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Conserved domains on  [gi|63054463|ref|NP_588472|]
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SWI/SNF ATP-dependent chromatin remodeler Snf22 [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
866-1098 7.03e-167

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: 503.83  E-value: 7.03e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  866 GGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVK 945
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  946 KIAYKGPPQLRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYYHSQYRLILT 1025
Cdd:cd17996   81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054463 1026 GTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGGQDKIGLNEEEALLIIKRLHKVLRPFLFRRLK 1098
Cdd:cd17996  161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLIIRRLHKVLRPFLLRRLK 233
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
753-1345 5.51e-165

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 528.60  E-value: 5.51e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   753 AHLEKEEKKRIERSARQRLQALRADDEAAYLQLLDKAKDTRITHLLKQTDQYLENLTRAvriQQSNIHSGNTSGKGSNSA 832
Cdd:PLN03142   58 SKREKARLKELKKQKKQEIQKILEQQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGD---QSASAKKAKGRGRHASKL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   833 ELEAPISEEDKNLDYFKVAHRIHEEVEQPKIfVGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLI 912
Cdd:PLN03142  135 TEEEEDEEYLKEEEDGLGGSGGTRLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLH 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   913 EKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIAYKGPPQLRKTLQSQ-IRSSNFNVLLTTFEYIIKDRPLLSRIKWV 991
Cdd:PLN03142  214 EYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWR 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   992 HMIIDEGHRIKNTQSKLTSTLSTYyHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPfantggqdki 1071
Cdd:PLN03142  294 YIIIDEAHRIKNENSLLSKTMRLF-STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQIS---------- 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  1072 GLNEEEAllIIKRLHKVLRPFLFRRLKKDVEKELPDKVEKVIKCPLSGLQLKLYQQMKKHGMLFVD--GEKGKtgikgLQ 1149
Cdd:PLN03142  363 GENDQQE--VVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNagGERKR-----LL 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  1150 NTVMQLKKICNHPFIFEDVERAidPSGTNVDLLWRAAGKFELLDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWK 1229
Cdd:PLN03142  436 NIAMQLRKCCNHPYLFQGAEPG--PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQ 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  1230 YLRLDGSTKSDDRCSLLAQFNDPKSDVYIFMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQTKEVRIL 1309
Cdd:PLN03142  514 YCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVF 593
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 63054463  1310 RLITEKSIEENILSRAQYKLDLDGKVIQAGKF-DNKS 1345
Cdd:PLN03142  594 RFCTEYTIEEKVIERAYKKLALDALVIQQGRLaEQKT 630
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1518-1620 1.31e-54

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: 185.24  E-value: 1.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1518 LRRYCMEIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYT 1597
Cdd:cd05519    1 LKAAMLEIYDAVLNCEDETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANART 80
                         90       100
                 ....*....|....*....|...
gi 63054463 1598 YNEEHSIVYEDAKLMEKTLKEVI 1620
Cdd:cd05519   81 YNQEGSIVYEDAVEMEKAFKKKY 103
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1395-1673 4.67e-54

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


:

Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 194.25  E-value: 4.67e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1395 LDKERAATDIYGKGKPL--ERLLTVNELPDFYKV-EVDSFAVQSSSEL-EDQYLERKRRRRNSISYTELTLDELNTVDDP 1470
Cdd:COG5076    1 LEFDEVSYSQLGRPSVLkeEFGNELLRLVDNDSSpFPNAPEEEGSKNLfQKQLKRMPKEYITSIVDDREPGSMANVNDDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1471 SSTLM----PRKRGRP---RKKTNSGSSLS--TPLSQESSLARSGRK------NTPSYKQKALRRYCMEIFERLYNLQSE 1535
Cdd:COG5076   81 ENVGGitysPFEKNRPeslRFDEIVFLAIEsvTPESGLGSLLMAHLKtsvkkrKTPKIEDELLYADNKAIAKFKKQLFLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1536 DGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKT 1615
Cdd:COG5076  161 DGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKY 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463 1616 LKEVIEDLEKNNSLHAYEEEALNEEQASLVFLENSEAELPLDSGIVSAEDDKVITYED 1673
Cdd:COG5076  241 FLKLIEEIPEEMLELSIKPGREEREERESVLITNSQAHVGAWPFLRPVSDEEVPDYYK 298
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
147-429 6.58e-12

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 69.99  E-value: 6.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    147 TSVPPAPSMVHPHTNTnANSNNLKVYANQLSQQ-NTSNP-TYHNAYDMASmmkngSRMNNSFPPTTPYPPANDTTVNSSL 224
Cdd:pfam17823   63 ATAAPAPVTLTKGTSA-AHLNSTEVTAEHTPHGtDLSEPaTREGAADGAA-----SRALAAAASSSPSSAAQSLPAAIAA 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    225 PHSFASPSSTFEQPHTVQSRAPSVDTTSSSHSFSARNIPANVSMQQQMGRRGSIPVNPSTFSASSPPSGSMLASPYN--- 301
Cdd:pfam17823  137 LPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGIStaa 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    302 -GYQNDAASFAHSKLP-SSANPNTPFNSTATVDVGAAGSHFPYPQ--PSNLDAINA----KTYFQSSSNSPAPYVYRNNL 373
Cdd:pfam17823  217 tATGHPAAGTALAAVGnSSPAAGTVTAAVGTVTPAALATLAAAAGtvASAAGTINMgdphARRLSPAKHMPSDTMARNPA 296
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463    374 PPSATSFQPSSSRSpSVDPNTVKSAqhiPRMSPSPSASAL-------------------KTQSHVPSAK---VPPTSK 429
Cdd:pfam17823  297 APMGAQAQGPIIQV-STDQPVHNTA---GEPTPSPSNTTLepntpksvastnlavvtttKAQAKEPSASpvpVLHTSM 370
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
428-463 1.20e-08

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: 52.15  E-value: 1.20e-08
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 63054463     428 SKLNHAQLAMLKSQIVAYNCLNSPNGQVPPAVQQAI 463
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKYLLARNQPVPPELLQAI 36
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
711-771 1.19e-06

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: 47.18  E-value: 1.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054463    711 RQKEKLLTHLRSIMLHRKSIVTKVdKQNKAKTQRC-KDIINFHAHLEKEEKKRIERSARQRL 771
Cdd:pfam07529    7 REKTHHDYLLEEILWHSKDFKQER-RWKRARAKKLaRAVAQYHKNIEKEEQKRIEREEKQRL 67
 
Name Accession Description Interval E-value
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
866-1098 7.03e-167

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: 503.83  E-value: 7.03e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  866 GGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVK 945
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  946 KIAYKGPPQLRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYYHSQYRLILT 1025
Cdd:cd17996   81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054463 1026 GTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGGQDKIGLNEEEALLIIKRLHKVLRPFLFRRLK 1098
Cdd:cd17996  161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLIIRRLHKVLRPFLLRRLK 233
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
753-1345 5.51e-165

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 528.60  E-value: 5.51e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   753 AHLEKEEKKRIERSARQRLQALRADDEAAYLQLLDKAKDTRITHLLKQTDQYLENLTRAvriQQSNIHSGNTSGKGSNSA 832
Cdd:PLN03142   58 SKREKARLKELKKQKKQEIQKILEQQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGD---QSASAKKAKGRGRHASKL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   833 ELEAPISEEDKNLDYFKVAHRIHEEVEQPKIfVGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLI 912
Cdd:PLN03142  135 TEEEEDEEYLKEEEDGLGGSGGTRLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLH 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   913 EKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIAYKGPPQLRKTLQSQ-IRSSNFNVLLTTFEYIIKDRPLLSRIKWV 991
Cdd:PLN03142  214 EYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWR 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   992 HMIIDEGHRIKNTQSKLTSTLSTYyHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPfantggqdki 1071
Cdd:PLN03142  294 YIIIDEAHRIKNENSLLSKTMRLF-STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQIS---------- 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  1072 GLNEEEAllIIKRLHKVLRPFLFRRLKKDVEKELPDKVEKVIKCPLSGLQLKLYQQMKKHGMLFVD--GEKGKtgikgLQ 1149
Cdd:PLN03142  363 GENDQQE--VVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNagGERKR-----LL 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  1150 NTVMQLKKICNHPFIFEDVERAidPSGTNVDLLWRAAGKFELLDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWK 1229
Cdd:PLN03142  436 NIAMQLRKCCNHPYLFQGAEPG--PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQ 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  1230 YLRLDGSTKSDDRCSLLAQFNDPKSDVYIFMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQTKEVRIL 1309
Cdd:PLN03142  514 YCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVF 593
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 63054463  1310 RLITEKSIEENILSRAQYKLDLDGKVIQAGKF-DNKS 1345
Cdd:PLN03142  594 RFCTEYTIEEKVIERAYKKLALDALVIQQGRLaEQKT 630
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
845-1331 2.20e-130

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 422.71  E-value: 2.20e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  845 LDYFKVAHRIHEEVEQPKIFvGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEkKNQQGPFLII 924
Cdd:COG0553  219 VDAFRLRRLREALESLPAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIV 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  925 VPLSTLTNWIMEFEKWAPSVKKIAYKGPPQlRKTLQSQIrsSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNT 1004
Cdd:COG0553  297 APTSLVGNWQRELAKFAPGLRVLVLDGTRE-RAKGANPF--EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNP 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1005 QSKLTS---TLStyyhSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPfantggqdkIGLNEEEALli 1081
Cdd:COG0553  374 ATKRAKavrALK----ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP---------IEKGDEEAL-- 438
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1082 iKRLHKVLRPFLFRRLKKDVEKELPDKVEKVIKCPLSGLQLKLYQQMKKHGMLFVDGEKG-KTGIKGLQnTVMQLKKICN 1160
Cdd:COG0553  439 -ERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGiRRRGLILA-ALTRLRQICS 516
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1161 HPFIF-EDVERAIDPSgtnvdllwraaGKFELLDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWKYLRLDGSTKS 1239
Cdd:COG0553  517 HPALLlEEGAELSGRS-----------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSA 585
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1240 DDRCSLLAQFNDpKSDVYIFMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQTKEVRILRLITEKSIEE 1319
Cdd:COG0553  586 EERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEE 664
                        490
                 ....*....|..
gi 63054463 1320 NILSRAQYKLDL 1331
Cdd:COG0553  665 KILELLEEKRAL 676
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
872-1165 5.60e-110

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: 351.22  E-value: 5.60e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    872 YQLKGLEWMLSLYNN-NLNGILADEMGLGKTIQTIAFITYLIE-KKNQQGPFLIIVPLSTLTNWIMEFEKWA--PSVKKI 947
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    948 AYKGPPQ-LRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYyHSQYRLILTG 1026
Cdd:pfam00176   81 VLHGNKRpQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL-KTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   1027 TPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGGQDkiglneeeallIIKRLHKVLRPFLFRRLKKDVEKELP 1106
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKK-----------GVSRLHKLLKPFLLRRTKKDVEKSLP 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054463   1107 DKVEKVIKCPLSGLQLKLYQ-QMKKHGMLFV-DGEKGKTGIKGLQNTVMQLKKICNHPFIF 1165
Cdd:pfam00176  229 PKVEYILFCRLSKLQRKLYQtFLLKKDLNAIkTGEGGREIKASLLNILMRLRKICNHPGLI 289
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1518-1620 1.31e-54

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: 185.24  E-value: 1.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1518 LRRYCMEIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYT 1597
Cdd:cd05519    1 LKAAMLEIYDAVLNCEDETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANART 80
                         90       100
                 ....*....|....*....|...
gi 63054463 1598 YNEEHSIVYEDAKLMEKTLKEVI 1620
Cdd:cd05519   81 YNQEGSIVYEDAVEMEKAFKKKY 103
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1395-1673 4.67e-54

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 194.25  E-value: 4.67e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1395 LDKERAATDIYGKGKPL--ERLLTVNELPDFYKV-EVDSFAVQSSSEL-EDQYLERKRRRRNSISYTELTLDELNTVDDP 1470
Cdd:COG5076    1 LEFDEVSYSQLGRPSVLkeEFGNELLRLVDNDSSpFPNAPEEEGSKNLfQKQLKRMPKEYITSIVDDREPGSMANVNDDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1471 SSTLM----PRKRGRP---RKKTNSGSSLS--TPLSQESSLARSGRK------NTPSYKQKALRRYCMEIFERLYNLQSE 1535
Cdd:COG5076   81 ENVGGitysPFEKNRPeslRFDEIVFLAIEsvTPESGLGSLLMAHLKtsvkkrKTPKIEDELLYADNKAIAKFKKQLFLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1536 DGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKT 1615
Cdd:COG5076  161 DGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKY 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463 1616 LKEVIEDLEKNNSLHAYEEEALNEEQASLVFLENSEAELPLDSGIVSAEDDKVITYED 1673
Cdd:COG5076  241 FLKLIEEIPEEMLELSIKPGREEREERESVLITNSQAHVGAWPFLRPVSDEEVPDYYK 298
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1187-1312 3.97e-53

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: 182.29  E-value: 3.97e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1187 GKFELLDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWKYLRLDGSTKSDDRCSLLAQFNDPkSDVYIFMLSTRAG 1266
Cdd:cd18793   11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 63054463 1267 GLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQTKEVRILRLI 1312
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
BROMO smart00297
bromo domain;
1516-1623 1.01e-30

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 117.38  E-value: 1.01e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    1516 KALRRYCMEIFERLYNLQSEDGRFVngLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNA 1595
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDSHPLSW--PFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNA 79
                            90       100
                    ....*....|....*....|....*...
gi 63054463    1596 YTYNEEHSIVYEDAKLMEKTLKEVIEDL 1623
Cdd:smart00297   80 RTYNGPDSEVYKDAKKLEKFFEKKLREL 107
DEXDc smart00487
DEAD-like helicases superfamily;
864-1058 1.64e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.29  E-value: 1.64e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463     864 FVGGTLKDYQLKGLEWMLSlynNNLNGILADEMGLGKTIQTIAFITYLIeKKNQQGPFLIIVPLSTLT-NWIMEFEKWAP 942
Cdd:smart00487    4 FGFEPLRPYQKEAIEALLS---GLRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAeQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463     943 S--VKKIAYKGPPQLRKTLQsQIRSSNFNVLLTTFEYIIKD--RPLLSRIKWVHMIIDEGHRIKN--TQSKLTSTLSTYY 1016
Cdd:smart00487   80 SlgLKVVGLYGGDSKREQLR-KLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLP 158
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|..
gi 63054463    1017 HSQYRLILTGTPLQNNLPELWALLNfvLPKIFNSIKSFDEWF 1058
Cdd:smart00487  159 KNVQLLLLSATPPEEIENLLELFLN--DPVFIDVGFTPLEPI 198
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1187-1301 1.67e-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: 111.15  E-value: 1.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   1187 GKFELLDRILPKLflTGHKTLMFFQMTQimTIMEDYLRSK-NWKYLRLDGSTKSDDRCSLLAQFNDPKSDVyifMLSTRA 1265
Cdd:pfam00271    1 EKLEALLELLKKE--RGGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDV---LVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 63054463   1266 GGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIG 1301
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
1218-1301 2.22e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.36  E-value: 2.22e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    1218 IMEDYLRSKNWKYLRLDGSTKSDDRCSLLAQFNDPKSDVyifMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRA 1297
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKV---LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 63054463    1298 HRIG 1301
Cdd:smart00490   79 GRAG 82
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1522-1611 8.95e-19

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: 82.36  E-value: 8.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   1522 CMEIFERLYNLQSedgrfvNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEE 1601
Cdd:pfam00439    1 CLEILDKLMEHPI------AAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGP 74
                           90
                   ....*....|
gi 63054463   1602 HSIVYEDAKL 1611
Cdd:pfam00439   75 GSVIYKAAEK 84
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
147-429 6.58e-12

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 69.99  E-value: 6.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    147 TSVPPAPSMVHPHTNTnANSNNLKVYANQLSQQ-NTSNP-TYHNAYDMASmmkngSRMNNSFPPTTPYPPANDTTVNSSL 224
Cdd:pfam17823   63 ATAAPAPVTLTKGTSA-AHLNSTEVTAEHTPHGtDLSEPaTREGAADGAA-----SRALAAAASSSPSSAAQSLPAAIAA 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    225 PHSFASPSSTFEQPHTVQSRAPSVDTTSSSHSFSARNIPANVSMQQQMGRRGSIPVNPSTFSASSPPSGSMLASPYN--- 301
Cdd:pfam17823  137 LPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGIStaa 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    302 -GYQNDAASFAHSKLP-SSANPNTPFNSTATVDVGAAGSHFPYPQ--PSNLDAINA----KTYFQSSSNSPAPYVYRNNL 373
Cdd:pfam17823  217 tATGHPAAGTALAAVGnSSPAAGTVTAAVGTVTPAALATLAAAAGtvASAAGTINMgdphARRLSPAKHMPSDTMARNPA 296
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463    374 PPSATSFQPSSSRSpSVDPNTVKSAqhiPRMSPSPSASAL-------------------KTQSHVPSAK---VPPTSK 429
Cdd:pfam17823  297 APMGAQAQGPIIQV-STDQPVHNTA---GEPTPSPSNTTLepntpksvastnlavvtttKAQAKEPSASpvpVLHTSM 370
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
428-463 1.20e-08

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: 52.15  E-value: 1.20e-08
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 63054463     428 SKLNHAQLAMLKSQIVAYNCLNSPNGQVPPAVQQAI 463
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKYLLARNQPVPPELLQAI 36
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1398-1463 2.52e-08

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: 52.26  E-value: 2.52e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054463   1398 ERAATDIYGKGKPLERLLTVNELPDFYKVEVDSFAVQSSSELEDQYLERKRRRRNSISYTE-LTLDE 1463
Cdd:pfam14619    1 ERRREEAEQLPPLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDgLTEEQ 67
PHA03247 PHA03247
large tegument protein UL36; Provisional
109-559 5.89e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   109 SNGPTPPNPgngnvglnnpsymnsQASPnimnaPLQRDTSVPP---APSMVHPHTNTNANSNNLKvyanqlSQQNTSNPT 185
Cdd:PHA03247 2548 AGDPPPPLP---------------PAAP-----PAAPDRSVPPprpAPRPSEPAVTSRARRPDAP------PQSARPRAP 2601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   186 YHNAYDMAsmmknGSRMNNSFPPTT--PYPPANDTtvnSSLPHSFASPSSTFEQPHTVQSRAPSVDTTSSSHSFSARNIP 263
Cdd:PHA03247 2602 VDDRGDPR-----GPAPPSPLPPDThaPDPPPPSP---SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   264 ANVSMQQQMGRRGSIP--VNPSTFSASSPPSGSM------LASPYNGYQNDAASFAHSKLPSSANPNTPFNSTATVdvgA 335
Cdd:PHA03247 2674 AQASSPPQRPRRRAARptVGSLTSLADPPPPPPTpepaphALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---T 2750
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   336 AGSHFPYPQPSNldainaktyfQSSSNSPAPYVYRNNLPPSATSFQPSSSRSPSVDPNTVKSAQHIPRMSPSPSASALKT 415
Cdd:PHA03247 2751 PGGPARPARPPT----------TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP 2820
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   416 QSHVPSAKVPPTSKLnhaqlamlksqivaynclnspngQVPPAVQQAIFGRVYGASNEVSPSMPFQQNVPQMSSVKKDTP 495
Cdd:PHA03247 2821 AASPAGPLPPPTSAQ-----------------------PTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA 2877
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054463   496 TRDANMRTSKAPYIQNIPNQFqrraysATIPVKNESLAKPSVSPMPLQQSTGKTEVAKRAQFPT 559
Cdd:PHA03247 2878 PARPPVRRLARPAVSRSTESF------ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
711-771 1.19e-06

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: 47.18  E-value: 1.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054463    711 RQKEKLLTHLRSIMLHRKSIVTKVdKQNKAKTQRC-KDIINFHAHLEKEEKKRIERSARQRL 771
Cdd:pfam07529    7 REKTHHDYLLEEILWHSKDFKQER-RWKRARAKKLaRAVAQYHKNIEKEEQKRIEREEKQRL 67
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
158-569 8.43e-05

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 47.43  E-value: 8.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  158 PHTNTNANSNNLKvyANQLSQQNTSNPTYHNAydmASMMKNGSRMNNSFPPTTPyppandttvnsslphsfASPSSTFEQ 237
Cdd:COG5099    1 PNSDTMNNLLPSI--KSQLHHSKKSPPSSTTS---QELMNGNSTPNSFSPIPSK-----------------ASSSATFTL 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  238 PHTVQSRAPSVDTTSSS-----HSFSARNIPANVSMQQQ-MGRRGSIPVNPSTFSASSppSGSMLASPYngYQNDAASFA 311
Cdd:COG5099   59 NLPINNSVNHKITSSSSsrrkpSGSWSVAISSSTSGSQSlLMELPSSSFNPSTSSRNK--SNSALSSTQ--QGNANSSVT 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  312 HSKLPSSANPNtpFNSTATVDVGAAGSHFPYPQPSNLDAINAKTYFQSSSNSPAPYVYRNNLPPSATSFQpsssrSPSVD 391
Cdd:COG5099  135 LSSSTASSMFN--SNKLPLPNPNHSNSATTNQSGSSFINTPASSSSQPLTNLVVSSIKRFPYLTSLSPFF-----NYLID 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  392 PNtvksaqhiprmSPSPSASALKTQSHVPSAKVPPTsklnhaqlamlksqivaynclnspNGQVPPAVQQAIFGRVYGAS 471
Cdd:COG5099  208 PS-----------SDSATASADTSPSFNPPPNLSPN------------------------NLFSTSDLSPLPDTQSVENN 252
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  472 NEVSPSMPFQQNVPQMSSVKKDTPTRDANM---------RTSKAPYIQNIPNQFqrraySATIPVKNeSLAKPSVSPMPL 542
Cdd:COG5099  253 IILNSSSSINELTSIYGSVPSIRNLRGLNSalvsflnvsSSSLAFSALNGKEVS-----PTGSPSTR-SFARVLPKSSPN 326
                        410       420
                 ....*....|....*....|....*..
gi 63054463  543 QQSTGktevakraQFPTNVNYSSCVDP 569
Cdd:COG5099  327 NLLTE--------ILTTGVNPPQSLPS 345
 
Name Accession Description Interval E-value
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
866-1098 7.03e-167

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: 503.83  E-value: 7.03e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  866 GGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVK 945
Cdd:cd17996    1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  946 KIAYKGPPQLRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYYHSQYRLILT 1025
Cdd:cd17996   81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054463 1026 GTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGGQDKIGLNEEEALLIIKRLHKVLRPFLFRRLK 1098
Cdd:cd17996  161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVKIELNEEETLLIIRRLHKVLRPFLLRRLK 233
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
753-1345 5.51e-165

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 528.60  E-value: 5.51e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   753 AHLEKEEKKRIERSARQRLQALRADDEAAYLQLLDKAKDTRITHLLKQTDQYLENLTRAvriQQSNIHSGNTSGKGSNSA 832
Cdd:PLN03142   58 SKREKARLKELKKQKKQEIQKILEQQNAAIDADMNNKGKGRLKYLLQQTEIFAHFAKGD---QSASAKKAKGRGRHASKL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   833 ELEAPISEEDKNLDYFKVAHRIHEEVEQPKIfVGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLI 912
Cdd:PLN03142  135 TEEEEDEEYLKEEEDGLGGSGGTRLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLH 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   913 EKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIAYKGPPQLRKTLQSQ-IRSSNFNVLLTTFEYIIKDRPLLSRIKWV 991
Cdd:PLN03142  214 EYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWR 293
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   992 HMIIDEGHRIKNTQSKLTSTLSTYyHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPfantggqdki 1071
Cdd:PLN03142  294 YIIIDEAHRIKNENSLLSKTMRLF-STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQIS---------- 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  1072 GLNEEEAllIIKRLHKVLRPFLFRRLKKDVEKELPDKVEKVIKCPLSGLQLKLYQQMKKHGMLFVD--GEKGKtgikgLQ 1149
Cdd:PLN03142  363 GENDQQE--VVQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNagGERKR-----LL 435
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  1150 NTVMQLKKICNHPFIFEDVERAidPSGTNVDLLWRAAGKFELLDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWK 1229
Cdd:PLN03142  436 NIAMQLRKCCNHPYLFQGAEPG--PPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQ 513
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  1230 YLRLDGSTKSDDRCSLLAQFNDPKSDVYIFMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQTKEVRIL 1309
Cdd:PLN03142  514 YCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVF 593
                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 63054463  1310 RLITEKSIEENILSRAQYKLDLDGKVIQAGKF-DNKS 1345
Cdd:PLN03142  594 RFCTEYTIEEKVIERAYKKLALDALVIQQGRLaEQKT 630
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
845-1331 2.20e-130

Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, and repair];


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 422.71  E-value: 2.20e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  845 LDYFKVAHRIHEEVEQPKIFvGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEkKNQQGPFLII 924
Cdd:COG0553  219 VDAFRLRRLREALESLPAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKE-RGLARPVLIV 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  925 VPLSTLTNWIMEFEKWAPSVKKIAYKGPPQlRKTLQSQIrsSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNT 1004
Cdd:COG0553  297 APTSLVGNWQRELAKFAPGLRVLVLDGTRE-RAKGANPF--EDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNP 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1005 QSKLTS---TLStyyhSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPfantggqdkIGLNEEEALli 1081
Cdd:COG0553  374 ATKRAKavrALK----ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP---------IEKGDEEAL-- 438
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1082 iKRLHKVLRPFLFRRLKKDVEKELPDKVEKVIKCPLSGLQLKLYQQMKKHGMLFVDGEKG-KTGIKGLQnTVMQLKKICN 1160
Cdd:COG0553  439 -ERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAEGiRRRGLILA-ALTRLRQICS 516
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1161 HPFIF-EDVERAIDPSgtnvdllwraaGKFELLDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWKYLRLDGSTKS 1239
Cdd:COG0553  517 HPALLlEEGAELSGRS-----------AKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSA 585
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1240 DDRCSLLAQFNDpKSDVYIFMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQTKEVRILRLITEKSIEE 1319
Cdd:COG0553  586 EERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEE 664
                        490
                 ....*....|..
gi 63054463 1320 NILSRAQYKLDL 1331
Cdd:COG0553  665 KILELLEEKRAL 676
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
847-1098 2.38e-112

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: 356.30  E-value: 2.38e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  847 YFKVAHRIHEEVE-QPKIFVGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIV 925
Cdd:cd18063    1 YYTVAHAITERVEkQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  926 PLSTLTNWIMEFEKWAPSVKKIAYKGPPQLRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQ 1005
Cdd:cd18063   81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1006 SKLTSTLSTYYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGgqDKIGLNEEEALLIIKRL 1085
Cdd:cd18063  161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG--ERVDLNEEETILIIRRL 238
                        250
                 ....*....|...
gi 63054463 1086 HKVLRPFLFRRLK 1098
Cdd:cd18063  239 HKVLRPFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
847-1098 1.29e-110

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: 351.27  E-value: 1.29e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  847 YFKVAHRIHEEVE-QPKIFVGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIV 925
Cdd:cd18062    1 YYAVAHAVTEKVEkQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  926 PLSTLTNWIMEFEKWAPSVKKIAYKGPPQLRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQ 1005
Cdd:cd18062   81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1006 SKLTSTLSTYYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGgqDKIGLNEEEALLIIKRL 1085
Cdd:cd18062  161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTG--EKVDLNEEETILIIRRL 238
                        250
                 ....*....|...
gi 63054463 1086 HKVLRPFLFRRLK 1098
Cdd:cd18062  239 HKVLRPFLLRRLK 251
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
872-1165 5.60e-110

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: 351.22  E-value: 5.60e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    872 YQLKGLEWMLSLYNN-NLNGILADEMGLGKTIQTIAFITYLIE-KKNQQGPFLIIVPLSTLTNWIMEFEKWA--PSVKKI 947
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    948 AYKGPPQ-LRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYyHSQYRLILTG 1026
Cdd:pfam00176   81 VLHGNKRpQERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL-KTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   1027 TPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGGQDkiglneeeallIIKRLHKVLRPFLFRRLKKDVEKELP 1106
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKK-----------GVSRLHKLLKPFLLRRTKKDVEKSLP 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054463   1107 DKVEKVIKCPLSGLQLKLYQ-QMKKHGMLFV-DGEKGKTGIKGLQNTVMQLKKICNHPFIF 1165
Cdd:pfam00176  229 PKVEYILFCRLSKLQRKLYQtFLLKKDLNAIkTGEGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
866-1098 5.75e-94

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: 303.54  E-value: 5.75e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  866 GGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKnQQGPFLIIVPLSTLTNWIMEFEKWAPSVK 945
Cdd:cd18009    1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERG-VWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  946 KIAYKGPPQLRKTLQSQIRS-----SNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYYHSQy 1020
Cdd:cd18009   80 VLLYHGTKEERERLRKKIMKregtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDN- 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463 1021 RLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGGQDKIGLNEEEALLIIKRLHKVLRPFLFRRLK 1098
Cdd:cd18009  159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDFSSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
866-1098 1.34e-92

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: 299.24  E-value: 1.34e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  866 GGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVK 945
Cdd:cd17997    1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  946 KIAYKGPPQLRKT-LQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTyYHSQYRLIL 1024
Cdd:cd17997   81 VVVLIGDKEERADiIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRL-FNSRNRLLL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054463 1025 TGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTpfantggQDKIGLNEEeallIIKRLHKVLRPFLFRRLK 1098
Cdd:cd17997  160 TGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNV-------NNCDDDNQE----VVQRLHKVLRPFLLRRIK 222
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
869-1045 1.06e-82

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: 269.05  E-value: 1.06e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIA 948
Cdd:cd17919    1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTyYHSQYRLILTGTP 1028
Cdd:cd17919   81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKA-LRAKRRLLLTGTP 159
                        170
                 ....*....|....*..
gi 63054463 1029 LQNNLPELWALLNFVLP 1045
Cdd:cd17919  160 LQNNLEELWALLDFLDP 176
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
869-1096 1.21e-82

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: 270.76  E-value: 1.21e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIA 948
Cdd:cd18003    1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTL-QSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTyYHSQYRLILTGT 1027
Cdd:cd18003   81 YYGSAKERKLKrQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLLLTGT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054463 1028 PLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFanTGGQDKiglNEEEALLIIKRLHKVLRPFLFRR 1096
Cdd:cd18003  160 PLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL--TAMSEG---SQEENEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
868-1096 2.70e-82

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: 269.61  E-value: 2.70e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  868 TLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKI 947
Cdd:cd17993    1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  948 AYKGPPQLRKTLQ------SQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTyYHSQYR 1021
Cdd:cd17993   81 VYLGDIKSRDTIReyefyfSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-FKTNNR 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054463 1022 LILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEwfntpfantggqdkigLNEEEALLIIKRLHKVLRPFLFRR 1096
Cdd:cd17993  160 LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEE----------------EHDEEQEKGIADLHKELEPFILRR 218
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
869-1096 1.74e-73

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: 244.47  E-value: 1.74e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPsVKKIA 948
Cdd:cd17995    1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTLQ--------SQIRSSN----FNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTyY 1016
Cdd:cd17995   80 YHGSGESRQIIQqyemyfkdAQGRKKKgvykFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKK-L 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1017 HSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFntpfantgGQdkigLNEEEAlliIKRLHKVLRPFLFRR 1096
Cdd:cd17995  159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF--------GD----LKTAEQ---VEKLQALLKPYMLRR 223
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
869-1096 1.77e-71

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: 238.94  E-value: 1.77e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIA 948
Cdd:cd18002    1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTLQSQI-------RSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTyYHSQYR 1021
Cdd:cd18002   81 YWGNPKDRKVLRKFWdrknlytRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLS-FHCRNR 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054463 1022 LILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTgGQDKIGLNEEEalliIKRLHKVLRPFLFRR 1096
Cdd:cd18002  160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESH-AENKTGLNEHQ----LKRLHMILKPFMLRR 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
859-1108 1.20e-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: 237.26  E-value: 1.20e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  859 EQPKIFVGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFE 938
Cdd:cd18064    6 DSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  939 KWAPSVKKIAYKGPPQLRKT-LQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLtSTLSTYYH 1017
Cdd:cd18064   86 RWVPTLRAVCLIGDKDQRAAfVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKL-SEIVREFK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1018 SQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTpfANTGGQDKiglneeeallIIKRLHKVLRPFLFRRL 1097
Cdd:cd18064  165 TTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT--NNCLGDQK----------LVERLHMVLRPFLLRRI 232
                        250
                 ....*....|.
gi 63054463 1098 KKDVEKELPDK 1108
Cdd:cd18064  233 KADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
859-1098 1.96e-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: 236.07  E-value: 1.96e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  859 EQPKIFVGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFE 938
Cdd:cd18065    6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  939 KWAPSVKKIAYKGPPQLRKT-LQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLtSTLSTYYH 1017
Cdd:cd18065   86 RWVPSLRAVCLIGDKDARAAfIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKL-SEIVREFK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1018 SQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTpfANTGGQDKiglneeeallIIKRLHKVLRPFLFRRL 1097
Cdd:cd18065  165 TTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDT--KNCLGDQK----------LVERLHAVLKPFLLRRI 232

                 .
gi 63054463 1098 K 1098
Cdd:cd18065  233 K 233
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
859-1096 3.93e-66

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: 223.73  E-value: 3.93e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  859 EQPKiFVGGT---LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIM 935
Cdd:cd18054    9 KQPS-YIGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  936 EFEKWAPSVKKIAYKGPPQLRKTLQ------SQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLT 1009
Cdd:cd18054   88 EFEIWAPEINVVVYIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1010 STLSTyYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFdewfntpfantggQDKIGLNEEEALliiKRLHKVL 1089
Cdd:cd18054  168 KTLID-FKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDF-------------EEDHGKGRENGY---QSLHKVL 230

                 ....*..
gi 63054463 1090 RPFLFRR 1096
Cdd:cd18054  231 EPFLLRR 237
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
869-1096 1.34e-62

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: 213.07  E-value: 1.34e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIA 948
Cdd:cd18006    1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTLQSQIRS-SNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYYhSQYRLILTGT 1027
Cdd:cd18006   81 YMGDKEKRLDLQQDIKStNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS-VDFRLLLTGT 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054463 1028 PLQNNLPELWALLNFVLPKIFNSIKSfdEWFNTPFANTggQDKIGLNEEealliikrLHKVLRPFLFRR 1096
Cdd:cd18006  160 PIQNSLQELYALLSFIEPNVFPKDKL--DDFIKAYSET--DDESETVEE--------LHLLLQPFLLRR 216
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
867-1098 6.72e-61

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: 208.19  E-value: 6.72e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  867 GTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYlIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKK 946
Cdd:cd18012    3 ATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLS-RKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  947 IAYKGPPQLRKTLQsqiRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLT---STLStyyhSQYRLI 1023
Cdd:cd18012   82 LVIHGTKRKREKLR---ALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAkavKALK----ADHRLA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054463 1024 LTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANtggqdkigLNEEEALliiKRLHKVLRPFLFRRLK 1098
Cdd:cd18012  155 LTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEK--------DGDEEAL---EELKKLISPFILRRLK 218
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
869-1096 4.67e-60

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: 204.98  E-value: 4.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIA 948
Cdd:cd17994    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPpqlrktlqsqirssnfNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTyYHSQYRLILTGTP 1028
Cdd:cd17994   81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNS-YKIGYKLLLTGTP 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463 1029 LQNNLPELWALLNFVLPKIFNSIKSFDEwfntPFANTGGQDKiglneeealliIKRLHKVLRPFLFRR 1096
Cdd:cd17994  144 LQNNLEELFHLLNFLTPERFNNLQGFLE----EFADISKEDQ-----------IKKLHDLLGPHMLRR 196
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
869-1048 2.06e-58

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: 199.53  E-value: 2.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEkKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIA 948
Cdd:cd17998    1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTLQSQIRSS--NFNVLLTTFEYII---KDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTyYHSQYRLI 1023
Cdd:cd17998   80 YYGSQEERKHLRYDILKGleDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INANFRLL 158
                        170       180
                 ....*....|....*....|....*
gi 63054463 1024 LTGTPLQNNLPELWALLNFVLPKIF 1048
Cdd:cd17998  159 LTGTPLQNNLLELMSLLNFIMPKPF 183
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1518-1620 1.31e-54

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: 185.24  E-value: 1.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1518 LRRYCMEIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYT 1597
Cdd:cd05519    1 LKAAMLEIYDAVLNCEDETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANART 80
                         90       100
                 ....*....|....*....|...
gi 63054463 1598 YNEEHSIVYEDAKLMEKTLKEVI 1620
Cdd:cd05519   81 YNQEGSIVYEDAVEMEKAFKKKY 103
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1395-1673 4.67e-54

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 194.25  E-value: 4.67e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1395 LDKERAATDIYGKGKPL--ERLLTVNELPDFYKV-EVDSFAVQSSSEL-EDQYLERKRRRRNSISYTELTLDELNTVDDP 1470
Cdd:COG5076    1 LEFDEVSYSQLGRPSVLkeEFGNELLRLVDNDSSpFPNAPEEEGSKNLfQKQLKRMPKEYITSIVDDREPGSMANVNDDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1471 SSTLM----PRKRGRP---RKKTNSGSSLS--TPLSQESSLARSGRK------NTPSYKQKALRRYCMEIFERLYNLQSE 1535
Cdd:COG5076   81 ENVGGitysPFEKNRPeslRFDEIVFLAIEsvTPESGLGSLLMAHLKtsvkkrKTPKIEDELLYADNKAIAKFKKQLFLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1536 DGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKT 1615
Cdd:COG5076  161 DGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKY 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463 1616 LKEVIEDLEKNNSLHAYEEEALNEEQASLVFLENSEAELPLDSGIVSAEDDKVITYED 1673
Cdd:COG5076  241 FLKLIEEIPEEMLELSIKPGREEREERESVLITNSQAHVGAWPFLRPVSDEEVPDYYK 298
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
869-1096 2.52e-53

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: 186.79  E-value: 2.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQG-----PFLIIVPlSTLT-NWIMEFEKWAP 942
Cdd:cd17999    1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSFnsenlPSLVVCP-PTLVgHWVAEIKKYFP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  943 --SVKKIAYKGPPQLRKTLQSQirSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYyHSQY 1020
Cdd:cd17999   80 naFLKPLAYVGPPQERRRLREQ--GEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQL-KANH 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054463 1021 RLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGGQDKIGLNEEEALLIIKRLHKVLRPFLFRR 1096
Cdd:cd17999  157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
859-1096 3.33e-53

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: 186.79  E-value: 3.33e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  859 EQPKiFVGGT----LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWI 934
Cdd:cd18053    8 KQPS-YIGGHegleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  935 MEFEKWAPSVKKIAYKGPPQLRKTLQS------QIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKL 1008
Cdd:cd18053   87 REIQTWAPQMNAVVYLGDINSRNMIRThewmhpQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1009 TSTLsTYYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEwfntpfaNTGGQDKIGLNEeealliikrLHKV 1088
Cdd:cd18053  167 YKTL-IDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE-------EHGKGREYGYAS---------LHKE 229

                 ....*...
gi 63054463 1089 LRPFLFRR 1096
Cdd:cd18053  230 LEPFLLRR 237
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1187-1312 3.97e-53

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: 182.29  E-value: 3.97e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1187 GKFELLDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWKYLRLDGSTKSDDRCSLLAQFNDPkSDVYIFMLSTRAG 1266
Cdd:cd18793   11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKAG 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 63054463 1267 GLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQTKEVRILRLI 1312
Cdd:cd18793   90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
869-1045 1.83e-50

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: 177.13  E-value: 1.83e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAP------ 942
Cdd:cd18000    1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPpfrvvv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  943 ------SVKKIAYKGPPQLRKTLQSQIRSSNfNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTST---LS 1013
Cdd:cd18000   81 lhssgsGTGSEEKLGSIERKSQLIRKVVGDG-GILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAckqLR 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 63054463 1014 TyyhsQYRLILTGTPLQNNLPELWALLNFVLP 1045
Cdd:cd18000  160 T----PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
869-1096 2.24e-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: 178.33  E-value: 2.24e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIA 948
Cdd:cd18057    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTLQSQ--------IRSS------------NFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKL 1008
Cdd:cd18057   81 YTGDKESRSVIRENefsfednaIRSGkkvfrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1009 TSTLSTyYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEwfntPFANTGGQDKiglneeealliIKRLHKV 1088
Cdd:cd18057  161 FRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLE----EFADISKEDQ-----------IKKLHDL 224

                 ....*...
gi 63054463 1089 LRPFLFRR 1096
Cdd:cd18057  225 LGPHMLRR 232
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
872-1096 1.37e-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: 176.36  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  872 YQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIAYKG 951
Cdd:cd18055    4 YQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  952 PPQLRKTL-----------------------QSQIRssnFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKL 1008
Cdd:cd18055   84 DKDSRAIIrenefsfddnavkggkkafkmkrEAQVK---FHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1009 TSTLSTyYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEwfntPFANTGGQDKiglneeealliIKRLHKV 1088
Cdd:cd18055  161 FRVLNG-YKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLE----EFADISKEDQ-----------IKKLHDL 224

                 ....*...
gi 63054463 1089 LRPFLFRR 1096
Cdd:cd18055  225 LGPHMLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
869-1096 1.35e-48

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: 173.33  E-value: 1.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPfLIIVPLSTLTNWIMEFEKWAPSVKKIA 948
Cdd:cd18001    1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGP-PQLRKTLQSQIRsSNFNVLLTTFEYIIKDRPLLS-----RIKWVHMIIDEGHRIKNTQSKLTSTLSTyYHSQYRL 1022
Cdd:cd18001   80 FHGTsKKERERNLERIQ-RGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSLRE-IPAKNRI 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054463 1023 ILTGTPLQNNLPELWALLNFVLP-KIFNSIKSFDEWFNTPFanTGGQDKIGLNEEEAL--LIIKRLHKVLRPFLFRR 1096
Cdd:cd18001  158 ILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPI--TRGRDKDATQGEKALgsEVAENLRQIIKPYFLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
869-1096 5.02e-48

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: 171.79  E-value: 5.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIA 948
Cdd:cd18056    1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTLQSQ--------IR------------SSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKL 1008
Cdd:cd18056   81 YVGDKDSRAIIRENefsfednaIRggkkasrmkkeaSVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1009 TSTLSTyYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEwfntPFANTGGQDKiglneeealliIKRLHKV 1088
Cdd:cd18056  161 FRVLNG-YSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLE----EFADIAKEDQ-----------IKKLHDM 224

                 ....*...
gi 63054463 1089 LRPFLFRR 1096
Cdd:cd18056  225 LGPHMLRR 232
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
869-1096 6.55e-47

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: 168.30  E-value: 6.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFItYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWApSVKKIA 948
Cdd:cd18058    1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFL-SEIFLMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTL----------QSQIRSS--NFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLStYY 1016
Cdd:cd18058   79 YHGSQISRQMIqqyemyyrdeQGNPLSGifKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLK-LM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1017 HSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTpfantggqdkigLNEEEAlliIKRLHKVLRPFLFRR 1096
Cdd:cd18058  158 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD------------LKTEEQ---VKKLQSILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
869-1096 6.23e-45

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: 162.53  E-value: 6.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIeKKNQQGPFLIIVPLSTLTNWIMEFEKWApSVKKIA 948
Cdd:cd18060    1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-NVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTLQ--------SQIR----SSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLStYY 1016
Cdd:cd18060   79 YHGSLASRQMIQqyemyckdSRGRlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK-HM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1017 HSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTpfantggqdkigLNEEEAlliIKRLHKVLRPFLFRR 1096
Cdd:cd18060  158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD------------LKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
869-1096 1.79e-44

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: 161.78  E-value: 1.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKK--------------------NQQGPFLIIVPLS 928
Cdd:cd18005    1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKTgtrrdrennrprfkkkppasSAKKPVLIVAPLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  929 TLTNWIMEFEKWApSVKKIAYKGPpqlRKT--LQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQS 1006
Cdd:cd18005   81 VLYNWKDELDTWG-HFEVGVYHGS---RKDdeLEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1007 KLTSTLSTyYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPF----ANTGGQDKIGLNEEeallII 1082
Cdd:cd18005  157 KLTQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgqRHTATARELRLGRK----RK 231
                        250
                 ....*....|....
gi 63054463 1083 KRLHKVLRPFLFRR 1096
Cdd:cd18005  232 QELAVKLSKFFLRR 245
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
869-1096 9.98e-44

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: 159.04  E-value: 9.98e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFItYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWApSVKKIA 948
Cdd:cd18059    1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTLQ--------SQIR----SSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTyY 1016
Cdd:cd18059   79 YHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKM-M 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1017 HSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTpfantggqdkigLNEEEAlliIKRLHKVLRPFLFRR 1096
Cdd:cd18059  158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD------------LKTEEQ---VQKLQAILKPMMLRR 222
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
869-1096 2.85e-43

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: 158.22  E-value: 2.85e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLynnnlNGILADEMGLGKTIQTIAfityLIEKKNQQGPF---------------------LIIVPL 927
Cdd:cd18008    1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALA----LILATRPQDPKipeeleenssdpkklylskttLIVVPL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  928 STLTNWIMEFEK--WAPSVKKIAYKGPPqlRKTLQSQIrsSNFNVLLTTF-----EY-----------IIKDRPLLSRIK 989
Cdd:cd18008   72 SLLSQWKDEIEKhtKPGSLKVYVYHGSK--RIKSIEEL--SDYDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  990 WVHMIIDEGHRIKNTQSKLT---STLStyyhSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANtg 1066
Cdd:cd18008  148 WYRVILDEAHNIKNRSTKTSravCALK----AERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSK-- 221
                        250       260       270
                 ....*....|....*....|....*....|
gi 63054463 1067 gqdkiglNEEEAlliIKRLHKVLRPFLFRR 1096
Cdd:cd18008  222 -------NDRKA---LERLQALLKPILLRR 241
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
869-1096 2.23e-41

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: 152.08  E-value: 2.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFItYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWApSVKKIA 948
Cdd:cd18061    1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 YKGPPQLRKTLQ--------SQIR----SSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLStYY 1016
Cdd:cd18061   79 YHGSLISRQMIQqyemyfrdSQGRiirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLK-LM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1017 HSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTpfantggqdkigLNEEEAlliIKRLHKVLRPFLFRR 1096
Cdd:cd18061  158 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD------------LKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
869-1084 1.92e-40

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: 150.13  E-value: 1.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLslynNNLNG-----------ILADEMGLGKTIQTIAFI-TYLIEKKNQQGPfLIIVPLSTLTNWIME 936
Cdd:cd18007    1 LKPHQVEGVRFLW----SNLVGtdvgsdegggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  937 FEKWAPSvKKIAYKGPPQLRKTLQSQIRSSNFN-------VLLTTFE-------YIIKDRPL-LSRIKWVHM------II 995
Cdd:cd18007   76 FKKWLPP-DLRPLLVLVSLSASKRADARLRKINkwhkeggVLLIGYElfrnlasNATTDPRLkQEFIAALLDpgpdllVL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  996 DEGHRIKNTQSKLTSTLSTYyHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANtgGQdKIGLNE 1075
Cdd:cd18007  155 DEGHRLKNEKSQLSKALSKV-KTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEA--GQ-CVDSTE 230

                 ....*....
gi 63054463 1076 EEALLIIKR 1084
Cdd:cd18007  231 EDVRLMLKR 239
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
869-1096 2.84e-37

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: 140.88  E-value: 2.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLS--LYNNNLNG---ILADEMGLGKTIQTIAFITYLIekknQQGPF--------LIIVPLSTLTNWIM 935
Cdd:cd18004    1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLL----KQGPYgkptakkaLIVCPSSLVGNWKA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  936 EFEKWAPSVKKIAY----KGPPQlRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMII-DEGHRIKNTQSKLTS 1010
Cdd:cd18004   77 EFDKWLGLRRIKVVtadgNAKDV-KASLDFFSSASTYPVLIISYETLRRHAEKLSKKISIDLLIcDEGHRLKNSESKTTK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1011 TLSTYyHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFanTGGQDKiGLNEEEALLIIKRLH---K 1087
Cdd:cd18004  156 ALNSL-PCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPI--LRSRDP-DASEEDKELGAERSQelsE 231

                 ....*....
gi 63054463 1088 VLRPFLFRR 1096
Cdd:cd18004  232 LTSRFILRR 240
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
869-1068 2.81e-31

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: 123.39  E-value: 2.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWM-------LSLYNNN--LNGILADEMGLGKTIQTIAFItYLIEKKNQQGPFLIIVPLSTLTNWIMEFEK 939
Cdd:cd18069    1 LKPHQIGGIRFLydniiesLERYKGSsgFGCILAHSMGLGKTLQVISFL-DVLLRHTGAKTVLAIVPVNTLQNWLSEFNK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  940 WAPSVKKIAYKGPPQLR--------KTLQSQIR-----SSNFNVLLTTFE-YIIKDRPLLsrikwvhMIIDEGHRIKNTQ 1005
Cdd:cd18069   80 WLPPPEALPNVRPRPFKvfilndehKTTAARAKviedwVKDGGVLLMGYEmFRLRPGPDV-------VICDEGHRIKNCH 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054463 1006 SKLTSTLSTYyHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANtgGQ 1068
Cdd:cd18069  153 ASTSQALKNI-RSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILN--GQ 212
BROMO smart00297
bromo domain;
1516-1623 1.01e-30

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 117.38  E-value: 1.01e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    1516 KALRRYCMEIFERLYNLQSEDGRFVngLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNA 1595
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDSHPLSW--PFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNA 79
                            90       100
                    ....*....|....*....|....*...
gi 63054463    1596 YTYNEEHSIVYEDAKLMEKTLKEVIEDL 1623
Cdd:smart00297   80 RTYNGPDSEVYKDAKKLEKFFEKKLREL 107
DEXDc smart00487
DEAD-like helicases superfamily;
864-1058 1.64e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.29  E-value: 1.64e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463     864 FVGGTLKDYQLKGLEWMLSlynNNLNGILADEMGLGKTIQTIAFITYLIeKKNQQGPFLIIVPLSTLT-NWIMEFEKWAP 942
Cdd:smart00487    4 FGFEPLRPYQKEAIEALLS---GLRDVILAAPTGSGKTLAALLPALEAL-KRGKGGRVLVLVPTRELAeQWAEELKKLGP 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463     943 S--VKKIAYKGPPQLRKTLQsQIRSSNFNVLLTTFEYIIKD--RPLLSRIKWVHMIIDEGHRIKN--TQSKLTSTLSTYY 1016
Cdd:smart00487   80 SlgLKVVGLYGGDSKREQLR-KLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLP 158
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|..
gi 63054463    1017 HSQYRLILTGTPLQNNLPELWALLNfvLPKIFNSIKSFDEWF 1058
Cdd:smart00487  159 KNVQLLLLSATPPEEIENLLELFLN--DPVFIDVGFTPLEPI 198
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
869-1061 1.68e-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: 118.41  E-value: 1.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEW-----MLSLYNNNLNGILADEMGLGKTIQTIAFITYLIekknQQGPF---------LIIVPLSTLTNWI 934
Cdd:cd18066    1 LRPHQREGIEFlyecvMGMRVNERFGAILADEMGLGKTLQCISLIWTLL----RQGPYggkpvikraLIVTPGSLVKNWK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  935 MEFEKWAPS--VKKIAYKGPPQLRKTlqsqIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTL 1012
Cdd:cd18066   77 KEFQKWLGSerIKVFTVDQDHKVEEF----IASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 63054463 1013 sTYYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTP 1061
Cdd:cd18066  153 -TSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEP 200
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1523-1618 1.82e-29

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: 113.69  E-value: 1.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1523 MEIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEH 1602
Cdd:cd05518    6 LALFLYVLEYREGSGRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEG 85
                         90
                 ....*....|....*.
gi 63054463 1603 SIVYEDAKLMEKTLKE 1618
Cdd:cd05518   86 SQVYEDANILEKVLKE 101
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1518-1620 1.37e-28

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: 110.92  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1518 LRRYCMEIFERLYNLQSEDGrfvnGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYT 1597
Cdd:cd04369    1 LKKKLRSLLDALKKLKRDLS----EPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKT 76
                         90       100
                 ....*....|....*....|...
gi 63054463 1598 YNEEHSIVYEDAKLMEKTLKEVI 1620
Cdd:cd04369   77 YNGPGSPIYKDAKKLEKLFEKLL 99
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1187-1301 1.67e-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: 111.15  E-value: 1.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   1187 GKFELLDRILPKLflTGHKTLMFFQMTQimTIMEDYLRSK-NWKYLRLDGSTKSDDRCSLLAQFNDPKSDVyifMLSTRA 1265
Cdd:pfam00271    1 EKLEALLELLKKE--RGGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRKGKIDV---LVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 63054463   1266 GGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIG 1301
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
869-1084 8.35e-27

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: 109.99  E-value: 8.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSlynNNLNGILADEMGLGKTIQTIAFITYLiekkNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKkia 948
Cdd:cd18010    1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYY----REEWPLLIVCPSSLRLTWADEIERWLPSLP--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  949 yKGPPQLRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTS-TLSTYYHSQYRLILTGT 1027
Cdd:cd18010   71 -PDDIQVIVKSKDGLRDGDAKVVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKaALPLLKRAKRVILLSGT 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463 1028 PLQNNLPELWALLNFVLPKIFNSIKSFDE-WFNTPFANTGGQDKIGLNEEEALLIIKR 1084
Cdd:cd18010  150 PALSRPIELFTQLDALDPKLFGRFHDFGRrYCAAKQGGFGWDYSGSSNLEELHLLLLA 207
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
872-1096 1.59e-26

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: 109.87  E-value: 1.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  872 YQLKGLEWMLSLYNNNL-----------------------------NGILADEMGLGKTIQTIAFITYliekknqqGPFL 922
Cdd:cd18071    4 HQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLILA--------NFTL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  923 IIVPLSTLTNWIMEFEKWAPSV--KKIAYKGPPQLRktlqSQIRSSNFNVLLTTF-----EYIIKDRPLLSRIKWVHMII 995
Cdd:cd18071   76 IVCPLSVLSNWETQFEEHVKPGqlKVYTYHGGERNR----DPKLLSKYDIVLTTYntlasDFGAKGDSPLHTINWLRVVL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  996 DEGHRIKNT---QSKLTSTLStyyhSQYRLILTGTPLQNNLPELWALLNFVLPKIFnSIKsfdEWFNTPFantggQDKIG 1072
Cdd:cd18071  152 DEGHQIRNPnaqQTKAVLNLS----SERRWVLTGTPIQNSPKDLGSLLSFLHLKPF-SNP---EYWRRLI-----QRPLT 218
                        250       260
                 ....*....|....*....|....
gi 63054463 1073 LNEEEALliiKRLHKVLRPFLFRR 1096
Cdd:cd18071  219 MGDPTGL---KRLQVLMKQITLRR 239
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1518-1622 1.14e-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: 1.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1518 LRRYCMEIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYT 1597
Cdd:cd05515    1 MQQKLWELYNAVKNYTDGRGRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACK 80
                         90       100
                 ....*....|....*....|....*
gi 63054463 1598 YNEEHSIVYEDAKLMEKTLKEVIED 1622
Cdd:cd05515   81 YNEPDSQIYKDALTLQKVLLETKRE 105
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
869-1096 6.64e-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: 105.24  E-value: 6.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWML----SLYNNNLNG-ILADEMGLGKTIQTIAFITYLIEKKNQQGPFL---IIV-PLSTLTNWIMEFEK 939
Cdd:cd18067    1 LRPHQREGVKFLYrcvtGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaIVVsPSSLVKNWANELGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  940 W-APSVKKIAYKGPPQ---LRKTLQS-QIRSSNFN--VLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSkLTSTL 1012
Cdd:cd18067   81 WlGGRLQPLAIDGGSKkeiDRKLVQWaSQQGRRVStpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDN-QTYQA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1013 STYYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANtgGQDKIGLNEEEALLI--IKRLHKVLR 1090
Cdd:cd18067  160 LDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILK--GRDADASEKERQLGEekLQELISIVN 237

                 ....*.
gi 63054463 1091 PFLFRR 1096
Cdd:cd18067  238 RCIIRR 243
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
869-1064 3.83e-24

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: 103.43  E-value: 3.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWM---------LSLYNNNLNGILADEMGLGKTIQTIAFI-TYLI-EKKNQQGPFLIIVPLSTLTNWIMEF 937
Cdd:cd18068    1 LKPHQVDGVQFMwdccceslkKTKKSPGSGCILAHCMGLGKTLQVVTFLhTVLLcEKLENFSRVLVVCPLNTVLNWLNEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  938 EKWAPSVKKI---------AYKGPPQLRKTLQSQIRSSNFNVL-LTTFEYIIKDRPLLSRIKWVH-------------MI 994
Cdd:cd18068   81 EKWQEGLKDEekievnelaTYKRPQERSYKLQRWQEEGGVMIIgYDMYRILAQERNVKSREKLKEifnkalvdpgpdfVV 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  995 IDEGHRIKNTQSKLTSTLsTYYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFAN 1064
Cdd:cd18068  161 CDEGHILKNEASAVSKAM-NSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQN 229
HELICc smart00490
helicase superfamily c-terminal domain;
1218-1301 2.22e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 95.36  E-value: 2.22e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    1218 IMEDYLRSKNWKYLRLDGSTKSDDRCSLLAQFNDPKSDVyifMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRA 1297
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKV---LVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 63054463    1298 HRIG 1301
Cdd:smart00490   79 GRAG 82
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1523-1614 5.02e-23

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: 95.10  E-value: 5.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1523 MEIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEH 1602
Cdd:cd05520    6 WQLYDTIRNARNNQGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPN 85
                         90
                 ....*....|..
gi 63054463 1603 SIVYEDAKLMEK 1614
Cdd:cd05520   86 SRIYKDAEKLQK 97
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
869-1096 1.63e-22

DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called Forkhead-box E1/FOXE1 ) is a transcription termination factor that couples ATP hydrolysis with the removal of RNA polymerase II from the DNA template. Single nucleotide polymorphism (SNP) within the 5'-UTR of TTF2 is associated with thyroid cancer risk.TTF2 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 98.32  E-value: 1.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLNG-ILADEMGLGKTIQTIAFITYLIEKKNQQ----------------------GPFLIIV 925
Cdd:cd18072    1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALILAQKNTQNRKeeekekalteweskkdstlvpsAGTLVVC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  926 PLSTLTNWIMEFEKWAPS--VKKIAYKGPPQLRKTlqSQIRSsnFNVLLTTFEYIIKDRPLLS---------RIKWVHMI 994
Cdd:cd18072   81 PASLVHQWKNEVESRVASnkLRVCLYHGPNRERIG--EVLRD--YDIVITTYSLVAKEIPTYKeesrssplfRIAWARII 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  995 IDEGHRIKNTQSKlTSTLSTYYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGgqdkigln 1074
Cdd:cd18072  157 LDEAHNIKNPKVQ-ASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGG-------- 227
                        250       260
                 ....*....|....*....|..
gi 63054463 1075 eeealliiKRLHKVLRPFLFRR 1096
Cdd:cd18072  228 --------ERLNILTKSLLLRR 241
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1524-1619 2.47e-22

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: 93.26  E-value: 2.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1524 EIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHS 1603
Cdd:cd05516    8 KIVDVVIKYKDSDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFNLEGS 87
                         90
                 ....*....|....*.
gi 63054463 1604 IVYEDAKLMEKTLKEV 1619
Cdd:cd05516   88 LIYEDSIVLQSVFKSA 103
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1522-1621 6.45e-20

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: 86.62  E-value: 6.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1522 CMEIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEE 1601
Cdd:cd05524    7 CQELYDTIRNYKSEDGRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKP 86
                         90       100
                 ....*....|....*....|....
gi 63054463 1602 HSIVYEDA----KLMEKTLKEVIE 1621
Cdd:cd05524   87 DSPEHKDAcklwELFLSARNEVLS 110
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1522-1611 8.95e-19

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: 82.36  E-value: 8.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   1522 CMEIFERLYNLQSedgrfvNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEE 1601
Cdd:pfam00439    1 CLEILDKLMEHPI------AAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGP 74
                           90
                   ....*....|
gi 63054463   1602 HSIVYEDAKL 1611
Cdd:pfam00439   75 GSVIYKAAEK 84
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1548-1620 1.95e-18

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: 82.29  E-value: 1.95e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054463 1548 PNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKTLKEVI 1620
Cdd:cd05522   32 PDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNENDSQEYKDAVLLEKEARLLA 104
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1525-1620 1.01e-17

Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99952  Cd Length: 106  Bit Score: 80.06  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1525 IFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNdrYGDVGELIADFMLMFNNAYTYNEEHSI 1604
Cdd:cd05521    9 LYDGIYTLKEENGIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLPH--YTNAQEFVNDLAQIPWNARLYNTKGSV 86
                         90
                 ....*....|....*.
gi 63054463 1605 VYEDAKLMEKTLKEVI 1620
Cdd:cd05521   87 IYKYALILEKYINDVI 102
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
891-1056 6.52e-17

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: 81.18  E-value: 6.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  891 ILADEMGLGKTIQTIAFITYLiEKKNQQGPFLIIVPLSTLTNWIMEFEkwapsvKKIAYKGPPQLRKTLQSQIRSSN--- 967
Cdd:cd18011   21 LLADEVGLGKTIEAGLIIKEL-LLRGDAKRVLILCPASLVEQWQDELQ------DKFGLPFLILDRETAAQLRRLIGnpf 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  968 --FNVLLTTFEYI---IKDRPLLSRIKWVHMIIDEGHRIKNTQ-------SKLTSTLSTyyHSQYRLILTGTPLQNNLPE 1035
Cdd:cd18011   94 eeFPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGggketkrYKLGRLLAK--RARHVLLLTATPHNGKEED 171
                        170       180
                 ....*....|....*....|.
gi 63054463 1036 LWALLNFVLPKIFNSIKSFDE 1056
Cdd:cd18011  172 FRALLSLLDPGRFAVLGRFLR 192
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1544-1623 1.02e-16

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: 77.21  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1544 FLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKTLKEVIEDL 1623
Cdd:cd05509   22 FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGPDTEYYKCANKLEKFFWKKLKEL 101
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1524-1615 2.92e-15

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: 73.24  E-value: 2.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1524 EIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHS 1603
Cdd:cd05517    7 QLLEAVMTATDPSGRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGS 86
                         90
                 ....*....|..
gi 63054463 1604 IVYEDAKLMEKT 1615
Cdd:cd05517   87 QVYKDANAIKKI 98
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1544-1606 7.76e-15

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: 72.43  E-value: 7.76e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054463 1544 FLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVY 1606
Cdd:cd05504   33 FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVY 95
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1518-1619 9.66e-15

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: 71.71  E-value: 9.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1518 LRRYCMEIFERLYNlQSEDGRfvngLFLYPPNRKLY--PDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNA 1595
Cdd:cd05495    4 LRQALMPTLEKLYK-QDPESL----PFRQPVDPKLLgiPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNA 78
                         90       100
                 ....*....|....*....|....*
gi 63054463 1596 YTYNEEHSIVYEDA-KLMEKTLKEV 1619
Cdd:cd05495   79 WLYNRKTSRVYKYCtKLAEVFEQEI 103
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1520-1623 5.30e-14

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: 69.62  E-value: 5.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1520 RYCMEIFERLYNLQSEDgrfVNGLFLYP--PNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYT 1597
Cdd:cd05499    3 KFCEEVLKELMKPKHSA---YNWPFLDPvdPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYT 79
                         90       100
                 ....*....|....*....|....*.
gi 63054463 1598 YNEEHSIVYEdaklMEKTLKEVIEDL 1623
Cdd:cd05499   80 FNPEGTDVYM----MGHQLEEVFNDK 101
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
869-1060 5.94e-14

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: 72.77  E-value: 5.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSlynNNLNGILADeMGLGKTIQTIAFITYLIEkKNQQGPFLIIVPLSTLTN-WIMEFEKWAPSVK-- 945
Cdd:cd18013    1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQL-DDFTRRVLVIAPLRVARStWPDEVEKWNHLRNlt 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  946 -KIAYKGPPQLRKTLQS--QIRSSNFNVLLTTFEYIIKDRPllsrikWVHMIIDEGHRIKNTQSKLTSTLSTYYHSQYRL 1022
Cdd:cd18013   76 vSVAVGTERQRSKAANTpaDLYVINRENLKWLVNKSGDPWP------FDMVVIDELSSFKSPRSKRFKALRKVRPVIKRL 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 63054463 1023 I-LTGTPLQNNLPELWALLNFV--LPKIFNSIKSF-DEWFNT 1060
Cdd:cd18013  150 IgLTGTPSPNGLMDLWAQIALLdqGERLGRSITAYrERWFDP 191
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1544-1626 6.14e-14

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: 69.60  E-value: 6.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1544 FLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLM----EKTLKEV 1619
Cdd:cd05511   21 FHTPVNKKKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVYTKKAKEMlelaEELLAER 100
                         90
                 ....*....|
gi 63054463 1620 IE---DLEKN 1626
Cdd:cd05511  101 EEkltQLEKN 110
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
869-1042 8.80e-14

DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously expressed protein that contains motifs characteristic of several DNA repair proteins, transcription factors, and helicases. SHPRH is a functional homolog of S. cerevisiae RAD5 and is involved in DNA repair. SHPRH is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 73.15  E-value: 8.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLslynnNLNGILADEMGLGKTIQTIAFI------------TYLIEKKNQQ-------------GPFLI 923
Cdd:cd18070    1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCcpdclvaetpvssKATLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  924 IVPLSTLTNWIMEFEKWAP-SVKKIAYKGPPQlRKTLQSQI--RSSNFNVLLTTFEYIIKDR------------------ 982
Cdd:cd18070   76 VCPSAILAQWLDEINRHVPsSLKVLTYQGVKK-DGALASPApeILAEYDIVVTTYDVLRTELhyaeanrsnrrrrrqkry 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63054463  983 -----PLLsRIKWVHMIIDEGHRIKNTQSKLTSTLSTYYHSQyRLILTGTPLQNNLPELWALLNF 1042
Cdd:cd18070  155 eappsPLV-LVEWWRVCLDEAQMVESSTSKAAEMARRLPRVN-RWCVSGTPIQRGLDDLFGLLSF 217
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1554-1623 1.47e-12

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: 65.52  E-value: 1.47e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1554 PDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKTLKEVIEDL 1623
Cdd:cd05497   38 PDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPGDDVVLMAQTLEKLFLQKLAQM 107
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1554-1615 3.28e-12

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: 64.26  E-value: 3.28e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054463 1554 PDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKT 1615
Cdd:cd05500   37 PHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAA 98
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
147-429 6.58e-12

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 69.99  E-value: 6.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    147 TSVPPAPSMVHPHTNTnANSNNLKVYANQLSQQ-NTSNP-TYHNAYDMASmmkngSRMNNSFPPTTPYPPANDTTVNSSL 224
Cdd:pfam17823   63 ATAAPAPVTLTKGTSA-AHLNSTEVTAEHTPHGtDLSEPaTREGAADGAA-----SRALAAAASSSPSSAAQSLPAAIAA 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    225 PHSFASPSSTFEQPHTVQSRAPSVDTTSSSHSFSARNIPANVSMQQQMGRRGSIPVNPSTFSASSPPSGSMLASPYN--- 301
Cdd:pfam17823  137 LPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGIStaa 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    302 -GYQNDAASFAHSKLP-SSANPNTPFNSTATVDVGAAGSHFPYPQ--PSNLDAINA----KTYFQSSSNSPAPYVYRNNL 373
Cdd:pfam17823  217 tATGHPAAGTALAAVGnSSPAAGTVTAAVGTVTPAALATLAAAAGtvASAAGTINMgdphARRLSPAKHMPSDTMARNPA 296
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463    374 PPSATSFQPSSSRSpSVDPNTVKSAqhiPRMSPSPSASAL-------------------KTQSHVPSAK---VPPTSK 429
Cdd:pfam17823  297 APMGAQAQGPIIQV-STDQPVHNTA---GEPTPSPSNTTLepntpksvastnlavvtttKAQAKEPSASpvpVLHTSM 370
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1544-1614 9.73e-12

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: 62.78  E-value: 9.73e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054463 1544 FLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEK 1614
Cdd:cd05503   21 FLEPVNTKLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRK 91
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1554-1621 1.61e-11

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: 62.35  E-value: 1.61e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463 1554 PDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYedakLMEKTLKEVIE 1621
Cdd:cd05506   33 PDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVH----TMAKELLKIFE 96
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1544-1621 2.06e-11

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: 62.46  E-value: 2.06e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63054463 1544 FLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVY-EDAKLMEKTLKEVIE 1621
Cdd:cd05510   29 FLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYNSDPSHPLrRHANFMKKKAEHLLK 107
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1554-1622 2.19e-11

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: 62.31  E-value: 2.19e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054463 1554 PDYYIIIKRPIALGKIKRNIK---NDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEK----TLKEVIED 1622
Cdd:cd05502   34 PNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMFKNCYKFNEEDSEVAQAGKELELffeeQLKEILPD 109
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1524-1610 4.20e-11

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: 60.89  E-value: 4.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1524 EIFERLYN-LQSEDgrfVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEH 1602
Cdd:cd05513    4 KALEQLIRqLQRKD---PHGFFAFPVTDFIAPGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNKPD 80

                 ....*...
gi 63054463 1603 SIVYEDAK 1610
Cdd:cd05513   81 TIYYKAAK 88
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1520-1623 1.31e-10

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: 59.60  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1520 RYCMEIFERLYNLQSEdgRFVnGLFLYP--PNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYT 1597
Cdd:cd05498    3 KFCSGILKELFSKKHK--AYA-WPFYKPvdPEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYK 79
                         90       100
                 ....*....|....*....|....*.
gi 63054463 1598 YNEEHSIVYEdaklMEKTLKEVIEDL 1623
Cdd:cd05498   80 YNPPDHPVHA----MARKLQDVFEDR 101
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
867-1451 7.13e-10

Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 63.89  E-value: 7.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  867 GTLKDYQLKGLE-WMLSLYNNNLNGILADEMGLGKTIqTIAFItylIEKKNQQGPFLIIVPLSTLTN-WIMEFEKWAPsv 944
Cdd:COG1061   79 FELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV-LALAL---AAELLRGKRVLVLVPRRELLEqWAEELRRFLG-- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  945 KKIAYKGPPQLRK-----TLQSQIRSSNFNVLLTTFEYIIkdrpllsrikwvhmiIDEGHRIkntQSKLTSTLSTYYHSQ 1019
Cdd:COG1061  153 DPLAGGGKKDSDApitvaTYQSLARRAHLDELGDRFGLVI---------------IDEAHHA---GAPSYRRILEAFPAA 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1020 YRLILTGTPL-QNNLPELWALLNfvlPKIFNsiksfdewfntpfantggqdkIGLNEEEAlliikrlHKVLRPFLFRRLK 1098
Cdd:COG1061  215 YRLGLTATPFrSDGREILLFLFD---GIVYE---------------------YSLKEAIE-------DGYLAPPEYYGIR 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1099 KDVEKELPDkvekvikcplsglqlklYQQMKkhgmlfvdgekgktgikglqntvmqlkkicnhpfifEDVERAIDPSgtn 1178
Cdd:COG1061  264 VDLTDERAE-----------------YDALS------------------------------------ERLREALAAD--- 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1179 vdllwrAAGKFELLDRILPKlFLTGHKTLMFFQMTQIMTIMEDYLRSKNWKYLRLDGSTKSDDRCSLLAQFNDPKSDVyi 1258
Cdd:COG1061  288 ------AERKDKILRELLRE-HPDDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRI-- 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1259 fMLSTRAGGLGLNLQTADTVIIFDtdwnPHQDLQ--AQdrahRIGqtkevRILRLITEKS-------IEENILSRAQYKL 1329
Cdd:COG1061  359 -LVTVDVLNEGVDVPRLDVAILLR----PTGSPRefIQ----RLG-----RGLRPAPGKEdalvydfVGNDVPVLEELAK 424
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1330 DLDGKVIQAGKFDNKSTPEEREAFLRSLLEHDGDDDHDLTYGELQDDELNELISRTDEELVLFKKLDKERAATDIYGKGK 1409
Cdd:COG1061  425 DLRDLAGYRVEFLDEEESEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGK 504
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|..
gi 63054463 1410 PLERLLTVNELPDFYKVEVDSFAVQSSSELEDQYLERKRRRR 1451
Cdd:COG1061  505 AEEEEEEKELLLLLALAKLLKLLLLLLLLLLLELLELLAALL 546
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1492-1623 1.92e-09

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: 57.35  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1492 LSTPLSQESSLARSGRKNTPSYKQKalrryCMEIFERLYNLQSEDGRFVNGLFLYPPN-RKLYPDYYIIIKRPIALGKIK 1570
Cdd:cd05529    1 LYNPLSSEWELFDPGWEQPHIRDEE-----RERLISGLDKLLLSLQLEIAEYFEYPVDlRAWYPDYWNRVPVPMDLETIR 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 63054463 1571 RNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKTLKEVIEDL 1623
Cdd:cd05529   76 SRLENRYYRSLEALRHDVRLILSNAETFNEPNSEIAKKAKRLSDWLLRILSSL 128
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1544-1624 2.18e-09

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: 56.22  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1544 FLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEktlKEVIEDL 1623
Cdd:cd05507   24 FLKPVTEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSSDHDVYLMAVEMQ---REVMSQI 100

                 .
gi 63054463 1624 E 1624
Cdd:cd05507  101 Q 101
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
428-463 1.20e-08

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: 52.15  E-value: 1.20e-08
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 63054463     428 SKLNHAQLAMLKSQIVAYNCLNSPNGQVPPAVQQAI 463
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKYLLARNQPVPPELLQAI 36
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1532-1609 1.58e-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: 53.56  E-value: 1.58e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63054463 1532 LQSEDgrfVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDA 1609
Cdd:cd05512   13 LQEKD---TAEIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDTIFYRAA 87
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1398-1463 2.52e-08

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: 52.26  E-value: 2.52e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63054463   1398 ERAATDIYGKGKPLERLLTVNELPDFYKVEVDSFAVQSSSELEDQYLERKRRRRNSISYTE-LTLDE 1463
Cdd:pfam14619    1 ERRREEAEQLPPLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDgLTEEQ 67
ResIII pfam04851
Type III restriction enzyme, res subunit;
868-1028 5.21e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.22  E-value: 5.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    868 TLKDYQLKGLE-WMLSLYNNNLNGILADEMGLGKTIqTIAFITYLIEKKNQQGPFLIIVP-LSTLTNWIMEFEKWAPSVK 945
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTL-TAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    946 KIA--YKGPPQLRKTLQSQI----RSSNFNVLLTTFEYIIKDRPLLsrikwvhMIIDEGHR-IKNTQSKLTStlstYYHS 1018
Cdd:pfam04851   82 EIGeiISGDKKDESVDDNKIvvttIQSLYKALELASLELLPDFFDV-------IIIDEAHRsGASSYRNILE----YFKP 150
                          170
                   ....*....|
gi 63054463   1019 QYRLILTGTP 1028
Cdd:pfam04851  151 AFLLGLTATP 160
PHA03247 PHA03247
large tegument protein UL36; Provisional
109-559 5.89e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.03  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   109 SNGPTPPNPgngnvglnnpsymnsQASPnimnaPLQRDTSVPP---APSMVHPHTNTNANSNNLKvyanqlSQQNTSNPT 185
Cdd:PHA03247 2548 AGDPPPPLP---------------PAAP-----PAAPDRSVPPprpAPRPSEPAVTSRARRPDAP------PQSARPRAP 2601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   186 YHNAYDMAsmmknGSRMNNSFPPTT--PYPPANDTtvnSSLPHSFASPSSTFEQPHTVQSRAPSVDTTSSSHSFSARNIP 263
Cdd:PHA03247 2602 VDDRGDPR-----GPAPPSPLPPDThaPDPPPPSP---SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   264 ANVSMQQQMGRRGSIP--VNPSTFSASSPPSGSM------LASPYNGYQNDAASFAHSKLPSSANPNTPFNSTATVdvgA 335
Cdd:PHA03247 2674 AQASSPPQRPRRRAARptVGSLTSLADPPPPPPTpepaphALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA---T 2750
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   336 AGSHFPYPQPSNldainaktyfQSSSNSPAPYVYRNNLPPSATSFQPSSSRSPSVDPNTVKSAQHIPRMSPSPSASALKT 415
Cdd:PHA03247 2751 PGGPARPARPPT----------TAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPP 2820
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   416 QSHVPSAKVPPTSKLnhaqlamlksqivaynclnspngQVPPAVQQAIFGRVYGASNEVSPSMPFQQNVPQMSSVKKDTP 495
Cdd:PHA03247 2821 AASPAGPLPPPTSAQ-----------------------PTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA 2877
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63054463   496 TRDANMRTSKAPYIQNIPNQFqrraysATIPVKNESLAKPSVSPMPLQQSTGKTEVAKRAQFPT 559
Cdd:PHA03247 2878 PARPPVRRLARPAVSRSTESF------ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP 2935
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
869-1028 1.03e-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: 52.69  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  869 LKDYQLKGLEWMLSLYNNNLnGILADEMGLGKTIQTIAFITYLiekknQQGPFLIIVP-LSTLTNWIMEFEKWAPSVKKI 947
Cdd:cd17926    1 LRPYQEEALEAWLAHKNNRR-GILVLPTGSGKTLTALALIAYL-----KELRTLIVVPtDALLDQWKERFEDFLGDSSIG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  948 AYKGPPQLRKTlqsqirssNFNVLLTTFEYIIKDRPLLSRIK--WVHMIIDEGHRIknTQSKLTSTLSTYYHSqYRLILT 1025
Cdd:cd17926   75 LIGGGKKKDFD--------DANVVVATYQSLSNLAEEEKDLFdqFGLLIVDEAHHL--PAKTFSEILKELNAK-YRLGLT 143

                 ...
gi 63054463 1026 GTP 1028
Cdd:cd17926  144 ATP 146
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
98-429 3.38e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.56  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    98 AGMQTLPGRPASNGPTPPNPGNGNvglnnPSYMNSQASPNIMNAPLQRDTSVPPAPSMVHPHTNTNANSNnlkvyanqlS 177
Cdd:PHA03307   16 EGGEFFPRPPATPGDAADDLLSGS-----QGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAP---------A 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   178 QQNTSNPTYHNAYDMASMMKN------GSRMNNSFPPTTPYPPANDTTVNSSLPHSFASPSSTFEQPHTVQSRAPSVDTT 251
Cdd:PHA03307   82 NESRSTPTWSLSTLAPASPARegsptpPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   252 SSSHSFSARNIPANVSMQQQMGRRGSIP---VNPSTFSASSPPSGSMLASPYNGYQNDAASfAHSKLPSSANPNTPFNST 328
Cdd:PHA03307  162 VASDAASSRQAALPLSSPEETARAPSSPpaePPPSTPPAAASPRPPRRSSPISASASSPAP-APGRSAADDAGASSSDSS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   329 ATVDVGAAG---SHFPYPQPSNLDAinaktyfQSSSNSPAPYVYRNNLPPSATSFQPSSSRSPSVDPNTVKSAQHIPR-- 403
Cdd:PHA03307  241 SSESSGCGWgpeNECPLPRPAPITL-------PTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSpr 313
                         330       340       350
                  ....*....|....*....|....*....|..
gi 63054463   404 ----MSPSPSASALKT--QSHVPSAKVPPTSK 429
Cdd:PHA03307  314 asssSSSSRESSSSSTssSSESSRGAAVSPGP 345
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1513-1599 1.04e-06

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: 49.38  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1513 YKQKALRRYCMEIFERLYnlQSEDGRfvngLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMF 1592
Cdd:cd05496    1 YDESDWKKQCKELVNLMW--DCEDSE----PFRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIF 74

                 ....*..
gi 63054463 1593 NNAYTYN 1599
Cdd:cd05496   75 SNSKSYT 81
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1520-1623 1.15e-06

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: 48.89  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463 1520 RYCM-EIFERLynlqSEDGRFVngLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTY 1598
Cdd:cd05528    5 RLFLrDVLKRL----ASDKRFN--AFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEY 78
                         90       100
                 ....*....|....*....|....*..
gi 63054463 1599 NeeHSIVYEDAKL--MEKTLKEVIEDL 1623
Cdd:cd05528   79 N--PDRDPADKLIrsRACELRDEVHAM 103
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
711-771 1.19e-06

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: 47.18  E-value: 1.19e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054463    711 RQKEKLLTHLRSIMLHRKSIVTKVdKQNKAKTQRC-KDIINFHAHLEKEEKKRIERSARQRL 771
Cdd:pfam07529    7 REKTHHDYLLEEILWHSKDFKQER-RWKRARAKKLaRAVAQYHKNIEKEEQKRIEREEKQRL 67
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
65-520 1.74e-06

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: 53.23  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463     65 NQSSEFPDAENTNLRKQQDTLPTTgfNNLPEGKAGMQTLPGRPASNGPTPPNPGngnvglnnpsyMNSQASPNIMNAPLQ 144
Cdd:pfam03154  154 NESDSDSSAQQQILQTQPPVLQAQ--SGAASPPSPPPPGTTQAATAGPTPSAPS-----------VPPQGSPATSQPPNQ 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    145 RDTSVPP-----------APSMVHPHTNTNANSNNLKvyANQLSQQNTSNPTYHnaydmaSMMKNGSRMNNSFPPTTPYP 213
Cdd:pfam03154  221 TQSTAAPhtliqqtptlhPQRLPSPHPPLQPMTQPPP--PSQVSPQPLPQPSLH------GQMPPMPHSLQTGPSHMQHP 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    214 PAndttvnsslPHSFASPsstfeqPHTVQSRAPSVDTTSSSHSFSAR-NIPANVSM--QQQMGRRGSIPVNPSTFSASSP 290
Cdd:pfam03154  293 VP---------PQPFPLT------PQSSQSQVPPGPSPAAPGQSQQRiHTPPSQSQlqSQQPPREQPLPPAPLSMPHIKP 357
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    291 PSGSMLASPYNGYQNDAASFAHSKLPSSANPNTPFNSTATVDVGAAGSHFPYPQPSNLDAINAKTYFQSSSNSPAPYVYR 370
Cdd:pfam03154  358 PPTTPIPQLPNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQS 437
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    371 NNLPPSATSFQPSSSRSPsvdpntvksaqhIPRMSPSPSASALKTQS-HVPSAKVPPTSKLNhaqlAMlksqivayncln 449
Cdd:pfam03154  438 QSLPPPAASHPPTSGLHQ------------VPSQSPFPQHPFVPGGPpPITPPSGPPTSTSS----AM------------ 489
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054463    450 sPNGQVPPAVQQAIFGRVYGASNEVSPSMPFQQNVPQMSSVKKDTPTrdANMRTSKAPYIQNIPNQFQRRA 520
Cdd:pfam03154  490 -PGIQPPSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPP--PPRSPSPEPTVVNTPSHASQSA 557
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
889-1027 2.24e-06

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: 48.94  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  889 NGILADEMGLGKTIqtIAFITYLIEKKNQQGPFLIIVPLSTLTN-WIMEFEKWAPSVKKIAY------KGPPQLRKTLQS 961
Cdd:cd00046    3 NVLITAPTGSGKTL--AALLAALLLLLKKGKKVLVLVPTKALALqTAERLRELFGPGIRVAVlvggssAEEREKNKLGDA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63054463  962 QIrssnfnvLLTTFEYIIKD--RPLLSRIK-WVHMIIDEGHRI-KNTQSKLTSTLSTYYHSQ---YRLILTGT 1027
Cdd:cd00046   81 DI-------IIATPDMLLNLllREDRLFLKdLKLIIVDEAHALlIDSRGALILDLAVRKAGLknaQVILLSAT 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
897-1028 2.58e-05

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 46.47  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    897 GLGKTIqtIAFITYL--IEKKNQQGPFLIIVPLSTLTNWIME-FEKWAPSVKKIA---YKGPPqlRKTLQSQIRSSNfnV 970
Cdd:pfam00270   24 GSGKTL--AFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEeLKKLGKGLGLKVaslLGGDS--RKEQLEKLKGPD--I 97
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 63054463    971 LLTT---FEYIIKDRPLLSRIKWVhmIIDEGHRIkntqskltstLSTYYHSQYRLILTGTP 1028
Cdd:pfam00270   98 LVGTpgrLLDLLQERKLLKNLKLL--VLDEAHRL----------LDMGFGPDLEEILRRLP 146
PTZ00395 PTZ00395
Sec24-related protein; Provisional
52-423 4.49e-05

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 48.53  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    52 VQRAHYARMQQMRNQSSEFPDAENTN-LR----------KQQDTLPTTGFNNLPEGKAGMQTLPGRPASNGPTPPN---- 116
Cdd:PTZ00395  108 VGRAYGAGACEQSNQQSNIPIGDPVNhLRghpnfgepreRAEDAAPHAQHNHSGKTNGDNPPTGGQYHQSGGTSRNhqmm 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   117 ------PGNGNVGLNNPS----------------YMNSQasPNIMNapLQRDTsvPPAPSMVHPHTNTNANSNNLKVYAN 174
Cdd:PTZ00395  188 dsnkncPADALFNETNPSgehkrnsidgdipsdiYIDSQ--PNEGD--VQKTN--PWQGKQGNSATSPPANENNAVTLSC 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   175 QLSQQNTSNPTYHNAY------DMASMMKNGSRMNNSFPPTTPYPPANDTTVNSSLPHSFASPSSTFEQ--PHTVQSRAP 246
Cdd:PTZ00395  262 SNDQQRGASSAAESGYahhrgsNIASHTPNDNIMHAANNPLNNTNDAQRNAIQGDLVRGAPNDKNSFDRgnEKTYQIYGG 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   247 SVDTTSSSHSFSArniPANvSMQQQMGR----------RGSIPVNPSTFSASSPPSGSMLASPYNGYQNdaASFAHSKLP 316
Cdd:PTZ00395  342 FHDGSPNAASAGA---PFN-GLGNQADGghinqvhpdaRGAWAGGPHSNASYNCAAYSNAAQSNAAQSN--AGFSNAGYS 415
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   317 SSANPNTPFNStatvdvgAAGSHFPYPQPSNldainAKTYFQSSSNSPAPYvyrNNLPPSATSF-QPSSSRSP---SVDP 392
Cdd:PTZ00395  416 NPGNSNPGYNN-------APNSNTPYNNPPN-----SNTPYSNPPNSNPPY---SNLPYSNTPYsNAPLSNAPpssAKDH 480
                         410       420       430
                  ....*....|....*....|....*....|.
gi 63054463   393 NTVKSAQHIPRMSPSPSASalKTQSHVPSAK 423
Cdd:PTZ00395  481 HSAYHAAYQHRAANQPAAN--LPTANQPAAN 509
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
158-569 8.43e-05

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 47.43  E-value: 8.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  158 PHTNTNANSNNLKvyANQLSQQNTSNPTYHNAydmASMMKNGSRMNNSFPPTTPyppandttvnsslphsfASPSSTFEQ 237
Cdd:COG5099    1 PNSDTMNNLLPSI--KSQLHHSKKSPPSSTTS---QELMNGNSTPNSFSPIPSK-----------------ASSSATFTL 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  238 PHTVQSRAPSVDTTSSS-----HSFSARNIPANVSMQQQ-MGRRGSIPVNPSTFSASSppSGSMLASPYngYQNDAASFA 311
Cdd:COG5099   59 NLPINNSVNHKITSSSSsrrkpSGSWSVAISSSTSGSQSlLMELPSSSFNPSTSSRNK--SNSALSSTQ--QGNANSSVT 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  312 HSKLPSSANPNtpFNSTATVDVGAAGSHFPYPQPSNLDAINAKTYFQSSSNSPAPYVYRNNLPPSATSFQpsssrSPSVD 391
Cdd:COG5099  135 LSSSTASSMFN--SNKLPLPNPNHSNSATTNQSGSSFINTPASSSSQPLTNLVVSSIKRFPYLTSLSPFF-----NYLID 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  392 PNtvksaqhiprmSPSPSASALKTQSHVPSAKVPPTsklnhaqlamlksqivaynclnspNGQVPPAVQQAIFGRVYGAS 471
Cdd:COG5099  208 PS-----------SDSATASADTSPSFNPPPNLSPN------------------------NLFSTSDLSPLPDTQSVENN 252
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  472 NEVSPSMPFQQNVPQMSSVKKDTPTRDANM---------RTSKAPYIQNIPNQFqrraySATIPVKNeSLAKPSVSPMPL 542
Cdd:COG5099  253 IILNSSSSINELTSIYGSVPSIRNLRGLNSalvsflnvsSSSLAFSALNGKEVS-----PTGSPSTR-SFARVLPKSSPN 326
                        410       420
                 ....*....|....*....|....*..
gi 63054463  543 QQSTGktevakraQFPTNVNYSSCVDP 569
Cdd:COG5099  327 NLLTE--------ILTTGVNPPQSLPS 345
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1254-1312 1.02e-04

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: 42.31  E-value: 1.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 63054463 1254 SDVYIFMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQtKEVRILRLI 1312
Cdd:cd18785   20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILFV 77
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1544-1615 1.17e-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: 1.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63054463 1544 FLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEdakLMEKT 1615
Cdd:cd05505   21 FREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYYENGSYVLS---CMRKT 89
PTZ00395 PTZ00395
Sec24-related protein; Provisional
67-261 1.54e-04

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 46.61  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463    67 SSEFPDAENTNLRKQQDTLPTTGFNNLPEGKAGMQTLP--GRPASNGP---TP-PNPGNGNVGLNNPSYMNSQAS-PNIM 139
Cdd:PTZ00395  391 CAAYSNAAQSNAAQSNAGFSNAGYSNPGNSNPGYNNAPnsNTPYNNPPnsnTPySNPPNSNPPYSNLPYSNTPYSnAPLS 470
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463   140 NAPLQRDTSVPPAPSMVHPHTNTNANSNNLkVYANQLSQQNtsnptYHNAYDMASMMKNGSRMNNSFP----PTTPYPPa 215
Cdd:PTZ00395  471 NAPPSSAKDHHSAYHAAYQHRAANQPAANL-PTANQPAANN-----FHGAAGNSVGNPFASRPFGSAPyggnAATTADP- 543
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 63054463   216 ndttvnSSLPHSFASPSSTFEQPHTVQSRAPSVDTTSSSHSFSARN 261
Cdd:PTZ00395  544 ------NGIAKREDHPEGGTNRQKYEQSDEESVESSSSENSSENEN 583
PTZ00110 PTZ00110
helicase; Provisional
1192-1303 9.95e-04

helicase; Provisional


Pssm-ID: 240273 [Multi-domain]  Cd Length: 545  Bit Score: 43.61  E-value: 9.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  1192 LDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWKYLRLDGSTKSDDRCSLLAQFNDPKSDVyifMLSTRAGGLGLN 1271
Cdd:PTZ00110  366 LKMLLQRIMRDGDKILIFVETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPI---MIATDVASRGLD 442
                          90       100       110
                  ....*....|....*....|....*....|..
gi 63054463  1272 LQTADTVIIFDTdwnPHQdlqAQDRAHRIGQT 1303
Cdd:PTZ00110  443 VKDVKYVINFDF---PNQ---IEDYVHRIGRT 468
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
105-418 1.35e-03

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 43.58  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  105 GRPASNGPTP-PNPGNGNVGLNNPSYMNSQAS-------------PNIMNAPLQRDTSVPPAPSMVHPHTNTN--ANSNN 168
Cdd:COG5099   36 GNSTPNSFSPiPSKASSSATFTLNLPINNSVNhkitsssssrrkpSGSWSVAISSSTSGSQSLLMELPSSSFNpsTSSRN 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  169 LKVYANQLSQQNTSNPTYHNAYDMASMMKNGSrmNNSFPPTTPYPPANDTTVNSSLPHSFASPSSTFEQPHTVQSRAPSV 248
Cdd:COG5099  116 KSNSALSSTQQGNANSSVTLSSSTASSMFNSN--KLPLPNPNHSNSATTNQSGSSFINTPASSSSQPLTNLVVSSIKRFP 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  249 DTTSSSHSFSARNIPANVSMQ--QQMGRRGSIPVNPSTFSASSPPSGSMLAsPYNGYQNDAASFAHSKL--PSSANPNTP 324
Cdd:COG5099  194 YLTSLSPFFNYLIDPSSDSATasADTSPSFNPPPNLSPNNLFSTSDLSPLP-DTQSVENNIILNSSSSIneLTSIYGSVP 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63054463  325 FNSTATVDVGAAGSHFPYPqPSNLDAINAKTYFQSSSNSPAPYVYRNNLPPSATSFQPSSSRSPSVDPNTVKSAQHIPRM 404
Cdd:COG5099  273 SIRNLRGLNSALVSFLNVS-SSSLAFSALNGKEVSPTGSPSTRSFARVLPKSSPNNLLTEILTTGVNPPQSLPSLLNPVF 351
                        330
                 ....*....|....
gi 63054463  405 SPSPSASALKTQSH 418
Cdd:COG5099  352 LSTSTGFSLTNLSG 365
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1524-1599 3.57e-03

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: 38.91  E-value: 3.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63054463 1524 EIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYN 1599
Cdd:cd05525    9 EICDAIITYKDSNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYY 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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