|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
726-976 |
3.24e-171 |
|
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350820 [Multi-domain] Cd Length: 251 Bit Score: 518.83 E-value: 3.24e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 726 YYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 805
Cdd:cd18062 1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 806 PLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 885
Cdd:cd18062 81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 886 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 965
Cdd:cd18062 161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
|
250
....*....|.
gi 918660106 966 VLRPFLLRRLK 976
Cdd:cd18062 241 VLRPFLLRRLK 251
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
745-1227 |
4.32e-165 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 531.68 E-value: 4.32e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 745 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSV 824
Cdd:PLN03142 166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 825 VKVSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 900
Cdd:PLN03142 246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 901 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 980
Cdd:PLN03142 322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 981 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQHIEE----SFS 1055
Cdd:PLN03142 392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPgppyTTG 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1056 EHLgftggivqgldlYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLK 1135
Cdd:PLN03142 464 EHL------------VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASID 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1136 TFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKY 1215
Cdd:PLN03142 532 AFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYK 611
|
490
....*....|..
gi 918660106 1216 KLNVDQKVIQAG 1227
Cdd:PLN03142 612 KLALDALVIQQG 623
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
691-1211 |
7.62e-125 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 408.84 E-value: 7.62e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 691 DDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALmvNGVLKQYQIKGLEWLVSLYNNNLNG 770
Cdd:COG0553 186 LLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGL--KATLRPYQLEGAAWLLFLRRLGLGG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 771 ILADEMGLGKTIQTIALITYLMEHKRInGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPqlrSGKFNV 850
Cdd:COG0553 264 LLADDMGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANP---FEDADL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 851 LLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNthyvAPRRLLLTGTPLQNKLPELWALLNFLLPTI 927
Cdd:COG0553 340 VITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAvraLK----ARHRLALTGTPVENRLEELWSLLDFLNPGL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 928 FKSCSTFEQWFNAPfamtGEKVDLNEEEtiliirRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMq 1007
Cdd:COG0553 416 LGSLKAFRERFARP----IEKGDEEALE------RLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1008 akgVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHlgftggivqgldlyraSGKFELLDRILPKL 1087
Cdd:COG0553 485 ---LEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR----------------SAKLEALLELLEEL 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1088 RATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEpGSEYFIFLLSTRAGGLGLNLQSADTVI 1167
Cdd:COG0553 546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVI 624
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 918660106 1168 IFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1211
Cdd:COG0553 625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
752-1047 |
3.19e-116 |
|
SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.
Pssm-ID: 425504 [Multi-domain] Cd Length: 289 Bit Score: 369.32 E-value: 3.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 752 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLME-HKRINGPFLIIVPLSTLSNWAYEFDKWA--PSVVKV 827
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 828 SYKGSPAAR-RAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLTG 906
Cdd:pfam00176 81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 907 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetiLIIRRLHKVLRPFLLRRLKKEVEAQLPEK 986
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918660106 987 VEYVIKCDMSALQRVLY-RHMQAKGVLLTDGSEkdkKGKGGTKTLMNTIMQLRKICNHPYMF 1047
Cdd:pfam00176 231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
|
|
| Bromo_SNF2L2 |
cd05516 |
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ... |
1456-1562 |
4.14e-64 |
|
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99947 Cd Length: 107 Bit Score: 212.67 E-value: 4.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1456 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1535
Cdd:cd05516 2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
|
90 100
....*....|....*....|....*..
gi 918660106 1536 TFNLEGSLIYEDSIVLQSVFTSVRQKI 1562
Cdd:cd05516 81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1074-1200 |
1.83e-57 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 195.00 E-value: 1.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1074 SGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPgSEYFIFLLSTRA 1153
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 918660106 1154 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1200
Cdd:cd18793 89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| BROMO |
smart00297 |
bromo domain; |
1454-1562 |
2.55e-33 |
|
bromo domain;
Pssm-ID: 197636 [Multi-domain] Cd Length: 107 Bit Score: 124.70 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1454 PNLTKKMKKIVDAVIKYKDSssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQN 1533
Cdd:smart00297 2 PKLQKKLQELLKAVLDKLDS---HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
|
90 100
....*....|....*....|....*....
gi 918660106 1534 AQTFNLEGSLIYEDSIVLQSVFTSVRQKI 1562
Cdd:smart00297 79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
749-937 |
1.02e-32 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 126.84 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEHKriNGPFLIIVPLSTL-SNWAYEFDKWAPS-VV 825
Cdd:smart00487 9 LRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 826 KVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKD--KHILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYVAPRR 901
Cdd:smart00487 84 KVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQL 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 918660106 902 LLLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 937
Cdd:smart00487 164 LLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1075-1189 |
2.13e-28 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 110.76 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1075 GKFELLDRILPKLRatNHKVLLFCQMTSlmTIMEDYFAYR-GFKYLRLDGTTKAEDRGMLLKTFNEpgSEYFIfLLSTRA 1153
Cdd:pfam00271 1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRK--GKIDV-LVATDV 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 918660106 1154 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIG 1189
Cdd:pfam00271 74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SnAC |
pfam14619 |
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ... |
1317-1384 |
1.02e-23 |
|
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.
Pssm-ID: 464219 [Multi-domain] Cd Length: 69 Bit Score: 96.17 E-value: 1.02e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 918660106 1317 DRRREEARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWL 1384
Cdd:pfam14619 1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1106-1189 |
4.96e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 91.50 E-value: 4.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1106 IMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSeyfIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRA 1185
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI---KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78
|
....
gi 918660106 1186 HRIG 1189
Cdd:smart00490 79 GRAG 82
|
|
| Bromodomain |
pfam00439 |
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ... |
1460-1548 |
2.89e-20 |
|
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 425683 [Multi-domain] Cd Length: 84 Bit Score: 86.60 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1460 MKKIVDAVIKykdsssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNL 1539
Cdd:pfam00439 1 CLEILDKLME-------HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73
|
....*....
gi 918660106 1540 EGSLIYEDS 1548
Cdd:pfam00439 74 PGSVIYKAA 82
|
|
| COG5076 |
COG5076 |
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ... |
1431-1564 |
3.02e-18 |
|
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];
Pssm-ID: 227408 [Multi-domain] Cd Length: 371 Bit Score: 88.71 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1431 KDDESKKQKKRGRPPAEKLSPNPPN--LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKI 1508
Cdd:COG5076 116 SGLGSLLMAHLKTSVKKRKTPKIEDelLYADNKAIAKFKKQLFLRD-GRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTI 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 918660106 1509 KERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEK 1564
Cdd:COG5076 195 QKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPE 250
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
97-504 |
1.61e-13 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 76.52 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 97 ATLGSLRSYNMATPSLTAPSITPPQLGPPSLQQFFPQATRQSLLGPPPVGVPMNPSQLNLSGRNPQKQTRTHSSTTPnrk 176
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP--- 2766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 177 dsSSQTMPVEDGADPQegseeaeePRMDTPEDGDLAPCPDGILSekrTPTPEPEPCEVTEPLAKRSRSSElPTEKGPPGP 256
Cdd:PHA03247 2767 --PAPAPPAAPAAGPP--------RRLTRPAVASLSESRESLPS---PWDPADPPAAVLAPAAALPPAAS-PAGPLPPPT 2832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 257 SQVKVPPPaRMTVPKQTQTPERLPELPGARVLPRFQPRvlqiQAQVQPQTlPQMPPVDT----QVPLKLQKQAQTQTSPE 332
Cdd:PHA03247 2833 SAQPTAPP-PPPGPPPPSLPLGGSVAPGGDVRRRPPSR----SPAAKPAA-PARPPVRRlarpAVSRSTESFALPPDQPE 2906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 333 HLVPPQKETELQKQVPGQGQPRgqtwEQPSEQPSAQVAVQSAEQTRGQPEPQPQGLVPTPE-------RAPVPTDATVLG 405
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQ----PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlgalvpgRVAVPRFRVPQP 2982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 406 TPPNVTAEAGGGMEEALPEPvgaqvRVAASQESPASGLHPGECEKRAREMLGMWGAGGSLKVTILQSSDSRAFNTTPLTP 485
Cdd:PHA03247 2983 APSREAPASSTPPLTGHSLS-----RVSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDP 3057
|
410
....*....|....*....
gi 918660106 486 VPRPSDSSPATPAAASTPS 504
Cdd:PHA03247 3058 LPPEPHDPFAHEPDPATPE 3076
|
|
| PP1c_bdg |
pfam10488 |
Phosphatase-1 catalytic subunit binding region; This conserved C-terminus appears to be a ... |
1732-1803 |
4.95e-12 |
|
Phosphatase-1 catalytic subunit binding region; This conserved C-terminus appears to be a protein phosphatase-1 catalytic subunit (PP1C) binding region, which may in some circumstances also be retroviral in origin since it is found in both herpes simplex virus and in mouse and man. This domain is found in Gadd-34 apoptosis-associated proteins as well as the constitutive repressor of eIF2-alpha phosphorylation/protein phosphatase 1, regulatory (inhibitor) subunit 15b, otherwise known as CReP. Diverse stressful conditions are associated with phosphorylation of the {alpha} subunit of eukaryotic translation initiation factor 2 (eIF2{alpha}) on serine 51. This signaling event, which is conserved from yeast to mammals, negatively regulates the guanine nucleotide exchange factor, eIF2-B and inhibits the recycling of eIF2 to its active GTP bound form. In mammalian cells eIF2{alpha} phosphorylation emerges as an important event in stress signaling that impacts on gene expression at both the translational and transcriptional levels.
Pssm-ID: 431311 Cd Length: 287 Bit Score: 68.89 E-value: 4.95e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918660106 1732 KVSPKDRKVRFSEKVTVHLLAvwagpAQAARRGPWEQFARDRSRFARRIAQAQEELGPCLTPAWRARAWARL 1803
Cdd:pfam10488 221 HTSPKRKKVTFLEEVTEYYIS-----GDEDRKGPWEEFARDGCRFQKRIQETEDAIGYCLTFEHREKMFNRL 287
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
110-415 |
4.42e-09 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 61.71 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 110 PSLTAPSITPPQLGPPSlqqffPQATRQSLLGPPPvGVPMNPSQLNLSGRNPQKQTRT--------HSSTTPNRKDSSSQ 181
Cdd:pfam03154 172 PVLQAQSGAASPPSPPP-----PGTTQAATAGPTP-SAPSVPPQGSPATSQPPNQTQStaaphtliQQTPTLHPQRLPSP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 182 TMPVEDGADPQEGSEEAEEPRMDTPEDGDLAPCPDGiLSEKRTPTPEPEPcevTEPLAKRSRSSELPTEKGP----PGPS 257
Cdd:pfam03154 246 HPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHS-LQTGPSHMQHPVP---PQPFPLTPQSSQSQVPPGPspaaPGQS 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 258 QVKVPPPARMTVPKQTQTPERLPELPGARVLPRFQPrvlqiqaqvQPQT-LPQMP-PVDTQVPLKLQKQAQTQTsPEHLV 335
Cdd:pfam03154 322 QQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKP---------PPTTpIPQLPnPQSHKHPPHLSGPSPFQM-NSNLP 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 336 PPQKETELQK----------QVPGQGQPRGQTWEQPSEQPSAQVAVQSAEQTRGQpEPQPQGLVPTPERAPVPTDATVLG 405
Cdd:pfam03154 392 PPPALKPLSSlsthhppsahPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAAS-HPPTSGLHQVPSQSPFPQHPFVPG 470
|
330
....*....|
gi 918660106 406 TPPNVTAEAG 415
Cdd:pfam03154 471 GPPPITPPSG 480
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
690-908 |
2.07e-07 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 55.80 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 690 SDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNG--------VLKQYQIKGLE-WL 760
Cdd:COG1061 14 LRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGdeasgtsfELRPYQQEALEaLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 761 VSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRIngpfLIIVPLSTLSN-WAYEFDKWAPSVVKVSYKgspaarraf 839
Cdd:COG1061 94 AALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGDPLAGGGK--------- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 918660106 840 vpqlRSGKFNVLLTTYEYIIKDKHiLAKI--RWKYMIVDEGHrmknhHC---KLTQVLNtHYVAPRRLLLTGTP 908
Cdd:COG1061 161 ----KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEAH-----HAgapSYRRILE-AFPAAYRLGLTATP 223
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
190-445 |
1.17e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 50.15 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 190 DPQEGSEEAEEPRMDTPEDGDLAPCPDGILSEKRTPTPEPEP----------CEVTEPLAKRSRSSELPTEKGPPGPSQV 259
Cdd:NF033839 216 DIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIentvhkifadMDAVVTKFKKGLTQDTPKEPGNKKPSAP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 260 KV-------PPPARMTVPKQTQTPERLPELPGARVLPRFQPRvlQIQAQVQPQTLPQMPPVDTQvplklqkqaqtQTSPE 332
Cdd:NF033839 296 KPgmqpspqPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPE--KPKPEVKPQLETPKPEVKPQ-----------PEKPK 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 333 HLVPPQKETELQKQVPGQGQPRGQTWEQPsEQPSAQVAVQSaEQTRGQPEPQPQGlvPTPERAPVPTDATvlgtpPNVTA 412
Cdd:NF033839 363 PEVKPQPEKPKPEVKPQPETPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKPQPEK--PKPEVKPQPEKPK-----PEVKP 433
|
250 260 270
....*....|....*....|....*....|...
gi 918660106 413 EAGGGMEEALPEPVGAQVRVAASQESPASGLHP 445
Cdd:NF033839 434 QPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKP 466
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
192-425 |
2.73e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 49.00 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 192 QEGSEEAEEPRMDTPEDGdLAPCPDgilSEKRTPTPEPEPcevtePLAKRSRSSELPTEKGPPGPSQVKVPPPARMTVPK 271
Cdd:NF033839 281 QDTPKEPGNKKPSAPKPG-MQPSPQ---PEKKEVKPEPET-----PKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPK 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 272 QTQTPErlPELPGarvlPRFQPRVLQIQAQVQPQTLPQMPPVDTQVplklqkqaqtqTSPEHLVPPQKETELQKQVPGQG 351
Cdd:NF033839 352 PEVKPQ--PEKPK----PEVKPQPEKPKPEVKPQPETPKPEVKPQP-----------EKPKPEVKPQPEKPKPEVKPQPE 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918660106 352 QPRGQTWEQPsEQPSAQVAVQsAEQTRGQPEPQPQGlvPTPERAPVPtdatvlGTP-PNVTAEAGGGMEEALPEP 425
Cdd:NF033839 415 KPKPEVKPQP-EKPKPEVKPQ-PEKPKPEVKPQPEK--PKPEVKPQP------ETPkPEVKPQPEKPKPEVKPQP 479
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
184-428 |
3.12e-05 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 48.91 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 184 PVEDGADPQEGSEEAEEPRMDTPEDGDLapcpdgilsEKRTPTPEPEPCEVTEPLAKRSRSSELPTEKGPPGPSQVKVPP 263
Cdd:COG5180 166 PDGDSASTLPPPAEKLDKVLTEPRDALK---------DSPEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAASSPKVDP 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 264 PARMTVPKQTQTPERLPELPGARVLPRFQPRVLQIQAQVQPQTLPQMPPVDTQVPLKLQKQAQTQTSPEHLVPPQKETEL 343
Cdd:COG5180 237 PSTSEARSRPATVDAQPEMRPPADAKERRRAAIGDTPAAEPPGLPVLEAGSEPQSDAPEAETARPIDVKGVASAPPATRP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 344 QKQVPGQGQPRGQTWEQPSEQPSAQVAVQSAEQTRGQPEPQPQGLVPT---PERAPVPTDATVLG---TPPNVTAEAGGG 417
Cdd:COG5180 317 VRPPGGARDPGTPRPGQPTERPAGVPEAASDAGQPPSAYPPAEEAVPGkplEQGAPRPGSSGGDGapfQPPNGAPQPGLG 396
|
250
....*....|.
gi 918660106 418 MEEALPEPVGA 428
Cdd:COG5180 397 RRGAPGPPMGA 407
|
|
| zf-C2H2_jaz |
pfam12171 |
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ... |
603-627 |
8.70e-05 |
|
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.
Pssm-ID: 432381 [Multi-domain] Cd Length: 27 Bit Score: 41.00 E-value: 8.70e-05
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
176-413 |
1.33e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 43.60 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 176 KDSSSQTMPVEDG----ADPQEGSEEAEEPRMDTPEDGDLAPCPDgILSEKRTPTPEPEPcevtEPLAKRSrssELPTEK 251
Cdd:NF033839 276 KKGLTQDTPKEPGnkkpSAPKPGMQPSPQPEKKEVKPEPETPKPE-VKPQLEKPKPEVKP----QPEKPKP---EVKPQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 252 GPPGPSQVKVPPPARMTVPKQTQTPErlPELPG--ARVLPRFQPRVLQIQAQVQPQTLPQMPPVDTQVPLKLQKQAQTQT 329
Cdd:NF033839 348 ETPKPEVKPQPEKPKPEVKPQPEKPK--PEVKPqpETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 330 SPEHLVPPQKETELQKQVPGQGQPRGQTWEQPsEQPSAQVAVQSAEQtrgQPEPQPQGLVPTPERAPVPTDATVLGTPPN 409
Cdd:NF033839 426 KPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQP-ETPKPEVKPQPEKP---KPEVKPQPEKPKPDNSKPQADDKKPSTPNN 501
|
....
gi 918660106 410 VTAE 413
Cdd:NF033839 502 LSKD 505
|
|
| SP2_N |
cd22540 |
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ... |
292-440 |
2.07e-03 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.
Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 42.99 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 292 QPRVLQIQAQVQPQTLPQMPPVDTQvPLKLQkQAQTQTSPehlVPPQKETELQKQVPGQGQPRGQTWEQPSEQPSAqVAV 371
Cdd:cd22540 282 QPAVLQQVQVLQPKQEQQVVQIPQQ-ALRVV-QAASATLP---TVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQT-VLL 355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918660106 372 QSAeqtrGQPEPQPQGLVPTPERAPVPTDATVLGTPPNVTAEagggmEEALPE--PVGAQVRVAASQESPA 440
Cdd:cd22540 356 QEA----PAATATPSSSTSTVQQQVTANNGTGTSKPNYNVRK-----ERTLPKiaPAGGIISLNAAQLAAA 417
|
|
| ZnF_U1 |
smart00451 |
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ... |
510-538 |
4.60e-03 |
|
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.
Pssm-ID: 197732 [Multi-domain] Cd Length: 35 Bit Score: 36.46 E-value: 4.60e-03
10 20
....*....|....*....|....*....
gi 918660106 510 FFCYVCKTSCSSQQEFQDHMSEAQHLQRL 538
Cdd:smart00451 4 FYCKLCNVTFTDEISVEAHLKGKKHKKNV 32
|
|
| UFD2 |
COG5112 |
U1-like Zn-finger-containing protein [General function prediction only]; |
583-634 |
5.30e-03 |
|
U1-like Zn-finger-containing protein [General function prediction only];
Pssm-ID: 227443 Cd Length: 126 Bit Score: 38.91 E-value: 5.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 583 DLIQHRRTQDHKVAKQSLRP--------FCTICSRYFKTPRKFVEHVKSQGHKDKAKELK 634
Cdd:COG5112 29 DQIKNDLSTKESQKKLPYDPelpglgqhYCIECARYFITEKALMEHKKGKVHKRRAKELR 88
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
726-976 |
3.24e-171 |
|
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (SMARCA4, also known as transcription activator BRG1) is a component of the CREST-BRG1 complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. Mutation of SMARCA4 (BRG1), the ATPase of BAF (mSWI/SNF) and PBAF complexes, contributes to a range of malignancies and neurologic disorders. SMARCA4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350820 [Multi-domain] Cd Length: 251 Bit Score: 518.83 E-value: 3.24e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 726 YYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 805
Cdd:cd18062 1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 806 PLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 885
Cdd:cd18062 81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 886 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 965
Cdd:cd18062 161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
|
250
....*....|.
gi 918660106 966 VLRPFLLRRLK 976
Cdd:cd18062 241 VLRPFLLRRLK 251
|
|
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
746-976 |
5.74e-169 |
|
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, members 2 and 4 (SMARCA2 and SMARCA4) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350754 [Multi-domain] Cd Length: 233 Bit Score: 511.91 E-value: 5.74e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 746 NGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVV 825
Cdd:cd17996 1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 826 KVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLT 905
Cdd:cd17996 81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 918660106 906 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKV--DLNEEETILIIRRLHKVLRPFLLRRLK 976
Cdd:cd17996 161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
745-1227 |
4.32e-165 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 531.68 E-value: 4.32e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 745 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSV 824
Cdd:PLN03142 166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 825 VKVSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 900
Cdd:PLN03142 246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 901 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 980
Cdd:PLN03142 322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 981 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQHIEE----SFS 1055
Cdd:PLN03142 392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPgppyTTG 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1056 EHLgftggivqgldlYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLK 1135
Cdd:PLN03142 464 EHL------------VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASID 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1136 TFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKY 1215
Cdd:PLN03142 532 AFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYK 611
|
490
....*....|..
gi 918660106 1216 KLNVDQKVIQAG 1227
Cdd:PLN03142 612 KLALDALVIQQG 623
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
726-976 |
3.20e-163 |
|
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (SMARCA2, also known as brahma homolog) is a component of the BAF complex. SMARCA2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350821 [Multi-domain] Cd Length: 251 Bit Score: 497.28 E-value: 3.20e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 726 YYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 805
Cdd:cd18063 1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 806 PLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 885
Cdd:cd18063 81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 886 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 965
Cdd:cd18063 161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240
|
250
....*....|.
gi 918660106 966 VLRPFLLRRLK 976
Cdd:cd18063 241 VLRPFLLRRLK 251
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
691-1211 |
7.62e-125 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 408.84 E-value: 7.62e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 691 DDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALmvNGVLKQYQIKGLEWLVSLYNNNLNG 770
Cdd:COG0553 186 LLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGL--KATLRPYQLEGAAWLLFLRRLGLGG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 771 ILADEMGLGKTIQTIALITYLMEHKRInGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPqlrSGKFNV 850
Cdd:COG0553 264 LLADDMGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANP---FEDADL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 851 LLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNthyvAPRRLLLTGTPLQNKLPELWALLNFLLPTI 927
Cdd:COG0553 340 VITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAvraLK----ARHRLALTGTPVENRLEELWSLLDFLNPGL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 928 FKSCSTFEQWFNAPfamtGEKVDLNEEEtiliirRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMq 1007
Cdd:COG0553 416 LGSLKAFRERFARP----IEKGDEEALE------RLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV- 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1008 akgVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHlgftggivqgldlyraSGKFELLDRILPKL 1087
Cdd:COG0553 485 ---LEYLRRELEGAEGIRRRGLILAALTRLRQICSHPALLLEEGAELSGR----------------SAKLEALLELLEEL 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1088 RATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEpGSEYFIFLLSTRAGGLGLNLQSADTVI 1167
Cdd:COG0553 546 LAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVI 624
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 918660106 1168 IFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILA 1211
Cdd:COG0553 625 HYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
752-1047 |
3.19e-116 |
|
SNF2-related domain; This domain is found in proteins involved in a variety of processes including transcription regulation (e.g., SNF2, STH1, brahma, MOT1), DNA repair (e.g., ERCC6, RAD16, RAD5), DNA recombination (e.g., RAD54), and chromatin unwinding (e.g., ISWI) as well as a variety of other proteins with little functional information (e.g., lodestar, ETL1). SNF2 functions as the ATPase component of the SNF2/SWI multisubunit complex, which utilizes energy derived from ATP hydrolysis to disrupt histone-DNA interactions, resulting in the increased accessibility of DNA to transcription factors.
Pssm-ID: 425504 [Multi-domain] Cd Length: 289 Bit Score: 369.32 E-value: 3.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 752 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLME-HKRINGPFLIIVPLSTLSNWAYEFDKWA--PSVVKV 827
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 828 SYKGSPAAR-RAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLTG 906
Cdd:pfam00176 81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 907 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetiLIIRRLHKVLRPFLLRRLKKEVEAQLPEK 986
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918660106 987 VEYVIKCDMSALQRVLY-RHMQAKGVLLTDGSEkdkKGKGGTKTLMNTIMQLRKICNHPYMF 1047
Cdd:pfam00176 231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
746-976 |
2.46e-94 |
|
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350755 [Multi-domain] Cd Length: 222 Bit Score: 304.24 E-value: 2.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 746 NGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVV 825
Cdd:cd17997 1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 826 KVSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvaprR 901
Cdd:cd17997 81 VVVLIGDKEERADIIrDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVrlfNSRN----R 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918660106 902 LLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNApfamtgEKVDLNEEEtilIIRRLHKVLRPFLLRRLK 976
Cdd:cd17997 157 LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNV------NNCDDDNQE---VVQRLHKVLRPFLLRRIK 222
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
746-976 |
5.32e-92 |
|
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or SMARCA6) is a major epigenetic regulator crucial for normal heterochromatin structure and function. HELLS is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350767 [Multi-domain] Cd Length: 236 Bit Score: 298.15 E-value: 5.32e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 746 NGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKrINGPFLIIVPLSTLSNWAYEFDKWAPSVV 825
Cdd:cd18009 1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERG-VWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 826 KVSYKGSPAARRAFVPQLRS-----GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPR 900
Cdd:cd18009 80 VLLYHGTKEERERLRKKIMKregtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELK-TFNSDN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 918660106 901 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN--APFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLK 976
Cdd:cd18009 159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
749-974 |
1.55e-83 |
|
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or DOMO1) is the core catalytic component of the multiprotein chromatin-remodeling SRCAP complex, that is necessary for the incorporation of the histone variant H2A.Z into nucleosomes. SRCAP is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350761 [Multi-domain] Cd Length: 223 Bit Score: 273.46 E-value: 1.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARRAfvpqLRSG-----KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLL 903
Cdd:cd18003 81 YYGSAKERKL----KRQGwmkpnSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918660106 904 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF-AMTGEKVDLNEEetilIIRRLHKVLRPFLLRR 974
Cdd:cd18003 156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLtAMSEGSQEENEE----LVRRLHKVLRPFLLRR 223
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
749-925 |
3.07e-81 |
|
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350677 [Multi-domain] Cd Length: 182 Bit Score: 264.81 E-value: 3.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYvAPRRLLLTGTP 908
Cdd:cd17919 81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR-AKRRLLLTGTP 159
|
170
....*....|....*..
gi 918660106 909 LQNKLPELWALLNFLLP 925
Cdd:cd17919 160 LQNNLEELWALLDFLDP 176
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
749-974 |
6.49e-81 |
|
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and similar proteins; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as the substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but is also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. Both are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350751 [Multi-domain] Cd Length: 218 Bit Score: 265.76 E-value: 6.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd17993 2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARRA------FVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRL 902
Cdd:cd17993 82 YLGDIKSRDTireyefYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-FKTNNRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918660106 903 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgekVDLNEEETILiIRRLHKVLRPFLLRR 974
Cdd:cd17993 161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-------------EEHDEEQEKG-IADLHKELEPFILRR 218
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
749-974 |
1.07e-76 |
|
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; Chromodomain-helicase-DNA-binding protein 6-9 (CHD6, CHD7, CHD8, and CHD9) are members of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350753 [Multi-domain] Cd Length: 223 Bit Score: 253.71 E-value: 1.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVkVS 828
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDMNV-VV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARR------AFVPQL------RSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 896
Cdd:cd17995 80 YHGSGESRQiiqqyeMYFKDAqgrkkkGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK-KL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 918660106 897 VAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 974
Cdd:cd17995 159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG----------DLKTAEQ---VEKLQALLKPYMLRR 223
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
747-986 |
6.21e-73 |
|
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5 (SMARCA5, also called SNF2H) is the catalytic subunit of the four known chromatin-remodeling complexes: CHRAC, RSF, ACF/WCRF, and WICH. SMARCA5 plays a major role organising arrays of nucleosomes adjacent to the binding sites for the architectural transcription factor CTCF sites and acts to promote CTCF binding SMARCA5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350822 [Multi-domain] Cd Length: 244 Bit Score: 243.80 E-value: 6.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 747 GVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVK 826
Cdd:cd18064 14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 827 VSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLT 905
Cdd:cd18064 94 VCLIGDKDQRAAFVRDvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR-EFKTTNRLLLT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 906 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRRLKKEVEAQLPE 985
Cdd:cd18064 173 GTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQK----------LVERLHMVLRPFLLRRIKADVEKSLPP 242
|
.
gi 918660106 986 K 986
Cdd:cd18064 243 K 243
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
736-976 |
2.42e-72 |
|
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 (SMARCA1, also called SNF2L) is a component of NURF (nucleosome-remodeling factor) and CERF (CECR2-containing-remodeling factor) complexes which promote the perturbation of chromatin structure in an ATP-dependent manner. SMARCA1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350823 [Multi-domain] Cd Length: 233 Bit Score: 241.85 E-value: 2.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 736 RVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAY 815
Cdd:cd18065 3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 816 EFDKWAPSVVKVSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 894
Cdd:cd18065 83 EFKRWVPSLRAVCLIGDKDARAAFIrDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 895 HYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRR 974
Cdd:cd18065 162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRR 231
|
..
gi 918660106 975 LK 976
Cdd:cd18065 232 IK 233
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
749-974 |
2.92e-67 |
|
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350760 [Multi-domain] Cd Length: 229 Bit Score: 227.00 E-value: 2.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAAR---RAFVPQ----LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRR 901
Cdd:cd18002 81 YWGNPKDRkvlRKFWDRknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL-LSFHCRNR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 918660106 902 LLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGE-KVDLNEEEtiliIRRLHKVLRPFLLRR 974
Cdd:cd18002 160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAEnKTGLNEHQ----LKRLHMILKPFMLRR 229
|
|
| Bromo_SNF2L2 |
cd05516 |
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ... |
1456-1562 |
4.14e-64 |
|
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99947 Cd Length: 107 Bit Score: 212.67 E-value: 4.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1456 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1535
Cdd:cd05516 2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
|
90 100
....*....|....*....|....*..
gi 918660106 1536 TFNLEGSLIYEDSIVLQSVFTSVRQKI 1562
Cdd:cd05516 81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
749-974 |
4.28e-63 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; Chromodomain-helicase-DNA-binding protein 2 (CHD2) is a DNA-binding helicase that specifically binds to the promoter of target genes, leading to chromatin remodeling, possibly by promoting deposition of histone H3.3. It is involved in myogenesis via interaction with MYOD1; it binds to myogenic gene regulatory sequences and mediates incorporation of histone H3.3 prior to the onset of myogenic gene expression, promoting their expression. CHD2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350812 [Multi-domain] Cd Length: 237 Bit Score: 215.25 E-value: 4.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd18054 21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARRAFV------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRL 902
Cdd:cd18054 101 YIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918660106 903 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLRPFLLRR 974
Cdd:cd18054 180 LITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE-------DHGKGRENGYQS-------LHKVLEPFLLRR 237
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
745-976 |
5.86e-63 |
|
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350770 [Multi-domain] Cd Length: 218 Bit Score: 213.97 E-value: 5.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 745 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYlMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSV 824
Cdd:cd18012 1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLS-RKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 825 VKVSYKGSPAARRAfvpQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHYvaprR 901
Cdd:cd18012 80 KVLVIHGTKRKREK---LRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAvkaLKADH----R 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918660106 902 LLLTGTPLQNKLPELWALLNFLLPTIFKScstfEQWFNAPFAMTGEKvDLNEEEtiliIRRLHKVLRPFLLRRLK 976
Cdd:cd18012 153 LALTGTPIENHLGELWSIFDFLNPGLLGS----YKRFKKRFAKPIEK-DGDEEA----LEELKKLISPFILRRLK 218
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
749-974 |
1.89e-60 |
|
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, also known as ALC1) is involved in DNA repair by regulating chromatin relaxation following DNA damage. CHD1L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350764 [Multi-domain] Cd Length: 216 Bit Score: 206.90 E-value: 1.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARRAFVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVaPRRLLLTGT 907
Cdd:cd18006 81 YMGDKEKRLDLQQDIKStNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV-DFRLLLTGT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 918660106 908 PLQNKLPELWALLNFLLPTIFkSCSTFEQWFNApFAMTGEKVDLNEEetiliirrLHKVLRPFLLRR 974
Cdd:cd18006 160 PIQNSLQELYALLSFIEPNVF-PKDKLDDFIKA-YSETDDESETVEE--------LHLLLQPFLLRR 216
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
749-974 |
2.13e-58 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD3, CHD4, and CHD5 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350752 [Multi-domain] Cd Length: 196 Bit Score: 199.97 E-value: 2.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSpaarrafvpqlrsgkfNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRLLLTGTP 908
Cdd:cd17994 81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIG-YKLLLTGTP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 918660106 909 LQNKLPELWALLNFLLPTIFKSCSTFeqwfnapfamTGEKVDLNEEETiliIRRLHKVLRPFLLRR 974
Cdd:cd17994 144 LQNNLEELFHLLNFLTPERFNNLQGF----------LEEFADISKEDQ---IKKLHDLLGPHMLRR 196
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1074-1200 |
1.83e-57 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 195.00 E-value: 1.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1074 SGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPgSEYFIFLLSTRA 1153
Cdd:cd18793 10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 918660106 1154 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1200
Cdd:cd18793 89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
749-928 |
3.40e-54 |
|
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350756 [Multi-domain] Cd Length: 187 Bit Score: 187.59 E-value: 3.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARRafvpQLR------SGKFNVLLTTYEYII---KDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAP 899
Cdd:cd17998 80 YYGSQEERK----HLRydilkgLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INAN 154
|
170 180
....*....|....*....|....*....
gi 918660106 900 RRLLLTGTPLQNKLPELWALLNFLLPTIF 928
Cdd:cd17998 155 FRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
749-974 |
2.86e-51 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350811 [Multi-domain] Cd Length: 237 Bit Score: 181.40 E-value: 2.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd18053 21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARRAFV------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRL 902
Cdd:cd18053 101 YLGDINSRNMIRthewmhPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918660106 903 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLRPFLLRR 974
Cdd:cd18053 180 LITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE-------EHGKGREYGYAS-------LHKELEPFLLRR 237
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
749-974 |
7.49e-50 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350816 [Multi-domain] Cd Length: 222 Bit Score: 176.77 E-value: 7.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT--YLMEhkrINGPFLIIVPLSTLSNWAYEFDKWAPSVVK 826
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSeiFLMG---IRGPFLIIAPLSTITNWEREFRTWTEMNAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 827 VsYKGSPAARRAFV------------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNT 894
Cdd:cd18058 78 V-YHGSQISRQMIQqyemyyrdeqgnPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 895 HYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 974
Cdd:cd18058 157 MALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG----------DLKTEEQ---VKKLQSILKPMMLRR 222
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
749-974 |
7.90e-50 |
|
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in eukaryotes) regulates transcription in association with TATA binding protein (TBP). Mot1, Ino80C, and NC2 function coordinately to regulate pervasive transcription in yeast and mammals. Mot1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350757 [Multi-domain] Cd Length: 232 Bit Score: 177.16 E-value: 7.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKR------INGPFLIIVPLSTLSNWAYEFDKWAP 822
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 823 SVVK--VSYKGSPAARRAFVPQLrsGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPR 900
Cdd:cd17999 80 NAFLkpLAYVGPPQERRRLREQG--EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV-KQLKANH 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 918660106 901 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVD--LNEEETILIIRRLHKVLRPFLLRR 974
Cdd:cd17999 157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKAsaKEQEAGALALEALHKQVLPFLLRR 232
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
749-974 |
9.74e-50 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; Chromodomain-helicase-DNA-binding protein 3 (CHD3) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. It is required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity. CHD3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350813 [Multi-domain] Cd Length: 232 Bit Score: 176.74 E-value: 9.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAAR-------------------RAFVPQLRSG-KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 888
Cdd:cd18055 81 YTGDKDSRaiirenefsfddnavkggkKAFKMKREAQvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 889 TQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 968
Cdd:cd18055 161 FRVLNG-YKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226
|
....*.
gi 918660106 969 PFLLRR 974
Cdd:cd18055 227 PHMLRR 232
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
749-925 |
1.76e-49 |
|
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350758 [Multi-domain] Cd Length: 193 Bit Score: 174.43 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAP------ 822
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPpfrvvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 823 ------SVVKVSYKGSPAARRAFVPQLRsGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LN 893
Cdd:cd18000 81 lhssgsGTGSEEKLGSIERKSQLIRKVV-GDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAckqLR 159
|
170 180 190
....*....|....*....|....*....|..
gi 918660106 894 ThyvaPRRLLLTGTPLQNKLPELWALLNFLLP 925
Cdd:cd18000 160 T----PHRLILSGTPIQNNLKELWSLFDFVFP 187
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
749-974 |
6.85e-49 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; Chromodomain-helicase-DNA-binding protein 5 (CHD5) is a chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. It is thought to specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 and plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. As a tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. CHD5 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350815 [Multi-domain] Cd Length: 232 Bit Score: 174.48 E-value: 6.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARRAFVPQ--------LRSG------------KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 888
Cdd:cd18057 81 YTGDKESRSVIRENefsfednaIRSGkkvfrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 889 TQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 968
Cdd:cd18057 161 FRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226
|
....*.
gi 918660106 969 PFLLRR 974
Cdd:cd18057 227 PHMLRR 232
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
749-974 |
5.35e-48 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350818 [Multi-domain] Cd Length: 222 Bit Score: 171.39 E-value: 5.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYlMEHKRINGPFLIIVPLSTLSNWAYEFDKWApSVVKVS 828
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQE-VYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARRA--------------FVPQlrSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 894
Cdd:cd18060 79 YHGSLASRQMiqqyemyckdsrgrLIPG--AYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 895 HYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 974
Cdd:cd18060 156 HMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
749-974 |
1.50e-47 |
|
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as RAD26L) may play a role in DNA repair and mitochondrial function. In humans, mutations in the ERCC6L2 gene are associated with bone marrow failure syndrome 2. ERCC6L2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350763 [Multi-domain] Cd Length: 245 Bit Score: 171.02 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT-----------------YLMEHKRIN---GPFLIIVPLS 808
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrrdrennrpRFKKKPPASsakKPVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 809 TLSNWAYEFDKWAPSVVKVsYKGSpaaRRAFVPQLR--SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHC 886
Cdd:cd18005 81 VLYNWKDELDTWGHFEVGV-YHGS---RKDDELEGRlkAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 887 KLTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF----AMTGEKVDLNEEETilIIRR 962
Cdd:cd18005 157 KLTQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgqRHTATARELRLGRK--RKQE 233
|
250
....*....|..
gi 918660106 963 LHKVLRPFLLRR 974
Cdd:cd18005 234 LAVKLSKFFLRR 245
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
749-974 |
1.66e-47 |
|
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350759 [Multi-domain] Cd Length: 232 Bit Score: 170.24 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPfLIIVPLSTLSNWAYEFDKWAPSV-VKV 827
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLrVKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 828 SYKGSPAARRAfvpQLRS--GKFNVLLTTYEYIIKDKHILA-----KIRWKYMIVDEGHRMKNHHCKLTQVLntHYV-AP 899
Cdd:cd18001 80 FHGTSKKERER---NLERiqRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSL--REIpAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 918660106 900 RRLLLTGTPLQNKLPELWALLNFLLP-TIFKSCSTFEQWFNAPFAMTGEKVDLNEEETI--LIIRRLHKVLRPFLLRR 974
Cdd:cd18001 155 NRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKALgsEVAENLRQIIKPYFLRR 232
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
749-974 |
2.83e-47 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; Chromodomain-helicase-DNA-binding protein 7 (CHD7) is a probable transcription regulator. It may be involved in the 45S precursor rRNA production. CHD7 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350817 [Multi-domain] Cd Length: 222 Bit Score: 169.44 E-value: 2.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVkVS 828
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNV-VV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAARRAFV--------PQLR----SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHY 896
Cdd:cd18059 79 YHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 918660106 897 VApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 974
Cdd:cd18059 159 LE-HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
749-974 |
1.77e-46 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; Chromodomain-helicase-DNA-binding protein 4 (CHD4) is a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones. CHD4 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350814 [Multi-domain] Cd Length: 232 Bit Score: 167.55 E-value: 1.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 828
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 829 YKGSPAArRAFVPQ---------LRSG------------KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCK 887
Cdd:cd18056 81 YVGDKDS-RAIIREnefsfednaIRGGkkasrmkkeasvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 888 LTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVL 967
Cdd:cd18056 160 FFRVLNG-YSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF----------ADIAKEDQ---IKKLHDML 225
|
....*..
gi 918660106 968 RPFLLRR 974
Cdd:cd18056 226 GPHMLRR 232
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
749-974 |
3.54e-44 |
|
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350762 [Multi-domain] Cd Length: 240 Bit Score: 160.91 E-value: 3.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVS--LYNNNLNG---ILADEMGLGKTIQTIALITYLMEHKRINGP----FLIIVPLSTLSNWAYEFDK 819
Cdd:cd18004 1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 820 WAPSVVK--VSYKGSPAARRAFVPQLRSGK-FNVLLTTYE-YIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTh 895
Cdd:cd18004 81 WLGLRRIkvVTADGNAKDVKASLDFFSSAStYPVLIISYEtLRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALNS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 896 YVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvDLNEEETILIIRRLH---KVLRPFLL 972
Cdd:cd18004 160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDP-DASEEDKELGAERSQelsELTSRFIL 238
|
..
gi 918660106 973 RR 974
Cdd:cd18004 239 RR 240
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
749-974 |
3.78e-43 |
|
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; Chromodomain-helicase-DNA-binding protein 9 (CHD9) acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. It is proposed to be a ATP-dependent chromatin remodeling protein. CHD9 has DNA-dependent ATPase activity and binds to A/T-rich DNA. It also associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis. CHD9 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350819 [Multi-domain] Cd Length: 222 Bit Score: 157.47 E-value: 3.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTialITYLMEHKR--INGPFLIIVPLSTLSNWAYEFDKWAPSVVk 826
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQS---ITFLYEILLtgIRGPFLIIAPLSTIANWEREFRTWTDLNV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 827 VSYKGSPAARRAFV--------PQLR----SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNT 894
Cdd:cd18061 77 VVYHGSLISRQMIQqyemyfrdSQGRiirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 895 HYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 974
Cdd:cd18061 157 MNLE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
749-974 |
3.30e-41 |
|
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350766 [Multi-domain] Cd Length: 241 Bit Score: 152.44 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLynnnlNGILADEMGLGKTIQTIALI-------TYLMEHKRINGPF----------LIIVPLSTLS 811
Cdd:cd18008 1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdPKIPEELEENSSDpkklylskttLIVVPLSLLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 812 NWAYEFDK-WAPSVVKVS-YKGSPAARRAFVPQlrsgKFNVLLTTY-----EY-----------IIKDKHILAKIRWKYM 873
Cdd:cd18008 76 QWKDEIEKhTKPGSLKVYvYHGSKRIKSIEELS----DYDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIRWYRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 874 IVDEGHRMKNHHCKLTQV---LNTHyvapRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvd 950
Cdd:cd18008 152 ILDEAHNIKNRSTKTSRAvcaLKAE----RRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK-- 225
|
250 260
....*....|....*....|....
gi 918660106 951 lneeetilIIRRLHKVLRPFLLRR 974
Cdd:cd18008 226 --------ALERLQALLKPILLRR 241
|
|
| DEXHc_ATRX-like |
cd18007 |
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ... |
749-962 |
1.64e-37 |
|
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350765 [Multi-domain] Cd Length: 239 Bit Score: 141.66 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLE--W--LVSLYNNNLNG---ILADEMGLGKTIQTIALI-TYLMEHKRINGPfLIIVPLSTLSNWAYEFDKW 820
Cdd:cd18007 1 LKPHQVEGVRflWsnLVGTDVGSDEGggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 821 APSVVkVSYKGSPAARRAFVPQLRSGKFN-------VLLTTYEY---IIKDKHILAKIRWKYM-----------IVDEGH 879
Cdd:cd18007 80 LPPDL-RPLLVLVSLSASKRADARLRKINkwhkeggVLLIGYELfrnLASNATTDPRLKQEFIaalldpgpdllVLDEGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 880 RMKNHHCKLTQVLNTHYvAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGEKVDLNEEETILI 959
Cdd:cd18007 159 RLKNEKSQLSKALSKVK-TKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIE-AGQCVDSTEEDVRLM 236
|
...
gi 918660106 960 IRR 962
Cdd:cd18007 237 LKR 239
|
|
| BROMO |
smart00297 |
bromo domain; |
1454-1562 |
2.55e-33 |
|
bromo domain;
Pssm-ID: 197636 [Multi-domain] Cd Length: 107 Bit Score: 124.70 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1454 PNLTKKMKKIVDAVIKYKDSssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQN 1533
Cdd:smart00297 2 PKLQKKLQELLKAVLDKLDS---HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
|
90 100
....*....|....*....|....*....
gi 918660106 1534 AQTFNLEGSLIYEDSIVLQSVFTSVRQKI 1562
Cdd:smart00297 79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
749-937 |
1.02e-32 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 126.84 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEHKriNGPFLIIVPLSTL-SNWAYEFDKWAPS-VV 825
Cdd:smart00487 9 LRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 826 KVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKD--KHILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYVAPRR 901
Cdd:smart00487 84 KVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQL 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 918660106 902 LLLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 937
Cdd:smart00487 164 LLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
|
|
| Bromo_polybromo_V |
cd05515 |
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ... |
1456-1560 |
2.13e-31 |
|
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.
Pssm-ID: 99946 Cd Length: 105 Bit Score: 119.33 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1456 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1535
Cdd:cd05515 1 MQQKLWELYNAVKNYTDGR-GRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNAC 79
|
90 100
....*....|....*....|....*
gi 918660106 1536 TFNLEGSLIYEDSIVLQSVFTSVRQ 1560
Cdd:cd05515 80 KYNEPDSQIYKDALTLQKVLLETKR 104
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
749-974 |
6.57e-31 |
|
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350829 [Multi-domain] Cd Length: 239 Bit Score: 122.96 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNL-----------------------------NGILADEMGLGKTIQTIALItylmehkrING 799
Cdd:cd18071 1 LLPHQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLI--------LAN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 800 PFLIIVPLSTLSNWAYEF-DKWAPSVVKV-SYKGspAARRAFVPQLrsGKFNVLLTTY-----EYIIKDKHILAKIRWKY 872
Cdd:cd18071 73 FTLIVCPLSVLSNWETQFeEHVKPGQLKVyTYHG--GERNRDPKLL--SKYDIVLTTYntlasDFGAKGDSPLHTINWLR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 873 MIVDEGHRMKNHHCKLTQ-VLNTHyvAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVDL 951
Cdd:cd18071 149 VVLDEGHQIRNPNAQQTKaVLNLS--SERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTM-GDPTGL 225
|
250 260
....*....|....*....|...
gi 918660106 952 neeetiliiRRLHKVLRPFLLRR 974
Cdd:cd18071 226 ---------KRLQVLMKQITLRR 239
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
749-974 |
9.19e-30 |
|
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350824 [Multi-domain] Cd Length: 235 Bit Score: 119.18 E-value: 9.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSL-----YNNNLNGILADEMGLGKTIQTIALITYLMEH-----KRINGPFLIIVPLSTLSNWAYEFD 818
Cdd:cd18066 1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRQgpyggKPVIKRALIVTPGSLVKNWKKEFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 819 KWAPSV-VKVSYKGSPAARRAFVpqlRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYV 897
Cdd:cd18066 81 KWLGSErIKVFTVDQDHKVEEFI---ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL-TSLS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 918660106 898 APRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIR--RLHKVLRPFLLRR 974
Cdd:cd18066 157 CERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARaaELTRLTGLFILRR 235
|
|
| Bromodomain |
cd04369 |
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ... |
1456-1555 |
3.96e-29 |
|
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.
Pssm-ID: 99922 [Multi-domain] Cd Length: 99 Bit Score: 112.47 E-value: 3.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1456 LTKKMKKIVDAVIKYKdsssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1535
Cdd:cd04369 1 LKKKLRSLLDALKKLK-----RDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAK 75
|
90 100
....*....|....*....|
gi 918660106 1536 TFNLEGSLIYEDSIVLQSVF 1555
Cdd:cd04369 76 TYNGPGSPIYKDAKKLEKLF 95
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1075-1189 |
2.13e-28 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 110.76 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1075 GKFELLDRILPKLRatNHKVLLFCQMTSlmTIMEDYFAYR-GFKYLRLDGTTKAEDRGMLLKTFNEpgSEYFIfLLSTRA 1153
Cdd:pfam00271 1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRK--GKIDV-LVATDV 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 918660106 1154 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIG 1189
Cdd:pfam00271 74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| Bromo_SNF2 |
cd05519 |
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ... |
1456-1558 |
4.67e-28 |
|
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99950 Cd Length: 103 Bit Score: 109.74 E-value: 4.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1456 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1535
Cdd:cd05519 1 LKAAMLEIYDAVLNCEDET-GRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANAR 79
|
90 100
....*....|....*....|...
gi 918660106 1536 TFNLEGSLIYEDSIVLQSVFTSV 1558
Cdd:cd05519 80 TYNQEGSIVYEDAVEMEKAFKKK 102
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
749-962 |
6.43e-28 |
|
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350768 [Multi-domain] Cd Length: 213 Bit Score: 113.07 E-value: 6.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSlynNNLNGILADEMGLGKTIQTIALITYLmehkRINGPFLIIVPLSTLSNWAYEFDKWAPSV---- 824
Cdd:cd18010 1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYY----REEWPLLIVCPSSLRLTWADEIERWLPSLppdd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 825 VKVSYKGSPAARRafvpqlRSGKFNVllTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHyvAPRR 901
Cdd:cd18010 74 IQVIVKSKDGLRD------GDAKVVI--VSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAalpLLKR--AKRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 902 LLLTGTPLQNKLPELWALLNFLLPTIFKSCSTF-EQWFNA----PFAMTGEKVDLNEEETILI----IRR 962
Cdd:cd18010 144 ILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgRRYCAAkqggFGWDYSGSSNLEELHLLLLatimIRR 213
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
749-974 |
7.58e-28 |
|
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350825 [Multi-domain] Cd Length: 243 Bit Score: 114.10 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWL----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRINGPFL----IIVPLSTLSNWAYEFDK 819
Cdd:cd18067 1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 820 W-----APSVV--KVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL 892
Cdd:cd18067 81 WlggrlQPLAIdgGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 893 NThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLHK---VLRP 969
Cdd:cd18067 161 DS-LNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPI-LKGRDADASEKERQLGEEKLQElisIVNR 238
|
....*
gi 918660106 970 FLLRR 974
Cdd:cd18067 239 CIIRR 243
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
749-962 |
1.49e-25 |
|
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350827 [Multi-domain] Cd Length: 227 Bit Score: 106.82 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEHKRINgPFLIIVPLSTLSNWAYE 816
Cdd:cd18069 1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAK-TVLAIVPVNTLQNWLSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 817 FDKWAPSVV----------KVSYKGSPAARRAFVPQLRS---GKFNVLLTTYE-YIIKDKHILakirwkyMIVDEGHRMK 882
Cdd:cd18069 77 FNKWLPPPEalpnvrprpfKVFILNDEHKTTAARAKVIEdwvKDGGVLLMGYEmFRLRPGPDV-------VICDEGHRIK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 883 NHHCKLTQVLNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRR 962
Cdd:cd18069 150 NCHASTSQALK-NIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCVDSTPQDVKLMRYR 227
|
|
| Bromo_polybromo_IV |
cd05518 |
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ... |
1458-1554 |
1.59e-25 |
|
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.
Pssm-ID: 99949 [Multi-domain] Cd Length: 103 Bit Score: 102.52 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1458 KKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTF 1537
Cdd:cd05518 3 KRMLALFLYVLEYREGS-GRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHY 81
|
90
....*....|....*..
gi 918660106 1538 NLEGSLIYEDSIVLQSV 1554
Cdd:cd05518 82 NEEGSQVYEDANILEKV 98
|
|
| Bromo_polybromo_II |
cd05517 |
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ... |
1463-1556 |
7.80e-24 |
|
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.
Pssm-ID: 99948 Cd Length: 103 Bit Score: 97.51 E-value: 7.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1463 IVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGS 1542
Cdd:cd05517 8 LLEAVMTATDPS-GRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGS 86
|
90
....*....|....
gi 918660106 1543 LIYEDSIVLQSVFT 1556
Cdd:cd05517 87 QVYKDANAIKKIFT 100
|
|
| SnAC |
pfam14619 |
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ... |
1317-1384 |
1.02e-23 |
|
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.
Pssm-ID: 464219 [Multi-domain] Cd Length: 69 Bit Score: 96.17 E-value: 1.02e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 918660106 1317 DRRREEARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWL 1384
Cdd:pfam14619 1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
|
|
| Bromo_polybromo_I |
cd05524 |
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ... |
1463-1562 |
2.34e-22 |
|
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.
Pssm-ID: 99954 [Multi-domain] Cd Length: 113 Bit Score: 93.94 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1463 IVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGS 1542
Cdd:cd05524 10 LYDTIRNYKSED-GRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDS 88
|
90 100
....*....|....*....|
gi 918660106 1543 LIYEDSIVLQSVFTSVRQKI 1562
Cdd:cd05524 89 PEHKDACKLWELFLSARNEV 108
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1106-1189 |
4.96e-22 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 91.50 E-value: 4.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1106 IMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSeyfIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRA 1185
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI---KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78
|
....
gi 918660106 1186 HRIG 1189
Cdd:smart00490 79 GRAG 82
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
749-974 |
6.09e-22 |
|
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350830 [Multi-domain] Cd Length: 241 Bit Score: 96.78 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSLYNNNLNG-ILADEMGLGKTIQTIALI------------------TYLMEHKRIN----GPFLIIV 805
Cdd:cd18072 1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALIlaqkntqnrkeeekekalTEWESKKDSTlvpsAGTLVVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 806 PLSTLSNWAYEFD-KWAPSVVKV-SYKGSPAARRAFVpqLRSgkFNVLLTTYEYIIKD---------KHILAKIRWKYMI 874
Cdd:cd18072 81 PASLVHQWKNEVEsRVASNKLRVcLYHGPNRERIGEV--LRD--YDIVITTYSLVAKEiptykeesrSSPLFRIAWARII 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 875 VDEGHRMKNHH-------CKltqvLNTHYvaprRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGE 947
Cdd:cd18072 157 LDEAHNIKNPKvqasiavCK----LRAHA----RWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGE 228
|
250 260
....*....|....*....|....*..
gi 918660106 948 kvdlneeetiliirRLHKVLRPFLLRR 974
Cdd:cd18072 229 --------------RLNILTKSLLLRR 241
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
770-962 |
1.81e-21 |
|
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350826 [Multi-domain] Cd Length: 246 Bit Score: 95.73 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 770 GILADEMGLGKTIQTIALITYLMEHKRING--PFLIIVPLSTLSNWAYEFDKWA-----PSVVKV----SYKGSPaaRRA 838
Cdd:cd18068 31 CILAHCMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEFEKWQeglkdEEKIEVnelaTYKRPQ--ERS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 839 FVPQLRSGKFNVLLTTYE-YII----KDKHILAKIRWKYM-----------IVDEGHRMKNHHCKLTQVLNThYVAPRRL 902
Cdd:cd18068 109 YKLQRWQEEGGVMIIGYDmYRIlaqeRNVKSREKLKEIFNkalvdpgpdfvVCDEGHILKNEASAVSKAMNS-IRTKRRI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 903 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGEKVDLNEEETILIIRR 962
Cdd:cd18068 188 VLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQ-NGQCADSTLVDVRVMKKR 246
|
|
| Bromo_polybromo_III |
cd05520 |
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ... |
1475-1554 |
2.74e-21 |
|
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.
Pssm-ID: 99951 Cd Length: 103 Bit Score: 90.48 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1475 SGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSV 1554
Cdd:cd05520 19 QGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKLQKL 98
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
771-928 |
2.96e-21 |
|
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350769 [Multi-domain] Cd Length: 207 Bit Score: 93.89 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 771 ILADEMGLGKTIQTIALITYLM---EHKRIngpfLIIVPLSTLSNWAYEF--DKWAPSVVKVSYKGSPAARRAFVPQLRs 845
Cdd:cd18011 21 LLADEVGLGKTIEAGLIIKELLlrgDAKRV----LILCPASLVEQWQDELqdKFGLPFLILDRETAAQLRRLIGNPFEE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 846 gkFNVLLTTYEYI---IKDKHILAKIRWKYMIVDEGHRMKNHHC-------KLTQVLNTHyvAPRRLLLTGTPLQNKLPE 915
Cdd:cd18011 96 --FPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKR--ARHVLLLTATPHNGKEED 171
|
170
....*....|...
gi 918660106 916 LWALLNFLLPTIF 928
Cdd:cd18011 172 FRALLSLLDPGRF 184
|
|
| Bromodomain |
pfam00439 |
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ... |
1460-1548 |
2.89e-20 |
|
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 425683 [Multi-domain] Cd Length: 84 Bit Score: 86.60 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1460 MKKIVDAVIKykdsssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNL 1539
Cdd:pfam00439 1 CLEILDKLME-------HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73
|
....*....
gi 918660106 1540 EGSLIYEDS 1548
Cdd:pfam00439 74 PGSVIYKAA 82
|
|
| COG5076 |
COG5076 |
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ... |
1431-1564 |
3.02e-18 |
|
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];
Pssm-ID: 227408 [Multi-domain] Cd Length: 371 Bit Score: 88.71 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1431 KDDESKKQKKRGRPPAEKLSPNPPN--LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKI 1508
Cdd:COG5076 116 SGLGSLLMAHLKTSVKKRKTPKIEDelLYADNKAIAKFKKQLFLRD-GRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTI 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 918660106 1509 KERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEK 1564
Cdd:COG5076 195 QKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPE 250
|
|
| Bromo_Rsc1_2_I |
cd05521 |
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ... |
1456-1553 |
2.23e-17 |
|
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99952 Cd Length: 106 Bit Score: 79.29 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1456 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNhkYRSLNDLEKDVMLLCQNAQ 1535
Cdd:cd05521 2 LSKKLKPLYDGIYTLKEEN-GIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLPH--YTNAQEFVNDLAQIPWNAR 78
|
90
....*....|....*...
gi 918660106 1536 TFNLEGSLIYEDSIVLQS 1553
Cdd:cd05521 79 LYNTKGSVIYKYALILEK 96
|
|
| Bromo_Rsc1_2_II |
cd05522 |
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ... |
1459-1558 |
7.58e-17 |
|
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99953 [Multi-domain] Cd Length: 104 Bit Score: 77.67 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1459 KMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1538
Cdd:cd05522 5 RIKNILKGLRKERDEN-GRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYN 83
|
90 100
....*....|....*....|
gi 918660106 1539 LEGSLIYEDSIVLQSVFTSV 1558
Cdd:cd05522 84 ENDSQEYKDAVLLEKEARLL 103
|
|
| Bromo_gcn5_like |
cd05509 |
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ... |
1459-1564 |
1.87e-14 |
|
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99941 [Multi-domain] Cd Length: 101 Bit Score: 70.66 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1459 KMKKIVDAVIKYKDSSSgrqlsevFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1538
Cdd:cd05509 5 QLKKVLDSLKNHKSAWP-------FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77
|
90 100
....*....|....*....|....*.
gi 918660106 1539 LEGSLIYEDSIVLQSVFtsvRQKIEK 1564
Cdd:cd05509 78 GPDTEYYKCANKLEKFF---WKKLKE 100
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
749-923 |
5.20e-14 |
|
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350828 [Multi-domain] Cd Length: 257 Bit Score: 73.92 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVslynnNLNGILADEMGLGKTIQTIALItylMEHKRIN----------------------------GP 800
Cdd:cd18070 1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLALI---LLHPRPDndldaadddsdemvccpdclvaetpvssKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 801 FLIIVPLSTLSNWAYEFDKWAPSVVKVS-YKGspaARRAFVPQLRSGKF----NVLLTTYEYIIKDKHI----------- 864
Cdd:cd18070 73 TLIVCPSAILAQWLDEINRHVPSSLKVLtYQG---VKKDGALASPAPEIlaeyDIVVTTYDVLRTELHYaeanrsnrrrr 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918660106 865 -----------LAKIRWKYMIVDEghrMKNHHCKLTQVLNTHYVAPR--RLLLTGTPLQNKLPELWALLNFL 923
Cdd:cd18070 150 rqkryeappspLVLVEWWRVCLDE---AQMVESSTSKAAEMARRLPRvnRWCVSGTPIQRGLDDLFGLLSFL 218
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
97-504 |
1.61e-13 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 76.52 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 97 ATLGSLRSYNMATPSLTAPSITPPQLGPPSLQQFFPQATRQSLLGPPPVGVPMNPSQLNLSGRNPQKQTRTHSSTTPnrk 176
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP--- 2766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 177 dsSSQTMPVEDGADPQegseeaeePRMDTPEDGDLAPCPDGILSekrTPTPEPEPCEVTEPLAKRSRSSElPTEKGPPGP 256
Cdd:PHA03247 2767 --PAPAPPAAPAAGPP--------RRLTRPAVASLSESRESLPS---PWDPADPPAAVLAPAAALPPAAS-PAGPLPPPT 2832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 257 SQVKVPPPaRMTVPKQTQTPERLPELPGARVLPRFQPRvlqiQAQVQPQTlPQMPPVDT----QVPLKLQKQAQTQTSPE 332
Cdd:PHA03247 2833 SAQPTAPP-PPPGPPPPSLPLGGSVAPGGDVRRRPPSR----SPAAKPAA-PARPPVRRlarpAVSRSTESFALPPDQPE 2906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 333 HLVPPQKETELQKQVPGQGQPRgqtwEQPSEQPSAQVAVQSAEQTRGQPEPQPQGLVPTPE-------RAPVPTDATVLG 405
Cdd:PHA03247 2907 RPPQPQAPPPPQPQPQPPPPPQ----PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlgalvpgRVAVPRFRVPQP 2982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 406 TPPNVTAEAGGGMEEALPEPvgaqvRVAASQESPASGLHPGECEKRAREMLGMWGAGGSLKVTILQSSDSRAFNTTPLTP 485
Cdd:PHA03247 2983 APSREAPASSTPPLTGHSLS-----RVSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDP 3057
|
410
....*....|....*....
gi 918660106 486 VPRPSDSSPATPAAASTPS 504
Cdd:PHA03247 3058 LPPEPHDPFAHEPDPATPE 3076
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
749-939 |
2.06e-13 |
|
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprise a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. The bacterial SNF2 present in this family are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350771 [Multi-domain] Cd Length: 218 Bit Score: 71.23 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLEWLVSlynNNLNGILADeMGLGKTIQTIALITYLMEHKRInGPFLIIVPLSTLSN-WAYEFDKW-APSVVK 826
Cdd:cd18013 1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQLDDFT-RRVLVIAPLRVARStWPDEVEKWnHLRNLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 827 VSYK-GSPAARRAfvpqLRSGKFNVLLTTYEyIIKDKHILAKIRWKY--MIVDEGHRMKNHHCKLTQVLNTH-YVAPRRL 902
Cdd:cd18013 76 VSVAvGTERQRSK----AANTPADLYVINRE-NLKWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKALRKVrPVIKRLI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 918660106 903 LLTGTPLQNKLPELWALLNFL--LPTIFKSCSTF-EQWFN 939
Cdd:cd18013 151 GLTGTPSPNGLMDLWAQIALLdqGERLGRSITAYrERWFD 190
|
|
| Bromo_Acf1_like |
cd05504 |
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ... |
1463-1555 |
2.34e-13 |
|
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was identified as a novel human bromodomain gene by cDNA library screening. The Drosophila homologue, Acf1, is part of the CHRAC (chromatin accessibility complex) and regulates ISWI-induced nucleosome remodeling. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99936 Cd Length: 115 Bit Score: 68.19 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1463 IVDAVIKYKDSSSgrqlsevFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGS 1542
Cdd:cd05504 20 LLVEIVKHKDSWP-------FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHT 92
|
90
....*....|...
gi 918660106 1543 LIYEDSIVLQSVF 1555
Cdd:cd05504 93 SVYKAGTRLQRFF 105
|
|
| PP1c_bdg |
pfam10488 |
Phosphatase-1 catalytic subunit binding region; This conserved C-terminus appears to be a ... |
1732-1803 |
4.95e-12 |
|
Phosphatase-1 catalytic subunit binding region; This conserved C-terminus appears to be a protein phosphatase-1 catalytic subunit (PP1C) binding region, which may in some circumstances also be retroviral in origin since it is found in both herpes simplex virus and in mouse and man. This domain is found in Gadd-34 apoptosis-associated proteins as well as the constitutive repressor of eIF2-alpha phosphorylation/protein phosphatase 1, regulatory (inhibitor) subunit 15b, otherwise known as CReP. Diverse stressful conditions are associated with phosphorylation of the {alpha} subunit of eukaryotic translation initiation factor 2 (eIF2{alpha}) on serine 51. This signaling event, which is conserved from yeast to mammals, negatively regulates the guanine nucleotide exchange factor, eIF2-B and inhibits the recycling of eIF2 to its active GTP bound form. In mammalian cells eIF2{alpha} phosphorylation emerges as an important event in stress signaling that impacts on gene expression at both the translational and transcriptional levels.
Pssm-ID: 431311 Cd Length: 287 Bit Score: 68.89 E-value: 4.95e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918660106 1732 KVSPKDRKVRFSEKVTVHLLAvwagpAQAARRGPWEQFARDRSRFARRIAQAQEELGPCLTPAWRARAWARL 1803
Cdd:pfam10488 221 HTSPKRKKVTFLEEVTEYYIS-----GDEDRKGPWEEFARDGCRFQKRIQETEDAIGYCLTFEHREKMFNRL 287
|
|
| Bromo_ASH1 |
cd05525 |
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ... |
1456-1560 |
5.11e-12 |
|
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99955 [Multi-domain] Cd Length: 106 Bit Score: 63.95 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1456 LTKKMKKIVDAVIKYKDSSSGrQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1535
Cdd:cd05525 3 LAQVLKEICDAIITYKDSNGQ-SLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAE 81
|
90 100
....*....|....*....|....*
gi 918660106 1536 TFNLEGSLIYEDSIVLQSVFTSVRQ 1560
Cdd:cd05525 82 KYYGRKSPIGRDVCRLRKAYYQAKH 106
|
|
| Bromo_BDF1_2_II |
cd05499 |
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ... |
1487-1555 |
2.76e-11 |
|
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99931 Cd Length: 102 Bit Score: 61.92 E-value: 2.76e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 918660106 1487 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1555
Cdd:cd05499 30 PVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVF 98
|
|
| Bromo_AAA |
cd05528 |
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ... |
1491-1538 |
3.36e-11 |
|
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver
Pssm-ID: 99957 Cd Length: 112 Bit Score: 61.99 E-value: 3.36e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 918660106 1491 ELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1538
Cdd:cd05528 32 EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
|
|
| Bromo_WDR9_I_like |
cd05529 |
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ... |
1454-1557 |
7.93e-10 |
|
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99958 Cd Length: 128 Bit Score: 58.50 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1454 PNLTKKMKKIVDavikykdsSSGRQLSEVFIQ-LPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQ 1532
Cdd:cd05529 27 ERLISGLDKLLL--------SLQLEIAEYFEYpVDLRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILS 98
|
90 100
....*....|....*....|....*
gi 918660106 1533 NAQTFNLEGSLIYEDSIVLQSVFTS 1557
Cdd:cd05529 99 NAETFNEPNSEIAKKAKRLSDWLLR 123
|
|
| Bromo_Brdt_II_like |
cd05498 |
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ... |
1487-1556 |
1.41e-09 |
|
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99930 Cd Length: 102 Bit Score: 56.90 E-value: 1.41e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1487 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFT 1556
Cdd:cd05498 30 PEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFE 99
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
108-502 |
1.74e-09 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 63.16 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 108 ATPSLTAPSIT---PP------QLGPPSLQQFF--------PQATRQSLLGPPPVGVPMNPSQLNLSGRNPQKQTRTHSS 170
Cdd:PHA03378 443 ATPHSQAPTVVlhrPPtqplegPTGPLSVQAPLepwqplphPQVTPVILHQPPAQGVQAHGSMLDLLEKDDEDMEQRVMA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 171 T----TPNR------------------KDSSSQTMPVEDGADPQEGSEEAEEPRMDTPEDGDLAP-CPdgilSEKRTPTP 227
Cdd:PHA03378 523 TllppSPPQpragrrapcvytedldieSDEPASTEPVHDQLLPAPGLGPLQIQPLTSPTTSQLASsAP----SYAQTPWP 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 228 EPEPCEVTEPLAKRSRSSELPTEKGPPGPSQVKVPPPARMTV--------PKQTQTPERLPEL----------------- 282
Cdd:PHA03378 599 VPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPitfnvlvfPTPHQPPQVEITPykptwtqighipyqpsp 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 283 --PGARVLPRFQPRVLQIQAQV-QPQTLPQMPPVDTQVPLKLQKQAQ-TQTSPEHLVPPQKetelqkqVPGQGQPRGQTW 358
Cdd:PHA03378 679 tgANTMLPIQWAPGTMQPPPRApTPMRPPAAPPGRAQRPAAATGRARpPAAAPGRARPPAA-------APGRARPPAAAP 751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 359 EQPSEQPSAQVAVQSAEQTRGQPEPQPQGLVP-----TPERAPVPTdatvlgTPPnvtaeagggmeEALPEPVGAQVRVA 433
Cdd:PHA03378 752 GRARPPAAAPGRARPPAAAPGAPTPQPPPQAPpapqqRPRGAPTPQ------PPP-----------QAGPTSMQLMPRAA 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 434 ASQESPASGLHPGECE---KRAREMLGMWGAGGSLKVTILQSS----------DSRAFNTTPLTPVPRPSDSSPATPAAA 500
Cdd:PHA03378 815 PGQQGPTKQILRQLLTggvKRGRPSLKKPAALERQAAAGPTPSpgsgtsdkivQAPVFYPPVLQPIQVMRQLGSVRAAAA 894
|
..
gi 918660106 501 ST 502
Cdd:PHA03378 895 ST 896
|
|
| Bromo_BAZ2A_B_like |
cd05503 |
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ... |
1490-1557 |
2.92e-09 |
|
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99935 Cd Length: 97 Bit Score: 55.84 E-value: 2.92e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 918660106 1490 KELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTS 1557
Cdd:cd05503 28 KLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFFEK 95
|
|
| Bromo_brd7_like |
cd05513 |
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ... |
1493-1545 |
4.36e-09 |
|
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown to inhibit cell growth and the progression of the cell cycle by regulating cell-cycle genes at the transcriptional level. BRD7 has been identified as a gene involved in nasopharyngeal carcinoma. The protein interacts with acetylated histone H3 via its bromodomain. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99945 Cd Length: 98 Bit Score: 55.49 E-value: 4.36e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 918660106 1493 PEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIY 1545
Cdd:cd05513 32 PGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNKPDTIYY 84
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
748-908 |
4.41e-09 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 57.30 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 748 VLKQYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINgPFLIIVP-LSTLSNWAYEFDKWAPSVV 825
Cdd:pfam04851 3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK-KVLFLVPrKDLLEQALEEFKKFLPNYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 826 KVSYKGSPaarRAFVPQLRSGKfnVLLTTYEYIIKD----KHILAKIRWKYMIVDEGHRM--KNHhcklTQVLNtHYVAP 899
Cdd:pfam04851 82 EIGEIISG---DKKDESVDDNK--IVVTTIQSLYKAlelaSLELLPDFFDVIIIDEAHRSgaSSY----RNILE-YFKPA 151
|
....*....
gi 918660106 900 RRLLLTGTP 908
Cdd:pfam04851 152 FLLGLTATP 160
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
110-415 |
4.42e-09 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 61.71 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 110 PSLTAPSITPPQLGPPSlqqffPQATRQSLLGPPPvGVPMNPSQLNLSGRNPQKQTRT--------HSSTTPNRKDSSSQ 181
Cdd:pfam03154 172 PVLQAQSGAASPPSPPP-----PGTTQAATAGPTP-SAPSVPPQGSPATSQPPNQTQStaaphtliQQTPTLHPQRLPSP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 182 TMPVEDGADPQEGSEEAEEPRMDTPEDGDLAPCPDGiLSEKRTPTPEPEPcevTEPLAKRSRSSELPTEKGP----PGPS 257
Cdd:pfam03154 246 HPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHS-LQTGPSHMQHPVP---PQPFPLTPQSSQSQVPPGPspaaPGQS 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 258 QVKVPPPARMTVPKQTQTPERLPELPGARVLPRFQPrvlqiqaqvQPQT-LPQMP-PVDTQVPLKLQKQAQTQTsPEHLV 335
Cdd:pfam03154 322 QQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKP---------PPTTpIPQLPnPQSHKHPPHLSGPSPFQM-NSNLP 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 336 PPQKETELQK----------QVPGQGQPRGQTWEQPSEQPSAQVAVQSAEQTRGQpEPQPQGLVPTPERAPVPTDATVLG 405
Cdd:pfam03154 392 PPPALKPLSSlsthhppsahPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPPPAAS-HPPTSGLHQVPSQSPFPQHPFVPG 470
|
330
....*....|
gi 918660106 406 TPPNVTAEAG 415
Cdd:pfam03154 471 GPPPITPPSG 480
|
|
| Bromo_brd1_like |
cd05512 |
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ... |
1456-1552 |
6.81e-09 |
|
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein assumed to be a transcriptional regulator. BRD1 has been implicated with brain development and susceptibility to schizophrenia and bipolar affective disorder. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99944 Cd Length: 98 Bit Score: 54.71 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1456 LTKKMKKIVDAViKYKDSSsgrqlsEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1535
Cdd:cd05512 2 LEVLLRKTLDQL-QEKDTA------EIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCL 74
|
90
....*....|....*..
gi 918660106 1536 TFNLEGSLIYEDSIVLQ 1552
Cdd:cd05512 75 AYNAKDTIFYRAAVRLR 91
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
749-908 |
1.61e-08 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 55.39 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 749 LKQYQIKGLE-WLvsLYNNNLNGILADEMGLGKTIQTIALITYLMEHKringpFLIIVP-LSTLSNWAYEFDKWAPSVVk 826
Cdd:cd17926 1 LRPYQEEALEaWL--AHKNNRRGILVLPTGSGKTLTALALIAYLKELR-----TLIVVPtDALLDQWKERFEDFLGDSS- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 827 vsykgspaarrafVPQLRSGK------FNVLLTTYEYIIKDKHILAKI--RWKYMIVDEGHrmknHHC--KLTQVLnTHY 896
Cdd:cd17926 73 -------------IGLIGGGKkkdfddANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAH----HLPakTFSEIL-KEL 134
|
170
....*....|..
gi 918660106 897 VAPRRLLLTGTP 908
Cdd:cd17926 135 NAKYRLGLTATP 146
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
198-505 |
1.75e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.95 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 198 AEEPRMDTPEDGDLAPCPDgilsekrTPTPEPEPCE-VTEPLAKRSRS-----SELPTEK--GPPGPSQVKVPPPA-RMT 268
Cdd:PHA03247 2495 APDPGGGGPPDPDAPPAPS-------RLAPAILPDEpVGEPVHPRMLTwirglEELASDDagDPPPPLPPAAPPAApDRS 2567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 269 VPkqtqTPERLPELPGarvlPRFQPRVLQIQAQVQPQTlPQMPPVDTQVPlklQKQAQTQTSPEHLVPPqketelqkqvp 348
Cdd:PHA03247 2568 VP----PPRPAPRPSE----PAVTSRARRPDAPPQSAR-PRAPVDDRGDP---RGPAPPSPLPPDTHAP----------- 2624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 349 gqgqprgqtwEQPSEQPSAQVAVQSAEQTRGQPEPQPQGLVPTPERAPVPTDATVLGTPPNVTAEAGGGMEEALPEPVGA 428
Cdd:PHA03247 2625 ----------DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGS 2694
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 918660106 429 qvrVAASQESPASGLHPgecEKRARemlgmwGAGGSLKVTILQSSDSRAFNTTPLTPVPRPSDSSPATPAAASTPSK 505
Cdd:PHA03247 2695 ---LTSLADPPPPPPTP---EPAPH------ALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759
|
|
| Bromo_tif1_like |
cd05502 |
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ... |
1477-1562 |
2.28e-08 |
|
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99934 [Multi-domain] Cd Length: 109 Bit Score: 53.83 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1477 RQLSEVFIQLPSR-------KELPEYYELIRKPVDFKKIKERIR----NHkYRSLNDLEKDVMLLCQNAQTFNLEGSLIY 1545
Cdd:cd05502 11 RLLLELYCHELSLpfhepvsPSVPNYYKIIKTPMDLSLIRKKLQpkspQH-YSSPEEFVADVRLMFKNCYKFNEEDSEVA 89
|
90
....*....|....*..
gi 918660106 1546 EDSIVLQSVFTSVRQKI 1562
Cdd:cd05502 90 QAGKELELFFEEQLKEI 106
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
119-508 |
3.45e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.18 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 119 PPQLGPPSLQqffPQATRQSLlgPPPVGVPmNPSQlnlsgrnPQKQTRTHSSTTPnrKDSSSQTMPVEDGADPQEGSEEA 198
Cdd:PHA03247 2551 PPPPLPPAAP---PAAPDRSV--PPPRPAP-RPSE-------PAVTSRARRPDAP--PQSARPRAPVDDRGDPRGPAPPS 2615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 199 EEPRMDTPEDgdlaPCPdgilsekrtPTPEPEPCEVTEPlakrsrsselPTEKGPPGPSQVKVPPPARMTVPKQTQTPER 278
Cdd:PHA03247 2616 PLPPDTHAPD----PPP---------PSPSPAANEPDPH----------PPPTVPPPERPRDDPAPGRVSRPRRARRLGR 2672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 279 LPelpGARVLPRfQPRVLQIQAQVQPQTLPQMPPvdtqvplklqKQAQTQTSPEHLVPPQKETELQKQVPGQGQPRGQTW 358
Cdd:PHA03247 2673 AA---QASSPPQ-RPRRRAARPTVGSLTSLADPP----------PPPPTPEPAPHALVSATPLPPGPAAARQASPALPAA 2738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 359 EQPSEQPSAQvAVQSAEQTRGQPEPQPQGLVPTPERAPVPTDATVLGTPPNVTAEAGggmEEALPEPvGAQVRVAASQES 438
Cdd:PHA03247 2739 PAPPAVPAGP-ATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSES---RESLPSP-WDPADPPAAVLA 2813
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 439 PASGLHPgecekraremlgmwgaggslkvtilqssdsrafNTTPLTPVPRPSDSSPATPAAASTPSKQGL 508
Cdd:PHA03247 2814 PAAALPP---------------------------------AASPAGPLPPPTSAQPTAPPPPPGPPPPSL 2850
|
|
| Bromo_WDR9_II |
cd05496 |
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ... |
1458-1562 |
3.73e-08 |
|
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99928 Cd Length: 119 Bit Score: 53.62 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1458 KKMKKIVDAVIKYKDSSSGRQLSEVFiqlpsrkELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTF 1537
Cdd:cd05496 8 KQCKELVNLMWDCEDSEPFRQPVDLL-------KYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSY 80
|
90 100
....*....|....*....|....*.
gi 918660106 1538 NL-EGSLIYEDSIVLQSVFTSVRQKI 1562
Cdd:cd05496 81 TPnKRSRIYSMTLRLSALFEEHIKKI 106
|
|
| Bromo_TFIID |
cd05511 |
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ... |
1490-1563 |
3.80e-08 |
|
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99943 [Multi-domain] Cd Length: 112 Bit Score: 53.04 E-value: 3.80e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 918660106 1490 KELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIyedSIVLQSVFTSVRQKIE 1563
Cdd:cd05511 28 KKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVY---TKKAKEMLELAEELLA 98
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
202-508 |
7.20e-08 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 57.79 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 202 RMDTPED-----GDLAPCPDGILSEKRTPTP----EPEPC----EVTEPLAKRSRSSEL------PTEKGPPGPSQVKV- 261
Cdd:PRK10263 271 RMDDDEEitytaRGVAADPDDVLFSGNRATQpeydEYDPLlngaPITEPVAVAAAATTAtqswaaPVEPVTQTPPVASVd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 262 PPPARMTVPKQT----QTPERL--PELPGARVLPRF-QPRVLQIQAQVQP--QTLPQMPPVDTQVPLKLQKQAQTQTSPE 332
Cdd:PRK10263 351 VPPAQPTVAWQPvpgpQTGEPViaPAPEGYPQQSQYaQPAVQYNEPLQQPvqPQQPYYAPAAEQPAQQPYYAPAPEQPAQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 333 HLVPPQKETELQKQVPGQGQPRGQTWE-QPSEQPsaqvavqsaEQTRGQPEPQpqglvPTPERAPVPtdatvlgTPPNVT 411
Cdd:PRK10263 431 QPYYAPAPEQPVAGNAWQAEEQQSTFApQSTYQT---------EQTYQQPAAQ-----EPLYQQPQP-------VEQQPV 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 412 AEagggmeealPEPVGAQVRVAasqESPASGLHPGEcEKRA--REMLGMWgaggslkVTILQSSDSRAFNTTPLTPVPRP 489
Cdd:PRK10263 490 VE---------PEPVVEETKPA---RPPLYYFEEVE-EKRAreREQLAAW-------YQPIPEPVKEPEPIKSSLKAPSV 549
|
330
....*....|....*....
gi 918660106 490 SDSSPATPAAASTPSKQGL 508
Cdd:PRK10263 550 AAVPPVEAAAAVSPLASGV 568
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
769-907 |
1.65e-07 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 52.41 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 769 NGILADEMGLGKTIQTIALITYLMEHKRinGPFLIIVPLSTLSN-WAYEFDKWAPSVVKVSY--KGSPAARRAfvpQLRS 845
Cdd:cd00046 3 NVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALqTAERLRELFGPGIRVAVlvGGSSAEERE---KNKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 918660106 846 GKFNVLLTTYEYIIKDKHILAKI---RWKYMIVDEGHRM----KNHHCKLTQVLNTHYVAPRRLLLTGT 907
Cdd:cd00046 78 GDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
15-414 |
1.76e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 56.31 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 15 QQQLMQLQQLLQQSPPQAPLPMAVSRSLPQQQPQQQLLNLQATSllngsmlqralLLQQLQGLDQFAMPPATYDSAGLSM 94
Cdd:pfam03154 169 TQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSP-----------ATSQPPNQTQSTAAPHTLIQQTPTL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 95 PTATLGSLRSYNMATPSLTAPSITPPQ-LGPPSLQQFFPQATRQSLLGPPPVGVPMNPSQLNLSGRNPQKQTRTHSSTTP 173
Cdd:pfam03154 238 HPQRLPSPHPPLQPMTQPPPPSQVSPQpLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 174 NRKDSSSQTMPvedgadPQEGSEEAEEPrmdtPEDGDLAPCPDGIlsekrtPTPEPEPcevTEPLakrsrsSELPTEKGP 253
Cdd:pfam03154 318 PGQSQQRIHTP------PSQSQLQSQQP----PREQPLPPAPLSM------PHIKPPP---TTPI------PQLPNPQSH 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 254 PGPSQVKVPPPARMtvpkqtqtPERLPELPGARVL--------PRFQPRVLQIQAQVQP-QTLPQMPPVDTQVP-LKLQK 323
Cdd:pfam03154 373 KHPPHLSGPSPFQM--------NSNLPPPPALKPLsslsthhpPSAHPPPLQLMPQSQQlPPPPAQPPVLTQSQsLPPPA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 324 QAQTQTSPEHLVPPQKETELQKQVPG--------QGQPRGQTWEQPSEQPSAQVAVQSAEQTRGQP-------------- 381
Cdd:pfam03154 445 ASHPPTSGLHQVPSQSPFPQHPFVPGgpppitppSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVscplppvqikeeal 524
|
410 420 430
....*....|....*....|....*....|....
gi 918660106 382 -EPQPQGLVPTPERAPVPtDATVLGTPPNVTAEA 414
Cdd:pfam03154 525 dEAEEPESPPPPPRSPSP-EPTVVNTPSHASQSA 557
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
690-908 |
2.07e-07 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 55.80 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 690 SDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNG--------VLKQYQIKGLE-WL 760
Cdd:COG1061 14 LRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGdeasgtsfELRPYQQEALEaLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 761 VSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRIngpfLIIVPLSTLSN-WAYEFDKWAPSVVKVSYKgspaarraf 839
Cdd:COG1061 94 AALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGDPLAGGGK--------- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 918660106 840 vpqlRSGKFNVLLTTYEYIIKDKHiLAKI--RWKYMIVDEGHrmknhHC---KLTQVLNtHYVAPRRLLLTGTP 908
Cdd:COG1061 161 ----KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEAH-----HAgapSYRRILE-AFPAAYRLGLTATP 223
|
|
| Bromo_BDF1_2_I |
cd05500 |
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ... |
1487-1555 |
2.15e-07 |
|
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99932 Cd Length: 103 Bit Score: 50.77 E-value: 2.15e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 918660106 1487 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1555
Cdd:cd05500 31 PVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAAF 99
|
|
| Bromo_Brdt_I_like |
cd05497 |
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ... |
1491-1563 |
3.59e-07 |
|
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99929 Cd Length: 107 Bit Score: 50.11 E-value: 3.59e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918660106 1491 ELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGsliyeDSIVL--QSVFTSVRQKIE 1563
Cdd:cd05497 36 NLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPG-----DDVVLmaQTLEKLFLQKLA 105
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
253-452 |
8.17e-07 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 54.27 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 253 PPGPSQVKVPPPARMTVPKQTQTPER----LPELPGARvlpRFQPRVLQIQAQVQPQTLPQMPPVDTQvplklQKQAQTQ 328
Cdd:pfam09770 166 APKKAAAPAPAPQPAAQPASLPAPSRkmmsLEEVEAAM---RAQAKKPAQQPAPAPAQPPAAPPAQQA-----QQQQQFP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 329 TSPEHLVPPQKETELQKQVPGQGQP-----RGQTWEQPSEQPSAQVAVQSAEQTRGQPEPQPQGLVPTPERAPvptdATV 403
Cdd:pfam09770 238 PQIQQQQQPQQQPQQPQQHPGQGHPvtilqRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLS----AAR 313
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 918660106 404 LGTPPNVTAEAGGGMEEALPEPVGAQVRVAASQESPASGLHPGECEKRA 452
Cdd:pfam09770 314 VGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQLAQLSEEEKAA 362
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
81-464 |
1.45e-06 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 53.53 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 81 AMPPATYDSAGLSMPTATLgSLRSYNMATPSLTAPSITPPQLgPPSLQQFFPQATRQSLLGPPPVGVPMNPSQLNLSGRN 160
Cdd:PHA03378 613 SHIPETSAPRQWPMPLRPI-PMRPLRMQPITFNVLVFPTPHQ-PPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWA 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 161 PQKQTRTHSSTTPNRKDSSSQTMPVEDGADPQEGSEEAEEPRMDTPEDGDLAPCPDGILSEKRTPTPEPEPCEVTEPLAK 240
Cdd:PHA03378 691 PGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 241 RSRSSELPTEKGPPGPSQVKVPPPARMTVPKQTQTPERLpelpGARVLPRFQPRVLQIQAQVQPQTLPQMPPvDTQVPLK 320
Cdd:PHA03378 771 PGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGPTSMQL----MPRAAPGQQGPTKQILRQLLTGGVKRGRP-SLKKPAA 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 321 LQKQAQTQTSPEhlvpPQKETE---LQKQV--PGQGQPRGQTWEQPSEQPSAQVAVQSA--EQT--RGQPEPQPQGLVPT 391
Cdd:PHA03378 846 LERQAAAGPTPS----PGSGTSdkiVQAPVfyPPVLQPIQVMRQLGSVRAAAASTVTQAptEYTgeRRGVGPMHPTDIPP 921
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 918660106 392 PERApvPTDATVLGTPPNvtaeagggmEEALPEPVGAQVRVAASQEspaSGLHPGECEKRAREMLGMWGAGGS 464
Cdd:PHA03378 922 SKRA--KTDAYVESQPPH---------GGQSHSFSVIWENVSQGQQ---QTLECGGTTKQERAMLGTGDIAVS 980
|
|
| Bromo_brd8_like |
cd05507 |
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ... |
1460-1538 |
1.60e-06 |
|
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with the thyroid hormone receptor in a ligand-dependent fashion and enhances thyroid hormone-dependent activation from thyroid response elements. Brd8 is thought to be a nuclear receptor coactivator. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99939 Cd Length: 104 Bit Score: 48.51 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1460 MKKIVDAVikYKDSSSGRQlSEVFIQ-LPSRKElPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1538
Cdd:cd05507 4 WKKAILLV--YRTLASHRY-ASVFLKpVTEDIA-PGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYN 79
|
|
| PRK10927 |
PRK10927 |
cell division protein FtsN; |
225-399 |
1.99e-06 |
|
cell division protein FtsN;
Pssm-ID: 236797 [Multi-domain] Cd Length: 319 Bit Score: 51.99 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 225 PTPEpEPCEVTEPLAKRSRSSELPTEkgPPGPSQVKVP----PPARMTVPKQT----QTPERLPELPGARVLPRFQPRVL 296
Cdd:PRK10927 77 PKPE-ERWRYIKELESRQPGVRAPTE--PSAGGEVKTPeqltPEQRQLLEQMQadmrQQPTQLVEVPWNEQTPEQRQQTL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 297 QIQAQVQPQTlpqmppvdtqvplKLQKQAQTQTSPEhlVPPQKETELQKQVPGQGQPRgQTWEQPSEQPSaQVAVQSAEQ 376
Cdd:PRK10927 154 QRQRQAQQLA-------------EQQRLAQQSRTTE--QSWQQQTRTSQAAPVQAQPR-QSKPASTQQPY-QDLLQTPAH 216
|
170 180
....*....|....*....|...
gi 918660106 377 TRGQPEPQPQGLVPTPERAPVPT 399
Cdd:PRK10927 217 TTAQSKPQQAAPVTRAADAPKPT 239
|
|
| Bromo_plant1 |
cd05506 |
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ... |
1487-1555 |
2.13e-06 |
|
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global transcription factor. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99938 Cd Length: 99 Bit Score: 47.71 E-value: 2.13e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 918660106 1487 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1555
Cdd:cd05506 27 VVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELLKIF 95
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
205-507 |
2.14e-06 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 52.70 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 205 TPEDGDLAPCPDGILSEKRTPtpepePCEVTEPLAKRSRSSELPTEKGPPGPSQ--VKVPPPARMTVPKQTQTPERLPEL 282
Cdd:pfam09606 96 PQMMGPMGPGPGGPMGQQMGG-----PGTASNLLASLGRPQMPMGGAGFPSQMSrvGRMQPGGQAGGMMQPSSGQPGSGT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 283 PGARVLPR--FQPRVLQIQAQVQPQTLPQMPPVDTQ----VPLKLQKQAQTQTSPEHLVPPQKETELQKQVPGQGQPRGQ 356
Cdd:pfam09606 171 PNQMGPNGgpGQGQAGGMNGGQQGPMGGQMPPQMGVpgmpGPADAGAQMGQQAQANGGMNPQQMGGAPNQVAMQQQQPQQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 357 TweqpSEQPSAQVAVQSAEQ-TRGQPEPQPQG-----LVPTPERAPVPTDATVLGTPPNVTAE--------AGGGMEEAL 422
Cdd:pfam09606 251 Q----GQQSQLGMGINQMQQmPQGVGGGAGQGgpgqpMGPPGQQPGAMPNVMSIGDQNNYQQQqtrqqqqqQGGNHPAAH 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 423 PEPVGAQVRVAASQESPASGLHPGECEKRAREMLGMWGAGGslKVTILQSSDSRAFNTTP--------LTPVPRPSDSSP 494
Cdd:pfam09606 327 QQQMNQSVGQGGQVVALGGLNHLETWNPGNFGGLGANPMQR--GQPGMMSSPSPVPGQQVrqvtpnqfMRQSPQPSVPSP 404
|
330
....*....|...
gi 918660106 495 ATPAAASTPSKQG 507
Cdd:pfam09606 405 QGPGSQPPQSHPG 417
|
|
| Bromo_WSTF_like |
cd05505 |
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ... |
1458-1544 |
2.28e-06 |
|
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99937 Cd Length: 97 Bit Score: 47.53 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1458 KKMKKIVDAVIKYKDSSSGRQLsevfiqlPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTF 1537
Cdd:cd05505 3 QKCEEILSKILKYRFSWPFREP-------VTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKY 75
|
....*..
gi 918660106 1538 NLEGSLI 1544
Cdd:cd05505 76 YENGSYV 82
|
|
| Bromo_SPT7_like |
cd05510 |
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ... |
1480-1538 |
4.80e-06 |
|
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, and SLIK. SAGA is involved in the RNA polymerase II-dependent transcriptional regulation of about 10% of all yeast genes. The SPT7 bromodomain has been shown to weakly interact with acetylated histone H3, but not H4. The human representative of this subfamily is cat eye syndrome critical region protein 2 (CECR2). Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99942 [Multi-domain] Cd Length: 112 Bit Score: 47.05 E-value: 4.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 918660106 1480 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1538
Cdd:cd05510 26 STPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYN 84
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
280-500 |
5.45e-06 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 51.39 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 280 PELPGARVLPRFQPrvlqiQAQVQPQTLPQMPPVDTQVPLKLQKQAQTQTSPEHLVPPQketelqkqvpgQGQPRGQTWE 359
Cdd:PRK07003 374 ARVAGAVPAPGARA-----AAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP-----------AAPAPPATAD 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 360 QPSEQPSAQVAVQSAEQTRGQPEPQPQGLVPTPERAPVPTDATVLGTPPNVTAE----AGGGMEEALPEPVGAQVRVAAS 435
Cdd:PRK07003 438 RGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEpaprAAAPSAATPAAVPDARAPAAAS 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 918660106 436 -------QESPASGLHPGEcEKRAREMLGMWGAGGSLKVT----ILQSSD-SRAFNTTPLTPVPRPSDSSPATPAAA 500
Cdd:PRK07003 518 redapaaAAPPAPEARPPT-PAAAAPAARAGGAAAALDVLrnagMRVSSDrGARAAAAAKPAAAPAAAPKPAAPRVA 593
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
289-403 |
1.06e-05 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 50.85 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 289 PRFQPRVLQIQAQVQPqTLPQMPPVDTQVPLKLQKQAQtqtSPEHLVPPQKETElQKQVPGQGQPRGQtweqpseQPSAQ 368
Cdd:PRK10263 743 PLFTPIVEPVQQPQQP-VAPQQQYQQPQQPVAPQPQYQ---QPQQPVAPQPQYQ-QPQQPVAPQPQYQ-------QPQQP 810
|
90 100 110
....*....|....*....|....*....|....*.
gi 918660106 369 VAVQSAEQTRGQP-EPQPQGLVPTPERAPVPTDATV 403
Cdd:PRK10263 811 VAPQPQYQQPQQPvAPQPQYQQPQQPVAPQPQDTLL 846
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
190-445 |
1.17e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 50.15 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 190 DPQEGSEEAEEPRMDTPEDGDLAPCPDGILSEKRTPTPEPEP----------CEVTEPLAKRSRSSELPTEKGPPGPSQV 259
Cdd:NF033839 216 DIQKHHLQKEKHRQIVALIKELDELKKQALSEIDNVNTKVEIentvhkifadMDAVVTKFKKGLTQDTPKEPGNKKPSAP 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 260 KV-------PPPARMTVPKQTQTPERLPELPGARVLPRFQPRvlQIQAQVQPQTLPQMPPVDTQvplklqkqaqtQTSPE 332
Cdd:NF033839 296 KPgmqpspqPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQPE--KPKPEVKPQLETPKPEVKPQ-----------PEKPK 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 333 HLVPPQKETELQKQVPGQGQPRGQTWEQPsEQPSAQVAVQSaEQTRGQPEPQPQGlvPTPERAPVPTDATvlgtpPNVTA 412
Cdd:NF033839 363 PEVKPQPEKPKPEVKPQPETPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKPQPEK--PKPEVKPQPEKPK-----PEVKP 433
|
250 260 270
....*....|....*....|....*....|...
gi 918660106 413 EAGGGMEEALPEPVGAQVRVAASQESPASGLHP 445
Cdd:NF033839 434 QPEKPKPEVKPQPEKPKPEVKPQPETPKPEVKP 466
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
1142-1190 |
1.38e-05 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 45.00 E-value: 1.38e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 918660106 1142 SEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQ 1190
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
111-503 |
2.07e-05 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 49.53 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 111 SLTAPSITPPQLGPPSLQQFFPQATRqsllgpppvgVPMNPSQLNLSGrnpqKQTRTHSSTTPNRKDSSSQTMPVEDGAD 190
Cdd:pfam05109 428 TTTSPTLNTTGFAAPNTTTGLPSSTH----------VPTNLTAPASTG----PTVSTADVTSPTPAGTTSGASPVTPSPS 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 191 PQEGSEEAEEPRMDTPEDGDLAPCPDGIlsekrTPTP---EPEPCEVTEPLAKRSRSSEL--PTEKGPPGPSQVKVPPPa 265
Cdd:pfam05109 494 PRDNGTESKAPDMTSPTSAVTTPTPNAT-----SPTPavtTPTPNATSPTLGKTSPTSAVttPTPNATSPTPAVTTPTP- 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 266 RMTVP---KQTQTPERLPELPGARvlprfQPRVLQI--QAQVQPQTL--PQMPPVDTQVPLKLQKQAQT--------QTS 330
Cdd:pfam05109 568 NATIPtlgKTSPTSAVTTPTPNAT-----SPTVGETspQANTTNHTLggTSSTPVVTSPPKNATSAVTTgqhnitssSTS 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 331 PEHLVP--------PQKETELQKQVP--GQGQPRGQtwEQPSEQPSAQVAVQSAEQTRGQPEPQPQGLVPTPERAPV--- 397
Cdd:pfam05109 643 SMSLRPssisetlsPSTSDNSTSHMPllTSAHPTGG--ENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSSTstk 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 398 PTDATVL-GTPP-NVTA-EAGGGMEEALPepvgAQVRVAASQESPASGLH-PGECEKRAREMLGMWGAGGSlkvtilqSS 473
Cdd:pfam05109 721 PGEVNVTkGTPPkNATSpQAPSGQKTAVP----TVTSTGGKANSTTGGKHtTGHGARTSTEPTTDYGGDST-------TP 789
|
410 420 430
....*....|....*....|....*....|....*..
gi 918660106 474 DSRAFNTTPLTPVP----RPS---DSSPATPAAASTP 503
Cdd:pfam05109 790 RTRYNATTYLPPSTssklRPRwtfTSPPVTTAQATVP 826
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
192-425 |
2.73e-05 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 49.00 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 192 QEGSEEAEEPRMDTPEDGdLAPCPDgilSEKRTPTPEPEPcevtePLAKRSRSSELPTEKGPPGPSQVKVPPPARMTVPK 271
Cdd:NF033839 281 QDTPKEPGNKKPSAPKPG-MQPSPQ---PEKKEVKPEPET-----PKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPK 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 272 QTQTPErlPELPGarvlPRFQPRVLQIQAQVQPQTLPQMPPVDTQVplklqkqaqtqTSPEHLVPPQKETELQKQVPGQG 351
Cdd:NF033839 352 PEVKPQ--PEKPK----PEVKPQPEKPKPEVKPQPETPKPEVKPQP-----------EKPKPEVKPQPEKPKPEVKPQPE 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918660106 352 QPRGQTWEQPsEQPSAQVAVQsAEQTRGQPEPQPQGlvPTPERAPVPtdatvlGTP-PNVTAEAGGGMEEALPEP 425
Cdd:NF033839 415 KPKPEVKPQP-EKPKPEVKPQ-PEKPKPEVKPQPEK--PKPEVKPQP------ETPkPEVKPQPEKPKPEVKPQP 479
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
184-428 |
3.12e-05 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 48.91 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 184 PVEDGADPQEGSEEAEEPRMDTPEDGDLapcpdgilsEKRTPTPEPEPCEVTEPLAKRSRSSELPTEKGPPGPSQVKVPP 263
Cdd:COG5180 166 PDGDSASTLPPPAEKLDKVLTEPRDALK---------DSPEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAASSPKVDP 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 264 PARMTVPKQTQTPERLPELPGARVLPRFQPRVLQIQAQVQPQTLPQMPPVDTQVPLKLQKQAQTQTSPEHLVPPQKETEL 343
Cdd:COG5180 237 PSTSEARSRPATVDAQPEMRPPADAKERRRAAIGDTPAAEPPGLPVLEAGSEPQSDAPEAETARPIDVKGVASAPPATRP 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 344 QKQVPGQGQPRGQTWEQPSEQPSAQVAVQSAEQTRGQPEPQPQGLVPT---PERAPVPTDATVLG---TPPNVTAEAGGG 417
Cdd:COG5180 317 VRPPGGARDPGTPRPGQPTERPAGVPEAASDAGQPPSAYPPAEEAVPGkplEQGAPRPGSSGGDGapfQPPNGAPQPGLG 396
|
250
....*....|.
gi 918660106 418 MEEALPEPVGA 428
Cdd:COG5180 397 RRGAPGPPMGA 407
|
|
| Bromo_polybromo_VI |
cd05526 |
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which ... |
1474-1564 |
3.60e-05 |
|
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.
Pssm-ID: 99956 Cd Length: 110 Bit Score: 44.67 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 1474 SSGRQLSEVFIQLPSRKELPEyyELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQS 1553
Cdd:cd05526 21 EEGRCYSDSLAELPELAVDGV--GPKKIPLTLDIIKRNVDKGRYRRLDKFQEDMFEVLERARRLSRTDSEIYEDAVELQQ 98
|
90
....*....|.
gi 918660106 1554 VFTSVRQKIEK 1564
Cdd:cd05526 99 FFIKIRDELCK 109
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
171-453 |
4.26e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 171 TTPNRKDSSSQTmpvedgadpQEGSEEAEEPRmdtpEDGDLAPCPDGILSEKRTPTPEPEPCEVTEPLAKRSRSSELPTE 250
Cdd:PTZ00449 522 KAPGDKEGEEGE---------HEDSKESDEPK----EGGKPGETKEGEVGKKPGPAKEHKPSKIPTLSKKPEFPKDPKHP 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 251 KGPPGPSQVKVP-PPARMTVPKQTQTPE--RLPELPGARVLPRFQPRVLQIQAQVQPQTlPQ--------MPPVDTQVPL 319
Cdd:PTZ00449 589 KDPEEPKKPKRPrSAQRPTRPKSPKLPEllDIPKSPKRPESPKSPKRPPPPQRPSSPER-PEgpkiikspKPPKSPKPPF 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 320 K-----------LQKQAQT-QTSPEHLVPPQKETELQKQVPGQ-GQPRGQTWEQPSEQPSAQVAVQS--AEQTRGQPEPQ 384
Cdd:PTZ00449 668 DpkfkekfyddyLDAAAKSkETKTTVVLDESFESILKETLPETpGTPFTTPRPLPPKLPRDEEFPFEpiGDPDAEQPDDI 747
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 918660106 385 PQGLVP---------TPERAPVPTDATVLGTPPNVTAEAGGGmEEALPEPvgaqvRVAASQESPASGLHPGECEKRAR 453
Cdd:PTZ00449 748 EFFTPPeeertffheTPADTPLPDILAEEFKEEDIHAETGEP-DEAMKRP-----DSPSEHEDKPPGDHPSLPKKRHR 819
|
|
| Bromo_cbp_like |
cd05495 |
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ... |
1487-1557 |
6.19e-05 |
|
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.
Pssm-ID: 99927 Cd Length: 108 Bit Score: 43.97 E-value: 6.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918660106 1487 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTS 1557
Cdd:cd05495 31 PKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRVYKYCTKLAEVFEQ 101
|
|
| DDXDc_reverse_gyrase |
cd17924 |
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ... |
777-876 |
7.73e-05 |
|
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350682 [Multi-domain] Cd Length: 189 Bit Score: 45.40 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 777 GLGKTiqTIALITYLMEHKRiNGPFLIIVPLSTLSNWAYE----FDKWAPSVVK--VSYKGSPA-ARRAFVPQLRSGKFN 849
Cdd:cd17924 42 GVGKT--TFGLATSLYLASK-GKRSYLIFPTKSLVKQAYErlskYAEKAGVEVKilVYHSRLKKkEKEELLEKIEKGDFD 118
|
90 100
....*....|....*....|....*..
gi 918660106 850 VLLTTYEYIIKDKHILAKIRWKYMIVD 876
Cdd:cd17924 119 ILVTTNQFLSKNFDLLSNKKFDFVFVD 145
|
|
| zf-C2H2_jaz |
pfam12171 |
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ... |
603-627 |
8.70e-05 |
|
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.
Pssm-ID: 432381 [Multi-domain] Cd Length: 27 Bit Score: 41.00 E-value: 8.70e-05
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
165-454 |
1.30e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 47.00 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 165 TRTHSSTTPNRKDSSSQTMPVEDGADPQEGSEEAEEPRMDTPEDGdLAPCPDGILSEKRTPTP---------EPEPCEVT 235
Cdd:PRK10263 328 TATQSWAAPVEPVTQTPPVASVDVPPAQPTVAWQPVPGPQTGEPV-IAPAPEGYPQQSQYAQPavqyneplqQPVQPQQP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 236 EPLAKRSRSSELPTEKGPPGPSQVKVPPPARMTVPKQTQTPERLPELPGARVLPRFQPRVLQIQAQVQPQTLPQMPPVDT 315
Cdd:PRK10263 407 YYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQTYQQPAAQEPLYQQPQPVEQ 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 316 QVPLKLQKQAQtQTSPEHlvPPQKETELQKQVPGQGQPRGQTWEQPSEQPSAQ-VAVQSAEQTRGQPEPQPQGLVPT--P 392
Cdd:PRK10263 487 QPVVEPEPVVE-ETKPAR--PPLYYFEEVEEKRAREREQLAAWYQPIPEPVKEpEPIKSSLKAPSVAAVPPVEAAAAvsP 563
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 918660106 393 ERAPVPTDATVLGTPPNVTAEA-----GGGMEEALPEPVGAQ------VRVAASQESPASGLH-PGE--CEKRARE 454
Cdd:PRK10263 564 LASGVKKATLATGAAATVAAPVfslanSGGPRPQVKEGIGPQlprpkrIRVPTRRELASYGIKlPSQraAEEKARE 639
|
|
| PHA03377 |
PHA03377 |
EBNA-3C; Provisional |
83-398 |
1.86e-04 |
|
EBNA-3C; Provisional
Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 46.58 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 83 PPATYDSAGLSMPTATLGSLRSYNMATPSLTAPSITPPQLGPPSLQqffPQATRQSLLGPPPVGvpmnpsqlnlsgrnpQ 162
Cdd:PHA03377 536 VQDGFQRSGRRQKRATPPKVSPSDRGPPKASPPVMAPPSTGPRVMA---TPSTGPRDMAPPSTG---------------P 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 163 KQTRTHSSTTPnrkdsssqtmpvedGADPQEGSEEAEEPRMDTPedgdlaPCPDGILSEKRTPTPE-PEPCEVTEPLAKR 241
Cdd:PHA03377 598 RQQAKCKDGPP--------------ASGPHEKQPPSSAPRDMAP------SVVRMFLRERLLEQSTgPKPKSFWEMRAGR 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 242 srssELPTEKGPPGPSQvkvPPPARMTVPKQTQTPE--RLPELPGARVLPRFQPRVLQIQAQvQPQTLPQMPPV-DTQVP 318
Cdd:PHA03377 658 ----DGSGIQQEPSSRR---QPATQSTPPRPSWLPSvfVLPSVDAGRAQPSEESHLSSMSPT-QPISHEEQPRYeDPDDP 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 319 LKLQKQAQTQTSPEHLVPPQKETELQ-KQVPGQGqprgqtWEQPSEQPSAQVAVQSAEQTRGQPEPQPQGLVPTPERAPV 397
Cdd:PHA03377 730 LDLSLHPDQAPPPSHQAPYSGHEEPQaQQAPYPG------YWEPRPPQAPYLGYQEPQAQGVQVSSYPGYAGPWGLRAQH 803
|
.
gi 918660106 398 P 398
Cdd:PHA03377 804 P 804
|
|
| motB |
PRK05996 |
MotB family protein; |
345-489 |
4.69e-04 |
|
MotB family protein;
Pssm-ID: 235665 [Multi-domain] Cd Length: 423 Bit Score: 44.69 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 345 KQVP----GQGQPRGQTWEQPSEQPSAQVAVQSAEQTRGQPEPQPQglvpTPERAPVPTDATVLGTPPNVTAEAGGG-ME 419
Cdd:PRK05996 188 KQVEvttaGDLLPPGQAREQAQGAKSATAAPATVPQAAPLPQAQPK----KAATEEELIADAKKAATGEPAANAAKAaKP 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 420 EALPEPVGAQVRVAASQESPASGLHPGecekRAREMLGMWGAGGSLKVTILQSSDSRAFNTTplTPVPRP 489
Cdd:PRK05996 264 EPMPDDQQKEAEQLQAAIAQAIGGVAG----KLAEGVTVTPVEGGLLISLTDQVDYGMFAIG--SAVPRA 327
|
|
| PRK10927 |
PRK10927 |
cell division protein FtsN; |
314-413 |
6.32e-04 |
|
cell division protein FtsN;
Pssm-ID: 236797 [Multi-domain] Cd Length: 319 Bit Score: 43.90 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 314 DTQVPLKLQKQAQTQTSPEHL--VPPQKETELQKQVPGQGQPRGQTWE--QPSEQPSAQVAVQSAEQTR-GQPEPQPQGL 388
Cdd:PRK10927 116 PEQRQLLEQMQADMRQQPTQLveVPWNEQTPEQRQQTLQRQRQAQQLAeqQRLAQQSRTTEQSWQQQTRtSQAAPVQAQP 195
|
90 100
....*....|....*....|....*
gi 918660106 389 VPTPERAPVPTDATVLGTPPNVTAE 413
Cdd:PRK10927 196 RQSKPASTQQPYQDLLQTPAHTTAQ 220
|
|
| ECM1 |
pfam05782 |
Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic ... |
280-393 |
7.10e-04 |
|
Extracellular matrix protein 1 (ECM1); This family consists of several eukaryotic extracellular matrix protein 1 (ECM1) sequences. ECM1 has been shown to regulate endochondral bone formation, stimulate the proliferation of endothelial cells and induce angiogenesis. Mutations in the ECM1 gene can cause lipoid proteinosis, a disorder which causes generalized thickening of skin, mucosae and certain viscera. Classical features include beaded eyelid papules and laryngeal infiltration leading to hoarseness.
Pssm-ID: 461739 Cd Length: 518 Bit Score: 44.45 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 280 PELPGARVLPRFQPRVLQI------QAQVQPQTLPQMPPVDTQVPLKLQKQAQTQTSPEHlvpPQKETELQKQVPGQGQP 353
Cdd:pfam05782 7 PSPPQTRGLPVDHPDTSQHdppfegQSEVQPPPSQEAIPVQEEELPPPQLPVEKKVDPPL---PQEAIPLQEELPPPQLP 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 918660106 354 RGQTWEQPSEQPsaQVAVQSAEQTRGQPEPQPQGLVPTPE 393
Cdd:pfam05782 84 IEQKEIDPPFPQ--QEEITPSKQREEKPAPLVGQGHPEPE 121
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
291-556 |
7.36e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 44.48 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 291 FQPRvlQIQAQVQPQTlPQMPPVDTQVPLKLQKQAQTQTSPEHLVPPqketelqKQVPGQGQPRGQTWEQPSEQPSAQVA 370
Cdd:PRK12323 363 FRPG--QSGGGAGPAT-AAAAPVAQPAPAAAAPAAAAPAPAAPPAAP-------AAAPAAAAAARAVAAAPARRSPAPEA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 371 VQSAEQTRGQPEPQPQGLVPTPERAPVPTDATVLGT--PPNVTAEAGGGMEEALPEPVGAQVRVAASQESPASGLHPGEC 448
Cdd:PRK12323 433 LAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGprPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPA 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 449 EKRAreMLGMWGAGGSLKVTILQSSDSRAFNTTPLTPVPRPSDSSPATPAAASTPSKQGlhffcyVCKTSCSSQQEFQDH 528
Cdd:PRK12323 513 QPDA--APAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRAS------ASGLPDMFDGDWPAL 584
|
250 260 270
....*....|....*....|....*....|....
gi 918660106 529 MSE------AQHLQRLVELQHTNHACLLSLLPMP 556
Cdd:PRK12323 585 AARlpvrglAQQLARQSELAGVEGDTVRLRVPVP 618
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
156-507 |
9.36e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.39 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 156 LSGRNPQKQTRTH--SSTTPNRKDSSSQTMPVEDGADPQEGSEEAEEPRMDTPEdgdLAPCPDGILSEKRTPTPEPEPCE 233
Cdd:PHA03307 36 LSGSQGQLVSDSAelAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPT---WSLSTLAPASPAREGSPTPPGPS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 234 VTEPlAKRSRSSELPTEKGPPGPSQVKVPPPARMTVPKQTQTPERLPELPGARVLPRfqPRVLQIQAQVQPQTLPQMPPV 313
Cdd:PHA03307 113 SPDP-PPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAAS--SRQAALPLSSPEETARAPSSP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 314 DTQVPLKLQKQAQTQTSPEHLVPPQKETELQKQVPGQGQPRGqtweqPSEQPSAQVAVQSAEQTRGQPEPQPQGlVPTPE 393
Cdd:PHA03307 190 PAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADD-----AGASSSDSSSSESSGCGWGPENECPLP-RPAPI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 394 RAPVPTDATVLGTPPNVTAEAGGGmEEALPEPVGAQVRVAASQESPASGLHPGECEKRAREMlgmwGAGGSLKVTilQSS 473
Cdd:PHA03307 264 TLPTRIWEASGWNGPSSRPGPASS-SSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRES----SSSSTSSSS--ESS 336
|
330 340 350
....*....|....*....|....*....|....
gi 918660106 474 DSRAFNTTPlTPVPRPSDSSPATPAAASTPSKQG 507
Cdd:PHA03307 337 RGAAVSPGP-SPSRSPSPSRPPPPADPSSPRKRP 369
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
209-413 |
1.32e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 43.71 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 209 GDLAPCPDGILSEKRTPTPEPEPCEVTEPLAKRSRSSELPTEKGPPGPSQVKVP---PPARMTVPKQTQTPerlPELPGA 285
Cdd:PRK12323 370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAParrSPAPEALAAARQAS---ARGPGG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 286 RVLPRFQPRVLQIQAQVQPQTLPQMPPVDTQVPLKLQKQAQTQTSPEHLVPPQKETELQKQVPGQGQPRGQTWEQPSEQP 365
Cdd:PRK12323 447 APAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESI 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 918660106 366 SAQVAVQSAEQTRGQPEPQPQGLVPTPER------APVPTDATVLGTPPNVTAE 413
Cdd:PRK12323 527 PDPATADPDDAFETLAPAPAAAPAPRAAAatepvvAPRPPRASASGLPDMFDGD 580
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
176-413 |
1.33e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 43.60 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 176 KDSSSQTMPVEDG----ADPQEGSEEAEEPRMDTPEDGDLAPCPDgILSEKRTPTPEPEPcevtEPLAKRSrssELPTEK 251
Cdd:NF033839 276 KKGLTQDTPKEPGnkkpSAPKPGMQPSPQPEKKEVKPEPETPKPE-VKPQLEKPKPEVKP----QPEKPKP---EVKPQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 252 GPPGPSQVKVPPPARMTVPKQTQTPErlPELPG--ARVLPRFQPRVLQIQAQVQPQTLPQMPPVDTQVPLKLQKQAQTQT 329
Cdd:NF033839 348 ETPKPEVKPQPEKPKPEVKPQPEKPK--PEVKPqpETPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 330 SPEHLVPPQKETELQKQVPGQGQPRGQTWEQPsEQPSAQVAVQSAEQtrgQPEPQPQGLVPTPERAPVPTDATVLGTPPN 409
Cdd:NF033839 426 KPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQP-ETPKPEVKPQPEKP---KPEVKPQPEKPKPDNSKPQADDKKPSTPNN 501
|
....
gi 918660106 410 VTAE 413
Cdd:NF033839 502 LSKD 505
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
777-908 |
1.81e-03 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 41.07 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 777 GLGKTIqtIALITYL--MEHKRINGPFLIIVPLSTLSNWAYE-FDKWA-PSVVKVSYKGSPAARRAFVPQLRSGkfNVLL 852
Cdd:pfam00270 24 GSGKTL--AFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEeLKKLGkGLGLKVASLLGGDSRKEQLEKLKGP--DILV 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918660106 853 TTYE---YIIKDKHILAKIrwKYMIVDEGHRM--KNHHCKLTQVLNTHYVAPRRLLLTGTP 908
Cdd:pfam00270 100 GTPGrllDLLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRQILLLSATL 158
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
188-337 |
1.91e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 43.15 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 188 GADPQEGSEEAEEPRMDTPEDGDLAPCpdgilsekRTPTPEPEPCEVTEPLAKRSRSSelptekgppgpSQVKVPPPARM 267
Cdd:PRK10263 718 GANPFSLDDFEFSPMKALLDDGPHEPL--------FTPIVEPVQQPQQPVAPQQQYQQ-----------PQQPVAPQPQY 778
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 918660106 268 TVPKQTQTPERLPELPGARVLPrfQPRVLQIQAQVQPQTLPQMP--PVDTQVPLKLQKQAQTQTSPEHLVPP 337
Cdd:PRK10263 779 QQPQQPVAPQPQYQQPQQPVAP--QPQYQQPQQPVAPQPQYQQPqqPVAPQPQYQQPQQPVAPQPQDTLLHP 848
|
|
| Treacle |
pfam03546 |
Treacher Collins syndrome protein Treacle; |
108-507 |
1.99e-03 |
|
Treacher Collins syndrome protein Treacle;
Pssm-ID: 460967 [Multi-domain] Cd Length: 531 Bit Score: 42.75 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 108 ATPSLTAPSITPPQLGPPslQQFFPQATRQSLLG---PPPVGVPMNPSQLNLSGRNPQKQTRTHSSTTPNRKDSSSQTMP 184
Cdd:pfam03546 74 VPPGKTGPAAAQAQAGKP--EEDSESSSEESDSDgetPAAATLTTSPAQVKPLGKNSQVRPASTVGKGPSGKGANPAPPG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 185 VEDGADPQEGSEEAEEPRMDTPEDGDlapcpdgilSEKRTPTPEPEPCEVTEPLAKRSRS------SELPTEKGPPGPSQ 258
Cdd:pfam03546 152 KAGSAAPLVQVGKKEEDSESSSEESD---------SEGEAPPAATQAKPSGKILQVRPASgpakgaAPAPPQKAGPVATQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 259 VKVPPPARMTVPKQTQTpERLPELPGARVLPRFQPRVLQIQAQVQPQ-------TLPQMPP--VDTQVPLKlqkqAQTQT 329
Cdd:pfam03546 223 VKAERSKEDSESSEESS-DSEEEAPAAATPAQAKPALKTPQTKASPRkgtpitpTSAKVPPvrVGTPAPWK----AGTVT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 330 SPEHLVPPQKETELQKqvpgQGQPRGQTWEQPSEQPSAQVAvqsaeqTRGQPEPQPQGLvpTPERAPVPTDA-TVLGTPP 408
Cdd:pfam03546 298 SPACASSPAVARGAQR----PEEDSSSSEESESEEETAPAA------AVGQAKSVGKGL--QGKAASAPTKGpSGQGTAP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 409 NVTAEAGggmeealpePVGAQVRVAASQESPASGlhpgecEKRAREMLGMWGAGGSLKVTILQSSDSRAFNTTPLTPVPr 488
Cdd:pfam03546 366 VPPGKTG---------PAVAQVKAEAQEDSESSE------EESDSEEAAATPAQVKASGKTPQAKANPAPTKASSAKGA- 429
|
410
....*....|....*....
gi 918660106 489 psDSSPATPAAASTPSKQG 507
Cdd:pfam03546 430 --ASAPGKVVAAAAQAKQG 446
|
|
| SP2_N |
cd22540 |
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ... |
292-440 |
2.07e-03 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.
Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 42.99 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 292 QPRVLQIQAQVQPQTLPQMPPVDTQvPLKLQkQAQTQTSPehlVPPQKETELQKQVPGQGQPRGQTWEQPSEQPSAqVAV 371
Cdd:cd22540 282 QPAVLQQVQVLQPKQEQQVVQIPQQ-ALRVV-QAASATLP---TVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQT-VLL 355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918660106 372 QSAeqtrGQPEPQPQGLVPTPERAPVPTDATVLGTPPNVTAEagggmEEALPE--PVGAQVRVAASQESPA 440
Cdd:cd22540 356 QEA----PAATATPSSSTSTVQQQVTANNGTGTSKPNYNVRK-----ERTLPKiaPAGGIISLNAAQLAAA 417
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
205-441 |
2.14e-03 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 42.99 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 205 TPEDGDLAPCPdgilsEKRTPTPEPEPCEVTEPLAKRSRSSELPT---EKGPPGPSQVKVPPPARMTVPKQTQTPER-LP 280
Cdd:PLN03209 314 TPMEELLAKIP-----SQRVPPKESDAADGPKPVPTKPVTPEAPSppiEEEPPQPKAVVPRPLSPYTAYEDLKPPTSpIP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 281 ELPGARvlPRFQPRVLQIQAQVQPQTLPqMPPVDTQVPLKLQKQAQTQTSpEHLVPPQKETELQKqvPGQGQPRGQTWEQ 360
Cdd:PLN03209 389 TPPSSS--PASSKSVDAVAKPAEPDVVP-SPGSASNVPEVEPAQVEAKKT-RPLSPYARYEDLKP--PTSPSPTAPTGVS 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 361 PSEQPSAQV-------AVQSAEQTRGQPEPQPQGLVP-------TPERAPVPTdATVLGTPPNVTAEAGGGMEEALPEPV 426
Cdd:PLN03209 463 PSVSSTSSVpavpdtaPATAATDAAAPPPANMRPLSPyavyddlKPPTSPSPA-APVGKVAPSSTNEVVKVGNSAPPTAL 541
|
250
....*....|....*
gi 918660106 427 GAQVRVAASQESPAS 441
Cdd:PLN03209 542 ADEQHHAQPKPRPLS 556
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
108-505 |
3.23e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 108 ATPSLTAPSI---TPPQLGPPS--LQQFFPQATRQSLLGPPPVGVPmNPSQLNLSGRNPQKQTRTHSSTTPnrkdssSQT 182
Cdd:PHA03307 26 ATPGDAADDLlsgSQGQLVSDSaeLAAVTVVAGAAACDRFEPPTGP-PPGPGTEAPANESRSTPTWSLSTL------APA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 183 MPVEDGAdPQEGSEEAEEPRMDTPEDGDLAPCPDGILSEKRTPTPEPEPCEVTEPLAKRSRSSELPT-EKGPPGPSQV-- 259
Cdd:PHA03307 99 SPAREGS-PTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASdAASSRQAALPls 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 260 KVPPPARMTVPKQtqtPERLPELPGARVLPRFQPRVLQIQAqvqPQTLPQMPPVDTQVPLKLQKQAQTQTSPEHLVPPQK 339
Cdd:PHA03307 178 SPEETARAPSSPP---AEPPPSTPPAAASPRPPRRSSPISA---SASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 340 ETELQKQVPGQGQPRGQTWEqpseqpsaqvAVQSAEQTRGQPEPQPQGlvPTPERAPVPTDATVLGTPPNVTAEAGGgmE 419
Cdd:PHA03307 252 ENECPLPRPAPITLPTRIWE----------ASGWNGPSSRPGPASSSS--SPRERSPSPSPSSPGSGPAPSSPRASS--S 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 420 EALPEPVGAQVRVAASQESPASGLHPGECEKRAremlgmwGAGGSlkvtilqSSDSRAFNTTPLTPVPRPSDSSPATPAA 499
Cdd:PHA03307 318 SSSSRESSSSSTSSSSESSRGAAVSPGPSPSRS-------PSPSR-------PPPPADPSSPRKRPRPSRAPSSPAASAG 383
|
....*.
gi 918660106 500 ASTPSK 505
Cdd:PHA03307 384 RPTRRR 389
|
|
| Treacle |
pfam03546 |
Treacher Collins syndrome protein Treacle; |
147-505 |
3.55e-03 |
|
Treacher Collins syndrome protein Treacle;
Pssm-ID: 460967 [Multi-domain] Cd Length: 531 Bit Score: 41.98 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 147 VPMNPSQLNLSGRNPQkqtrTHSSTTPNRKDSSSQTMPVEDG-ADPQEGSEEAEEPRMD---TPEDGDlapcpdgilSEK 222
Cdd:pfam03546 40 AAKTPLQAKPSGKTPQ----VRAASAPAKESPRKGAPPVPPGkTGPAAAQAQAGKPEEDsesSSEESD---------SDG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 223 RTPTPEP---EPCEVtEPLAKRSRSSELPT-EKGPPGPSQVKVPPPARMTVPKQTQTPERLP-------------ELPGA 285
Cdd:pfam03546 107 ETPAAATlttSPAQV-KPLGKNSQVRPASTvGKGPSGKGANPAPPGKAGSAAPLVQVGKKEEdsessseesdsegEAPPA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 286 RVLPRFQPRVLQIQAQVQPQTLPQMPPVDTQVPLKlqKQAQTQTSPEHLVPPQKETELQKQV-----PGQGQP---RGQT 357
Cdd:pfam03546 186 ATQAKPSGKILQVRPASGPAKGAAPAPPQKAGPVA--TQVKAERSKEDSESSEESSDSEEEApaaatPAQAKPalkTPQT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 358 WEQPSE-QPSAQVAVQSAEQTRGQPEPQPQGLVPTPERAPVPTDATVLGTPPNVTA---EAGGGMEEALPEPV------- 426
Cdd:pfam03546 264 KASPRKgTPITPTSAKVPPVRVGTPAPWKAGTVTSPACASSPAVARGAQRPEEDSSsseESESEEETAPAAAVgqaksvg 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 427 -GAQVRVAASQESPASG-----LHPGEcekraremlgMWGAGGSLKVTILQSSDS-----------------RAFNTTPL 483
Cdd:pfam03546 344 kGLQGKAASAPTKGPSGqgtapVPPGK----------TGPAVAQVKAEAQEDSESseeesdseeaaatpaqvKASGKTPQ 413
|
410 420
....*....|....*....|..
gi 918660106 484 TPVPRPSDSSPATPAAASTPSK 505
Cdd:pfam03546 414 AKANPAPTKASSAKGAASAPGK 435
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
186-313 |
4.23e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.49 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 186 EDGADPQEGSEEAEEPRMDTPEDGDLAPCPDGILSEKRTPTPEPEPCEVTEPLAKRSRSSELPTEKGPPGPSQVkvpPPA 265
Cdd:PHA03169 196 ETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSHSYTVVGWKPSTRPGGV---PKL 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 918660106 266 RMTVPKQTQTPERLPE--LPGARVLPRFQPRvLQIQAQVQPQTLPQMPPV 313
Cdd:PHA03169 273 CLRCTSHPSHRSRLPEgqQSEDKVPRKYQAR-RRFFRQVLPSILPPRPGP 321
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
346-442 |
4.40e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.90 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 346 QVPGQGQPRGQTWEQPSEQPSAQVAVQSAEQTRGQPEPQPQGlVPTPERAPVPTDATVLGTPPNVTAEAGGGMEEALPEP 425
Cdd:PRK07764 392 GAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAP-APAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAP 470
|
90
....*....|....*..
gi 918660106 426 VGAQVRVAASQESPASG 442
Cdd:PRK07764 471 AAAPEPTAAPAPAPPAA 487
|
|
| ZnF_U1 |
smart00451 |
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ... |
510-538 |
4.60e-03 |
|
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.
Pssm-ID: 197732 [Multi-domain] Cd Length: 35 Bit Score: 36.46 E-value: 4.60e-03
10 20
....*....|....*....|....*....
gi 918660106 510 FFCYVCKTSCSSQQEFQDHMSEAQHLQRL 538
Cdd:smart00451 4 FYCKLCNVTFTDEISVEAHLKGKKHKKNV 32
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
275-413 |
4.78e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.99 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 275 TPERLPELPGARVlPRFQPRVLQIQAQVQPQTLPQMPpvdtQVPLKLQKQAQtqtSPEHLVPPQKETElQKQVPGQGQPR 354
Cdd:PRK10263 746 TPIVEPVQQPQQP-VAPQQQYQQPQQPVAPQPQYQQP----QQPVAPQPQYQ---QPQQPVAPQPQYQ-QPQQPVAPQPQ 816
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 918660106 355 GQTWEQP-SEQPSAQvavqsaeQTRGQPEPQPQGLVPTP-----------ERAPVPTDATVLGTPPNVTAE 413
Cdd:PRK10263 817 YQQPQQPvAPQPQYQ-------QPQQPVAPQPQDTLLHPllmrngdsrplHKPTTPLPSLDLLTPPPSEVE 880
|
|
| UFD2 |
COG5112 |
U1-like Zn-finger-containing protein [General function prediction only]; |
583-634 |
5.30e-03 |
|
U1-like Zn-finger-containing protein [General function prediction only];
Pssm-ID: 227443 Cd Length: 126 Bit Score: 38.91 E-value: 5.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 918660106 583 DLIQHRRTQDHKVAKQSLRP--------FCTICSRYFKTPRKFVEHVKSQGHKDKAKELK 634
Cdd:COG5112 29 DQIKNDLSTKESQKKLPYDPelpglgqhYCIECARYFITEKALMEHKKGKVHKRRAKELR 88
|
|
| |
