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Conserved domains on  [gi|238624120|ref|NP_001121770|]
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chromodomain-helicase-DNA-binding protein 1 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
457-987 2.20e-173

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: 551.33  E-value: 2.20e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  457 QPHYIGGEgleLRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREI 536
Cdd:PLN03142  162 QPSCIKGK---MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEI 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  537 QLWAPLMNVVVYLGDINSRNMIRtHEWMHPQtkrlKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKT 616
Cdd:PLN03142  239 RRFCPVLRAVKFHGNPEERAHQR-EELLVAG----KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKT 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  617 MIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSGYTS----LHKELEPFLLRRVKKDVEKS 692
Cdd:PLN03142  314 MRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEvvqqLHKVLRPFLLRRLKSDVEKG 393
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  693 LPAKVEQILRVEMSAVQKQYYKWILTRNYKALSKGtkGSTSGFLNIMMELKKCCNHCYLIKPPDDNEFYNRQEglqHLVR 772
Cdd:PLN03142  394 LPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGE---HLVE 468
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  773 SSGKLILLDKLLVRLKERGHRVLIFSQMVRMLDILAEYLKYRQFLFQRLDGSIKGEMRKQALDHFNADGSEDFCFLLSTR 852
Cdd:PLN03142  469 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTR 548
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  853 AGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGSVEEEIIERAKKKMVLDHLVIQ--RMdTT 930
Cdd:PLN03142  549 AGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQqgRL-AE 627
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 238624120  931 GKTVlhtgaapssstpfNKEELSAILKFGAEELFKEPEGEEQEPqemDIDEILKRAE 987
Cdd:PLN03142  628 QKTV-------------NKDELLQMVRYGAEMVFSSKDSTITDE---DIDRIIAKGE 668
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
258-340 7.50e-46

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


:

Pssm-ID: 349313  Cd Length: 85  Bit Score: 159.76  E-value: 7.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  258 EFETLERVMEMRIGRKGVTGAVTTVYAVEADGDPNANFDPNRQPGEVQYLIKWKNWSHIHNTWETEETLKQQNVKGMKKL 337
Cdd:cd18666     1 EFETIERVLDHRIGRKGATGASTTIYAVEADGDPNAGFDPEDEETEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKL 80

                  ...
gi 238624120  338 DNF 340
Cdd:cd18666    81 ENY 83
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
375-431 3.29e-34

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


:

Pssm-ID: 349308  Cd Length: 58  Bit Score: 125.49  E-value: 3.29e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 238624120  375 QYQLVERIIGHSNQKSA-AGYPDYLCKWQGLPYSECSWEDGALISKKFQKCIDEYMSR 431
Cdd:cd18661     1 QYQIVERIIAHSPQKSAaSGYPDYLCKWQGLPYSECTWEDGALISKKFQACIDEYHSR 58
CDH1_2_SANT_HL1 super family cl39715
CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays ...
1111-1197 2.24e-31

CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays an important role in regulating nucleosome assembly and mobilization. CHD1 consists of double chromodomain, SNF2-related ATPase domain, and a C-terminal DNA-binding domain. The DNA-binding domain contains SANT (Swi3, Ada2, N-CoR, TFIIIB) and SLIDE (SANT-like ISWI) domains in its C-terminal region. SANT domains are structurally related to Myb-like domains are common motifs found in chromatin interacting proteins. Deletion of individual SANT or SLIDE domains in CDH1 does not significantly affect nucleosome binding, but combined deletion of both domains severely compromise binding, suggesting that the SANT-SLIDE motif recognizes DNA/nucleosomes as a single cooperative unit. SANT sequences of Chd1 proteins are the most distantly relation group of sequences relation to other SANT/Myb sequences, and are more diverse than other SANT proteins. The SANT and SLIDE regions are well conserved in both Chd1 and ISWI (imitation switch) remodelling enzymes. This domain comprises the SANT region and the helical linker region 1 (HL1).


The actual alignment was detected with superfamily member pfam18375:

Pssm-ID: 477096  Cd Length: 90  Bit Score: 118.61  E-value: 2.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1111 KGFTDAEIRRFIKSYKKFGGPLERLDAIARDAELVDKSEHDLRRLAETVHNGCLRTLKENPCGPER---TSGRRGKVKGP 1187
Cdd:pfam18375    1 KGFTDAEIRRFVKSYKKFSAPLKRLDAIACDAELQEKPLSDLRRLGELLKERCDEAMEEYTEKEDEnpgADGGKKRIRGP 80
                           90
                   ....*....|
gi 238624120  1188 TFRISGVQVN 1197
Cdd:pfam18375   81 SFKLGGVSVN 90
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1396-1486 2.30e-28

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


:

Pssm-ID: 464035  Cd Length: 93  Bit Score: 110.04  E-value: 2.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1396 ELDQKTFS-VCKERMRPVKAALKQLDRPEKGLSEREQLEHTRQCLIKIGDHITECLREYtNPEQIKQWRKNLWIFVSKFT 1474
Cdd:pfam13907    1 DEYESMDEeECKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEET-KKEKKEKLRKHLWSFVSKFW 79
                           90
                   ....*....|....
gi 238624120  1475 E--FDARKLHKLYK 1486
Cdd:pfam13907   80 PnkVSGKKLKEMYK 93
U2AF_lg super family cl36941
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
1576-1666 3.11e-06

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


The actual alignment was detected with superfamily member TIGR01642:

Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 51.82  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1576 RERERDQYRERG-ERPDSRYYSESKHRklDEHRSSREHRSESNSKDRthSEHRFHSEHRSgSSDYSHHKSSRdyryhsdw 1654
Cdd:TIGR01642    9 REKSRGRDRDRSsERPRRRSRDRSRFR--DRHRRSRERSYREDSRPR--DRRRYDSRSPR-SLRYSSVRRSR-------- 75
                           90
                   ....*....|..
gi 238624120  1655 qmeHRSPRDQRS 1666
Cdd:TIGR01642   76 ---DRPRRRSRS 84
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
457-987 2.20e-173

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 551.33  E-value: 2.20e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  457 QPHYIGGEgleLRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREI 536
Cdd:PLN03142  162 QPSCIKGK---MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEI 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  537 QLWAPLMNVVVYLGDINSRNMIRtHEWMHPQtkrlKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKT 616
Cdd:PLN03142  239 RRFCPVLRAVKFHGNPEERAHQR-EELLVAG----KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKT 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  617 MIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSGYTS----LHKELEPFLLRRVKKDVEKS 692
Cdd:PLN03142  314 MRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEvvqqLHKVLRPFLLRRLKSDVEKG 393
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  693 LPAKVEQILRVEMSAVQKQYYKWILTRNYKALSKGtkGSTSGFLNIMMELKKCCNHCYLIKPPDDNEFYNRQEglqHLVR 772
Cdd:PLN03142  394 LPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGE---HLVE 468
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  773 SSGKLILLDKLLVRLKERGHRVLIFSQMVRMLDILAEYLKYRQFLFQRLDGSIKGEMRKQALDHFNADGSEDFCFLLSTR 852
Cdd:PLN03142  469 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTR 548
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  853 AGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGSVEEEIIERAKKKMVLDHLVIQ--RMdTT 930
Cdd:PLN03142  549 AGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQqgRL-AE 627
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 238624120  931 GKTVlhtgaapssstpfNKEELSAILKFGAEELFKEPEGEEQEPqemDIDEILKRAE 987
Cdd:PLN03142  628 QKTV-------------NKDELLQMVRYGAEMVFSSKDSTITDE---DIDRIIAKGE 668
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
448-684 5.42e-162

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: 491.06  E-value: 5.42e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  448 RPRFVPMKKQPHYIGGEGLELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLS 527
Cdd:cd18054     1 RPRFVALKKQPSYIGGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  528 TLTSWQREIQLWAPLMNVVVYLGDINSRNMIRTHEWMHPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLK 607
Cdd:cd18054    81 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238624120  608 NDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSGYTSLHKELEPFLLRR 684
Cdd:cd18054   161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 237
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
465-923 9.22e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 410.39  E-value: 9.22e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  465 GLELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLyGPFLLVVPLSTLTSWQREIQLWAPLMN 544
Cdd:COG0553   239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  545 VVVYLGdinSRNMIRTHEWMHPQtkrlklNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNH 624
Cdd:COG0553   318 VLVLDG---TRERAKGANPFEDA------DLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARH 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  625 RLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSGYTS----LHKELEPFLLRRVKKDVEKSLPAKVEQI 700
Cdd:COG0553   389 RLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEalerLRRLLRPFLLRRTKEDVLKDLPEKTEET 468
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  701 LRVEMSAVQKQYYKwILTRNYKALSKGTKGSTSGF--LNIMMELKKCCNHCYLIKppddnefynrqEGLQHLVRSSGKLI 778
Cdd:COG0553   469 LYVELTPEQRALYE-AVLEYLRRELEGAEGIRRRGliLAALTRLRQICSHPALLL-----------EEGAELSGRSAKLE 536
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  779 LLDKLLVRLKERGHRVLIFSQMVRMLDILAEYLKYRQFLFQRLDGSIKGEMRKQALDHFNADGSEDFcFLLSTRAGGLGI 858
Cdd:COG0553   537 ALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPV-FLISLKAGGEGL 615
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238624120  859 NLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGSVEEEIIER-AKKKMVLDHLV 923
Cdd:COG0553   616 NLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELlEEKRALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
471-752 2.63e-111

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: 354.68  E-value: 2.63e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120   471 YQLDGLNWMAHSWCK-GNSCILADEMGLGKTIQTISFLNYLFHEHQLYG-PFLLVVPLSTLTSWQREIQLWA--PLMNVV 546
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120   547 VYLGDINSRnmirtHEWMHPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRL 626
Cdd:pfam00176   81 VLHGNKRPQ-----ERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120   627 LITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGK-----GRDSGYTSLHKELEPFLLRRVKKDVEKSLPAKVEQIL 701
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRpiergGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYIL 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 238624120   702 RVEMSAVQKQYYK-WILTRNYKALSKGTKGST--SGFLNIMMELKKCCNHCYLI 752
Cdd:pfam00176  236 FCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
258-340 7.50e-46

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349313  Cd Length: 85  Bit Score: 159.76  E-value: 7.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  258 EFETLERVMEMRIGRKGVTGAVTTVYAVEADGDPNANFDPNRQPGEVQYLIKWKNWSHIHNTWETEETLKQQNVKGMKKL 337
Cdd:cd18666     1 EFETIERVLDHRIGRKGATGASTTIYAVEADGDPNAGFDPEDEETEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKL 80

                  ...
gi 238624120  338 DNF 340
Cdd:cd18666    81 ENY 83
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
375-431 3.29e-34

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349308  Cd Length: 58  Bit Score: 125.49  E-value: 3.29e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 238624120  375 QYQLVERIIGHSNQKSA-AGYPDYLCKWQGLPYSECSWEDGALISKKFQKCIDEYMSR 431
Cdd:cd18661     1 QYQIVERIIAHSPQKSAaSGYPDYLCKWQGLPYSECTWEDGALISKKFQACIDEYHSR 58
CDH1_2_SANT_HL1 pfam18375
CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays ...
1111-1197 2.24e-31

CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays an important role in regulating nucleosome assembly and mobilization. CHD1 consists of double chromodomain, SNF2-related ATPase domain, and a C-terminal DNA-binding domain. The DNA-binding domain contains SANT (Swi3, Ada2, N-CoR, TFIIIB) and SLIDE (SANT-like ISWI) domains in its C-terminal region. SANT domains are structurally related to Myb-like domains are common motifs found in chromatin interacting proteins. Deletion of individual SANT or SLIDE domains in CDH1 does not significantly affect nucleosome binding, but combined deletion of both domains severely compromise binding, suggesting that the SANT-SLIDE motif recognizes DNA/nucleosomes as a single cooperative unit. SANT sequences of Chd1 proteins are the most distantly relation group of sequences relation to other SANT/Myb sequences, and are more diverse than other SANT proteins. The SANT and SLIDE regions are well conserved in both Chd1 and ISWI (imitation switch) remodelling enzymes. This domain comprises the SANT region and the helical linker region 1 (HL1).


Pssm-ID: 465731  Cd Length: 90  Bit Score: 118.61  E-value: 2.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1111 KGFTDAEIRRFIKSYKKFGGPLERLDAIARDAELVDKSEHDLRRLAETVHNGCLRTLKENPCGPER---TSGRRGKVKGP 1187
Cdd:pfam18375    1 KGFTDAEIRRFVKSYKKFSAPLKRLDAIACDAELQEKPLSDLRRLGELLKERCDEAMEEYTEKEDEnpgADGGKKRIRGP 80
                           90
                   ....*....|
gi 238624120  1188 TFRISGVQVN 1197
Cdd:pfam18375   81 SFKLGGVSVN 90
DEXDc smart00487
DEAD-like helicases superfamily;
465-651 1.81e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.51  E-value: 1.81e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120    465 GLELRDYQLDGLNWMAHSWckgNSCILADEMGLGKTIQTISFLNYLFHEHQlYGPFLLVVPLSTLT-SWQREIQLWAPLM 543
Cdd:smart00487    6 FEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAeQWAEELKKLGPSL 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120    544 N--VVVYLGDINSRNMIRthewmhpQTKRLKLNILLTTYEILLKD--KSFLGNVSWAFIGVDEAHRLKND---DSLLYKT 616
Cdd:smart00487   82 GlkVVGLYGGDSKREQLR-------KLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfgDQLEKLL 154
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 238624120    617 MIEFKSNHRLLITGTP---LQNSLKELWSLLHFIMPEK 651
Cdd:smart00487  155 KLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGF 192
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1396-1486 2.30e-28

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


Pssm-ID: 464035  Cd Length: 93  Bit Score: 110.04  E-value: 2.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1396 ELDQKTFS-VCKERMRPVKAALKQLDRPEKGLSEREQLEHTRQCLIKIGDHITECLREYtNPEQIKQWRKNLWIFVSKFT 1474
Cdd:pfam13907    1 DEYESMDEeECKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEET-KKEKKEKLRKHLWSFVSKFW 79
                           90
                   ....*....|....
gi 238624120  1475 E--FDARKLHKLYK 1486
Cdd:pfam13907   80 PnkVSGKKLKEMYK 93
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
379-431 5.22e-11

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 59.13  E-value: 5.22e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 238624120   379 VERIIGHSNQKSaaGYPDYLCKWQGLPYSECSWEDGALISKKfQKCIDEYMSR 431
Cdd:pfam00385    3 VERILDHRKDKG--GKEEYLVKWKGYPYDENTWEPEENLSKC-PELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
379-428 1.53e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 49.52  E-value: 1.53e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 238624120    379 VERIIGHSNQKSaaGYPDYLCKWQGLPYSECSWEDGALISkKFQKCIDEY 428
Cdd:smart00298    4 VEKILDHRWKKK--GELEYLVKWKGYSYSEDTWEPEENLL-NCSKKLDNY 50
CHROMO smart00298
Chromatin organization modifier domain;
302-340 1.72e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 49.52  E-value: 1.72e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 238624120    302 GEVQYLIKWKNWSHIHNTWETEETLKQqnvkGMKKLDNF 340
Cdd:smart00298   16 GELEYLVKWKGYSYSEDTWEPEENLLN----CSKKLDNY 50
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
1576-1666 3.11e-06

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 51.82  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1576 RERERDQYRERG-ERPDSRYYSESKHRklDEHRSSREHRSESNSKDRthSEHRFHSEHRSgSSDYSHHKSSRdyryhsdw 1654
Cdd:TIGR01642    9 REKSRGRDRDRSsERPRRRSRDRSRFR--DRHRRSRERSYREDSRPR--DRRRYDSRSPR-SLRYSSVRRSR-------- 75
                           90
                   ....*....|..
gi 238624120  1655 qmeHRSPRDQRS 1666
Cdd:TIGR01642   76 ---DRPRRRSRS 84
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
302-327 2.84e-05

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 42.95  E-value: 2.84e-05
                           10        20
                   ....*....|....*....|....*.
gi 238624120   302 GEVQYLIKWKNWSHIHNTWETEETLK 327
Cdd:pfam00385   15 GKEEYLVKWKGYPYDENTWEPEENLS 40
PHA03118 PHA03118
multifunctional expression regulator; Provisional
1546-1648 6.88e-04

multifunctional expression regulator; Provisional


Pssm-ID: 165391  Cd Length: 474  Bit Score: 44.29  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120 1546 SKEHHASDSYRKSSDSRKRPYSSFSNGKDHRERERDQYR-ERGERPDSRYYSESKHRKLDEHRSSREHRSESNSKDRTHS 1624
Cdd:PHA03118   88 KKAHGRREGYHHDDEKCLVTFLDDINHHGGRDTEPGHAHiENGERKSPKSYNQQSRKKHRDESLRNKHGRPSGPPAMSPG 167
                          90       100
                  ....*....|....*....|....
gi 238624120 1625 EHRFHSEHRSGSSDYSHHKSSRDY 1648
Cdd:PHA03118  168 EHFDQTHDAEYRLRFNERDARRDR 191
HisXaaSer_A3 NF038309
His-Xaa-Ser repeat protein HxsA3; This model represents an alternate form of the His-Xaa-Ser ...
1621-1652 4.99e-03

His-Xaa-Ser repeat protein HxsA3; This model represents an alternate form of the His-Xaa-Ser repeat protein HxsA, while TIGR03979 represents a more common form. The model covers a conserved N-terminal region, followed by the His-Xaa-Ser repeat region, but does not cover the C-terminal region, which is highly variable in this branch of His-Xaa-Ser repeat family protein.


Pssm-ID: 439608  Cd Length: 81  Bit Score: 37.67  E-value: 4.99e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 238624120 1621 RTHSEHRFHSEHRSGSSD-YSHHKSSRDYRYHS 1652
Cdd:NF038309   48 RSHSSHSSHSSHSSGSSGgHSSHSSHSSHSSHS 80
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
457-987 2.20e-173

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 551.33  E-value: 2.20e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  457 QPHYIGGEgleLRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREI 536
Cdd:PLN03142  162 QPSCIKGK---MRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEI 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  537 QLWAPLMNVVVYLGDINSRNMIRtHEWMHPQtkrlKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKT 616
Cdd:PLN03142  239 RRFCPVLRAVKFHGNPEERAHQR-EELLVAG----KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKT 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  617 MIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSGYTS----LHKELEPFLLRRVKKDVEKS 692
Cdd:PLN03142  314 MRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEvvqqLHKVLRPFLLRRLKSDVEKG 393
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  693 LPAKVEQILRVEMSAVQKQYYKWILTRNYKALSKGtkGSTSGFLNIMMELKKCCNHCYLIKPPDDNEFYNRQEglqHLVR 772
Cdd:PLN03142  394 LPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEPGPPYTTGE---HLVE 468
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  773 SSGKLILLDKLLVRLKERGHRVLIFSQMVRMLDILAEYLKYRQFLFQRLDGSIKGEMRKQALDHFNADGSEDFCFLLSTR 852
Cdd:PLN03142  469 NSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTR 548
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  853 AGGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGSVEEEIIERAKKKMVLDHLVIQ--RMdTT 930
Cdd:PLN03142  549 AGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQqgRL-AE 627
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 238624120  931 GKTVlhtgaapssstpfNKEELSAILKFGAEELFKEPEGEEQEPqemDIDEILKRAE 987
Cdd:PLN03142  628 QKTV-------------NKDELLQMVRYGAEMVFSSKDSTITDE---DIDRIIAKGE 668
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
448-684 5.42e-162

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: 491.06  E-value: 5.42e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  448 RPRFVPMKKQPHYIGGEGLELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLS 527
Cdd:cd18054     1 RPRFVALKKQPSYIGGENLELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  528 TLTSWQREIQLWAPLMNVVVYLGDINSRNMIRTHEWMHPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLK 607
Cdd:cd18054    81 TLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238624120  608 NDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSGYTSLHKELEPFLLRR 684
Cdd:cd18054   161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 237
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
449-684 1.84e-160

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: 486.86  E-value: 1.84e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  449 PRFVPMKKQPHYIGG-EGLELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLS 527
Cdd:cd18053     1 PRFVALKKQPSYIGGhEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  528 TLTSWQREIQLWAPLMNVVVYLGDINSRNMIRTHEWMHPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLK 607
Cdd:cd18053    81 TLTSWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238624120  608 NDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSGYTSLHKELEPFLLRR 684
Cdd:cd18053   161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRR 237
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
467-684 2.87e-151

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: 461.44  E-value: 2.87e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  467 ELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVV 546
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  547 VYLGDINSRNMIRTHEWMHPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRL 626
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 238624120  627 LITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSGYTSLHKELEPFLLRR 684
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKGIADLHKELEPFILRR 218
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
465-923 9.22e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 410.39  E-value: 9.22e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  465 GLELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLyGPFLLVVPLSTLTSWQREIQLWAPLMN 544
Cdd:COG0553   239 KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  545 VVVYLGdinSRNMIRTHEWMHPQtkrlklNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNH 624
Cdd:COG0553   318 VLVLDG---TRERAKGANPFEDA------DLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARH 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  625 RLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSGYTS----LHKELEPFLLRRVKKDVEKSLPAKVEQI 700
Cdd:COG0553   389 RLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARPIEKGDEEalerLRRLLRPFLLRRTKEDVLKDLPEKTEET 468
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  701 LRVEMSAVQKQYYKwILTRNYKALSKGTKGSTSGF--LNIMMELKKCCNHCYLIKppddnefynrqEGLQHLVRSSGKLI 778
Cdd:COG0553   469 LYVELTPEQRALYE-AVLEYLRRELEGAEGIRRRGliLAALTRLRQICSHPALLL-----------EEGAELSGRSAKLE 536
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  779 LLDKLLVRLKERGHRVLIFSQMVRMLDILAEYLKYRQFLFQRLDGSIKGEMRKQALDHFNADGSEDFcFLLSTRAGGLGI 858
Cdd:COG0553   537 ALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPV-FLISLKAGGEGL 615
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238624120  859 NLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLVTKGSVEEEIIER-AKKKMVLDHLV 923
Cdd:COG0553   616 NLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELlEEKRALAESVL 681
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
471-752 2.63e-111

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: 354.68  E-value: 2.63e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120   471 YQLDGLNWMAHSWCK-GNSCILADEMGLGKTIQTISFLNYLFHEHQLYG-PFLLVVPLSTLTSWQREIQLWA--PLMNVV 546
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120   547 VYLGDINSRnmirtHEWMHPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRL 626
Cdd:pfam00176   81 VLHGNKRPQ-----ERWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120   627 LITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGK-----GRDSGYTSLHKELEPFLLRRVKKDVEKSLPAKVEQIL 701
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRpiergGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYIL 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 238624120   702 RVEMSAVQKQYYK-WILTRNYKALSKGTKGST--SGFLNIMMELKKCCNHCYLI 752
Cdd:pfam00176  236 FCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREikASLLNILMRLRKICNHPGLI 289
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
468-684 9.18e-90

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: 291.07  E-value: 9.18e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPlMNVVV 547
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHEWMHPQTKRL------KLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFK 621
Cdd:cd17995    80 YHGSGESRQIIQQYEMYFKDAQGRkkkgvyKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238624120  622 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGR-DSGYTSLHKELEPFLLRR 684
Cdd:cd17995   160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKtAEQVEKLQALLKPYMLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
468-649 2.52e-81

DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350677 [Multi-domain]  Cd Length: 182  Bit Score: 265.20  E-value: 2.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHEWmhpqtkRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRLL 627
Cdd:cd17919    81 YHGSQRERAQIRAKEK------LDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLL 154
                         170       180
                  ....*....|....*....|..
gi 238624120  628 ITGTPLQNSLKELWSLLHFIMP 649
Cdd:cd17919   155 LTGTPLQNNLEELWALLDFLDP 176
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
467-686 1.14e-73

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: 244.92  E-value: 1.14e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  467 ELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVV 546
Cdd:cd17997     3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  547 VYLGDINSRNMIRTHewmhpQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRL 626
Cdd:cd17997    83 VLIGDKEERADIIRD-----VLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238624120  627 LITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEE-----EHGKGRDSGYTSLHKELEPFLLRRVK 686
Cdd:cd17997   158 LLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEwfnvnNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
465-686 9.70e-71

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: 236.88  E-value: 9.70e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  465 GLELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMN 544
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  545 VVVYLGDINSRNMIrthewmHPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTM-IEFKSN 623
Cdd:cd17996    81 KIVYKGTPDVRKKL------QSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLnTYYHAR 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238624120  624 HRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEE--------EHGKGRDSGYTS--------LHKELEPFLLRRVK 686
Cdd:cd17996   155 YRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQwfntpfanTGEQVKIELNEEetlliirrLHKVLRPFLLRRLK 233
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
465-686 3.58e-70

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: 235.36  E-value: 3.58e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  465 GLELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMN 544
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLR-ERGVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  545 VVVYLGDINSRNMIRTHEWMHPQTKRlKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNH 624
Cdd:cd18009    80 VLLYHGTKEERERLRKKIMKREGTLQ-DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238624120  625 RLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFE---EEHGKGRDSGYTS-------------LHKELEPFLLRRVK 686
Cdd:cd18009   159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFEswfDFSSLSDNAADISnlseereqnivhmLHAILKPFLLRRLK 236
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
468-684 1.36e-67

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: 226.55  E-value: 1.36e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDinsrnmirthewmhpqtkrlklNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRLL 627
Cdd:cd17994    81 YVGD----------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLL 138
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 238624120  628 ITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGK-GRDSGYTSLHKELEPFLLRR 684
Cdd:cd17994   139 LTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADiSKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
468-684 1.52e-67

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: 226.94  E-value: 1.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSR-----NMIRTHEWmhpqtkrlklNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKS 622
Cdd:cd18006    81 YMGDKEKRldlqqDIKSTNRF----------HVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238624120  623 NHRLLITGTPLQNSLKELWSLLHFIMPEKF--HSWEMFEEEHGK-GRDSG-YTSLHKELEPFLLRR 684
Cdd:cd18006   151 DFRLLLTGTPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYSEtDDESEtVEELHLLLQPFLLRR 216
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
468-684 1.32e-62

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: 213.37  E-value: 1.32e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRThEWMHPQTkrlkLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRLL 627
Cdd:cd18003    81 YYGSAKERKLKRQ-GWMKPNS----FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238624120  628 ITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEE----------EHGKGRDSG-YTSLHKELEPFLLRR 684
Cdd:cd18003   156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEwfsnpltamsEGSQEENEElVRRLHKVLRPFLLRR 223
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
468-684 8.43e-62

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: 211.41  E-value: 8.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHEWMHPQT--------------KRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLL 613
Cdd:cd18055    81 YTGDKDSRAIIRENEFSFDDNavkggkkafkmkreAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238624120  614 YKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGK-GRDSGYTSLHKELEPFLLRR 684
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADiSKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
468-684 8.70e-60

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: 205.68  E-value: 8.70e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHEWMH--------------PQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLL 613
Cdd:cd18056    81 YVGDKDSRAIIRENEFSFednairggkkasrmKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238624120  614 YKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGK-GRDSGYTSLHKELEPFLLRR 684
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADiAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
468-684 1.94e-59

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: 204.53  E-value: 1.94e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHEWMH--------------PQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLL 613
Cdd:cd18057    81 YTGDKESRSVIRENEFSFednairsgkkvfrmKKEAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238624120  614 YKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGK-GRDSGYTSLHKELEPFLLRR 684
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADiSKEDQIKKLHDLLGPHMLRR 232
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
774-900 8.34e-59

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: 198.85  E-value: 8.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  774 SGKLILLDKLLVRLKERGHRVLIFSQMVRMLDILAEYLKYRQFLFQRLDGSIKGEMRKQALDHFNADgSEDFCFLLSTRA 853
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 238624120  854 GGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQKKQVNIYRLV 900
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
468-684 1.49e-58

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: 201.96  E-value: 1.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHeW--MHPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHR 625
Cdd:cd18002    81 YWGNPKDRKVLRKF-WdrKNLYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  626 LLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSGYTS-----------LHKELEPFLLRR 684
Cdd:cd18002   160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENktglnehqlkrLHMILKPFMLRR 229
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
468-652 4.24e-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: 198.76  E-value: 4.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFhEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLK-EIGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHEwmhpQTKRLKLNILLTTYEILL---KDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNH 624
Cdd:cd17998    80 YYGSQEERKHLRYDI----LKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANF 155
                         170       180
                  ....*....|....*....|....*...
gi 238624120  625 RLLITGTPLQNSLKELWSLLHFIMPEKF 652
Cdd:cd17998   156 RLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
467-696 4.08e-57

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: 198.35  E-value: 4.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  467 ELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVV 546
Cdd:cd18064    15 KLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRAV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  547 VYLGDINSR-----NMIRTHEWmhpqtkrlklNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFK 621
Cdd:cd18064    95 CLIGDKDQRaafvrDVLLPGEW----------DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFK 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238624120  622 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWE----MFEEEHGKGRDSGYTSLHKELEPFLLRRVKKDVEKSLPAK 696
Cdd:cd18064   165 TTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEdfdsWFDTNNCLGDQKLVERLHMVLRPFLLRRIKADVEKSLPPK 243
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
468-684 1.36e-56

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: 196.03  E-value: 1.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHeHQLYGPFLLVVPLSTLTSWQREIQLWAPlMNVVV 547
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFL-MGIRGPFLIIAPLSTITNWEREFRTWTE-MNAIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHEWMH------PQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFK 621
Cdd:cd18058    79 YHGSQISRQMIQQYEMYYrdeqgnPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238624120  622 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGR-DSGYTSLHKELEPFLLRR 684
Cdd:cd18058   159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKtEEQVKKLQSILKPMMLRR 222
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
467-686 5.64e-55

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: 191.24  E-value: 5.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  467 ELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLyGPFLLVVPLSTLTSWQREIQLWAPLMNVV 546
Cdd:cd18012     4 TLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRK-GPSLVVAPTSLIYNWEEEAAKFAPELKVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  547 VYLGDINSRNMIRTHEwmhpqtkrlKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRL 626
Cdd:cd18012    83 VIHGTKRKREKLRALE---------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRL 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238624120  627 LITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGK-----GRDSGYTSLHKELEPFLLRRVK 686
Cdd:cd18012   154 ALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKpiekdGDEEALEELKKLISPFILRRLK 218
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
452-686 3.14e-54

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: 189.46  E-value: 3.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  452 VPMKKQPHYIggEGLELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTS 531
Cdd:cd18065     2 VRFEESPSYV--KGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  532 WQREIQLWAPLMNVVVYLGDINSRNMIRTHEWMHPQtkrlkLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDS 611
Cdd:cd18065    80 WMNEFKRWVPSLRAVCLIGDKDARAAFIRDVMMPGE-----WDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238624120  612 LLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWE----MFEEEHGKGRDSGYTSLHKELEPFLLRRVK 686
Cdd:cd18065   155 KLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADdfdsWFDTKNCLGDQKLVERLHAVLKPFLLRRIK 233
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
468-684 3.29e-54

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: 189.11  E-value: 3.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEhQLYGPFLLVVPLSTLTSWQREIQLWAPlMNVVV 547
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHEWMHPQTK-RL-----KLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFK 621
Cdd:cd18060    79 YHGSLASRQMIQQYEMYCKDSRgRLipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238624120  622 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGR-DSGYTSLHKELEPFLLRR 684
Cdd:cd18060   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKtEEQVQKLQAILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
468-684 9.86e-52

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: 182.15  E-value: 9.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLnYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLmNVVV 547
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTEL-NVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHE--WMHPQTKRLK----LNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFK 621
Cdd:cd18059    79 YHGSQASRRTIQLYEmyFKDPQGRVIKgsykFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238624120  622 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGR-DSGYTSLHKELEPFLLRR 684
Cdd:cd18059   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKtEEQVQKLQAILKPMMLRR 222
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
468-686 1.01e-49

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: 177.18  E-value: 1.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd18063    24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRthewmhPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTM-IEFKSNHRL 626
Cdd:cd18063   104 YKGTPAMRRSLV------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRI 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238624120  627 LITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEE-------EHGKGRDSGYTS-------LHKELEPFLLRRVK 686
Cdd:cd18063   178 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGERVDLNEEEtiliirrLHKVLRPFLLRRLK 251
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
467-686 2.12e-49

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: 176.39  E-value: 2.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  467 ELRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVV 546
Cdd:cd18062    23 VLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAPSVVKV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  547 VYLGDINSRNMIRthewmhPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTM-IEFKSNHR 625
Cdd:cd18062   103 SYKGSPAARRAFV------PQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRR 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238624120  626 LLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEE-------EHGKGRDSGYTS-------LHKELEPFLLRRVK 686
Cdd:cd18062   177 LLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLRPFLLRRLK 251
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
468-684 3.59e-49

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: 174.81  E-value: 3.59e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLnYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLmNVVV 547
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWTDL-NVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGDINSRNMIRTHE-WMHPQTKRL-----KLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFK 621
Cdd:cd18061    79 YHGSLISRQMIQQYEmYFRDSQGRIirgayRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238624120  622 SNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGR-DSGYTSLHKELEPFLLRR 684
Cdd:cd18061   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKtEEQVQKLQAILKPMMLRR 222
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
468-649 3.04e-48

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: 170.97  E-value: 3.04e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 Y---LGDINSRNMIRTHEWMHPQTKRLKLN--ILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKS 622
Cdd:cd18000    81 LhssGSGTGSEEKLGSIERKSQLIRKVVGDggILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
                         170       180
                  ....*....|....*....|....*..
gi 238624120  623 NHRLLITGTPLQNSLKELWSLLHFIMP 649
Cdd:cd18000   161 PHRLILSGTPIQNNLKELWSLFDFVFP 187
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
258-340 7.50e-46

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349313  Cd Length: 85  Bit Score: 159.76  E-value: 7.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  258 EFETLERVMEMRIGRKGVTGAVTTVYAVEADGDPNANFDPNRQPGEVQYLIKWKNWSHIHNTWETEETLKQQNVKGMKKL 337
Cdd:cd18666     1 EFETIERVLDHRIGRKGATGASTTIYAVEADGDPNAGFDPEDEETEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKL 80

                  ...
gi 238624120  338 DNF 340
Cdd:cd18666    81 ENY 83
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
468-684 1.50e-44

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: 161.77  E-value: 1.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEhQLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVV 547
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDS-GLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  548 YLGdinSRNMIRTHEWMHPQTKRlklNILLTTYEILLKDKSFLGNV-----SWAFIGVDEAHRLKNDDSLLYKTMIEFKS 622
Cdd:cd18001    80 FHG---TSKKERERNLERIQRGG---GVLLTTYGMVLSNTEQLSADdhdefKWDYVILDEGHKIKNSKTKSAKSLREIPA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238624120  623 NHRLLITGTPLQNSLKELWSLLHFIMPEKF----HSWEM-FEEEHGKGRDSGYT------------SLHKELEPFLLRR 684
Cdd:cd18001   154 KNRIILTGTPIQNNLKELWALFDFACNGSLlgtrKTFKMeFENPITRGRDKDATqgekalgsevaeNLRQIIKPYFLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
468-684 1.66e-44

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: 161.75  E-value: 1.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYG-----PFLLVVPlSTLTS-WQREIQLWAP 541
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCILASDHHKRANSFnsenlPSLVVCP-PTLVGhWVAEIKKYFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  542 --LMNVVVYLGDINSRNMIRThewmhpqtKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIE 619
Cdd:cd17999    80 naFLKPLAYVGPPQERRRLRE--------QGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  620 FKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGK----GRDSGYTS------------LHKELEPFLLR 683
Cdd:cd17999   152 LKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKpilaSRDSKASAkeqeagalaleaLHKQVLPFLLR 231

                  .
gi 238624120  684 R 684
Cdd:cd17999   232 R 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
468-684 7.02e-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: 160.24  E-value: 7.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHE--------------------HQLYGPFLLVVPLS 527
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLGKtgtrrdrennrprfkkkppaSSAKKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  528 TLTSWQREIQLWAPLmNVVVYLGDINSRNMIRThewmhpqTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLK 607
Cdd:cd18005    81 VLYNWKDELDTWGHF-EVGVYHGSRKDDELEGR-------LKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  608 NDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEE------EHG-----------KGRDSGy 670
Cdd:cd18005   153 NPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKhfsepiKRGqrhtatarelrLGRKRK- 231
                         250
                  ....*....|....
gi 238624120  671 TSLHKELEPFLLRR 684
Cdd:cd18005   232 QELAVKLSKFFLRR 245
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
468-684 6.06e-40

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: 148.59  E-value: 6.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAhswCKGNscILADEMGLGKTIQTIS---------------FLNYLFHEHQLY--GPFLLVVPLSTLT 530
Cdd:cd18008     1 LLPYQKQGLAWML---PRGG--ILADEMGLGKTIQALAlilatrpqdpkipeeLEENSSDPKKLYlsKTTLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  531 SWQREIQ--LWAPLMNVVVYLGdinSRNMIRTHEWMHPqtkrlklNILLTTYEILLKD----------------KSFLGN 592
Cdd:cd18008    76 QWKDEIEkhTKPGSLKVYVYHG---SKRIKSIEELSDY-------DIVITTYGTLASEfpknkkgggrdskekeASPLHR 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  593 VSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEE----HGKGRDS 668
Cdd:cd18008   146 IRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDiskpFSKNDRK 225
                         250
                  ....*....|....*.
gi 238624120  669 GYTSLHKELEPFLLRR 684
Cdd:cd18008   226 ALERLQALLKPILLRR 241
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
468-684 5.20e-35

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: 134.34  E-value: 5.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWM-----AHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGP----FLLVVPLSTLTSWQREIQL 538
Cdd:cd18004     1 LRPHQREGVQFLydcltGRRGYGGGGAILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  539 WAPLMNVVVYLGDINSRNMIRTHEWMHPQTKRlklNILLTTYEILLKDKSFLGNVSwaFIGV---DEAHRLKNDDSLLYK 615
Cdd:cd18004    81 WLGLRRIKVVTADGNAKDVKASLDFFSSASTY---PVLIISYETLRRHAEKLSKKI--SIDLlicDEGHRLKNSESKTTK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  616 TMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWE----MFEEEHGKGRDSGYTSLHKEL------------EP 679
Cdd:cd18004   156 ALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLAsfrkVFEEPILRSRDPDASEEDKELgaersqelseltSR 235

                  ....*
gi 238624120  680 FLLRR 684
Cdd:cd18004   236 FILRR 240
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
375-431 3.29e-34

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349308  Cd Length: 58  Bit Score: 125.49  E-value: 3.29e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 238624120  375 QYQLVERIIGHSNQKSA-AGYPDYLCKWQGLPYSECSWEDGALISKKFQKCIDEYMSR 431
Cdd:cd18661     1 QYQIVERIIAHSPQKSAaSGYPDYLCKWQGLPYSECTWEDGALISKKFQACIDEYHSR 58
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
468-658 7.28e-34

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: 131.26  E-value: 7.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWM----AHSWC---KGNSCILADEMGLGKTIQTISFLnylfHEHQLYGP----FLLVVPLSTLTSWQREI 536
Cdd:cd18007     1 LKPHQVEGVRFLwsnlVGTDVgsdEGGGCILAHTMGLGKTLQVITFL----HTYLAAAPrrsrPLVLCPASTLYNWEDEF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  537 QLWAPLMNVVVYLGDINSRN--------MIRTheWMHpqtkrlKLNILLTTYEI---LLKDKSFLGNVSWAFIG------ 599
Cdd:cd18007    77 KKWLPPDLRPLLVLVSLSASkradarlrKINK--WHK------EGGVLLIGYELfrnLASNATTDPRLKQEFIAalldpg 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238624120  600 -----VDEAHRLKNDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMF 658
Cdd:cd18007   149 pdllvLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEF 212
CDH1_2_SANT_HL1 pfam18375
CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays ...
1111-1197 2.24e-31

CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays an important role in regulating nucleosome assembly and mobilization. CHD1 consists of double chromodomain, SNF2-related ATPase domain, and a C-terminal DNA-binding domain. The DNA-binding domain contains SANT (Swi3, Ada2, N-CoR, TFIIIB) and SLIDE (SANT-like ISWI) domains in its C-terminal region. SANT domains are structurally related to Myb-like domains are common motifs found in chromatin interacting proteins. Deletion of individual SANT or SLIDE domains in CDH1 does not significantly affect nucleosome binding, but combined deletion of both domains severely compromise binding, suggesting that the SANT-SLIDE motif recognizes DNA/nucleosomes as a single cooperative unit. SANT sequences of Chd1 proteins are the most distantly relation group of sequences relation to other SANT/Myb sequences, and are more diverse than other SANT proteins. The SANT and SLIDE regions are well conserved in both Chd1 and ISWI (imitation switch) remodelling enzymes. This domain comprises the SANT region and the helical linker region 1 (HL1).


Pssm-ID: 465731  Cd Length: 90  Bit Score: 118.61  E-value: 2.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1111 KGFTDAEIRRFIKSYKKFGGPLERLDAIARDAELVDKSEHDLRRLAETVHNGCLRTLKENPCGPER---TSGRRGKVKGP 1187
Cdd:pfam18375    1 KGFTDAEIRRFVKSYKKFSAPLKRLDAIACDAELQEKPLSDLRRLGELLKERCDEAMEEYTEKEDEnpgADGGKKRIRGP 80
                           90
                   ....*....|
gi 238624120  1188 TFRISGVQVN 1197
Cdd:pfam18375   81 SFKLGGVSVN 90
DEXDc smart00487
DEAD-like helicases superfamily;
465-651 1.81e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.51  E-value: 1.81e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120    465 GLELRDYQLDGLNWMAHSWckgNSCILADEMGLGKTIQTISFLNYLFHEHQlYGPFLLVVPLSTLT-SWQREIQLWAPLM 543
Cdd:smart00487    6 FEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTRELAeQWAEELKKLGPSL 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120    544 N--VVVYLGDINSRNMIRthewmhpQTKRLKLNILLTTYEILLKD--KSFLGNVSWAFIGVDEAHRLKND---DSLLYKT 616
Cdd:smart00487   82 GlkVVGLYGGDSKREQLR-------KLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfgDQLEKLL 154
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 238624120    617 MIEFKSNHRLLITGTP---LQNSLKELWSLLHFIMPEK 651
Cdd:smart00487  155 KLLPKNVQLLLLSATPpeeIENLLELFLNDPVFIDVGF 192
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1396-1486 2.30e-28

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


Pssm-ID: 464035  Cd Length: 93  Bit Score: 110.04  E-value: 2.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1396 ELDQKTFS-VCKERMRPVKAALKQLDRPEKGLSEREQLEHTRQCLIKIGDHITECLREYtNPEQIKQWRKNLWIFVSKFT 1474
Cdd:pfam13907    1 DEYESMDEeECKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEET-KKEKKEKLRKHLWSFVSKFW 79
                           90
                   ....*....|....
gi 238624120  1475 E--FDARKLHKLYK 1486
Cdd:pfam13907   80 PnkVSGKKLKEMYK 93
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
775-889 1.64e-27

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: 108.07  E-value: 1.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120   775 GKLILLDKLLvrLKERGHRVLIFSQMVRMLDilAEYLKYRQ-FLFQRLDGSIKGEMRKQALDHFNadgSEDFCFLLSTRA 853
Cdd:pfam00271    1 EKLEALLELL--KKERGGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFR---KGKIDVLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 238624120   854 GGLGINLASADTVVIFDSDWNPQNDLQAQARAHRIG 889
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
487-693 4.53e-26

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: 108.71  E-value: 4.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  487 NSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFL----LVVPLSTLTSWQREIQLW-APLMNVVVYLGDINSRNMIRTH 561
Cdd:cd18067    25 HGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGKWlGGRLQPLAIDGGSKKEIDRKLV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  562 EWMHPQTKRLKLNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELW 641
Cdd:cd18067   105 QWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYF 184
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 238624120  642 SLLHFIMPEKFHSWEMFEEEHG----KGRDSGYTSLHKELEPFLLRRVKKDVEKSL 693
Cdd:cd18067   185 SLVNFVNPGILGTAAEFKKNFElpilKGRDADASEKERQLGEEKLQELISIVNRCI 240
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
468-658 8.95e-26

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: 106.91  E-value: 8.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNW-MAHswckGNSCILADEMGLGKTIQTISFLNYLFHEhqlyGPFLLVVPLSTLTSWQREIQLWAPLMNVv 546
Cdd:cd18010     1 LLPFQREGVCFaLRR----GGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLPP- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  547 vylGDINSRNMIRThEWMHPQTKrlklnILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEF--KSNH 624
Cdd:cd18010    72 ---DDIQVIVKSKD-GLRDGDAK-----VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlkRAKR 142
                         170       180       190
                  ....*....|....*....|....*....|....
gi 238624120  625 RLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMF 658
Cdd:cd18010   143 VILLSGTPALSRPIELFTQLDALDPKLFGRFHDF 176
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
490-684 2.41e-25

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: 106.40  E-value: 2.41e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  490 ILADEMGLGKTIQTISFLnylfhehqLYGPFLLVVPLSTLTSW--QREIQLWAPLMNVVVYLGDINSRNMirthewmhpq 567
Cdd:cd18071    52 ILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWetQFEEHVKPGQLKVYTYHGGERNRDP---------- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  568 TKRLKLNILLTTYEILL-----KDKSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWS 642
Cdd:cd18071   114 KLLSKYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGS 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 238624120  643 LLHF------IMPEKFHSweMFEEEHGKGRDSGYTSLHKELEPFLLRR 684
Cdd:cd18071   194 LLSFlhlkpfSNPEYWRR--LIQRPLTMGDPTGLKRLQVLMKQITLRR 239
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
468-649 1.13e-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: 104.97  E-value: 1.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHSWCK---------GNSCILADEMGLGKTIQTISFLNYLFHEHQLYG--PFLLVVPLSTLTSWQREI 536
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCEslkktkkspGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  537 QLWaplmnvVVYLGDINSRNMIRTHEWMHPQTKRLKLN-------ILLTTYEIL----------LKDK------SFLGNV 593
Cdd:cd18068    81 EKW------QEGLKDEEKIEVNELATYKRPQERSYKLQrwqeeggVMIIGYDMYrilaqernvkSREKlkeifnKALVDP 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 238624120  594 SWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMP 649
Cdd:cd18068   155 GPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKP 210
HELICc smart00490
helicase superfamily c-terminal domain;
805-889 2.78e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 92.27  E-value: 2.78e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120    805 DILAEYLKYRQFLFQRLDGSIKGEMRKQALDHFNADgseDFCFLLSTRAGGLGINLASADTVVIFDSDWNPQNDLQAQAR 884
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNG---KIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 238624120    885 AHRIG 889
Cdd:smart00490   78 AGRAG 82
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
457-649 1.26e-20

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: 92.57  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  457 QPHYIGGEGLeLRDYQLDGLNWMAHSwcKGNSCILADEMGLGKTIQTISFLnYLFHEHQLYGPFLLVVPLSTLTSWQREI 536
Cdd:cd18069     2 KPHQIGGIRF-LYDNIIESLERYKGS--SGFGCILAHSMGLGKTLQVISFL-DVLLRHTGAKTVLAIVPVNTLQNWLSEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  537 QLWAP----LMNV------VVYLGDINSRNMIRTH---EWMHpqtkrlKLNILLTTYEIL-LKDKSFLgnvswafIGVDE 602
Cdd:cd18069    78 NKWLPppeaLPNVrprpfkVFILNDEHKTTAARAKvieDWVK------DGGVLLMGYEMFrLRPGPDV-------VICDE 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 238624120  603 AHRLKNDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMP 649
Cdd:cd18069   145 GHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRP 191
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
468-677 1.92e-20

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: 92.22  E-value: 1.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAHS-----WCKGNSCILADEMGLGKTIQTISFLNYLFHEHQlYGP------FLLVVPLSTLTSWQREI 536
Cdd:cd18066     1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRQGP-YGGkpvikrALIVTPGSLVKNWKKEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  537 QLWAPLMNVVVYLGDINsrnmirthewmHPQTKRLK---LNILLTTYEILLKDKSFLGNVSWAFIGVDEAHRLKNDDSLL 613
Cdd:cd18066    80 QKWLGSERIKVFTVDQD-----------HKVEEFIAsplYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKT 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238624120  614 YKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSW----EMFEEEHGKGRDSGYTSLHKEL 677
Cdd:cd18066   149 TTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLstyrKVYEEPIVRSREPTATPEEKKL 216
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
489-684 2.33e-19

DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350769 [Multi-domain]  Cd Length: 207  Bit Score: 88.11  E-value: 2.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  489 CILADEMGLGKTIQTISFLNYLFHEHqLYGPFLLVVPLSTLTSWQREIQLWAPLMNVVVYLGDINS-RNMIRTHEWMHPq 567
Cdd:cd18011    20 LLLADEVGLGKTIEAGLIIKELLLRG-DAKRVLILCPASLVEQWQDELQDKFGLPFLILDRETAAQlRRLIGNPFEEFP- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  568 tkrlklnILLTTYEiLLKDK----SFLGNVSWAFIGVDEAHRLKN----DDSLLYKTM--IEFKSNHRLLITGTPLQNSL 637
Cdd:cd18011    98 -------IVIVSLD-LLKRSeerrGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGrlLAKRARHVLLLTATPHNGKE 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 238624120  638 KELWSLLHFIMPEKFHSWEMFEEEHGkgrdsgytsLHKELEPFLLRR 684
Cdd:cd18011   170 EDFRALLSLLDPGRFAVLGRFLRLDG---------LREVLAKVLLRR 207
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
375-428 7.14e-19

repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 81.47  E-value: 7.14e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 238624120  375 QYQLVERIIGHsnQKSAAGYPDYLCKWQGLPYSECSWEDGALISKKFQKCIDEY 428
Cdd:cd18659     1 EYTIVERIIAH--REDDEGVTEYLVKWKGLPYDECTWESEEDISDIFQEAIDEY 52
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
286-340 1.00e-15

repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 73.16  E-value: 1.00e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 238624120  286 EADGDPNANFDPNRQPGEVQYLIKWKNWSHIHNTWETEETLKQQnvKGMKKLDNF 340
Cdd:cd18660    16 PVEEASLDLTDPDEPWDEREFLVKWKGKSYLHCTWVTEETLEQL--RGKKKLKNY 68
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
468-684 1.36e-14

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: 75.21  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMahSW------CKGnscILADEMGLGKTIQTISFL-----------------NYLFHEHQLYGPF---- 520
Cdd:cd18072     1 LLLHQKQALAWL--LWrerqkpRGG---ILADDMGLGKTLTMIALIlaqkntqnrkeeekekaLTEWESKKDSTLVpsag 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  521 -LLVVPLSTLTSWQREIQLWAPLMNVVVYLGDINSRnmirthewmHPQTKRLK-LNILLTTYEILLKD---------KSF 589
Cdd:cd18072    76 tLVVCPASLVHQWKNEVESRVASNKLRVCLYHGPNR---------ERIGEVLRdYDIVITTYSLVAKEiptykeesrSSP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  590 LGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFHSWEMFEEEHGKGRDSG 669
Cdd:cd18072   147 LFRIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKG 226
                         250
                  ....*....|....*
gi 238624120  670 YTSLHKELEPFLLRR 684
Cdd:cd18072   227 GERLNILTKSLLLRR 241
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
468-683 1.28e-13

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: 72.76  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNWMAhsWCKGnscILADEMGLGKTIQTISFLnyLFH--------------------EHQLY-------GPF 520
Cdd:cd18070     1 LLPYQRRAVNWML--VPGG---ILADEMGLGKTVEVLALI--LLHprpdndldaadddsdemvccPDCLVaetpvssKAT 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  521 LLVVPLSTLTSWQREIQLWAPL-MNVVVYlgdinsrNMIRTHEWMHPQT-KRL-KLNILLTTYEILLKD----------- 586
Cdd:cd18070    74 LIVCPSAILAQWLDEINRHVPSsLKVLTY-------QGVKKDGALASPApEILaEYDIVVTTYDVLRTElhyaeanrsnr 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  587 -----------KSFLGNVSWAFIGVDEAHRLKNDDSLLYKTMIEFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKF--H 653
Cdd:cd18070   147 rrrrqkryeapPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFcdS 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 238624120  654 SWEMFEEEHGKGRDSGYTSLHKELEPFLLR 683
Cdd:cd18070   227 DWWARVLIRPQGRNKAREPLAALLKELLWR 256
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
285-340 7.35e-12

repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349312  Cd Length: 65  Bit Score: 62.02  E-value: 7.35e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 238624120  285 VEADGDPNANFDPNrqpGEVQYLIKWKNWSHIHNTWETEETLKQqnVKGMKKLDNF 340
Cdd:cd18665    13 LKEGLEEGELDDPK---ENYEFLIKWTDESHLHNTWETYESLKQ--VRGLKKVDNY 63
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
379-431 5.22e-11

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 59.13  E-value: 5.22e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 238624120   379 VERIIGHSNQKSaaGYPDYLCKWQGLPYSECSWEDGALISKKfQKCIDEYMSR 431
Cdd:pfam00385    3 VERILDHRKDKG--GKEEYLVKWKGYPYDENTWEPEENLSKC-PELIEEFKDR 52
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
468-647 1.30e-10

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: 63.14  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGLNW-MAHSWCkgnsCILADeMGLGKTIQTISFLNYLFHEhQLYGPFLLVVPLSTLTS-WQREIQLWAPLMNV 545
Cdd:cd18013     1 PHPYQKVAINFiIEHPYC----GLFLD-MGLGKTVTTLTALSDLQLD-DFTRRVLVIAPLRVARStWPDEVEKWNHLRNL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  546 VVYLGDINSRNMIRThewmhpqtkrLKLNILLTTYEI-LLKD--KSFLGNVSWAFIGVDEAHRLKNDDSLLYKTM--IEF 620
Cdd:cd18013    75 TVSVAVGTERQRSKA----------ANTPADLYVINReNLKWlvNKSGDPWPFDMVVIDELSSFKSPRSKRFKALrkVRP 144
                         170       180
                  ....*....|....*....|....*..
gi 238624120  621 KSNHRLLITGTPLQNSLKELWSLLHFI 647
Cdd:cd18013   145 VIKRLIGLTGTPSPNGLMDLWAQIALL 171
CHROMO smart00298
Chromatin organization modifier domain;
379-428 1.53e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 49.52  E-value: 1.53e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 238624120    379 VERIIGHSNQKSaaGYPDYLCKWQGLPYSECSWEDGALISkKFQKCIDEY 428
Cdd:smart00298    4 VEKILDHRWKKK--GELEYLVKWKGYSYSEDTWEPEENLL-NCSKKLDNY 50
CHROMO smart00298
Chromatin organization modifier domain;
302-340 1.72e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 49.52  E-value: 1.72e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 238624120    302 GEVQYLIKWKNWSHIHNTWETEETLKQqnvkGMKKLDNF 340
Cdd:smart00298   16 GELEYLVKWKGYSYSEDTWEPEENLLN----CSKKLDNY 50
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
378-428 9.77e-07

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and 4, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD3 and CHD4, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. Human CHD3 (also named Mi-2 alpha) and CHD4 (also named Mi-2 beta) are coexpressed in many cell lines and tissues and may act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). The proteins form distinct CHD3- and CHD4-NuRD complexes that repress, as well as activate gene transcription of overlapping and specific target genes. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 47.26  E-value: 9.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 238624120  378 LVERIIGHSnqKSAAGYPDYLCKWQGLPYSECSWE-DGALISkKFQKCIDEY 428
Cdd:cd18662     5 QIHRIINHR--VDKDGNTWYLVKWRDLPYDQSTWEsEDDDIP-DYEKHIQEY 53
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
463-1048 1.07e-06

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 53.49  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  463 GEGLELRDYQLDGLN-WMAHSWCKGNSCILADEMGLGKTIqTISFLnylFHEHQLYGPFLLVVPLSTL-TSWQREIQLWa 540
Cdd:COG1061    76 GTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTGKTV-LALAL---AAELLRGKRVLVLVPRRELlEQWAEELRRF- 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  541 plmnvvvyLGDINSrnmirthewmHPQTKRLKLNILLTTYEILLKDKSF--LGNvSWAFIGVDEAHRLKnddSLLYKTMI 618
Cdd:COG1061   151 --------LGDPLA----------GGGKKDSDAPITVATYQSLARRAHLdeLGD-RFGLVIIDEAHHAG---APSYRRIL 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  619 E-FKSNHRLLITGTPLqnslkelwsllhfimpekfhswemfeeehgkgRDSGytslhKELEPFLLRRVKkdVEKSLPAKV 697
Cdd:COG1061   209 EaFPAAYRLGLTATPF--------------------------------RSDG-----REILLFLFDGIV--YEYSLKEAI 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  698 EQilrvemsavqkqyyKWILTRNYKAlskgtkgstsgflnIMMELKKccnhcylikppDDNEFYNRQEGLQHLVRSSG-- 775
Cdd:COG1061   250 ED--------------GYLAPPEYYG--------------IRVDLTD-----------ERAEYDALSERLREALAADAer 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  776 KLILLDKLLVRLKeRGHRVLIFSQMVRMLDILAEYLKYRQFLFQRLDGSIKGEMRKQALDHFNADGSEdfcFLLSTRAGG 855
Cdd:COG1061   291 KDKILRELLREHP-DDRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELR---ILVTVDVLN 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  856 LGINLASADTVVIFDSDWNPQNDLQAQARAHRIGQ-KKQVNIYRLVTkgsVEEEIIERAKKKmvLDHLVIQRMDTTGKTV 934
Cdd:COG1061   367 EGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPgKEDALVYDFVG---NDVPVLEELAKD--LRDLAGYRVEFLDEEE 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  935 LHTGAAPSSSTPFNKEELSAILKFGAEELFKEPEGEEQEPQEMDIDEILKRAETRENDPGPSTVGEELLSQFKVANFSMM 1014
Cdd:COG1061   442 SEELALLIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALA 521
                         570       580       590
                  ....*....|....*....|....*....|....
gi 238624120 1015 EDEEIDMDTERNDRNWDDIIPEDHRRRLEEEERQ 1048
Cdd:COG1061   522 KLLKLLLLLLLLLLLELLELLAALLRLEELAALL 555
ResIII pfam04851
Type III restriction enzyme, res subunit;
466-632 1.29e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 49.98  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120   466 LELRDYQLDGLNWMAHSWCKGNSCILAdEM--GLGKTIqTISFLNYLFHEHQLYGPFLLVVP-LSTLTSWQREIQLWAPl 542
Cdd:pfam04851    2 LELRPYQIEAIENLLESIKNGQKRGLI-VMatGSGKTL-TAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLP- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120   543 mNVVVYLGDINSRNMIRthewmhpqtKRLKLNILLTTY-----EILLKDKSFLGNVSWAFIgVDEAHRLkNDDSllYKTM 617
Cdd:pfam04851   79 -NYVEIGEIISGDKKDE---------SVDDNKIVVTTIqslykALELASLELLPDFFDVII-IDEAHRS-GASS--YRNI 144
                          170
                   ....*....|....*.
gi 238624120   618 IE-FKSNHRLLITGTP 632
Cdd:pfam04851  145 LEyFKPAFLLGLTATP 160
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
299-328 1.51e-06

CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this group are chromodomains or chromo shadow domains; these are SH3-fold-beta-barrel domains of the chromo-like superfamily. Chromodomains lack the first strand of the SH3-fold-beta-barrel, this first strand is altered by insertion in the chromo shadow domains. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. Chromodomain-containing proteins include: i) those having an N-terminal chromodomain followed by a related chromo shadow domain, such as Drosophila and human heterochromatin protein Su(var)205 (HP1), and mammalian modifier 1 and 2; ii) those having a single chromodomain, such as Drosophila protein Polycomb (Pc), mammalian modifier 3, human Mi-2 autoantigen, and several yeast and Caenorhabditis elegans proteins of unknown function; iii) those having paired tandem chromodomains, such as mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1; (iv) and elongation factor eEF3, a member of the ATP-binding cassette (ABC) family of proteins, that serves an essential function in the translation cycle of fungi. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain.


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 46.70  E-value: 1.51e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 238624120  299 RQPGEVQYLIKWKNWSHIHNTWETEETLKQ 328
Cdd:cd00024    11 VRKGKLEYLVKWKGYPPEENTWEPEENLTN 40
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
302-324 2.46e-06

chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG (polycomb-group) chromodomain protein Polycomb (Pc) from Drosophila melanogaster, anthropod, worm, and sea cucumber, and similar proteins. Pc is a component of the Polycomb-group (PcG) multiprotein PRC1 complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. The core subunits of PRC1 are polycomb (Pc), polyhomeotic (Ph), posterior sex combs (Psc), and sex comb extra (Sce, also known as dRing). Polycomb (Pc) plays a role in modulating life span in flies, it negatively regulates longevity.


Pssm-ID: 349291  Cd Length: 54  Bit Score: 45.92  E-value: 2.46e-06
                          10        20
                  ....*....|....*....|...
gi 238624120  302 GEVQYLIKWKNWSHIHNTWETEE 324
Cdd:cd18644    17 GKVEYLVKWKGWSNKHNTWEPEE 39
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
1576-1666 3.11e-06

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 51.82  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1576 RERERDQYRERG-ERPDSRYYSESKHRklDEHRSSREHRSESNSKDRthSEHRFHSEHRSgSSDYSHHKSSRdyryhsdw 1654
Cdd:TIGR01642    9 REKSRGRDRDRSsERPRRRSRDRSRFR--DRHRRSRERSYREDSRPR--DRRRYDSRSPR-SLRYSSVRRSR-------- 75
                           90
                   ....*....|..
gi 238624120  1655 qmeHRSPRDQRS 1666
Cdd:TIGR01642   76 ---DRPRRRSRS 84
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
375-431 4.46e-06

repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349311  Cd Length: 59  Bit Score: 45.73  E-value: 4.46e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 238624120  375 QYQLVERIIG--HSNQKSAAGYPDYLCKWQGLPYSECSWEDGALISKKFQKCIDEYMSR 431
Cdd:cd18664     1 EFHVVERIIAsqRASLEDGTSQLQYLVKWRRLNYDECTWEDATLIAKLAPEQVDHFQNR 59
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
302-324 8.02e-06

chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier (chromo) domain of Polycomb and Polycomb-group (PcG) chromobox (CBX) family proteins such as CBX2, CBX4, CBX6, CBX7, and CBX8. These CBX proteins are components of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349277  Cd Length: 49  Bit Score: 44.30  E-value: 8.02e-06
                          10        20
                  ....*....|....*....|...
gi 238624120  302 GEVQYLIKWKNWSHIHNTWETEE 324
Cdd:cd18627    14 GKVEYLVKWKGWSQKYNTWEPEE 36
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
792-892 1.09e-05

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 45.00  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  792 HRVLIFSQMVRMLDILAEYLKyrqflfqrldgsikgemrkqaldhfnadgsedfcFLLSTRAGGLGINLASADTVVIFDS 871
Cdd:cd18785     4 VKIIVFTNSIEHAEEIASSLE----------------------------------ILVATNVLGEGIDVPSLDTVIFFDP 49
                          90       100
                  ....*....|....*....|.
gi 238624120  872 DWNPQNDLQAQARAHRIGQKK 892
Cdd:cd18785    50 PSSAASYIQRVGRAGRGGKDE 70
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
468-632 1.12e-05

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: 46.92  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  468 LRDYQLDGL-NWMAHSWCKGNSCILAdeMGLGKTIQTISFLNYLFHEhqlygPFLLVVP-LSTLTSWQREIQlwAPLMNV 545
Cdd:cd17926     1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTLTALALIAYLKEL-----RTLIVVPtDALLDQWKERFE--DFLGDS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  546 VVYLGDINSRNMIRThewmhpqtkrlkLNILLTTYEIL---LKDKSFLGNvSWAFIGVDEAHRLkndDSLLYKTMI-EFK 621
Cdd:cd17926    72 SIGLIGGGKKKDFDD------------ANVVVATYQSLsnlAEEEKDLFD-QFGLLIVDEAHHL---PAKTFSEILkELN 135
                         170
                  ....*....|.
gi 238624120  622 SNHRLLITGTP 632
Cdd:cd17926   136 AKYRLGLTATP 146
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
282-328 2.25e-05

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349324  Cd Length: 57  Bit Score: 43.49  E-value: 2.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 238624120  282 VYAVEADGDPNANFDPNRQPGEVQYLIKWKNWSHIHNTWETEETLKQ 328
Cdd:cd18968     1 EYEVEVILAARVVKDAESRKKGWKYLVKWAGYPDEENTWEPEESFDG 47
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
302-327 2.84e-05

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 42.95  E-value: 2.84e-05
                           10        20
                   ....*....|....*....|....*.
gi 238624120   302 GEVQYLIKWKNWSHIHNTWETEETLK 327
Cdd:pfam00385   15 GKEEYLVKWKGYPYDENTWEPEENLS 40
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
1553-1659 1.56e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 46.42  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1553 DSYRKSSDSRKRPYSSFSNGKDHRERERDQYRERGERpdsRYYSESKHRKLDEHRSSREHRSESNSKDRTH----SEHRF 1628
Cdd:TIGR01642    2 DEEPDREREKSRGRDRDRSSERPRRRSRDRSRFRDRH---RRSRERSYREDSRPRDRRRYDSRSPRSLRYSsvrrSRDRP 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 238624120  1629 HSEHRSGSSDYSHHKSSRDYRYHSDWQMEHR 1659
Cdd:TIGR01642   79 RRRSRSVRSIEQHRRRLRDRSPSNQWRKDDK 109
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
300-328 1.84e-04

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 41.17  E-value: 1.84e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 238624120  300 QPGEVQ-YLIKWKNWSHIHNTWETEETLKQ 328
Cdd:cd18668    25 EEIEVEeYLVKYKNFSYLHCEWKTEEELEK 54
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
302-326 2.34e-04

chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 2 (CBX2), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells.


Pssm-ID: 349294  Cd Length: 53  Bit Score: 40.42  E-value: 2.34e-04
                          10        20
                  ....*....|....*....|....*
gi 238624120  302 GEVQYLIKWKNWSHIHNTWETEETL 326
Cdd:cd18647    17 GKLEYLVKWRGWSSKHNSWEPEENI 41
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
379-412 2.37e-04

CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this group are chromodomains or chromo shadow domains; these are SH3-fold-beta-barrel domains of the chromo-like superfamily. Chromodomains lack the first strand of the SH3-fold-beta-barrel, this first strand is altered by insertion in the chromo shadow domains. The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. Chromodomain-containing proteins include: i) those having an N-terminal chromodomain followed by a related chromo shadow domain, such as Drosophila and human heterochromatin protein Su(var)205 (HP1), and mammalian modifier 1 and 2; ii) those having a single chromodomain, such as Drosophila protein Polycomb (Pc), mammalian modifier 3, human Mi-2 autoantigen, and several yeast and Caenorhabditis elegans proteins of unknown function; iii) those having paired tandem chromodomains, such as mammalian DNA-binding/helicase proteins CHD-1 to CHD-4 and yeast protein CHD1; (iv) and elongation factor eEF3, a member of the ATP-binding cassette (ABC) family of proteins, that serves an essential function in the translation cycle of fungi. eEF3 is a soluble factor lacking a transmembrane domain and having two ABC domains arranged in tandem, with a unique chromodomain inserted within the ABC2 domain.


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 40.15  E-value: 2.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 238624120  379 VERIIGHSNQKsaaGYPDYLCKWQGLPYSECSWE 412
Cdd:cd00024     3 VEKILDHRVRK---GKLEYLVKWKGYPPEENTWE 33
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
376-412 2.66e-04

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 40.35  E-value: 2.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 238624120  376 YQLVERIIG---HSNQKSAAGYPDYLCKWQGLPYSECSWE 412
Cdd:cd18663     3 YVEVDRILDvsvSTDPNTGEPVTHYLVKWCSLPYEDSTWE 42
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
1541-1656 2.92e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 45.27  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1541 RYHEHSKEHhasDSYRKSSDSRKRPYS-SFSNGKDHRERERDQYRERGERPDSRYYSESKHRKLDEHRSSREHRSESNSK 1619
Cdd:TIGR01642    7 REREKSRGR---DRDRSSERPRRRSRDrSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLRYSSVRRSRDRPRRRSR 83
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 238624120  1620 DRTH-SEHRFHSEHRSGSsdyshHKSSRDYRYHSDWQM 1656
Cdd:TIGR01642   84 SVRSiEQHRRRLRDRSPS-----NQWRKDDKKRSLWDI 116
PHA03118 PHA03118
multifunctional expression regulator; Provisional
1546-1648 6.88e-04

multifunctional expression regulator; Provisional


Pssm-ID: 165391  Cd Length: 474  Bit Score: 44.29  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120 1546 SKEHHASDSYRKSSDSRKRPYSSFSNGKDHRERERDQYR-ERGERPDSRYYSESKHRKLDEHRSSREHRSESNSKDRTHS 1624
Cdd:PHA03118   88 KKAHGRREGYHHDDEKCLVTFLDDINHHGGRDTEPGHAHiENGERKSPKSYNQQSRKKHRDESLRNKHGRPSGPPAMSPG 167
                          90       100
                  ....*....|....*....|....
gi 238624120 1625 EHRFHSEHRSGSSDYSHHKSSRDY 1648
Cdd:PHA03118  168 EHFDQTHDAEYRLRFNERDARRDR 191
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
1576-1686 8.21e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 44.11  E-value: 8.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1576 RERERDQYRErgerpdsryysesKHRKLDEHRSSREHRSESNSKDRTHSEHRFHSEHRSGSSDYSHHKSSRDYRYHSDWQ 1655
Cdd:TIGR01642    1 RDEEPDRERE-------------KSRGRDRDRSSERPRRRSRDRSRFRDRHRRSRERSYREDSRPRDRRRYDSRSPRSLR 67
                           90       100       110
                   ....*....|....*....|....*....|.
gi 238624120  1656 MEHRspRDQRSPIGHRSpfeYSSDHKSTPEQ 1686
Cdd:TIGR01642   68 YSSV--RRSRDRPRRRS---RSVRSIEQHRR 93
CD_HP1beta_Cbx1 cd18650
chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier ...
302-326 8.33e-04

chromodomain of heterochromatin protein 1 homolog beta; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog beta (also known as HP1beta, CBX1, and chromobox 1), and related proteins. HP1beta is a highly conserved non-histone protein, which is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta, and HP1gamma (also known as Cbx3).


Pssm-ID: 349297  Cd Length: 50  Bit Score: 38.77  E-value: 8.33e-04
                          10        20
                  ....*....|....*....|....*
gi 238624120  302 GEVQYLIKWKNWSHIHNTWETEETL 326
Cdd:cd18650    15 GKVEYLLKWKGFSDEDNTWEPEENL 39
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
302-326 8.55e-04

chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier (chromo) domain of heterochromatin protein 1 homolog alpha (also known as HP1alpha, Cbx5, and Chromobox 5), and related proteins. HP1alpha has diverse functions in heterochromatin formation, gene regulation, and mitotic progression, and forms complex networks of gene, RNA, and protein interactions. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha, HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349298  Cd Length: 50  Bit Score: 38.82  E-value: 8.55e-04
                          10        20
                  ....*....|....*....|....*
gi 238624120  302 GEVQYLIKWKNWSHIHNTWETEETL 326
Cdd:cd18651    15 GQVEYLLKWKGFSEEHNTWEPEKNL 39
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
486-613 1.06e-03

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 41.23  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  486 GNSCILADEMGLGKTIQtisFLNYLFHEHQLYGP-FLLVVPLSTLT-SWQREIQLWAPLMNVVVYLGDinSRNMIRTHEw 563
Cdd:cd00046     1 GENVLITAPTGSGKTLA---ALLAALLLLLKKGKkVLVLVPTKALAlQTAERLRELFGPGIRVAVLVG--GSSAEEREK- 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 238624120  564 mhpqTKRLKLNILLTTYEILLKDKSFLGNVS---WAFIGVDEAHR-LKNDDSLL 613
Cdd:cd00046    75 ----NKLGDADIIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHAlLIDSRGAL 124
CD_HP1_like cd18631
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
302-326 1.22e-03

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349281  Cd Length: 50  Bit Score: 38.19  E-value: 1.22e-03
                          10        20
                  ....*....|....*....|....*
gi 238624120  302 GEVQYLIKWKNWSHIHNTWETEETL 326
Cdd:cd18631    15 GKVEYLLKWKGYPDEDNTWEPEENL 39
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
1541-1635 1.28e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 43.37  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1541 RYHEHSKEHHaSDSYRKSSDSRKRPYSSFSNGKDHRERERDQYRERGERPDSRYYSESKHRKlDEHRSSREHRSESNSKD 1620
Cdd:TIGR01622    1 RYRDRERERL-RDSSSAGDRDRRRDKGRERSRDRSRDRERSRSRRRDRHRDRDYYRGRERRS-RSRRPNRRYRPREKRRR 78
                           90
                   ....*....|....*
gi 238624120  1621 RTHSEHRFHSEHRSG 1635
Cdd:TIGR01622   79 RGDSYRRRRDDRRSR 93
CD_HP1a_insect cd18653
chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. ...
302-331 2.02e-03

chromodomain of insect HP1a; CHRomatin Organization Modifier (chromo) domain of insect HP1a. HP1a is a member of the heterochromatin protein family, and is enriched in the heterochromatin and associated with centromeres. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. In Drosophila, there are at least five HP1 family proteins, this subgroup includes the CD of Drosophila melanogaster HP1a.


Pssm-ID: 349300  Cd Length: 50  Bit Score: 37.70  E-value: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 238624120  302 GEVQYLIKWKNWSHIHNTWETEETLKQQNV 331
Cdd:cd18653    15 GKVEYYLKWKGYPETENTWEPEENLDCQDL 44
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
302-326 3.09e-03

chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 4 (CBX4), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. In addition to a chromodomain with H3K27me3-binding activity, Cbx4 contains two SUMO-interacting motifs responsible for its small ubiquitin-related modifier (SUMO) E3 ligase activity. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, for example CBX8 promotes proliferation while suppressing metastasis, in colorectal carcinoma progression. CBX4 may serve as a tumor suppressor in colorectal carcinoma, and has been shown to be an oncogene in osteosarcoma and breast cancer.


Pssm-ID: 349292  Cd Length: 55  Bit Score: 37.34  E-value: 3.09e-03
                          10        20
                  ....*....|....*....|....*
gi 238624120  302 GEVQYLIKWKNWSHIHNTWETEETL 326
Cdd:cd18645    17 GRVEYLVKWRGWSPKYNTWEPEENI 41
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
302-326 4.74e-03

chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of chromobox homolog 8 (CBX8), a component of the PcG repressive complex PRC1, one of the two classes of PRCs. PcG proteins form large multiprotein complexes (PcG bodies) which are involved in the stable repression of genes involved in development, signaling or cancer via chromatin-based epigenetic modifications. Mammalian PRC1 includes canonical (cPRC1) and non-canonical complexes; cPRC1, contains four core subunits including one CBX protein (CBX2, CBX4, and CBX6-CBX8) that binds H3K27me3. CBX family members have different affinity for H3K27me3, with CBX7 having the highest binding capability. The human CBX proteins show distinct nuclear localizations and contribute differently to transcriptional repression. Some CBX proteins of the PRC1 complex have been implicated in transcriptional activation as well as in PRC1-independent roles in embryonic stem cells and in somatic cells. CBX proteins may act as an oncogene or tumor suppressor in a cell-type-dependent manner, CBX8 for example promotes proliferation while suppressing metastasis, in colorectal carcinoma progression.


Pssm-ID: 349296  Cd Length: 55  Bit Score: 37.01  E-value: 4.74e-03
                          10        20
                  ....*....|....*....|....*
gi 238624120  302 GEVQYLIKWKNWSHIHNTWETEETL 326
Cdd:cd18649    18 GRMEYLVKWKGWSQKYSTWEPEENI 42
HisXaaSer_A3 NF038309
His-Xaa-Ser repeat protein HxsA3; This model represents an alternate form of the His-Xaa-Ser ...
1621-1652 4.99e-03

His-Xaa-Ser repeat protein HxsA3; This model represents an alternate form of the His-Xaa-Ser repeat protein HxsA, while TIGR03979 represents a more common form. The model covers a conserved N-terminal region, followed by the His-Xaa-Ser repeat region, but does not cover the C-terminal region, which is highly variable in this branch of His-Xaa-Ser repeat family protein.


Pssm-ID: 439608  Cd Length: 81  Bit Score: 37.67  E-value: 4.99e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 238624120 1621 RTHSEHRFHSEHRSGSSD-YSHHKSSRDYRYHS 1652
Cdd:NF038309   48 RSHSSHSSHSSHSSGSSGgHSSHSSHSSHSSHS 80
CD_HP1_like cd18960
chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; ...
378-412 6.34e-03

chromodomain of heterochromatin protein 1 proteins, including HP1alpha, HP1beta, and HP1gamma; uncharacterized subgroup; CHRomatin Organization Modifier (chromo) domain of mammalian HP1alpha (Cbx5), HP1beta (Cbx1), HP1gamma (Cbx5), and similar proteins. HP1 has diverse functions in heterochromatin formation and impacts both gene expression and gene silencing. HP1 has two conserved protein-protein interaction domains, a single N-terminal chromodomain (CD) which can bind to histone proteins via methylated lysine residues, and a related C-terminal chromo shadow domain (CSD) which is responsible for the homodimerization and interaction with a number of chromatin-associated non-histone proteins; a flexible hinge region separates the CD and CSD and may bind nucleic acid. HP1 is a highly conserved non-histone chromosomal protein that is evolutionarily conserved from fission yeast to plants and animals. There are three human homologs of HP1 proteins: HP1alpha (also known as Cbx5), HP1beta (also known as Cbx1), and HP1gamma (also known as Cbx3).


Pssm-ID: 349316  Cd Length: 51  Bit Score: 36.38  E-value: 6.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 238624120  378 LVERIIghSNQKSAAGYPDYLCKWQGLPYSECSWE 412
Cdd:cd18960     3 VVERIL--DKRLGRNGGEEFLIKWQGFPESDSSWE 35
SF-CC1 TIGR01622
splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors ...
1556-1666 7.48e-03

splicing factor, CC1-like family; This model represents a subfamily of RNA splicing factors including the Pad-1 protein (N. crassa), CAPER (M. musculus) and CC1.3 (H.sapiens). These proteins are characterized by an N-terminal arginine-rich, low complexity domain followed by three (or in the case of 4 H. sapiens paralogs, two) RNA recognition domains (rrm: pfam00706). These splicing factors are closely related to the U2AF splicing factor family (TIGR01642). A homologous gene from Plasmodium falciparum was identified in the course of the analysis of that genome at TIGR and was included in the seed.


Pssm-ID: 273721 [Multi-domain]  Cd Length: 494  Bit Score: 41.06  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238624120  1556 RKSSDSRKRPYSSFSNGKDHRERERDQYRERG---ERPDSRYYSESKHRKLDEHRSSREHRSESNSKDRTHS---EHRFH 1629
Cdd:TIGR01622    1 RYRDRERERLRDSSSAGDRDRRRDKGRERSRDrsrDRERSRSRRRDRHRDRDYYRGRERRSRSRRPNRRYRPrekRRRRG 80
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 238624120  1630 SEHRSGSSDYSHHKSSRDYRYHSDWQMEHrSPRDQRS 1666
Cdd:TIGR01622   81 DSYRRRRDDRRSRREKPRARDGTPEPLTE-DERDRRT 116
 
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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