|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
766-996 |
2.56e-165 |
|
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: 498.82 E-value: 2.56e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 766 NGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVG 845
Cdd:cd17996 1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 846 VVSYKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYIAPYRLLLT 925
Cdd:cd17996 81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24664907 926 GTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKV--ELNEEETILIIRRLHKVLRPFLLRRLK 996
Cdd:cd17996 161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
735-1364 |
2.81e-165 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 528.60 E-value: 2.81e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 735 EDDEYRTEEQTYYSIAHTIheKVVEQASImVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDR 814
Cdd:PLN03142 139 EDEEYLKEEEDGLGGSGGT--RLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 815 KKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVSYKGSPQGRRLLQ-NQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYM 893
Cdd:PLN03142 216 RGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQReELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 894 IIDEGHRMKNHHCKLTQVLNThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfATTGEkvelNE 973
Cdd:PLN03142 296 IIDEAHRIKNENSLLSKTMRL-FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----ND 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 974 EETIliIRRLHKVLRPFLLRRLKKEVEHQLPDKVEYIIKCDMSALQRVLYKHMQSKGV-LLTDGSEKGKhgkggakaLMN 1052
Cdd:PLN03142 367 QQEV--VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLN 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1053 TIVQLRKLCNHPFMFQHIEEkycdhtgGHGVVSGPDLYRVSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGW 1132
Cdd:PLN03142 437 IAMQLRKCCNHPYLFQGAEP-------GPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMY 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1133 RQFGYLRLDGTTKAEDRGELLRKFNAKGSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNE 1212
Cdd:PLN03142 510 RGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKE 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1213 VRVLRLMTVNSVEERILAAARYKLNMDEKVIQAG-MFDQKSTGSErqQFLQTILHQDDNEEEEENEVPDDEMINMMIARS 1291
Cdd:PLN03142 590 VQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGrLAEQKTVNKD--ELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKG 667
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24664907 1292 EEEIeifKRMDAERKKEDEEIHpgRERLIDESELPDWLTKDDDEVERFhyqyDEDTILGRG-----SRQRKEvDYTDS 1364
Cdd:PLN03142 668 EEAT---AELDAKMKKFTEDAI--KFKMDDTAELYDFDDEDDKDENKL----DFKKIVSDNwidppKRERKR-NYSES 735
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
657-1244 |
8.17e-125 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 406.92 E-value: 8.17e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 657 TGKKLTGDDAPMLKHLHRWLNMHPGWDWIDDEEDSCGSNDDHKPKVEEQPTATEDATDKAQATGNDEDAKDLITKAKVED 736
Cdd:COG0553 132 LLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 737 DEYRTEEQTYYSIAHtiHEKVVEQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKK 816
Cdd:COG0553 212 ELLAEAAVDAFRLRR--LREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 817 VmGPYLIIVPLSTLPNWVLEFEKWAPAVGVVSYKGSPQgRRLLQNQMRatKFNVLLTTYEYVIKDKAVLAKIQWKYMIID 896
Cdd:COG0553 290 A-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE-RAKGANPFE--DADLVITSYGLLRRDIELLAAVDWDLVILD 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 897 EGHRMKNHHCKLTQV---LNthyiAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPfattgekVELNE 973
Cdd:COG0553 366 EAQHIKNPATKRAKAvraLK----ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP-------IEKGD 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 974 EETiliIRRLHKVLRPFLLRRLKKEVEHQLPDKVEYIIKCDMSALQRVLYKHMqskgVLLTDGSEKGKHGKGGAKALMNT 1053
Cdd:COG0553 435 EEA---LERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV----LEYLRRELEGAEGIRRRGLILAA 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1054 IVQLRKLCNHPFMFQHIEEKYCDHtgghgvvsgpdlyrvSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGWR 1133
Cdd:COG0553 508 LTRLRQICSHPALLLEEGAELSGR---------------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEER 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1134 QFGYLRLDGTTKAEDRGELLRKFNAkGSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNEV 1213
Cdd:COG0553 573 GIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDV 651
|
570 580 590
....*....|....*....|....*....|.
gi 24664907 1214 RVLRLMTVNSVEERILAAARYKLNMDEKVIQ 1244
Cdd:COG0553 652 QVYKLVAEGTIEEKILELLEEKRALAESVLG 682
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
772-1067 |
1.81e-117 |
|
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: 371.63 E-value: 1.81e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 772 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTISLVTYLMDRKKVMG-PYLIIVPLSTLPNWVLEFEKWA--PAVGVV 847
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 848 SYKGSPQGR-RLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHYIAPYRLLLTG 926
Cdd:pfam00176 81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 927 TPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKvelneeetiLIIRRLHKVLRPFLLRRLKKEVEHQLPDK 1006
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24664907 1007 VEYIIKCDMSALQRVLYKH-MQSKGVLLTDGSEkgkHGKGGAKALMNTIVQLRKLCNHPFMF 1067
Cdd:pfam00176 231 VEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
1092-1219 |
6.83e-56 |
|
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: 190.38 E-value: 6.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1092 VSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGWRQFGYLRLDGTTKAEDRGELLRKFNAkGSDVFVFLLSTR 1171
Cdd:cd18793 9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNE-DPDIRVFLLSTK 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 24664907 1172 AGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNEVRVLRLM 1219
Cdd:cd18793 88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| Bromo_SNF2L2 |
cd05516 |
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ... |
1421-1526 |
3.27e-55 |
|
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: 187.25 E-value: 3.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1421 RSKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQ 1499
Cdd:cd05516 1 ELTKKMNKIVDVVIKYKDsDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
|
90 100
....*....|....*....|....*..
gi 24664907 1500 IYNEEASLIYLDSIALQKVFVGARQRI 1526
Cdd:cd05516 81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
|
|
| BROMO |
smart00297 |
bromo domain; |
1419-1519 |
5.03e-30 |
|
bromo domain;
Pssm-ID: 197636 [Multi-domain] Cd Length: 107 Bit Score: 115.45 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1419 DKRSKKQMHKIMSAVIKHNQDGRtLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNA 1498
Cdd:smart00297 1 DPKLQKKLQELLKAVLDKLDSHP-LSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNA 79
|
90 100
....*....|....*....|.
gi 24664907 1499 QIYNEEASLIYLDSIALQKVF 1519
Cdd:smart00297 80 RTYNGPDSEVYKDAKKLEKFF 100
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
768-957 |
7.24e-29 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 115.28 E-value: 7.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 768 TLKEYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TISLVTYLMDRKKvmGPYLIIVPLSTL-PNWVLEFEKWAPAVG 845
Cdd:smart00487 8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGKG--GRVLVLVPTRELaEQWAEELKKLGPSLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 846 VVS---YKGSPQGRRLlqNQMRATKFNVLLTTYEYVIKD--KAVLAKIQWKYMIIDEGHRMKN--HHCKLTQVLNTHYIA 918
Cdd:smart00487 83 LKVvglYGGDSKREQL--RKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24664907 919 PYRLLLTGTPLQNKLPELWALLN--FLLPSIFKSCSTFEQW 957
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1094-1208 |
8.00e-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: 109.22 E-value: 8.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1094 GKFELLDRILPKLKatNHRVLLFCQMTQcmTIIEDYLGWRQ-FGYLRLDGTTKAEDRGELLRKFNAKGSDVfvfLLSTRA 1172
Cdd:pfam00271 1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKIDV---LVATDV 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 24664907 1173 GGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIG 1208
Cdd:pfam00271 74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| HSA |
smart00573 |
domain in helicases and associated with SANT domains; |
497-569 |
2.80e-23 |
|
domain in helicases and associated with SANT domains;
Pssm-ID: 214727 [Multi-domain] Cd Length: 73 Bit Score: 94.77 E-value: 2.80e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24664907 497 QKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERMRRLMA 569
Cdd:smart00573 1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1125-1208 |
8.18e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 93.82 E-value: 8.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1125 IIEDYLGWRQFGYLRLDGTTKAEDRGELLRKFNakgSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRA 1204
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78
|
....
gi 24664907 1205 HRIG 1208
Cdd:smart00490 79 GRAG 82
|
|
| HSA |
pfam07529 |
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ... |
498-564 |
1.67e-18 |
|
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.
Pssm-ID: 462194 [Multi-domain] Cd Length: 67 Bit Score: 81.08 E-value: 1.67e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664907 498 KLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERM 564
Cdd:pfam07529 1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
|
|
| COG5076 |
COG5076 |
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ... |
1401-1520 |
1.41e-17 |
|
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];
Pssm-ID: 227408 [Multi-domain] Cd Length: 371 Bit Score: 86.78 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1401 EESDDDslILKRRRRQNLDKRSKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDC 1479
Cdd:COG5076 124 AHLKTS--VKKRKTPKIEDELLYADNKAIAKFKKQLFLrDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNG 201
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24664907 1480 KYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVFV 1520
Cdd:COG5076 202 RYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFL 242
|
|
| BRK |
pfam07533 |
BRK domain; The function of this domain is unknown. It is often found associated with ... |
646-687 |
1.34e-16 |
|
BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.
Pssm-ID: 462196 Cd Length: 44 Bit Score: 74.85 E-value: 1.34e-16
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 24664907 646 ADMRVHVVEQCTGKKLTGDDAPMLKHLHRWLNMHPGWDWIDD 687
Cdd:pfam07533 3 GDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
|
|
| Bromodomain |
pfam00439 |
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ... |
1428-1512 |
1.52e-16 |
|
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: 76.20 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1428 KIMSAVIKHNqdgrtLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASL 1507
Cdd:pfam00439 3 EILDKLMEHP-----IAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSV 77
|
....*
gi 24664907 1508 IYLDS 1512
Cdd:pfam00439 78 IYKAA 82
|
|
| BRK |
smart00592 |
domain in transcription and CHROMO domain helicases; |
645-689 |
2.93e-16 |
|
domain in transcription and CHROMO domain helicases;
Pssm-ID: 197800 Cd Length: 45 Bit Score: 73.92 E-value: 2.93e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 24664907 645 VADMRVHVVEQCTGKKLTGDDAPMLKHLHRWLNMHPGWDWIDDEE 689
Cdd:smart00592 1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
721-928 |
2.44e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 58.88 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 721 NDEDAKDLITKAKVEDDEYRTEEQTYYSIAHTIHEKVVEQASIMVNGTLKEYQIKGLE-WLVSLYNNNLNGILADEMGLG 799
Cdd:COG1061 33 NLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 800 KTIQTISLVTYLMDRKKVmgpyLIIVPLSTLPN-WVLEFEKWAPAVGVVSYKgspqgrrllqnqmRATKFNVLLTTYEYV 878
Cdd:COG1061 113 KTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGDPLAGGGK-------------KDSDAPITVATYQSL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24664907 879 IKdKAVLAKIQ--WKYMIIDEGHrmknhHC---KLTQVLNtHYIAPYRLLLTGTP 928
Cdd:COG1061 176 AR-RAHLDELGdrFGLVIIDEAH-----HAgapSYRRILE-AFPAAYRLGLTATP 223
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
473-647 |
8.55e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 473 IKLYKRTKRQGLREARATE----KLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANA 548
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 549 EREQKKEQEriEKERMRRLMAEDEEGyRKLIDQKK----DKRLAFLLSQTDEYISNLTQMVK------QHKDDQMKKKEE 618
Cdd:PTZ00121 1678 EEAKKAEED--EKKAAEALKKEAEEA-KKAEELKKkeaeEKKKAEELKKAEEENKIKAEEAKkeaeedKKKAEEAKKDEE 1754
|
170 180
....*....|....*....|....*....
gi 24664907 619 EGKRLIQFKKELLMSGEYIGIDEGSIVAD 647
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-639 |
8.72e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 401 ITLLQERENRIAARISLRMQELQRLpATMSEDLRLQAAIELRALRVLNFQRQLrmefvqctrRDTTLETALNIKLYKRTK 480
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEE---------LEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 481 RQGLREARATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFhRNNKAQLARMNKAVMNHHANAEREQKKEQERIE 560
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24664907 561 KERMRRLMAEDEEGYRKLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKELLMSGEYIGI 639
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
403-641 |
3.99e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 403 LLQERENRIAARISLRMQELQRLPatmsEDLRLQAAIELRALRVLNFQRQLRMEFVQ----CTRRDTTLETALNIKLYKR 478
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELK----LKEQAKKALEYYQLKEKLELEEEYLLYLDylklNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 479 TKRQGLREARAtEKLEKQQKLEAERKRRQKHLEFLAAVLQhgkDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQER 558
Cdd:pfam02463 254 ESSKQEIEKEE-EKLAQVLKENKEEEKEKKLQEEELKLLA---KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 559 IEKERmrrlmaEDEEGYRKLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKELLMSGEYIG 638
Cdd:pfam02463 330 LKKEK------EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
...
gi 24664907 639 IDE 641
Cdd:pfam02463 404 EKE 406
|
|
| QLQ |
pfam08880 |
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ... |
169-198 |
4.86e-05 |
|
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.
Pssm-ID: 462622 Cd Length: 35 Bit Score: 41.94 E-value: 4.86e-05
10 20 30
....*....|....*....|....*....|
gi 24664907 169 HLNGNQVNLLRTQITAYRLLARNKPISMQM 198
Cdd:pfam08880 1 PFTPAQLQELRAQILAYKYLSRNQPVPPEL 30
|
|
| QLQ |
smart00951 |
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ... |
168-198 |
6.74e-05 |
|
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.
Pssm-ID: 214931 Cd Length: 36 Bit Score: 41.36 E-value: 6.74e-05
10 20 30
....*....|....*....|....*....|..
gi 24664907 168 QHLNGNQVNLLRTQITAYR-LLARNKPISMQM 198
Cdd:smart00951 1 SPFTPAQLELLRAQILAYKyLLARNQPVPPEL 32
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
447-565 |
2.80e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 447 LNFQRQLRMEFVQCTRRDTTLETALniKLYKRTKRQGLrearATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGK-DLRE 525
Cdd:PRK11637 164 LNQARQETIAELKQTREELAAQKAE--LEEKQSQQKTL----LYEQQAQQQKLEQARNERKKTLTGLESSLQKDQqQLSE 237
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 24664907 526 FhRNNKAQLarmnkavMNHHANAEREQKK--EQERIEKERMR 565
Cdd:PRK11637 238 L-RANESRL-------RDSIARAEREAKAraEREAREAARVR 271
|
|
| Pro-rich |
pfam15240 |
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
243-397 |
7.13e-04 |
|
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 41.95 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 243 QPPPSAGTPPQCSTPPASNPYGPPVPGQKMQVAPPPPHMQQgqplppqppqvggpppiqqqqppqqqqqqsqppppephq 322
Cdd:pfam15240 55 PPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPR--------------------------------------- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24664907 323 hqlPNGGKPLSMGPSGG-QPLIPSSPMQPQVrgtlPGMPPGSQVPQPGGGPQRQVPPAGMPMPKPNRITTVAKPVG 397
Cdd:pfam15240 96 ---PPPGKPQGPPPQGGnQQQGPPPPGKPQG----PPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRPPQPGNPQG 164
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
363-607 |
1.98e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 363 SQVPQPGGGP---QRQVPPAGMPMPKPNRITTVAKPVGLDPITLLQERENRIAARISLRMQELQRLPATMSEDLRLQAAI 439
Cdd:TIGR02794 26 SVKPEPGGGAeiiQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 440 --ELRALRVLNFQRQLrmefvqctrrdttLETALNIKLYKRTKRQGLREARATEKLEKQQKLEAERKR----RQKHLEFL 513
Cdd:TIGR02794 106 qaEQAAKQAEEKQKQA-------------EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAaaeaKKKAEEAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 514 AAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERMRRLMAEDEEGYRKL--------IDQKKDK 585
Cdd:TIGR02794 173 KKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIfglasgsnAEKQGGA 252
|
250 260
....*....|....*....|..
gi 24664907 586 RLAFLLSQTDEYISNLTQMVKQ 607
Cdd:TIGR02794 253 RGAAAGSEVDKYAAIIQQAIQQ 274
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
251-384 |
3.27e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 42.36 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 251 PPQCSTPPASNPYGPPVPGQKMQVAPPPphmqqgqplpPQPPQVGGPPPIQQQQPPQQQQQQSQPPPPEPhqhqlPNGGK 330
Cdd:PHA03378 696 PPPRAPTPMRPPAAPPGRAQRPAAATGR----------ARPPAAAPGRARPPAAAPGRARPPAAAPGRAR-----PPAAA 760
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 24664907 331 PLSMGPSGGQPLIPsSPMQPqvrgtlPGMPPGSQvPQPGGGPQRQVPPAGMPMP 384
Cdd:PHA03378 761 PGRARPPAAAPGAP-TPQPP------PQAPPAPQ-QRPRGAPTPQPPPQAGPTS 806
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DEXHc_SMARCA2_SMARCA4 |
cd17996 |
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ... |
766-996 |
2.56e-165 |
|
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: 498.82 E-value: 2.56e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 766 NGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVG 845
Cdd:cd17996 1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 846 VVSYKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYIAPYRLLLT 925
Cdd:cd17996 81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24664907 926 GTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKV--ELNEEETILIIRRLHKVLRPFLLRRLK 996
Cdd:cd17996 161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
|
|
| PLN03142 |
PLN03142 |
Probable chromatin-remodeling complex ATPase chain; Provisional |
735-1364 |
2.81e-165 |
|
Probable chromatin-remodeling complex ATPase chain; Provisional
Pssm-ID: 215601 [Multi-domain] Cd Length: 1033 Bit Score: 528.60 E-value: 2.81e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 735 EDDEYRTEEQTYYSIAHTIheKVVEQASImVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDR 814
Cdd:PLN03142 139 EDEEYLKEEEDGLGGSGGT--RLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 815 KKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVSYKGSPQGRRLLQ-NQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYM 893
Cdd:PLN03142 216 RGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQReELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 894 IIDEGHRMKNHHCKLTQVLNThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfATTGEkvelNE 973
Cdd:PLN03142 296 IIDEAHRIKNENSLLSKTMRL-FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----ND 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 974 EETIliIRRLHKVLRPFLLRRLKKEVEHQLPDKVEYIIKCDMSALQRVLYKHMQSKGV-LLTDGSEKGKhgkggakaLMN 1052
Cdd:PLN03142 367 QQEV--VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLN 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1053 TIVQLRKLCNHPFMFQHIEEkycdhtgGHGVVSGPDLYRVSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGW 1132
Cdd:PLN03142 437 IAMQLRKCCNHPYLFQGAEP-------GPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMY 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1133 RQFGYLRLDGTTKAEDRGELLRKFNAKGSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNE 1212
Cdd:PLN03142 510 RGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKE 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1213 VRVLRLMTVNSVEERILAAARYKLNMDEKVIQAG-MFDQKSTGSErqQFLQTILHQDDNEEEEENEVPDDEMINMMIARS 1291
Cdd:PLN03142 590 VQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGrLAEQKTVNKD--ELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKG 667
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24664907 1292 EEEIeifKRMDAERKKEDEEIHpgRERLIDESELPDWLTKDDDEVERFhyqyDEDTILGRG-----SRQRKEvDYTDS 1364
Cdd:PLN03142 668 EEAT---AELDAKMKKFTEDAI--KFKMDDTAELYDFDDEDDKDENKL----DFKKIVSDNwidppKRERKR-NYSES 735
|
|
| DEXHc_SMARCA4 |
cd18062 |
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ... |
746-996 |
2.81e-142 |
|
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: 437.94 E-value: 2.81e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 746 YYSIAHTIHEKVVEQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIV 825
Cdd:cd18062 1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 826 PLSTLPNWVLEFEKWAPAVGVVSYKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHH 905
Cdd:cd18062 81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 906 CKLTQVLNTHYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKVELNEEETILIIRRLHK 985
Cdd:cd18062 161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
|
250
....*....|.
gi 24664907 986 VLRPFLLRRLK 996
Cdd:cd18062 241 VLRPFLLRRLK 251
|
|
| DEXHc_SMARCA2 |
cd18063 |
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ... |
746-996 |
4.92e-139 |
|
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: 429.10 E-value: 4.92e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 746 YYSIAHTIHEKVVEQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIV 825
Cdd:cd18063 1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 826 PLSTLPNWVLEFEKWAPAVGVVSYKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHH 905
Cdd:cd18063 81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 906 CKLTQVLNTHYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKVELNEEETILIIRRLHK 985
Cdd:cd18063 161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240
|
250
....*....|.
gi 24664907 986 VLRPFLLRRLK 996
Cdd:cd18063 241 VLRPFLLRRLK 251
|
|
| HepA |
COG0553 |
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ... |
657-1244 |
8.17e-125 |
|
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];
Pssm-ID: 440319 [Multi-domain] Cd Length: 682 Bit Score: 406.92 E-value: 8.17e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 657 TGKKLTGDDAPMLKHLHRWLNMHPGWDWIDDEEDSCGSNDDHKPKVEEQPTATEDATDKAQATGNDEDAKDLITKAKVED 736
Cdd:COG0553 132 LLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 737 DEYRTEEQTYYSIAHtiHEKVVEQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKK 816
Cdd:COG0553 212 ELLAEAAVDAFRLRR--LREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 817 VmGPYLIIVPLSTLPNWVLEFEKWAPAVGVVSYKGSPQgRRLLQNQMRatKFNVLLTTYEYVIKDKAVLAKIQWKYMIID 896
Cdd:COG0553 290 A-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE-RAKGANPFE--DADLVITSYGLLRRDIELLAAVDWDLVILD 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 897 EGHRMKNHHCKLTQV---LNthyiAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPfattgekVELNE 973
Cdd:COG0553 366 EAQHIKNPATKRAKAvraLK----ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP-------IEKGD 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 974 EETiliIRRLHKVLRPFLLRRLKKEVEHQLPDKVEYIIKCDMSALQRVLYKHMqskgVLLTDGSEKGKHGKGGAKALMNT 1053
Cdd:COG0553 435 EEA---LERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV----LEYLRRELEGAEGIRRRGLILAA 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1054 IVQLRKLCNHPFMFQHIEEKYCDHtgghgvvsgpdlyrvSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGWR 1133
Cdd:COG0553 508 LTRLRQICSHPALLLEEGAELSGR---------------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEER 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1134 QFGYLRLDGTTKAEDRGELLRKFNAkGSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNEV 1213
Cdd:COG0553 573 GIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDV 651
|
570 580 590
....*....|....*....|....*....|.
gi 24664907 1214 RVLRLMTVNSVEERILAAARYKLNMDEKVIQ 1244
Cdd:COG0553 652 QVYKLVAEGTIEEKILELLEEKRALAESVLG 682
|
|
| SNF2-rel_dom |
pfam00176 |
SNF2-related domain; This domain is found in proteins involved in a variety of processes ... |
772-1067 |
1.81e-117 |
|
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: 371.63 E-value: 1.81e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 772 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTISLVTYLMDRKKVMG-PYLIIVPLSTLPNWVLEFEKWA--PAVGVV 847
Cdd:pfam00176 1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 848 SYKGSPQGR-RLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHYIAPYRLLLTG 926
Cdd:pfam00176 81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 927 TPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKvelneeetiLIIRRLHKVLRPFLLRRLKKEVEHQLPDK 1006
Cdd:pfam00176 160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24664907 1007 VEYIIKCDMSALQRVLYKH-MQSKGVLLTDGSEkgkHGKGGAKALMNTIVQLRKLCNHPFMF 1067
Cdd:pfam00176 231 VEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
|
|
| DEXHc_HELLS_SMARCA6 |
cd18009 |
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ... |
766-996 |
1.06e-93 |
|
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: 302.77 E-value: 1.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 766 NGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRkKVMGPYLIIVPLSTLPNWVLEFEKWAPAVG 845
Cdd:cd18009 1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRER-GVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 846 VVSYKGSPQGRR-----LLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHYIAPY 920
Cdd:cd18009 80 VLLYHGTKEERErlrkkIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELK-TFNSDN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24664907 921 RLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFN--APFATTGEKVELNEEETILIIRRLHKVLRPFLLRRLK 996
Cdd:cd18009 159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
|
|
| DEXHc_SMARCA1_SMARCA5 |
cd17997 |
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ... |
766-996 |
1.35e-93 |
|
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: 301.93 E-value: 1.35e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 766 NGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVG 845
Cdd:cd17997 1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 846 VVSYKGSPQGR-RLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYiAPYRLLL 924
Cdd:cd17997 81 VVVLIGDKEERaDIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFN-SRNRLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24664907 925 TGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNApfattgeKVELNEEETilIIRRLHKVLRPFLLRRLK 996
Cdd:cd17997 160 TGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNV-------NNCDDDNQE--VVQRLHKVLRPFLLRRIK 222
|
|
| DEXQc_SRCAP |
cd18003 |
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ... |
769-994 |
7.18e-85 |
|
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: 276.93 E-value: 7.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd18003 1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLL-QNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNThYIAPYRLLLTGT 927
Cdd:cd18003 81 YYGSAKERKLKrQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLLLTGT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664907 928 PLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFAttgEKVELNEEETILIIRRLHKVLRPFLLRR 994
Cdd:cd18003 160 PLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLT---AMSEGSQEENEELVRRLHKVLRPFLLRR 223
|
|
| DEXHc_CHD1_2 |
cd17993 |
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ... |
768-994 |
2.34e-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: 266.53 E-value: 2.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 768 TLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVV 847
Cdd:cd17993 1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 848 SYKGSPQGRRLLQ------NQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNThYIAPYR 921
Cdd:cd17993 81 VYLGDIKSRDTIReyefyfSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-FKTNNR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24664907 922 LLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEqwfnapfattgekVELNEEETILiIRRLHKVLRPFLLRR 994
Cdd:cd17993 160 LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-------------EEHDEEQEKG-IADLHKELEPFILRR 218
|
|
| DEXHc_Snf |
cd17919 |
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ... |
769-948 |
5.47e-79 |
|
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: 258.26 E-value: 5.47e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd17919 1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYiAPYRLLLTGTP 928
Cdd:cd17919 81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR-AKRRLLLTGTP 159
|
170 180
....*....|....*....|
gi 24664907 929 LQNKLPELWALLNFLLPSIF 948
Cdd:cd17919 160 LQNNLEELWALLDFLDPPFL 179
|
|
| DEXHc_CHD6_7_8_9 |
cd17995 |
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ... |
769-994 |
3.53e-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: 252.17 E-value: 3.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAvGVVS 848
Cdd:cd17995 1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDM-NVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQN-QM-----------RATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHY 916
Cdd:cd17995 80 YHGSGESRQIIQQyEMyfkdaqgrkkkGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK-KL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24664907 917 IAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNapfattgekvELNEEETiliIRRLHKVLRPFLLRR 994
Cdd:cd17995 159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG----------DLKTAEQ---VEKLQALLKPYMLRR 223
|
|
| DEXHc_SMARCA5 |
cd18064 |
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ... |
767-1006 |
6.92e-70 |
|
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: 234.95 E-value: 6.92e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 767 GTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGV 846
Cdd:cd18064 14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 847 VSYKGSPQGR-RLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHYIAPYRLLLT 925
Cdd:cd18064 94 VCLIGDKDQRaAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR-EFKTTNRLLLT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 926 GTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKvelneeetilIIRRLHKVLRPFLLRRLKKEVEHQLPD 1005
Cdd:cd18064 173 GTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQK----------LVERLHMVLRPFLLRRIKADVEKSLPP 242
|
.
gi 24664907 1006 K 1006
Cdd:cd18064 243 K 243
|
|
| DEXHc_SMARCA1 |
cd18065 |
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ... |
759-996 |
8.01e-70 |
|
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: 234.14 E-value: 8.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 759 EQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFE 838
Cdd:cd18065 6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 839 KWAPAVGVVSYKGSPQGR-RLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHYI 917
Cdd:cd18065 86 RWVPSLRAVCLIGDKDARaAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR-EFK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24664907 918 APYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKvelneeetilIIRRLHKVLRPFLLRRLK 996
Cdd:cd18065 165 TTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRRIK 233
|
|
| DEXQc_INO80 |
cd18002 |
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ... |
769-994 |
5.33e-66 |
|
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: 223.15 E-value: 5.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd18002 1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQN-------QMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLnTHYIAPYR 921
Cdd:cd18002 81 YWGNPKDRKVLRKfwdrknlYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL-LSFHCRNR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24664907 922 LLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGE-KVELNEEEtiliIRRLHKVLRPFLLRR 994
Cdd:cd18002 160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAEnKTGLNEHQ----LKRLHMILKPFMLRR 229
|
|
| DEXHc_CHD2 |
cd18054 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ... |
769-994 |
1.16e-64 |
|
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: 219.49 E-value: 1.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd18054 21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQN------QMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLnTHYIAPYRL 922
Cdd:cd18054 101 YIGDLMSRNTIREyewihsQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24664907 923 LLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQwfnapfaTTGEKVELNEEEtiliirrLHKVLRPFLLRR 994
Cdd:cd18054 180 LITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE-------DHGKGRENGYQS-------LHKVLEPFLLRR 237
|
|
| DEXHc_CHD1L |
cd18006 |
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ... |
769-994 |
6.25e-64 |
|
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: 216.53 E-value: 6.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd18006 1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQNQMRAT-KFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYIaPYRLLLTGT 927
Cdd:cd18006 81 YMGDKEKRLDLQQDIKSTnRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV-DFRLLLTGT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664907 928 PLQNKLPELWALLNFLLPSIFkSCSTFEQWFNApFATTGEKVELNEEetiliirrLHKVLRPFLLRR 994
Cdd:cd18006 160 PIQNSLQELYALLSFIEPNVF-PKDKLDDFIKA-YSETDDESETVEE--------LHLLLQPFLLRR 216
|
|
| DEXQc_arch_SWI2_SNF2 |
cd18012 |
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ... |
765-996 |
1.28e-60 |
|
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: 207.03 E-value: 1.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 765 VNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIslvTYLMDRK--KVMGPYLIIVPLSTLPNWVLEFEKWAP 842
Cdd:cd18012 1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTL---ALLLSRKeeGRKGPSLVVAPTSLIYNWEEEAAKFAP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 843 AVGVVSYKGSPQGRRLLQnqmRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQV---LNthyiAP 919
Cdd:cd18012 78 ELKVLVIHGTKRKREKLR---ALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAvkaLK----AD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664907 920 YRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPfattgekVELNEEETILiiRRLHKVLRPFLLRRLK 996
Cdd:cd18012 151 HRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKP-------IEKDGDEEAL--EELKKLISPFILRRLK 218
|
|
| DEXHc_CHD3_4_5 |
cd17994 |
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ... |
769-994 |
2.58e-59 |
|
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: 202.67 E-value: 2.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd17994 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSpqgrrllqnqmratkfNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYIApYRLLLTGTP 928
Cdd:cd17994 81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIG-YKLLLTGTP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24664907 929 LQNKLPELWALLNFLLPSIFKSCSTFeqwfnapfatTGEKVELNEEETiliIRRLHKVLRPFLLRR 994
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) ... |
1092-1219 |
6.83e-56 |
|
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: 190.38 E-value: 6.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1092 VSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGWRQFGYLRLDGTTKAEDRGELLRKFNAkGSDVFVFLLSTR 1171
Cdd:cd18793 9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNE-DPDIRVFLLSTK 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 24664907 1172 AGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNEVRVLRLM 1219
Cdd:cd18793 88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
|
|
| Bromo_SNF2L2 |
cd05516 |
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ... |
1421-1526 |
3.27e-55 |
|
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: 187.25 E-value: 3.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1421 RSKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQ 1499
Cdd:cd05516 1 ELTKKMNKIVDVVIKYKDsDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
|
90 100
....*....|....*....|....*..
gi 24664907 1500 IYNEEASLIYLDSIALQKVFVGARQRI 1526
Cdd:cd05516 81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
|
|
| DEXHc_SMARCAD1 |
cd17998 |
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ... |
769-948 |
4.41e-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: 187.21 E-value: 4.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKvMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd17998 1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQNQM--RATKFNVLLTTYEYVI---KDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNThYIAPYRLL 923
Cdd:cd17998 80 YYGSQEERKHLRYDIlkGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INANFRLL 158
|
170 180
....*....|....*....|....*
gi 24664907 924 LTGTPLQNKLPELWALLNFLLPSIF 948
Cdd:cd17998 159 LTGTPLQNNLLELMSLLNFIMPKPF 183
|
|
| DEXHc_CHD1 |
cd18053 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ... |
769-994 |
1.49e-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: 182.17 E-value: 1.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd18053 21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQN------QMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLnTHYIAPYRL 922
Cdd:cd18053 101 YLGDINSRNMIRThewmhpQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24664907 923 LLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQwfnapfaTTGEKVELNEEEtiliirrLHKVLRPFLLRR 994
Cdd:cd18053 180 LITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE-------EHGKGREYGYAS-------LHKELEPFLLRR 237
|
|
| DEXHc_ERCC6L |
cd18001 |
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ... |
769-994 |
2.15e-50 |
|
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: 178.33 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRkKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd18001 1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDS-GLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKG-SPQGRRllQNQMR-ATKFNVLLTTYEYVIKDKAVLA-----KIQWKYMIIDEGHRMKNHHCKLTQVLntHYI-APY 920
Cdd:cd18001 80 FHGtSKKERE--RNLERiQRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSL--REIpAKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 921 RLLLTGTPLQNKLPELWALLNFLLP-SIFKSCSTFEQWFNAPF-------ATTGEKVELNEeetilIIRRLHKVLRPFLL 992
Cdd:cd18001 156 RIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPItrgrdkdATQGEKALGSE-----VAENLRQIIKPYFL 230
|
..
gi 24664907 993 RR 994
Cdd:cd18001 231 RR 232
|
|
| DEXHc_Mot1 |
cd17999 |
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ... |
769-994 |
2.70e-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: 178.31 E-value: 2.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVtYLMDRKKVMG------PYLIIVPLSTLPNWVLEFEKWAP 842
Cdd:cd17999 1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRANSfnsenlPSLVVCPPTLVGHWVAEIKKYFP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 843 AVG--VVSYKGSPQGRRLLQNQMraTKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLnTHYIAPY 920
Cdd:cd17999 80 NAFlkPLAYVGPPQERRRLREQG--EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV-KQLKANH 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24664907 921 RLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATT--GEKVELNEEETILIIRRLHKVLRPFLLRR 994
Cdd:cd17999 157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASrdSKASAKEQEAGALALEALHKQVLPFLLRR 232
|
|
| DEXHc_CHD5 |
cd18057 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ... |
769-994 |
3.46e-50 |
|
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: 177.95 E-value: 3.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd18057 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQ--------NQMRA------------TKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKL 908
Cdd:cd18057 81 YTGDKESRSVIRenefsfedNAIRSgkkvfrmkkeaqIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 909 TQVLNTHYIaPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfattgekVELNEEETiliIRRLHKVLR 988
Cdd:cd18057 161 FRVLNSYKI-DYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226
|
....*.
gi 24664907 989 PFLLRR 994
Cdd:cd18057 227 PHMLRR 232
|
|
| DEXHc_ERCC6 |
cd18000 |
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ... |
769-945 |
1.34e-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: 174.82 E-value: 1.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVV- 847
Cdd:cd18000 1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 848 -----SYKGSPQG-----RRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQV---LNT 914
Cdd:cd18000 81 lhssgSGTGSEEKlgsieRKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAckqLRT 160
|
170 180 190
....*....|....*....|....*....|.
gi 24664907 915 hyiaPYRLLLTGTPLQNKLPELWALLNFLLP 945
Cdd:cd18000 161 ----PHRLILSGTPIQNNLKELWSLFDFVFP 187
|
|
| DEXHc_CHD6 |
cd18058 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ... |
769-994 |
4.32e-49 |
|
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: 174.46 E-value: 4.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRkKVMGPYLIIVPLSTLPNWVLEFEKWApAVGVVS 848
Cdd:cd18058 1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLM-GIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQ-----------NQMRAT-KFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHY 916
Cdd:cd18058 79 YHGSQISRQMIQqyemyyrdeqgNPLSGIfKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24664907 917 IApYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNapfattgekvELNEEETiliIRRLHKVLRPFLLRR 994
Cdd:cd18058 159 LE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG----------DLKTEEQ---VKKLQSILKPMMLRR 222
|
|
| DEXHc_CHD3 |
cd18055 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ... |
769-994 |
7.00e-49 |
|
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: 174.04 E-value: 7.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd18055 1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQN-----------------QMRA---TKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKL 908
Cdd:cd18055 81 YTGDKDSRAIIREnefsfddnavkggkkafKMKReaqVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 909 TQVLNTHYIaPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfattgekVELNEEETiliIRRLHKVLR 988
Cdd:cd18055 161 FRVLNGYKI-DHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226
|
....*.
gi 24664907 989 PFLLRR 994
Cdd:cd18055 227 PHMLRR 232
|
|
| DEXHc_CHD7 |
cd18059 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ... |
769-994 |
6.62e-48 |
|
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: 170.98 E-value: 6.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVtYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWApAVGVVS 848
Cdd:cd18059 1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQ--------NQMR----ATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHY 916
Cdd:cd18059 79 YHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24664907 917 IApYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNapfattgekvELNEEETiliIRRLHKVLRPFLLRR 994
Cdd:cd18059 159 LE-HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
|
|
| DEXHc_CHD8 |
cd18060 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ... |
769-994 |
1.90e-47 |
|
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: 169.46 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDrKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVs 848
Cdd:cd18060 1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYN-VGIHGPFLVIAPLSTITNWEREFNTWTEMNTIV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQN-QMR-----------ATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHY 916
Cdd:cd18060 79 YHGSLASRQMIQQyEMYckdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK-HM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24664907 917 IAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNapfattgekvELNEEETiliIRRLHKVLRPFLLRR 994
Cdd:cd18060 158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
|
|
| DEXHc_CHD4 |
cd18056 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ... |
769-994 |
5.18e-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: 166.01 E-value: 5.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 848
Cdd:cd18056 1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQ--------NQMR------------ATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKL 908
Cdd:cd18056 81 YVGDKDSRAIIRenefsfedNAIRggkkasrmkkeaSVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 909 TQVLNThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfattgekVELNEEETiliIRRLHKVLR 988
Cdd:cd18056 161 FRVLNG-YSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF----------ADIAKEDQ---IKKLHDMLG 226
|
....*.
gi 24664907 989 PFLLRR 994
Cdd:cd18056 227 PHMLRR 232
|
|
| DEXHc_ERCC6L2 |
cd18005 |
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ... |
769-994 |
3.90e-45 |
|
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: 163.70 E-value: 3.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLM-------DRKKVM-------------GPYLIIVPLS 828
Cdd:cd18005 1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrDRENNRprfkkkppassakKPVLIVAPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 829 TLPNWVLEFEKWAP-AVGVVSYKGSPQGrrlLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCK 907
Cdd:cd18005 81 VLYNWKDELDTWGHfEVGVYHGSRKDDE---LEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 908 LTQVLNThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPF------ATTGEKVELNEEetilIIR 981
Cdd:cd18005 158 LTQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgqrhTATARELRLGRK----RKQ 232
|
250
....*....|...
gi 24664907 982 RLHKVLRPFLLRR 994
Cdd:cd18005 233 ELAVKLSKFFLRR 245
|
|
| DEXHc_CHD9 |
cd18061 |
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ... |
769-994 |
1.46e-44 |
|
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: 161.33 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVtYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWApAVGVVS 848
Cdd:cd18061 1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 849 YKGSPQGRRLLQ--------NQMR----ATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHY 916
Cdd:cd18061 79 YHGSLISRQMIQqyemyfrdSQGRiirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24664907 917 IApYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNapfattgekvELNEEETiliIRRLHKVLRPFLLRR 994
Cdd:cd18061 159 LE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
|
|
| DEXHc_RAD54 |
cd18004 |
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ... |
769-994 |
3.81e-39 |
|
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: 146.28 E-value: 3.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVS--LYNNNLNG---ILADEMGLGKTIQTISLVTYLMDRKKVMGP----YLIIVPLSTLPNWVLEFEK 839
Cdd:cd18004 1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 840 W----APAVGVVSYKGSPQGRRLLQNQMRATkFNVLLTTYEYVIKDKAVLAK-IQWKYMIIDEGHRMKNHHCKLTQVLNT 914
Cdd:cd18004 81 WlglrRIKVVTADGNAKDVKASLDFFSSAST-YPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSESKTTKALNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 915 hYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKvELNEEETILIIRRLH---KVLRPFL 991
Cdd:cd18004 160 -LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDP-DASEEDKELGAERSQelsELTSRFI 237
|
...
gi 24664907 992 LRR 994
Cdd:cd18004 238 LRR 240
|
|
| DEXDc_SHPRH-like |
cd18008 |
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ... |
769-994 |
1.00e-38 |
|
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: 145.12 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLynnnlNGILADEMGLGKTIQTISLV------------TYLMDRKKVMGPY-----LIIVPLSTLP 831
Cdd:cd18008 1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdpkipeELEENSSDPKKLYlskttLIVVPLSLLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 832 NWVLEFEK-WAPAVG-VVSYKGSPQGRRLLQnqmrATKFNVLLTTY-----EY-----------VIKDKAVLAKIQWKYM 893
Cdd:cd18008 76 QWKDEIEKhTKPGSLkVYVYHGSKRIKSIEE----LSDYDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIRWYRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 894 IIDEGHRMKNHHCKLTQV---LNTHyiapYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKve 970
Cdd:cd18008 152 ILDEAHNIKNRSTKTSRAvcaLKAE----RRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK-- 225
|
250 260
....*....|....*....|....
gi 24664907 971 lneeetilIIRRLHKVLRPFLLRR 994
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 ... |
769-961 |
2.12e-35 |
|
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: 135.50 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLE--W--LVSLYNNNLNG---ILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWA 841
Cdd:cd18007 1 LKPHQVEGVRflWsnLVGTDVGSDEGggcILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 842 PAVGVVSY--KGSPQGRRLLQnqmRATKFN-------VLLTTYEY---VIKDKAVLAKIQWKYM-----------IIDEG 898
Cdd:cd18007 81 PPDLRPLLvlVSLSASKRADA---RLRKINkwhkeggVLLIGYELfrnLASNATTDPRLKQEFIaalldpgpdllVLDEG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24664907 899 HRMKNHHCKLTQVLNTHyIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAP 961
Cdd:cd18007 158 HRLKNEKSQLSKALSKV-KTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKP 219
|
|
| BROMO |
smart00297 |
bromo domain; |
1419-1519 |
5.03e-30 |
|
bromo domain;
Pssm-ID: 197636 [Multi-domain] Cd Length: 107 Bit Score: 115.45 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1419 DKRSKKQMHKIMSAVIKHNQDGRtLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNA 1498
Cdd:smart00297 1 DPKLQKKLQELLKAVLDKLDSHP-LSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNA 79
|
90 100
....*....|....*....|.
gi 24664907 1499 QIYNEEASLIYLDSIALQKVF 1519
Cdd:smart00297 80 RTYNGPDSEVYKDAKKLEKFF 100
|
|
| DEXHc_RAD54B |
cd18066 |
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ... |
769-994 |
5.04e-29 |
|
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: 116.87 E-value: 5.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSL-----YNNNLNGILADEMGLGKTIQTISLVTYLMDR-----KKVMGPYLIIVPLSTLPNWVLEFE 838
Cdd:cd18066 1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRQgpyggKPVIKRALIVTPGSLVKNWKKEFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 839 KW--APAVGVVSYKGSPQGRRLLQnqmrATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLnTHY 916
Cdd:cd18066 81 KWlgSERIKVFTVDQDHKVEEFIA----SPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL-TSL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 917 IAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKVELNEEETILIIR--RLHKVLRPFLLRR 994
Cdd:cd18066 156 SCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARaaELTRLTGLFILRR 235
|
|
| DEXHc_HLTF1_SMARC3 |
cd18071 |
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ... |
769-994 |
6.77e-29 |
|
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: 116.80 E-value: 6.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNL-----------------------------NGILADEMGLGKTIQTISLVtylmdrkkVMG 819
Cdd:cd18071 1 LLPHQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLI--------LAN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 820 PYLIIVPLSTLPNWVLEFEKWAP--AVGVVSYKGSPQGR--RLLqnqmraTKFNVLLTTY-----EYVIKDKAVLAKIQW 890
Cdd:cd18071 73 FTLIVCPLSVLSNWETQFEEHVKpgQLKVYTYHGGERNRdpKLL------SKYDIVLTTYntlasDFGAKGDSPLHTINW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 891 KYMIIDEGHRMKNHHCKLTQ-VLNTHyiAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFaTTGEKV 969
Cdd:cd18071 147 LRVVLDEGHQIRNPNAQQTKaVLNLS--SERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPL-TMGDPT 223
|
250 260
....*....|....*....|....*
gi 24664907 970 ELneeetiliiRRLHKVLRPFLLRR 994
Cdd:cd18071 224 GL---------KRLQVLMKQITLRR 239
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
768-957 |
7.24e-29 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 115.28 E-value: 7.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 768 TLKEYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TISLVTYLMDRKKvmGPYLIIVPLSTL-PNWVLEFEKWAPAVG 845
Cdd:smart00487 8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGKG--GRVLVLVPTRELaEQWAEELKKLGPSLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 846 VVS---YKGSPQGRRLlqNQMRATKFNVLLTTYEYVIKD--KAVLAKIQWKYMIIDEGHRMKN--HHCKLTQVLNTHYIA 918
Cdd:smart00487 83 LKVvglYGGDSKREQL--RKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24664907 919 PYRLLLTGTPLQNKLPELWALLN--FLLPSIFKSCSTFEQW 957
Cdd:smart00487 161 VQLLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
1094-1208 |
8.00e-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: 109.22 E-value: 8.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1094 GKFELLDRILPKLKatNHRVLLFCQMTQcmTIIEDYLGWRQ-FGYLRLDGTTKAEDRGELLRKFNAKGSDVfvfLLSTRA 1172
Cdd:pfam00271 1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKIDV---LVATDV 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 24664907 1173 GGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIG 1208
Cdd:pfam00271 74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| Bromo_SNF2 |
cd05519 |
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ... |
1423-1520 |
1.20e-26 |
|
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: 105.50 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1423 KKQMHKIMSAVIKH-NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIY 1501
Cdd:cd05519 2 KAAMLEIYDAVLNCeDETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANARTY 81
|
90
....*....|....*....
gi 24664907 1502 NEEASLIYLDSIALQKVFV 1520
Cdd:cd05519 82 NQEGSIVYEDAVEMEKAFK 100
|
|
| Bromodomain |
cd04369 |
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ... |
1423-1519 |
4.61e-26 |
|
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: 103.61 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1423 KKQMHKIMSAVIKHNQDgrtLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYN 1502
Cdd:cd04369 2 KKKLRSLLDALKKLKRD---LSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
|
90
....*....|....*..
gi 24664907 1503 EEASLIYLDSIALQKVF 1519
Cdd:cd04369 79 GPGSPIYKDAKKLEKLF 95
|
|
| Bromo_polybromo_V |
cd05515 |
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ... |
1436-1525 |
1.22e-25 |
|
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: 102.77 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1436 HNQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIAL 1515
Cdd:cd05515 16 TDGRGRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYKDALTL 95
|
90
....*....|
gi 24664907 1516 QKVFVGARQR 1525
Cdd:cd05515 96 QKVLLETKRE 105
|
|
| DEXHc_RAD54A |
cd18067 |
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ... |
769-994 |
1.45e-25 |
|
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: 107.17 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWL----VSLYNNNLNG-ILADEMGLGKTIQTISLVTYLM----DRKKVMGPYLIIVPLSTLPNWVLEFEK 839
Cdd:cd18067 1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLrqspQCKPEIDKAIVVSPSSLVKNWANELGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 840 W-APAVGVVSYKG--SPQGRRLLQNQMRATKFN----VLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVL 912
Cdd:cd18067 81 WlGGRLQPLAIDGgsKKEIDRKLVQWASQQGRRvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 913 NThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPF------ATTGEKVELNEEETiliiRRLHKV 986
Cdd:cd18067 161 DS-LNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPIlkgrdaDASEKERQLGEEKL----QELISI 235
|
....*...
gi 24664907 987 LRPFLLRR 994
Cdd:cd18067 236 VNRCIIRR 243
|
|
| DEXHc_HARP_SMARCAL1 |
cd18010 |
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ... |
769-948 |
5.19e-24 |
|
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: 101.90 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSlynNNLNGILADEMGLGKTIQTISLVTYLMDRkkvmGPYLIIVPLSTLPNWVLEFEKWAPAV---G 845
Cdd:cd18010 1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLppdD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 846 VVSYKGSPQGRRLLQNQmratkfnVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQV---LNTHyiAPYRL 922
Cdd:cd18010 74 IQVIVKSKDGLRDGDAK-------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAalpLLKR--AKRVI 144
|
170 180
....*....|....*....|....*.
gi 24664907 923 LLTGTPLQNKLPELWALLNFLLPSIF 948
Cdd:cd18010 145 LLSGTPALSRPIELFTQLDALDPKLF 170
|
|
| HSA |
smart00573 |
domain in helicases and associated with SANT domains; |
497-569 |
2.80e-23 |
|
domain in helicases and associated with SANT domains;
Pssm-ID: 214727 [Multi-domain] Cd Length: 73 Bit Score: 94.77 E-value: 2.80e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24664907 497 QKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERMRRLMA 569
Cdd:smart00573 1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
|
|
| Bromo_polybromo_II |
cd05517 |
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ... |
1422-1523 |
3.15e-23 |
|
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: 95.58 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1422 SKKQMHKIMSAVIKH-NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQI 1500
Cdd:cd05517 1 LKQILEQLLEAVMTAtDPSGRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKT 80
|
90 100
....*....|....*....|...
gi 24664907 1501 YNEEASLIYLDSIALQKVFVGAR 1523
Cdd:cd05517 81 FNEPGSQVYKDANAIKKIFTAKK 103
|
|
| DEXHc_ARIP4 |
cd18069 |
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ... |
769-961 |
5.44e-23 |
|
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: 99.50 E-value: 5.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTISLVTYLMdRKKVMGPYLIIVPLSTLPNWVLE 836
Cdd:cd18069 1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLL-RHTGAKTVLAIVPVNTLQNWLSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 837 FEKWAPavgvvSYKGSPQGRR------LLQNQMRATKFN------------VLLTTYE-YVIKDKAVLakiqwkyMIIDE 897
Cdd:cd18069 77 FNKWLP-----PPEALPNVRPrpfkvfILNDEHKTTAARakviedwvkdggVLLMGYEmFRLRPGPDV-------VICDE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24664907 898 GHRMKNHHCKLTQVLNtHYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAP 961
Cdd:cd18069 145 GHRIKNCHASTSQALK-NIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERP 207
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
1125-1208 |
8.18e-23 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 93.82 E-value: 8.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1125 IIEDYLGWRQFGYLRLDGTTKAEDRGELLRKFNakgSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRA 1204
Cdd:smart00490 2 ELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78
|
....
gi 24664907 1205 HRIG 1208
Cdd:smart00490 79 GRAG 82
|
|
| Bromo_polybromo_III |
cd05520 |
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ... |
1437-1518 |
1.74e-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: 90.86 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1437 NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQ 1516
Cdd:cd05520 17 NNQGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKLQ 96
|
..
gi 24664907 1517 KV 1518
Cdd:cd05520 97 KL 98
|
|
| DEXHc_TTF2 |
cd18072 |
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ... |
769-994 |
2.32e-20 |
|
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: 92.16 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSLYNNNLNG-ILADEMGLGKTIQTISLVTYLMDRKK----------------------VMGPYLIIV 825
Cdd:cd18072 1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkdstlvPSAGTLVVC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 826 PLSTLPNWVLEFEKW--APAVGVVSYKGSpqgrrllqNQMRATK----FNVLLTTYEYVIKD---------KAVLAKIQW 890
Cdd:cd18072 81 PASLVHQWKNEVESRvaSNKLRVCLYHGP--------NRERIGEvlrdYDIVITTYSLVAKEiptykeesrSSPLFRIAW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 891 KYMIIDEGHRMKNHH-------CKLTqvlnthyiAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFA 963
Cdd:cd18072 153 ARIILDEAHNIKNPKvqasiavCKLR--------AHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSR 224
|
250 260 270
....*....|....*....|....*....|.
gi 24664907 964 TTGEkvelneeetiliirRLHKVLRPFLLRR 994
Cdd:cd18072 225 KGGE--------------RLNILTKSLLLRR 241
|
|
| Bromo_polybromo_IV |
cd05518 |
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ... |
1422-1518 |
7.98e-20 |
|
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: 85.96 E-value: 7.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1422 SKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQI 1500
Cdd:cd05518 1 RKKRMLALFLYVLEYREgSGRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARH 80
|
90
....*....|....*...
gi 24664907 1501 YNEEASLIYLDSIALQKV 1518
Cdd:cd05518 81 YNEEGSQVYEDANILEKV 98
|
|
| DEXDc_RapA |
cd18011 |
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ... |
791-948 |
1.52e-19 |
|
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: 88.89 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 791 ILADEMGLGKTIQTISLVTYLMDRKKVmGPYLIIVPLSTLPNWVLE-FEKWAPAVGVVSYKGSPQGRRLLQNQMRAtkFN 869
Cdd:cd18011 21 LLADEVGLGKTIEAGLIIKELLLRGDA-KRVLILCPASLVEQWQDElQDKFGLPFLILDRETAAQLRRLIGNPFEE--FP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 870 VLLTTYEYV---IKDKAVLAKIQWKYMIIDEGHRMKNHHC-------KLTQVLNTHyiAPYRLLLTGTPLQNKLPELWAL 939
Cdd:cd18011 98 IVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKR--ARHVLLLTATPHNGKEEDFRAL 175
|
....*....
gi 24664907 940 LNFLLPSIF 948
Cdd:cd18011 176 LSLLDPGRF 184
|
|
| SnAC |
pfam14619 |
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ... |
1305-1371 |
4.06e-19 |
|
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: 82.69 E-value: 4.06e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664907 1305 RKKEDEEIHPGRERLIDESELPDWLTKDDDEVERFHYQYDEDTILGRGSRQRKEVDYTDSLTEKEWL 1371
Cdd:pfam14619 3 RREEAEQLPPLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
|
|
| DEXHc_ATRX |
cd18068 |
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ... |
790-982 |
5.92e-19 |
|
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: 88.02 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 790 GILADEMGLGKTIQTISLV-TYLM-DRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVG---------VVSYKgSPQGRRL 858
Cdd:cd18068 31 CILAHCMGLGKTLQVVTFLhTVLLcEKLENFSRVLVVCPLNTVLNWLNEFEKWQEGLKdeekievneLATYK-RPQERSY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 859 LQNQMRATKfNVLLTTYEYV--------IKDKAVLAKIQWKYM--------IIDEGHRMKNHHCKLTQVLNThYIAPYRL 922
Cdd:cd18068 110 KLQRWQEEG-GVMIIGYDMYrilaqernVKSREKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNS-IRTKRRI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 923 LLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFaTTGEKVELNEEETILIIRR 982
Cdd:cd18068 188 VLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPI-QNGQCADSTLVDVRVMKKR 246
|
|
| Bromo_polybromo_I |
cd05524 |
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ... |
1427-1526 |
6.02e-19 |
|
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: 83.92 E-value: 6.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1427 HKIMSAVIKH-NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEA 1505
Cdd:cd05524 8 QELYDTIRNYkSEDGRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPD 87
|
90 100
....*....|....*....|.
gi 24664907 1506 SLIYLDSIALQKVFVGARQRI 1526
Cdd:cd05524 88 SPEHKDACKLWELFLSARNEV 108
|
|
| HSA |
pfam07529 |
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ... |
498-564 |
1.67e-18 |
|
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.
Pssm-ID: 462194 [Multi-domain] Cd Length: 67 Bit Score: 81.08 E-value: 1.67e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664907 498 KLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERM 564
Cdd:pfam07529 1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
|
|
| COG5076 |
COG5076 |
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ... |
1401-1520 |
1.41e-17 |
|
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];
Pssm-ID: 227408 [Multi-domain] Cd Length: 371 Bit Score: 86.78 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1401 EESDDDslILKRRRRQNLDKRSKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDC 1479
Cdd:COG5076 124 AHLKTS--VKKRKTPKIEDELLYADNKAIAKFKKQLFLrDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNG 201
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24664907 1480 KYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVFV 1520
Cdd:COG5076 202 RYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFL 242
|
|
| BRK |
pfam07533 |
BRK domain; The function of this domain is unknown. It is often found associated with ... |
646-687 |
1.34e-16 |
|
BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.
Pssm-ID: 462196 Cd Length: 44 Bit Score: 74.85 E-value: 1.34e-16
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 24664907 646 ADMRVHVVEQCTGKKLTGDDAPMLKHLHRWLNMHPGWDWIDD 687
Cdd:pfam07533 3 GDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
|
|
| Bromodomain |
pfam00439 |
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ... |
1428-1512 |
1.52e-16 |
|
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: 76.20 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1428 KIMSAVIKHNqdgrtLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASL 1507
Cdd:pfam00439 3 EILDKLMEHP-----IAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSV 77
|
....*
gi 24664907 1508 IYLDS 1512
Cdd:pfam00439 78 IYKAA 82
|
|
| BRK |
smart00592 |
domain in transcription and CHROMO domain helicases; |
645-689 |
2.93e-16 |
|
domain in transcription and CHROMO domain helicases;
Pssm-ID: 197800 Cd Length: 45 Bit Score: 73.92 E-value: 2.93e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 24664907 645 VADMRVHVVEQCTGKKLTGDDAPMLKHLHRWLNMHPGWDWIDDEE 689
Cdd:smart00592 1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
|
|
| Bromo_ASH1 |
cd05525 |
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ... |
1429-1524 |
9.96e-15 |
|
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: 71.65 E-value: 9.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1429 IMSAVIKH-NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASL 1507
Cdd:cd05525 10 ICDAIITYkDSNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSP 89
|
90
....*....|....*..
gi 24664907 1508 IYLDSIALQKVFVGARQ 1524
Cdd:cd05525 90 IGRDVCRLRKAYYQAKH 106
|
|
| Bromo_gcn5_like |
cd05509 |
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ... |
1425-1520 |
2.69e-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: 70.28 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1425 QMHKIMSAVIKHNQdgrtlSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEE 1504
Cdd:cd05509 5 QLKKVLDSLKNHKS-----AWPFLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGP 79
|
90
....*....|....*.
gi 24664907 1505 ASLIYLDSIALQKVFV 1520
Cdd:cd05509 80 DTEYYKCANKLEKFFW 95
|
|
| Bromo_Rsc1_2_II |
cd05522 |
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ... |
1430-1519 |
2.72e-13 |
|
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: 67.27 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1430 MSAVIKH-----NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEE 1504
Cdd:cd05522 6 IKNILKGlrkerDENGRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNEN 85
|
90
....*....|....*
gi 24664907 1505 ASLIYLDSIALQKVF 1519
Cdd:cd05522 86 DSQEYKDAVLLEKEA 100
|
|
| Bromo_Acf1_like |
cd05504 |
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ... |
1412-1520 |
5.06e-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: 67.04 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1412 RRRRQNLD-KRSKKQMHKIMSAVIKHNQdgrtlSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKD 1490
Cdd:cd05504 2 RRSEGRHHgPLNLSALEQLLVEIVKHKD-----SWPFLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSD 76
|
90 100 110
....*....|....*....|....*....|
gi 24664907 1491 FMQLCQNAQIYNEEASLIYLDSIALQKVFV 1520
Cdd:cd05504 77 IQLVFSNCFLYNPEHTSVYKAGTRLQRFFI 106
|
|
| DEXQc_bact_SNF2 |
cd18013 |
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ... |
769-959 |
4.43e-12 |
|
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: 67.37 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVSlynNNLNGILADeMGLGKTIQTISLVTYLMDRKKVmGPYLIIVPLSTLPN-WVLEFEKWAPAVG-- 845
Cdd:cd18013 1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQLDDFT-RRVLVIAPLRVARStWPDEVEKWNHLRNlt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 846 VVSYKGSPQGRRLLQNqmraTKFNVLLTTYEYVIK-DKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHyiAPY--RL 922
Cdd:cd18013 76 VSVAVGTERQRSKAAN----TPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKV--RPVikRL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24664907 923 L-LTGTPLQNKLPELWALLNFL--LPSIFKSCSTF-EQWFN 959
Cdd:cd18013 150 IgLTGTPSPNGLMDLWAQIALLdqGERLGRSITAYrERWFD 190
|
|
| DEXQc_SHPRH |
cd18070 |
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ... |
769-958 |
1.89e-11 |
|
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: 66.21 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLEWLVslynnNLNGILADEMGLGKTIQTISLV------------TYLMDRKKVM-------------GPYLI 823
Cdd:cd18070 1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCcpdclvaetpvssKATLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 824 IVPLSTLPNWVLEFEKWAP-AVGVVSYKG--------SPQGRRLLQNQMRATKFNVL---------------LTTYEYVI 879
Cdd:cd18070 76 VCPSAILAQWLDEINRHVPsSLKVLTYQGvkkdgalaSPAPEILAEYDIVVTTYDVLrtelhyaeanrsnrrRRRQKRYE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 880 KDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQ-VLNTHYIApyRLLLTGTPLQNKLPELWALLNFLLPSIFksCSTFEQWF 958
Cdd:cd18070 156 APPSPLVLVEWWRVCLDEAQMVESSTSKAAEmARRLPRVN--RWCVSGTPIQRGLDDLFGLLSFLGVEPF--CDSDWWAR 231
|
|
| Bromo_Rsc1_2_I |
cd05521 |
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ... |
1437-1517 |
3.80e-11 |
|
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: 61.57 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1437 NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEdcKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQ 1516
Cdd:cd05521 18 EENGIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLAQIPWNARLYNTKGSVIYKYALILE 95
|
.
gi 24664907 1517 K 1517
Cdd:cd05521 96 K 96
|
|
| Bromo_brd7_like |
cd05513 |
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ... |
1457-1509 |
3.52e-10 |
|
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: 58.58 E-value: 3.52e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 24664907 1457 PDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIY 1509
Cdd:cd05513 32 PGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNKPDTIYY 84
|
|
| Bromo_Brdt_I_like |
cd05497 |
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ... |
1456-1527 |
9.37e-10 |
|
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: 57.43 E-value: 9.37e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24664907 1456 LPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVFvgaRQRIT 1527
Cdd:cd05497 37 LPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPGDDVVLMAQTLEKLF---LQKLA 105
|
|
| Bromo_Brdt_II_like |
cd05498 |
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ... |
1456-1519 |
3.28e-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: 55.75 E-value: 3.28e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24664907 1456 LPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVF 1519
Cdd:cd05498 35 LHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVF 98
|
|
| Bromo_cbp_like |
cd05495 |
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ... |
1444-1520 |
2.19e-08 |
|
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: 53.60 E-value: 2.19e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24664907 1444 SEPFMKL--PSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVFV 1520
Cdd:cd05495 22 SLPFRQPvdPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRVYKYCTKLAEVFE 100
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
721-928 |
2.44e-08 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 58.88 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 721 NDEDAKDLITKAKVEDDEYRTEEQTYYSIAHTIHEKVVEQASIMVNGTLKEYQIKGLE-WLVSLYNNNLNGILADEMGLG 799
Cdd:COG1061 33 NLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 800 KTIQTISLVTYLMDRKKVmgpyLIIVPLSTLPN-WVLEFEKWAPAVGVVSYKgspqgrrllqnqmRATKFNVLLTTYEYV 878
Cdd:COG1061 113 KTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGDPLAGGGK-------------KDSDAPITVATYQSL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24664907 879 IKdKAVLAKIQ--WKYMIIDEGHrmknhHC---KLTQVLNtHYIAPYRLLLTGTP 928
Cdd:COG1061 176 AR-RAHLDELGdrFGLVIIDEAH-----HAgapSYRRILE-AFPAAYRLGLTATP 223
|
|
| ResIII |
pfam04851 |
Type III restriction enzyme, res subunit; |
768-928 |
3.52e-08 |
|
Type III restriction enzyme, res subunit;
Pssm-ID: 398492 [Multi-domain] Cd Length: 162 Bit Score: 54.60 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 768 TLKEYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTISLVTYLM---DRKKVmgpyLIIVP-LSTLPNWVLEFEKWAP 842
Cdd:pfam04851 3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFkkgPIKKV----LFLVPrKDLLEQALEEFKKFLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 843 AVGVVSYKGSPQGRRLLQNQMRatkfnVLLTTYE--YVIKDKAVLAKI--QWKYMIIDEGHRM--KNHhcklTQVLNtHY 916
Cdd:pfam04851 79 NYVEIGEIISGDKKDESVDDNK-----IVVTTIQslYKALELASLELLpdFFDVIIIDEAHRSgaSSY----RNILE-YF 148
|
170
....*....|..
gi 24664907 917 IAPYRLLLTGTP 928
Cdd:pfam04851 149 KPAFLLGLTATP 160
|
|
| Bromo_brd1_like |
cd05512 |
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ... |
1457-1516 |
5.05e-08 |
|
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: 52.40 E-value: 5.05e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1457 PDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQ 1516
Cdd:cd05512 32 PDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDTIFYRAAVRLR 91
|
|
| Bromo_AAA |
cd05528 |
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ... |
1457-1502 |
6.93e-08 |
|
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: 52.36 E-value: 6.93e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 24664907 1457 PDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYN 1502
Cdd:cd05528 34 PDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
|
|
| Bromo_SPT7_like |
cd05510 |
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ... |
1444-1506 |
1.09e-07 |
|
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: 51.67 E-value: 1.09e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24664907 1444 SEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEAS 1506
Cdd:cd05510 26 STPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYNSDPS 88
|
|
| Bromo_TFIID |
cd05511 |
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ... |
1444-1506 |
3.85e-07 |
|
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: 50.34 E-value: 3.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24664907 1444 SEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEAS 1506
Cdd:cd05511 18 SWPFHTPVNKKKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDS 80
|
|
| Bromo_BDF1_2_II |
cd05499 |
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ... |
1443-1519 |
3.93e-07 |
|
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: 49.98 E-value: 3.93e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24664907 1443 LSEPFMKL--PSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVF 1519
Cdd:cd05499 20 YNWPFLDPvdPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVF 98
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
769-928 |
5.37e-07 |
|
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: 50.77 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 769 LKEYQIKGLE-WLvsLYNNNLNGILADEMGLGKTIQTISLVTYLMdRKKVmgpyLIIVPLSTLPN-WVLEFEKWAP--AV 844
Cdd:cd17926 1 LRPYQEEALEaWL--AHKNNRRGILVLPTGSGKTLTALALIAYLK-ELRT----LIVVPTDALLDqWKERFEDFLGdsSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 845 GVVSYKgspqgrrllqNQMRATKFNVLLTTYEYVIKDKAVLAKI--QWKYMIIDEGHrmknHHC--KLTQVLnTHYIAPY 920
Cdd:cd17926 74 GLIGGG----------KKKDFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAH----HLPakTFSEIL-KELNAKY 138
|
....*...
gi 24664907 921 RLLLTGTP 928
Cdd:cd17926 139 RLGLTATP 146
|
|
| Bromo_BAZ2A_B_like |
cd05503 |
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ... |
1446-1519 |
2.57e-06 |
|
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: 47.37 E-value: 2.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24664907 1446 PFMkLPSRQRL-PDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVF 1519
Cdd:cd05503 20 PFL-EPVNTKLvPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFF 93
|
|
| Bromo_BDF1_2_I |
cd05500 |
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ... |
1422-1519 |
2.99e-06 |
|
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: 47.31 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1422 SKKQmHKIMSAVIKHNQDGRTlSEPFMKL--PSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQ 1499
Cdd:cd05500 2 TKHQ-HKFLLSSIRSLKRLKD-ARPFLVPvdPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCL 79
|
90 100
....*....|....*....|
gi 24664907 1500 IYNEEASLIYLDSIALQKVF 1519
Cdd:cd05500 80 TFNGPEHPVSQMGKRLQAAF 99
|
|
| Bromo_tif1_like |
cd05502 |
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ... |
1443-1519 |
3.41e-06 |
|
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: 47.29 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1443 LSEPFMKlPSRQRLPDYYEIIKRPVD---IKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVF 1519
Cdd:cd05502 21 LSLPFHE-PVSPSVPNYYKIIKTPMDlslIRKKLQPKSPQHYSSPEEFVADVRLMFKNCYKFNEEDSEVAQAGKELELFF 99
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
473-647 |
8.55e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 473 IKLYKRTKRQGLREARATE----KLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANA 548
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 549 EREQKKEQEriEKERMRRLMAEDEEGyRKLIDQKK----DKRLAFLLSQTDEYISNLTQMVK------QHKDDQMKKKEE 618
Cdd:PTZ00121 1678 EEAKKAEED--EKKAAEALKKEAEEA-KKAEELKKkeaeEKKKAEELKKAEEENKIKAEEAKkeaeedKKKAEEAKKDEE 1754
|
170 180
....*....|....*....|....*....
gi 24664907 619 EGKRLIQFKKELLMSGEYIGIDEGSIVAD 647
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-639 |
8.72e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 401 ITLLQERENRIAARISLRMQELQRLpATMSEDLRLQAAIELRALRVLNFQRQLrmefvqctrRDTTLETALNIKLYKRTK 480
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEE---------LEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 481 RQGLREARATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFhRNNKAQLARMNKAVMNHHANAEREQKKEQERIE 560
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24664907 561 KERMRRLMAEDEEGYRKLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKELLMSGEYIGI 639
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| Bromo_WDR9_II |
cd05496 |
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ... |
1444-1519 |
2.46e-05 |
|
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: 45.14 E-value: 2.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664907 1444 SEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYN-EEASLIYLDSIALQKVF 1519
Cdd:cd05496 23 SEPFRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
403-641 |
3.99e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 403 LLQERENRIAARISLRMQELQRLPatmsEDLRLQAAIELRALRVLNFQRQLRMEFVQ----CTRRDTTLETALNIKLYKR 478
Cdd:pfam02463 178 LIEETENLAELIIDLEELKLQELK----LKEQAKKALEYYQLKEKLELEEEYLLYLDylklNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 479 TKRQGLREARAtEKLEKQQKLEAERKRRQKHLEFLAAVLQhgkDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQER 558
Cdd:pfam02463 254 ESSKQEIEKEE-EKLAQVLKENKEEEKEKKLQEEELKLLA---KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 559 IEKERmrrlmaEDEEGYRKLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKELLMSGEYIG 638
Cdd:pfam02463 330 LKKEK------EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
...
gi 24664907 639 IDE 641
Cdd:pfam02463 404 EKE 406
|
|
| QLQ |
pfam08880 |
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ... |
169-198 |
4.86e-05 |
|
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.
Pssm-ID: 462622 Cd Length: 35 Bit Score: 41.94 E-value: 4.86e-05
10 20 30
....*....|....*....|....*....|
gi 24664907 169 HLNGNQVNLLRTQITAYRLLARNKPISMQM 198
Cdd:pfam08880 1 PFTPAQLQELRAQILAYKYLSRNQPVPPEL 30
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
405-587 |
6.42e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.22 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 405 QERENRIAARISLRMQELQRLPATMSEDLRLQAAIE-LRALRVlnfqrqlrMEFVQCTRRDTTLETALNiklyKRTKRQG 483
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDeLRAKLY--------QEEQERKERQKEREEAEK----KARQRQE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 484 LREARATEKLEKQQKLEAERKRRQkhlEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHAN--AEREQKKEQERIEK 561
Cdd:pfam13868 237 LQQAREEQIELKERRLAEEAEREE---EEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKqiEEREEQRAAEREEE 313
|
170 180
....*....|....*....|....*.
gi 24664907 562 ERMRRLMAEDEEGYRKLIDQKKDKRL 587
Cdd:pfam13868 314 LEEGERLREEEAERRERIEEERQKKL 339
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
1161-1211 |
6.71e-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: 42.69 E-value: 6.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 24664907 1161 SDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRN 1211
Cdd:cd18785 20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
|
|
| QLQ |
smart00951 |
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ... |
168-198 |
6.74e-05 |
|
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.
Pssm-ID: 214931 Cd Length: 36 Bit Score: 41.36 E-value: 6.74e-05
10 20 30
....*....|....*....|....*....|..
gi 24664907 168 QHLNGNQVNLLRTQITAYR-LLARNKPISMQM 198
Cdd:smart00951 1 SPFTPAQLELLRAQILAYKyLLARNQPVPPEL 32
|
|
| Bromo_brd8_like |
cd05507 |
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ... |
1420-1502 |
8.83e-05 |
|
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: 43.12 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1420 KRSKKQMHKIMSAVIKHNQdgrtlSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQ 1499
Cdd:cd05507 2 RAWKKAILLVYRTLASHRY-----ASVFLKPVTEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAI 76
|
...
gi 24664907 1500 IYN 1502
Cdd:cd05507 77 MYN 79
|
|
| Bromo_WSTF_like |
cd05505 |
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ... |
1423-1508 |
1.11e-04 |
|
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: 42.91 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1423 KKQMHKIMSAVIKHNQdgrtlSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYN 1502
Cdd:cd05505 2 LQKCEEILSKILKYRF-----SWPFREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYY 76
|
....*.
gi 24664907 1503 EEASLI 1508
Cdd:cd05505 77 ENGSYV 82
|
|
| Bromo_plant1 |
cd05506 |
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ... |
1424-1519 |
1.20e-04 |
|
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: 42.70 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1424 KQMHKIMSAVIKHnQDGRTLSEPFMklPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNE 1503
Cdd:cd05506 3 KQCGTLLRKLMKH-KWGWVFNAPVD--VVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNP 79
|
90
....*....|....*.
gi 24664907 1504 EASLIYLDSIALQKVF 1519
Cdd:cd05506 80 PGNDVHTMAKELLKIF 95
|
|
| Bromo_polybromo_VI |
cd05526 |
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which ... |
1423-1527 |
1.63e-04 |
|
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: 42.74 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1423 KKQMHKIMSAVIKH-NQDGRTLSEPFMKLPSRQRLPDYYEiiKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIY 1501
Cdd:cd05526 5 QELLATLFVSVMNHqDEEGRCYSDSLAELPELAVDGVGPK--KIPLTLDIIKRNVDKGRYRRLDKFQEDMFEVLERARRL 82
|
90 100
....*....|....*....|....*.
gi 24664907 1502 NEEASLIYLDSIALQKVFVGARQRIT 1527
Cdd:cd05526 83 SRTDSEIYEDAVELQQFFIKIRDELC 108
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
481-632 |
1.79e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.10 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 481 RQGLREARAtekleKQQKLEAERKRRQKHleflaavlqhgkdlrEFHRNNKAQLARMNKavMNHHANAEREQKKEQERIE 560
Cdd:pfam15709 335 RDRLRAERA-----EMRRLEVERKRREQE---------------EQRRLQQEQLERAEK--MREELELEQQRRFEEIRLR 392
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24664907 561 KERMR--RLMAEDEEGYRKLIDQKKDKRLAfllSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRliqfKKELLM 632
Cdd:pfam15709 393 KQRLEeeRQRQEEEERKQRLQLQAAQERAR---QQQEEFRRKLQELQRKKQQEEAERAEAEKQR----QKELEM 459
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
447-565 |
2.80e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 447 LNFQRQLRMEFVQCTRRDTTLETALniKLYKRTKRQGLrearATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGK-DLRE 525
Cdd:PRK11637 164 LNQARQETIAELKQTREELAAQKAE--LEEKQSQQKTL----LYEQQAQQQKLEQARNERKKTLTGLESSLQKDQqQLSE 237
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 24664907 526 FhRNNKAQLarmnkavMNHHANAEREQKK--EQERIEKERMR 565
Cdd:PRK11637 238 L-RANESRL-------RDSIARAEREAKAraEREAREAARVR 271
|
|
| Bromo_WDR9_I_like |
cd05529 |
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ... |
1428-1508 |
3.07e-04 |
|
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: 42.32 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 1428 KIMSAVIKHNQDG-RTLSEPFM-KLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEA 1505
Cdd:cd05529 28 RLISGLDKLLLSLqLEIAEYFEyPVDLRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPN 107
|
...
gi 24664907 1506 SLI 1508
Cdd:cd05529 108 SEI 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
480-629 |
4.03e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 480 KRQGLREARATEKLEKQQKLEAERKRRQKHLEFL----AAVLQHGKDLREFHRNNKAQLARMN-----KAVMNHHANAER 550
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaeEARIEEVMKLYEEEKKMKAEEAKKAeeakiKAEELKKAEEEK 1632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 551 ---EQKKEQERIEKERMRRLMAEDEEGYRKLIDQKK----DKRLAFLLSQTDEYisnltqmvKQHKDDQMKKKEEEGKRL 623
Cdd:PTZ00121 1633 kkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeeDKKKAEEAKKAEED--------EKKAAEALKKEAEEAKKA 1704
|
....*.
gi 24664907 624 IQFKKE 629
Cdd:PTZ00121 1705 EELKKK 1710
|
|
| Pro-rich |
pfam15240 |
Proline-rich protein; This family includes several eukaryotic proline-rich proteins. |
243-397 |
7.13e-04 |
|
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
Pssm-ID: 464580 [Multi-domain] Cd Length: 167 Bit Score: 41.95 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 243 QPPPSAGTPPQCSTPPASNPYGPPVPGQKMQVAPPPPHMQQgqplppqppqvggpppiqqqqppqqqqqqsqppppephq 322
Cdd:pfam15240 55 PPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPR--------------------------------------- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24664907 323 hqlPNGGKPLSMGPSGG-QPLIPSSPMQPQVrgtlPGMPPGSQVPQPGGGPQRQVPPAGMPMPKPNRITTVAKPVG 397
Cdd:pfam15240 96 ---PPPGKPQGPPPQGGnQQQGPPPPGKPQG----PPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRPPQPGNPQG 164
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
247-394 |
8.25e-04 |
|
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: 44.37 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 247 SAGTPPQC-STPPASNPYGPPVPGQKMQVAPPPPHMQQGQPLPPQPPQVGGPPPIQQQQPPQQQQQQSQPPPPEPHQHQL 325
Cdd:pfam03154 196 TAGPTPSApSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQM 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 326 PNGGKPLSMGPS----------------GGQPLIPSSPmQPQVRG---TLPGMPPGSQVPQPGGGPQRQ-VPPAGMPMP- 384
Cdd:pfam03154 276 PPMPHSLQTGPShmqhpvppqpfpltpqSSQSQVPPGP-SPAAPGqsqQRIHTPPSQSQLQSQQPPREQpLPPAPLSMPh 354
|
170
....*....|.
gi 24664907 385 -KPNRITTVAK 394
Cdd:pfam03154 355 iKPPPTTPIPQ 365
|
|
| MISS |
pfam15822 |
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ... |
245-386 |
9.74e-04 |
|
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.
Pssm-ID: 318115 [Multi-domain] Cd Length: 238 Bit Score: 42.67 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 245 PPSAGTPP-----QCSTPPASNPYGPP-VPGQKMQVAPPPPHMQQGQPLPpqppqvggpppiqqqqppqqqqqqsqpppp 318
Cdd:pfam15822 75 GPSPGPPApfppsGPSCPPPGGPYPAPtVPGPGPIGPYPTPNMPFPELPR------------------------------ 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 319 ephqhqlPNGG--KPLSMGPSGGQPLIPSSPMQPqvrgTLPGMPPGSQVPQPGGGPQRQVPPAGMPMPKP 386
Cdd:pfam15822 125 -------PYGAptDPAAAAPSGPWGSMSSGPWAP----GMGGQYPAPNMPYPSPGPYPAVPPPQSPGAAP 183
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
474-760 |
1.33e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 474 KLYKRTKRQGLREARATEKLEKQQKLEAERKRRQKHleflAAVLQHGKDLREFHRnnKAQLARMNKAVMNHHANAEREQK 553
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK----NMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKK 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 554 KEQERIEKERMRRlmaedEEGYRKLIDQKKDKRlafllsqtDEYISNLTQMVKQH-----KDDQMKKKEEEGKRliqfKK 628
Cdd:PTZ00121 1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKKE--------AEEKKKAEELKKAEeenkiKAAEEAKKAEEDKK----KA 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 629 ELLMSGEyigidegsivaDMRVHVVEQCTGKKLTGDDAPMLKHLHRwlnmhpgwDWIDDEEDSCGSNDDHKPKVEEQPTA 708
Cdd:PTZ00121 1678 EEAKKAE-----------EDEKKAAEALKKEAEEAKKAEELKKKEA--------EEKKKAEELKKAEEENKIKAEEAKKE 1738
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24664907 709 TEDATDKAQATGNDEDAKDLITKAKVEddEYRTEEQTYYSIAHTIHEKVVEQ 760
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEEKKKIAHLKKE--EEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
402-573 |
1.95e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 402 TLLQERENRIAARislrmqelQRLPATMSEDLRLQAAielRALRVLNFQRQLRMEFVQctrRDTTLETALNIKLYKRTKR 481
Cdd:pfam15709 323 ALLEKREQEKASR--------DRLRAERAEMRRLEVE---RKRREQEEQRRLQQEQLE---RAEKMREELELEQQRRFEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 482 QGLREARATEklEKQQKLEAERKRrqkHLEFLAAVLQHGKDLREFHRNNKaQLARMNKAVMNHHANAEREQKKEQERIEK 561
Cdd:pfam15709 389 IRLRKQRLEE--ERQRQEEEERKQ---RLQLQAAQERARQQQEEFRRKLQ-ELQRKKQQEEAERAEAEKQRQKELEMQLA 462
|
170
....*....|..
gi 24664907 562 ERMRRLMAEDEE 573
Cdd:pfam15709 463 EEQKRLMEMAEE 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
403-573 |
1.97e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 403 LLQERENRIA-----ARISLRMQELQrlpatmsEDLRlQAAIELRALRVLNFQRQLRMEFVQCTRRDTTLETALNIKLYK 477
Cdd:COG1196 194 ILGELERQLEplerqAEKAERYRELK-------EELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 478 RTKRQGLREARATEKLEKQQKLEAERKRRQKHLEfLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQE 557
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELAR-LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170
....*....|....*.
gi 24664907 558 RIEKERMRRLMAEDEE 573
Cdd:COG1196 345 ELEEAEEELEEAEAEL 360
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
363-607 |
1.98e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 363 SQVPQPGGGP---QRQVPPAGMPMPKPNRITTVAKPVGLDPITLLQERENRIAARISLRMQELQRLPATMSEDLRLQAAI 439
Cdd:TIGR02794 26 SVKPEPGGGAeiiQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 440 --ELRALRVLNFQRQLrmefvqctrrdttLETALNIKLYKRTKRQGLREARATEKLEKQQKLEAERKR----RQKHLEFL 513
Cdd:TIGR02794 106 qaEQAAKQAEEKQKQA-------------EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAaaeaKKKAEEAK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 514 AAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERMRRLMAEDEEGYRKL--------IDQKKDK 585
Cdd:TIGR02794 173 KKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIfglasgsnAEKQGGA 252
|
250 260
....*....|....*....|..
gi 24664907 586 RLAFLLSQTDEYISNLTQMVKQ 607
Cdd:TIGR02794 253 RGAAAGSEVDKYAAIIQQAIQQ 274
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
251-384 |
3.27e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 42.36 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 251 PPQCSTPPASNPYGPPVPGQKMQVAPPPphmqqgqplpPQPPQVGGPPPIQQQQPPQQQQQQSQPPPPEPhqhqlPNGGK 330
Cdd:PHA03378 696 PPPRAPTPMRPPAAPPGRAQRPAAATGR----------ARPPAAAPGRARPPAAAPGRARPPAAAPGRAR-----PPAAA 760
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 24664907 331 PLSMGPSGGQPLIPsSPMQPqvrgtlPGMPPGSQvPQPGGGPQRQVPPAGMPMP 384
Cdd:PHA03378 761 PGRARPPAAAPGAP-TPQPP------PQAPPAPQ-QRPRGAPTPQPPPQAGPTS 806
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
474-630 |
3.55e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 474 KLYKRTKRQGLREARATEKLEKQ-QKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQ 552
Cdd:COG4717 57 ELFKPQGRKPELNLKELKELEEElKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24664907 553 KKEQERIEKERMRRLMAEDEEgYRKLIDQKKDKRLAflLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKEL 630
Cdd:COG4717 137 LEAELAELPERLEELEERLEE-LRELEEELEELEAE--LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
789-927 |
3.63e-03 |
|
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: 39.69 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 789 NGILADEMGLGKTIQ-TISLVTYLMD-RKKVmgpyLIIVPLSTLPN----WVLEFEKWAPAVGVVSYKGSPQGRRLLQNQ 862
Cdd:cd00046 3 NVLITAPTGSGKTLAaLLAALLLLLKkGKKV----LVLVPTKALALqtaeRLRELFGPGIRVAVLVGGSSAEEREKNKLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24664907 863 mratKFNVLLTTYEYVIKDKAVLAKI---QWKYMIIDEGHRM----KNHHCKLTQVLNTHYIAPYRLLLTGT 927
Cdd:cd00046 79 ----DADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILLSAT 146
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
404-625 |
4.26e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 404 LQERENRIAARISLRMQELQRLPATMSEDLRLQAAIELRALRVlnfQRQLRMEFVQCTRRDTTLETALNIKLYKRTKRQG 483
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA---LQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 484 LREARATEK-LEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERI--- 559
Cdd:TIGR00618 269 IEELRAQEAvLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllq 348
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 560 ----EKERMRRlMAEDEEGYRKLIDQKKDKRLAFLLSQTDeyISNLTQMVKQHKDDQMKKKEEEGKRLIQ 625
Cdd:TIGR00618 349 tlhsQEIHIRD-AHEVATSIREISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDILQREQATIDTR 415
|
|
| Drf_FH1 |
pfam06346 |
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ... |
247-386 |
4.96e-03 |
|
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.
Pssm-ID: 461881 [Multi-domain] Cd Length: 157 Bit Score: 39.47 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 247 SAGTPPqcsTPP----ASNPYGPPVPGQKmQVAPPPPhmqqgqplppqppqvggpppiqqqqppqqqqqqSQPPPPEPHQ 322
Cdd:pfam06346 42 SAAIPP---PPPlpggTSIPPPPPLPGAA-SIPPPPP---------------------------------LPGSTGIPPP 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24664907 323 HQLPNG-GKPLSMGPSGGQPLIPSSPmqPQVRGTlPGMPPGSQVPqpgGGPQRQVPPAGMPMPKP 386
Cdd:pfam06346 85 PPLPGGaGIPPPPPPLPGGAGVPPPP--PPLPGG-PGIPPPPPFP---GGPGIPPPPPGMGMPPP 143
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
406-582 |
5.03e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.18 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 406 ERENRIAARISLRMQELQRlpatMSEdLRLQAAIELRALRVLNFQRQLRME------FVQCTR--------RDTTLETAL 471
Cdd:pfam15558 4 ERDRKIAALMLARHKEEQR----MRE-LQQQAALAWEELRRRDQKRQETLErerrllLQQSQEqwqaekeqRKARLGREE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 472 NIKLYKRTKRQGLREARATEKLEKQQKL----------EAE-RKRRQKHLefLAAVLQHGKDLREfhRNNKAQLARMNKA 540
Cdd:pfam15558 79 RRRADRREKQVIEKESRWREQAEDQENQrqeklerarqEAEqRKQCQEQR--LKEKEEELQALRE--QNSLQLQERLEEA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24664907 541 VMNHHANAEREQKKEQ-----ERIEKERMRRLMA----EDEEGYRKLIDQK 582
Cdd:pfam15558 155 CHKRQLKEREEQKKVQennlsELLNHQARKVLVDcqakAEELLRRLSLEQS 205
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
482-625 |
5.59e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 482 QGLREARATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQK-------- 553
Cdd:pfam13868 161 LKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARqrqelqqa 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 554 ---------------KEQERIEKERMRRLMAEDEEGYRKLIDQKKDKRLafllsQTDEYISNLTQMVKQHKDDQMKKKEE 618
Cdd:pfam13868 241 reeqielkerrlaeeAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL-----EHRRELEKQIEEREEQRAAEREEELE 315
|
....*..
gi 24664907 619 EGKRLIQ 625
Cdd:pfam13868 316 EGERLRE 322
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
406-630 |
6.33e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 406 ERENRIAARISLRMQELQRLPATMSEDLRLQAAIELRALRVLNFQRQLRMEFVQctrrdtTLETALNIKLYKRTKRQGLR 485
Cdd:pfam17380 313 ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIR------QEEIAMEISRMRELERLQME 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664907 486 EARATEKLekQQKLEAERKrrQKHLEflaavlqhgkdlREFHRNNKAQLARMNKAvmnhhanaereqKKEQERIEKERMR 565
Cdd:pfam17380 387 RQQKNERV--RQELEAARK--VKILE------------EERQRKIQQQKVEMEQI------------RAEQEEARQREVR 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664907 566 RLMAEDEEGYR--KLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDdqmKKKEEEGKRLIqFKKEL 630
Cdd:pfam17380 439 RLEEERAREMErvRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD---RKRAEEQRRKI-LEKEL 501
|
|
| |
