|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00104 |
PLN00104 |
MYST -like histone acetyltransferase; Provisional |
387-813 |
5.99e-164 |
|
MYST -like histone acetyltransferase; Provisional
Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 483.49 E-value: 5.99e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 387 REDGTVHRGQVLQSRTTENAAAPD-EYYVHYVGLNRRLDGWVgrhrisdNADDLGGITVLPAPPLAPDQPSTSRemlaqq 465
Cdd:PLN00104 65 RFDGKYHPVKVIERRRGGSGGPNDyEYYVHYTEFNRRLDEWV-------KLEQLDLDTVETVGDEKVEDKVASL------ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 466 aaaaaaasserqkraankdyylsycensrydysdrKMTRYQKRRYDEINHVQkSHAELtatQAALEKEHESITKIKYIDK 545
Cdd:PLN00104 132 -----------------------------------KMTRHQKRKIDETHVEE-GHEEL---DAASLREHEEFTKVKNIAT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 546 LQFGNYEIDTWYFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHECDRRRPPGREIYRKG----NISIYEVNGKEES 621
Cdd:PLN00104 173 IELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRHPtrqeGLSMFEVDGKKNK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 622 LYCQLLCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSY 701
Cdd:PLN00104 253 VYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKGYGKFLIAFSY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 702 ELSRKEGVIGSPEKPLSDLGRLSYRSYWAYTLLELMKTrcAPEQITIKELSEMSGITHDDIIYTLQSMKMIKYWKGQNVI 781
Cdd:PLN00104 333 ELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKK--HKGNISIKELSDMTAIKAEDIVSTLQSLNLIQYRKGQHVI 410
|
410 420 430
....*....|....*....|....*....|..
gi 17530803 782 CVTSKTIQDHLQlpQFKQPKLTIDTDYLVWSP 813
Cdd:PLN00104 411 CADPKVLEEHLK--AAGRGGLEVDPSKLIWTP 440
|
|
| MOZ_SAS |
pfam01853 |
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
599-778 |
1.24e-125 |
|
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: 374.07 E-value: 1.24e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 599 PPGREIYRKGNISIYEVNGKEESLYCQLLCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNV 678
Cdd:pfam01853 1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 679 ACILVLPPHQRKGFGKLLIAFSYELSRKEGVIGSPEKPLSDLGRLSYRSYWAYTLLELMKtRCAPEQITIKELSEMSGIT 758
Cdd:pfam01853 81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLL-KHRKEGISIEDISKATGIT 159
|
170 180
....*....|....*....|
gi 17530803 759 HDDIIYTLQSMKMIKYWKGQ 778
Cdd:pfam01853 160 PEDIISTLQSLNMLKYYKGQ 179
|
|
| SAS2 |
COG5027 |
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
387-811 |
1.12e-119 |
|
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 367.17 E-value: 1.12e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 387 REDGTVHRGQVLQSRTTEnaaAPDEYYVHYVGLNRRLDGWVGRHRIsdnadDLGGITVLPAPPLAPDQpstsremlaqqa 466
Cdd:COG5027 15 EKDGEARKAEILEINTRK---SRIKFYVHYVELNRRLDEWITADLI-----NLGAAISIPKRKKQTEK------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 467 aaaaaASSERQKRAANKDYYLSYCENSRYDYSDRKMTRYQKRRyDEINHVQKSHaeltatqaalekeheSITKIKYIDKL 546
Cdd:COG5027 75 -----GKKEKKPKVSDRMDLDNENVQLEMLYSISNEREIRQLR-FGGSKVQNPH---------------EGARVKNINEI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 547 QFGNYEIDTWYFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHECDRRRPPGREIYRKGNISIYEVNGKEESLYCQL 626
Cdd:COG5027 134 KLGNYEIEPWYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 627 LCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSYELSRK 706
Cdd:COG5027 214 LCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 707 EGVIGSPEKPLSDLGRLSYRSYWAYTLLE-LMKTRcaPEQITIKELSEMSGITHDDIIYTLQSMKMIKYWKGQNVICVTS 785
Cdd:COG5027 294 EGKVGSPEKPLSDLGLLSYRAYWSEIVAKlLLKMD--KEITDINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNS 371
|
410 420
....*....|....*....|....*.
gi 17530803 786 KTIQDHLQLPQFKQPklTIDTDYLVW 811
Cdd:COG5027 372 DKLHNYLRLWSKKRR--RINPDLLLW 395
|
|
| CBD_MOF_like |
cd18984 |
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
380-452 |
1.63e-33 |
|
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: 123.05 E-value: 1.63e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17530803 380 DKIYFIRREDGTVHRGQVLQSRTTENAAaPDEYYVHYVGLNRRLDGWVGRHRISDNadDLGGITVLPAPPLAP 452
Cdd:cd18984 1 GSTYYCRRSDDTVHRAEVIQSRTTKQAG-REEYYVHYVGLNRRLDEWVDKSRLSLN--DLGKIVKTPAPPNAE 70
|
|
| CHROMO |
smart00298 |
Chromatin organization modifier domain; |
411-439 |
6.99e-04 |
|
Chromatin organization modifier domain;
Pssm-ID: 214605 [Multi-domain] Cd Length: 55 Bit Score: 38.35 E-value: 6.99e-04
10 20
....*....|....*....|....*....
gi 17530803 411 EYYVHYVGLNRRLDGWVGRHRISDNADDL 439
Cdd:smart00298 19 EYLVKWKGYSYSEDTWEPEENLLNCSKKL 47
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN00104 |
PLN00104 |
MYST -like histone acetyltransferase; Provisional |
387-813 |
5.99e-164 |
|
MYST -like histone acetyltransferase; Provisional
Pssm-ID: 215056 [Multi-domain] Cd Length: 450 Bit Score: 483.49 E-value: 5.99e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 387 REDGTVHRGQVLQSRTTENAAAPD-EYYVHYVGLNRRLDGWVgrhrisdNADDLGGITVLPAPPLAPDQPSTSRemlaqq 465
Cdd:PLN00104 65 RFDGKYHPVKVIERRRGGSGGPNDyEYYVHYTEFNRRLDEWV-------KLEQLDLDTVETVGDEKVEDKVASL------ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 466 aaaaaaasserqkraankdyylsycensrydysdrKMTRYQKRRYDEINHVQkSHAELtatQAALEKEHESITKIKYIDK 545
Cdd:PLN00104 132 -----------------------------------KMTRHQKRKIDETHVEE-GHEEL---DAASLREHEEFTKVKNIAT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 546 LQFGNYEIDTWYFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHECDRRRPPGREIYRKG----NISIYEVNGKEES 621
Cdd:PLN00104 173 IELGRYEIDTWYFSPFPPEYNDCSKLYFCEFCLKFMKRKEQLQRHMKKCDLKHPPGDEIYRHPtrqeGLSMFEVDGKKNK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 622 LYCQLLCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSY 701
Cdd:PLN00104 253 VYCQNLCYLAKLFLDHKTLYYDVDLFLFYVLCECDDRGCHMVGYFSKEKHSEEDYNLACILTLPPYQRKGYGKFLIAFSY 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 702 ELSRKEGVIGSPEKPLSDLGRLSYRSYWAYTLLELMKTrcAPEQITIKELSEMSGITHDDIIYTLQSMKMIKYWKGQNVI 781
Cdd:PLN00104 333 ELSKREGKVGTPERPLSDLGLVSYRGYWTRVLLEILKK--HKGNISIKELSDMTAIKAEDIVSTLQSLNLIQYRKGQHVI 410
|
410 420 430
....*....|....*....|....*....|..
gi 17530803 782 CVTSKTIQDHLQlpQFKQPKLTIDTDYLVWSP 813
Cdd:PLN00104 411 CADPKVLEEHLK--AAGRGGLEVDPSKLIWTP 440
|
|
| PLN03238 |
PLN03238 |
probable histone acetyltransferase MYST; Provisional |
528-813 |
1.91e-134 |
|
probable histone acetyltransferase MYST; Provisional
Pssm-ID: 215642 [Multi-domain] Cd Length: 290 Bit Score: 401.54 E-value: 1.91e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 528 AALEKEHESITKIKYIDKLQFGNYEIDTWYFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHECDRRRPPGREIYR- 606
Cdd:PLN03238 5 AELEREHEETTKVKNIEMIELGKYEMDTWYYSPYPEPYASCTKLYICEYCLKYMRKKKSLLRHLAKCDIRQPPGGGIYGa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 607 --KGNISIYEVNGKEESLYCQLLCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVL 684
Cdd:PLN03238 85 vtEGPLSVFEVDGKKAKVYCQNLCLLAKLFLDHKTLYYDVDPFLFYVMTEVDDHGSHIVGYFSKEKVSAEDYNLACILTL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 685 PPHQRKGFGKLLIAFSYELSRKEGVIGSPEKPLSDLGRLSYRSYWAYTLLELMktRCAPEQITIKELSEMSGITHDDIIY 764
Cdd:PLN03238 165 PPYQRKGYGKFLISFAYELSKREGKVGTPERPLSDLGKVSFRSYWTRVLLEQL--RDVKGDVSIKDLSLATGIRGEDIVS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17530803 765 TLQSMKMIKYWKGQNVICVTSKTIQDHLQLpqfKQPKLTIDTDYLVWSP 813
Cdd:PLN03238 243 TLQSLNLIKYWKGQHVIHVDQRVLDEHWAK---FAHQRVIEVDCLHWQP 288
|
|
| MOZ_SAS |
pfam01853 |
MOZ/SAS family; This region of these proteins has been suggested to be homologous to ... |
599-778 |
1.24e-125 |
|
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: 374.07 E-value: 1.24e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 599 PPGREIYRKGNISIYEVNGKEESLYCQLLCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNV 678
Cdd:pfam01853 1 PPGNEIYRKGNISIFEVDGRKQKLYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTETDETGCHIVGYFSKEKESSDNYNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 679 ACILVLPPHQRKGFGKLLIAFSYELSRKEGVIGSPEKPLSDLGRLSYRSYWAYTLLELMKtRCAPEQITIKELSEMSGIT 758
Cdd:pfam01853 81 ACILTLPPYQRKGYGKLLIEFSYELSKREGKIGGPEKPLSDLGLLSYRSYWSEVILEYLL-KHRKEGISIEDISKATGIT 159
|
170 180
....*....|....*....|
gi 17530803 759 HDDIIYTLQSMKMIKYWKGQ 778
Cdd:pfam01853 160 PEDIISTLQSLNMLKYYKGQ 179
|
|
| SAS2 |
COG5027 |
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics]; |
387-811 |
1.12e-119 |
|
Histone acetyltransferase (MYST family) [Chromatin structure and dynamics];
Pssm-ID: 227360 [Multi-domain] Cd Length: 395 Bit Score: 367.17 E-value: 1.12e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 387 REDGTVHRGQVLQSRTTEnaaAPDEYYVHYVGLNRRLDGWVGRHRIsdnadDLGGITVLPAPPLAPDQpstsremlaqqa 466
Cdd:COG5027 15 EKDGEARKAEILEINTRK---SRIKFYVHYVELNRRLDEWITADLI-----NLGAAISIPKRKKQTEK------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 467 aaaaaASSERQKRAANKDYYLSYCENSRYDYSDRKMTRYQKRRyDEINHVQKSHaeltatqaalekeheSITKIKYIDKL 546
Cdd:COG5027 75 -----GKKEKKPKVSDRMDLDNENVQLEMLYSISNEREIRQLR-FGGSKVQNPH---------------EGARVKNINEI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 547 QFGNYEIDTWYFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHECDRRRPPGREIYRKGNISIYEVNGKEESLYCQL 626
Cdd:COG5027 134 KLGNYEIEPWYFSPYPEEFSDLDIVYICEFCLKYYGSQTSLVRHRKKCSLQHPPGNEIYRDKYISFFEIDGRKQRLYCRN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 627 LCLMAKLFLDHKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSYELSRK 706
Cdd:COG5027 214 LCLLSKLFLDHKTLYYDVDPFLFYVLTERGDTGCHLVGYFSKEKESEQDYNLACILTLPPYQRRGYGKLLIDFSYLLSQK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 707 EGVIGSPEKPLSDLGRLSYRSYWAYTLLE-LMKTRcaPEQITIKELSEMSGITHDDIIYTLQSMKMIKYWKGQNVICVTS 785
Cdd:COG5027 294 EGKVGSPEKPLSDLGLLSYRAYWSEIVAKlLLKMD--KEITDINEISKETGMSTDDVIHTLEALNILREYKGQYIISLNS 371
|
410 420
....*....|....*....|....*.
gi 17530803 786 KTIQDHLQLPQFKQPklTIDTDYLVW 811
Cdd:COG5027 372 DKLHNYLRLWSKKRR--RINPDLLLW 395
|
|
| PLN03239 |
PLN03239 |
histone acetyltransferase; Provisional |
412-813 |
1.36e-98 |
|
histone acetyltransferase; Provisional
Pssm-ID: 178777 [Multi-domain] Cd Length: 351 Bit Score: 310.82 E-value: 1.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 412 YYVHYVGLNRRLDGWVGRHRISDNaddlggITVLPAPPLAPdqpstsremlaqqaaaaaaasserqkraankdyylsyce 491
Cdd:PLN03239 1 YYVHYKDFNRRMDEWISKDKSNEE------ILALPSDHLAT--------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 492 nsrYDYSDRKMTRYQKRRYDEinhvqksHAELTatQAALeKEHESITKIKYIDKLQFGNYEIDTWYFSPFPEEYGKAR-- 569
Cdd:PLN03239 36 ---HTVGEDVVATIAAPELDE-------HEGLD--DAAL-KEHEEVTKVKNVAFLELGPYQMDTWYFSPLPKELFKAGgf 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 570 --TLYVCEYCLKYMRFRSS---YAYHLHECDRRRPPGREIYRKGNISIYEVNGKEESLYCQLLCLMAKLFLDHKVLYFDM 644
Cdd:PLN03239 103 idVLYVCEFSFGFFARKSEllrFQAKELPKERRHPPGNEIYRCGDLAMFEVDGFEERIYCQNLCYIAKLFLDHKTLYFDV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 645 DPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSYELSRKEGVIGSPEKPLSDLGRLS 724
Cdd:PLN03239 183 DPFLFYVLCEVDERGFHPVGYYSKEKYSDVGYNLACILTFPAHQRKGYGRFLIAFSYELSKKEEKVGSPEKPMSDLGQQA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 725 YRSYWAYTLLELMKTRCAPE-QITIKELSEMSGITHDDIIYTLQSMKMIKYWKGQNVICVTSKTIQDHLQLPQFKQPKlt 803
Cdd:PLN03239 263 YIPYWGSTIVDFLLNHSGNDsSLSIMDIAKKTSIMAEDIVFALNQLGILKFINGIYFIAAEKGLLEELAEKHPVKEPR-- 340
|
410
....*....|
gi 17530803 804 IDTDYLVWSP 813
Cdd:PLN03239 341 VDPSKLHWTP 350
|
|
| PTZ00064 |
PTZ00064 |
histone acetyltransferase; Provisional |
398-813 |
5.39e-97 |
|
histone acetyltransferase; Provisional
Pssm-ID: 173359 [Multi-domain] Cd Length: 552 Bit Score: 313.49 E-value: 5.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 398 LQSRTTENAAAPD-EYYVHYVGLNRRLDGWVGRHRISDNADdlggITVLPAPPLAPDQPSTSREMLAQQAAAAAAASSER 476
Cdd:PTZ00064 136 VSSSSNESQIKEDyEFYVHFRGLNRRLDRWVKGKDIKLSFD----VEELNDPNLIERFQKQGIKFISSLSVSNSANKSGN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 477 QKRAANKDyylsycensRYDYSDRKmtryqkrryDEINHVQKSHAELtatqaaleKEHESITKIKYIDKLQFGNYEIDTW 556
Cdd:PTZ00064 212 KSKKRNVG---------VLDISDGE---------DPDEHEGMDHSAI--------LDHEETTRLRTIGRVRIGKFILDTW 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 557 YFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHECDRRRPPGREIYRKGNISIYEVNGKEESLYCQLLCLMAKLFLD 636
Cdd:PTZ00064 266 YFSPLPDEYQNVDTLHFCEYCLDFFCFEDELIRHLSRCQLRHPPGNEIYRKDNISVFEIDGALTRGYAENLCYLAKLFLD 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 637 HKVLYFDMDPFLFYILCETDKEGSHIVGYFSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSYELSRKEGVIGSPEKP 716
Cdd:PTZ00064 346 HKTLQYDVEPFLFYIVTEVDEEGCHIVGYFSKEKVSLLHYNLACILTLPCYQRKGYGKLLVDLSYKLSLKEGKWGHPERP 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17530803 717 LSDLGRLSYRSYWAY----TLLELMKT-----RCAPEQ--------ITIKELSEMSGITHDDIIYTLQSMKMIKYWKGQN 779
Cdd:PTZ00064 426 LSDLGRAIYNNWWAHriseYLLEYFKQnkiceRGGSKQplqvsnywKFIDNVVRSTGIRREDVIRILEENGIMRNIKDQH 505
|
410 420 430
....*....|....*....|....*....|....
gi 17530803 780 VICVTSKTIQDHLQlpQFKQPKLTIDTDYLVWSP 813
Cdd:PTZ00064 506 YIFCNQEFLKGIVK--RSGRPGITLIDKYFNWVP 537
|
|
| CBD_MOF_like |
cd18984 |
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
380-452 |
1.63e-33 |
|
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: 123.05 E-value: 1.63e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17530803 380 DKIYFIRREDGTVHRGQVLQSRTTENAAaPDEYYVHYVGLNRRLDGWVGRHRISDNadDLGGITVLPAPPLAP 452
Cdd:cd18984 1 GSTYYCRRSDDTVHRAEVIQSRTTKQAG-REEYYVHYVGLNRRLDEWVDKSRLSLN--DLGKIVKTPAPPNAE 70
|
|
| zf-MYST |
pfam17772 |
MYST family zinc finger domain; This zinc finger domain is found in the MYST family of histone ... |
540-594 |
5.19e-27 |
|
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: 103.85 E-value: 5.19e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 17530803 540 IKYIDKLQFGNYEIDTWYFSPFPEEYGKARTLYVCEYCLKYMRFRSSYAYHLHEC 594
Cdd:pfam17772 1 VKNIEKIQFGRYEIDTWYFSPYPEEYTNVDKLYVCEFCLKYMKSRKSYKRHRKKC 55
|
|
| CBD_MOF_like |
cd18642 |
chromo barrel domain of Drosophila melanogaster males-absent on the first protein, and similar ... |
379-452 |
7.17e-25 |
|
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: 98.27 E-value: 7.17e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17530803 379 PDKIYFIRREDgTVHRGQVLQSRTTENAaaPDEYYVHYVGLNRRLDGWVGRHRIsdnaDDLGGITVLPAPPLAP 452
Cdd:cd18642 1 IKCRCWVQRND-EEHLAEVLSRRTRKHA--PPEFYVHYVELNRRLDEWITTDRI----DLDLKECELPKKKATK 67
|
|
| CBD |
cd18643 |
chromo barrel domain of MOF acetyltransferase, and similar proteins; This group includes the ... |
381-432 |
9.06e-19 |
|
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: 80.68 E-value: 9.06e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 17530803 381 KIYFIRREDG---TVHRGQVLQSRTTENAAAPDEYYVHYVGLNRRLDGWVGRHRI 432
Cdd:cd18643 1 EKVLVFEPDPkarVLYDAKILSVITGKDGRAPPEYLVHYVGWNRRLDEWVAEDRV 55
|
|
| Tudor-knot |
pfam11717 |
RNA binding activity-knot of a chromodomain; This is a novel knotted tudor domain which is ... |
382-432 |
2.01e-15 |
|
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: 71.08 E-value: 2.01e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 17530803 382 IYFIRREDGTVHRGQVLQSRTTENaaaPDEYYVHYVGLNRRLDGWVGRHRI 432
Cdd:pfam11717 6 KVLVRKRDGEWRLAEILSIRPKKG---KYEYYVHYVGFNKRLDEWVPEDRI 53
|
|
| CHROMO |
smart00298 |
Chromatin organization modifier domain; |
411-439 |
6.99e-04 |
|
Chromatin organization modifier domain;
Pssm-ID: 214605 [Multi-domain] Cd Length: 55 Bit Score: 38.35 E-value: 6.99e-04
10 20
....*....|....*....|....*....
gi 17530803 411 EYYVHYVGLNRRLDGWVGRHRISDNADDL 439
Cdd:smart00298 19 EYLVKWKGYSYSEDTWEPEENLLNCSKKL 47
|
|
| CBD_ESA1_like |
cd18986 |
chromo barrel domain of yeast NuA4 histone acetyltransferase complex catalytic subunit ESA1, ... |
404-448 |
1.88e-03 |
|
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: 37.58 E-value: 1.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 17530803 404 ENAAAPDEYYVHYVGLNRRLDGWVGRHRIsdnadDLGGITVLPAP 448
Cdd:cd18986 22 NTRKAPPKFYVHYEDFNKRLDEWITADRI-----NLSKEVLYPKP 61
|
|
| NAT_SF |
cd04301 |
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ... |
649-709 |
2.15e-03 |
|
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.
Pssm-ID: 173926 [Multi-domain] Cd Length: 65 Bit Score: 37.26 E-value: 2.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17530803 649 FYILCETDKegshIVGY--FSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSYELSRKEGV 709
Cdd:cd04301 1 FLVAEDDGE----IVGFasLSPDGSGGDTAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGA 59
|
|
| Acetyltransf_1 |
pfam00583 |
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ... |
641-709 |
4.97e-03 |
|
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.
Pssm-ID: 395465 [Multi-domain] Cd Length: 116 Bit Score: 37.50 E-value: 4.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17530803 641 YFDMDPFLFYILCETDKegshIVGY--FSKEKKSLENYNVACILVLPPHQRKGFGKLLIAFSYELSRKEGV 709
Cdd:pfam00583 27 WDEDASEGFFVAEEDGE----LVGFasLSIIDDEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERGC 93
|
|
| |
