKLYICEYCLKYMRKKKSLLRHLAKCDIRQPPGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 266 IYR---KSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVAC 342
Cdd:PLN03238 81 IYGavtEGPLSVFEVDGKKAKVYCQNLCLLAKLFLDHKTLYYDVDPFLFYVMTEVDDHGSHIVGYFSKEKVSAEDYNLAC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 343 ILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDI 422
Cdd:PLN03238 161 ILTLPPYQRKGYGKFLISFAYELSKREGKVGTPERPLSDLGKVSFRSYWTRVLLEQLRDVKGDVSIKDLSLATGIRGEDI 240
|
250 260 270
....*....|....*....|....*....|.
gi 1622912030 423 ISTLQSLNMVKYWKGQHVICVTPKLVEEHLK 453
Cdd:PLN03238 241 VSTLQSLNLIKYWKGQHVIHVDQRVLDEHWA 271
|
|
| MOZ_SAS |
pfam01853 |
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
261-438 |
8.14e-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: 393.72 E-value: 8.14e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 261 PPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNV 340
Cdd:pfam01853 1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 341 ACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFR-GTLSIKDLSQMTSITQ 419
Cdd:pfam01853 81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLLKHRkEGISIEDISKATGITP 160
|
170
....*....|....*....
gi 1622912030 420 NDIISTLQSLNMVKYWKGQ 438
Cdd:pfam01853 161 EDIISTLQSLNMLKYYKGQ 179
|
|
| SAS2 |
COG5027 |
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
65-471 |
3.66e-127 |
|
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 375.26 E-value: 3.66e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 65 RPDSTWHSAEVIQSRVNdqEGREEFYVHYVgcewlgasgpgcgelgalaalswpilTVNRRLDEWVDKNRLAL------- 137
Cdd:COG5027 15 EKDGEARKAEILEINTR--KSRIKFYVHYV--------------------------ELNRRLDEWITADLINLgaaisip 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 138 TKTVKDAVQKNSEKylSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTtAALEKEHEaITKVKYVDKIHIGNYEIDA 217
Cdd:COG5027 67 KRKKQTEKGKKEKK--PKVSDRMDLDNENVQLEMLYSISNEREIRQLRFGG-SKVQNPHE-GARVKNINEIKLGNYEIEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 218 WYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFL 297
Cdd:COG5027 143 WYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRNLCLLSKLFL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 298 DHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEK 377
Cdd:COG5027 223 DHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQKEGKVGSPEK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 378 PLSDLGKLSYRSYWSWVLLEILRDFRG-TLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQ 456
Cdd:COG5027 303 PLSDLGLLSYRAYWSEIVAKLLLKMDKeITDINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNSDKLHNYLRLWS 382
|
410
....*....|....*
gi 1622912030 457 YKKPPITVDSvcLKW 471
Cdd:COG5027 383 KKRRRINPDL--LLW 395
|
|
| PLN03239 |
PLN03239 |
histone acetyltransferase; Provisional |
123-473 |
1.76e-105 |
|
histone acetyltransferase; Provisional
Pssm-ID: 178777 [Multi-domain] Cd Length: 351 Bit Score: 318.14 E-value: 1.76e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 123 NRRLDEWVDKnrlaltktvkdavqknsEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEKEHEAITKV 202
Cdd:PLN03239 9 NRRMDEWISK-----------------DKSNEEILALPSDHLATHTVGEDVVATIAAPELDEHEGLDDAALKEHEEVTKV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 203 KYVDKIHIGNYEIDAWYFSPFPE----DYGKQPKLWLCEYCLK-YMKYEKSYRFHLGQC--QWRQPPGKEIYRKSNISVY 275
Cdd:PLN03239 72 KNVAFLELGPYQMDTWYFSPLPKelfkAGGFIDVLYVCEFSFGfFARKSELLRFQAKELpkERRHPPGNEIYRCGDLAMF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 276 EVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYG 355
Cdd:PLN03239 152 EVDGFEERIYCQNLCYIAKLFLDHKTLYFDVDPFLFYVLCEVDERGFHPVGYYSKEKYSDVGYNLACILTFPAHQRKGYG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 356 KFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRG---TLSIKDLSQMTSITQNDIISTLQSLNMV 432
Cdd:PLN03239 232 RFLIAFSYELSKKEEKVGSPEKPMSDLGQQAYIPYWGSTIVDFLLNHSGndsSLSIMDIAKKTSIMAEDIVFALNQLGIL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622912030 433 KYWKGQHVICVTPKLVEEHLKSAQYKKPpiTVDSVCLKWAP 473
Cdd:PLN03239 312 KFINGIYFIAAEKGLLEELAEKHPVKEP--RVDPSKLHWTP 350
|
|
| PTZ00064 |
PTZ00064 |
histone acetyltransferase; Provisional |
76-473 |
1.01e-97 |
|
histone acetyltransferase; Provisional
Pssm-ID: 173359 [Multi-domain] Cd Length: 552 Bit Score: 305.02 E-value: 1.01e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 76 IQSRVNDQEGRE--EFYVHYVGcewlgasgpgcgelgalaalswpiltVNRRLDEWVDKNRLALTKTVKD--------AV 145
Cdd:PTZ00064 136 VSSSSNESQIKEdyEFYVHFRG--------------------------LNRRLDRWVKGKDIKLSFDVEElndpnlieRF 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 146 QKNSEKYLSEL--AEQPERKITRNQKRKhdeINHVQKTYAEmDPTT------AALEkEHEAITKVKYVDKIHIGNYEIDA 217
Cdd:PTZ00064 190 QKQGIKFISSLsvSNSANKSGNKSKKRN---VGVLDISDGE-DPDEhegmdhSAIL-DHEETTRLRTIGRVRIGKFILDT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 218 WYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFL 297
Cdd:PTZ00064 265 WYFSPLPDEYQNVDTLHFCEYCLDFFCFEDELIRHLSRCQLRHPPGNEIYRKDNISVFEIDGALTRGYAENLCYLAKLFL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 298 DHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEK 377
Cdd:PTZ00064 345 DHKTLQYDVEPFLFYIVTEVDEEGCHIVGYFSKEKVSLLHYNLACILTLPCYQRKGYGKLLVDLSYKLSLKEGKWGHPER 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 378 PLSDLGKLSYRSYW----SWVLLEILRD----FRG-----------TLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQ 438
Cdd:PTZ00064 425 PLSDLGRAIYNNWWahriSEYLLEYFKQnkicERGgskqplqvsnyWKFIDNVVRSTGIRREDVIRILEENGIMRNIKDQ 504
|
410 420 430
....*....|....*....|....*....|....*
gi 1622912030 439 HVICVTPKLVEEHLKSAqyKKPPITVDSVCLKWAP 473
Cdd:PTZ00064 505 HYIFCNQEFLKGIVKRS--GRPGITLIDKYFNWVP 537
|
|
| zf-MYST |
pfam17772 |
MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone ... |
202-256 |
3.95e-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: 100.38 E-value: 3.95e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622912030 202 VKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQC 256
Cdd:pfam17772 1 VKNIEKIQFGRYEIDTWYFSPYPEEYTNVDKLYVCEFCLKYMKSRKSYKRHRKKC 55
|
|
| CBD_MOF_like |
cd18984 |
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
58-150 |
5.33e-26 |
|
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: 100.71 E-value: 5.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 58 GETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGcewlgasgpgcgelgalaalswpiltVNRRLDEWVDKNRLAL 137
Cdd:cd18984 1 GSTYYCRRSDDTVHRAEVIQSRTTKQAGREEYYVHYVG--------------------------LNRRLDEWVDKSRLSL 54
|
90
....*....|....*.
gi 1622912030 138 T---KTVKDAVQKNSE 150
Cdd:cd18984 55 NdlgKIVKTPAPPNAE 70
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| Tudor-knot |
pfam11717 |
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ... |
55-137 |
4.03e-14 |
|
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: 66.46 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 55 VEIGETYLCRRPDSTWHSAEVIQSRvnDQEGREEFYVHYVGCewlgasgpgcgelgalaalswpiltvNRRLDEWVDKNR 134
Cdd:pfam11717 1 IEIGCKVLVRKRDGEWRLAEILSIR--PKKGKYEYYVHYVGF--------------------------NKRLDEWVPEDR 52
|
...
gi 1622912030 135 LAL 137
Cdd:pfam11717 53 IDL 55
|
|
| CBD_MOF_like |
cd18642 |
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
62-137 |
2.98e-09 |
|
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: 53.20 E-value: 2.98e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622912030 62 LCRRPDSTWHSAEVIQSRVNdQEGREEFYVHYVGCewlgasgpgcgelgalaalswpiltvNRRLDEWVDKNRLAL 137
Cdd:cd18642 5 CWVQRNDEEHLAEVLSRRTR-KHAPPEFYVHYVEL--------------------------NRRLDEWITTDRIDL 53
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|
| CBD |
cd18643 |
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ... |
59-135 |
2.49e-03 |
|
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: 36.39 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622912030 59 ETYLCRRPDS---TWHSAEVIQSRVNDQEGRE-EFYVHYVGcewlgasgpgcgelgalaalswpiltVNRRLDEWVDKNR 134
Cdd:cd18643 1 EKVLVFEPDPkarVLYDAKILSVITGKDGRAPpEYLVHYVG--------------------------WNRRLDEWVAEDR 54
|
.
gi 1622912030 135 L 135
Cdd:cd18643 55 V 55
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