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Conserved domains on  [gi|164448642|ref|NP_001106734|]
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chromodomain-helicase-DNA-binding protein 1 [Bombyx mori]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
204-421 9.72e-154

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: 462.21  E-value: 9.72e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  204 HLRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVV 283
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  284 TYIGDVSSRDIIRQFEWSFSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRL 363
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164448642  364 LVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKGYEKLHKQLEPFILRR 421
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKGIADLHKELEPFILRR 218
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
205-779 8.46e-150

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: 481.22  E-value: 8.46e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWckDNSV--ILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINV 282
Cdd:PLN03142  170 MRDYQLAGLNWLIRLY--ENGIngILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  283 VTYIGDVSSRDIIRQfewsfSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHR 362
Cdd:PLN03142  248 VKFHGNPEERAHQRE-----ELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYR 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  363 LLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEK----DHEDAATKGYEKLHKQLEPFILRRQKKDVEKSLPAKVEQIL 438
Cdd:PLN03142  323 LLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEwfqiSGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETIL 402
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  439 RVEMTSIQKQYYKWILTKNYSALRKGvkGSINTFINIVIELKKCCNHALLtkpedFESRASLATSDAVEKLLRGSGKLLL 518
Cdd:PLN03142  403 KVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYL-----FQGAEPGPPYTTGEHLVENSGKMVL 475
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  519 LDKLLCRLKETGHRVLIFSQMVRMLDILAEYLQRRHFPFQRLDGSIKGELRKQALDHFNAEGSQDFCFLLSTRAGGLGIN 598
Cdd:PLN03142  476 LDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGIN 555
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  599 LATADTVIIFDSDWNPQNDLQAQARAHRIGQKNQVNIYRLVTARSVEEDIVERAKRKMVLDHLVIQRmdttGKTVLNKRd 678
Cdd:PLN03142  556 LATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ----GRLAEQKT- 630
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  679 asgttannpFNKEDLNAILKFGAEELFKDDEENDEDPvcDIDEILQRAEtrdEGPAMVgDELLSAF--KVASFTFDEEKA 756
Cdd:PLN03142  631 ---------VNKDELLQMVRYGAEMVFSSKDSTITDE--DIDRIIAKGE---EATAEL-DAKMKKFteDAIKFKMDDTAE 695
                         570       580
                  ....*....|....*....|....
gi 164448642  757 VNELK-KDNADEEPKDWDDIIPEN 779
Cdd:PLN03142  696 LYDFDdEDDKDENKLDFKKIVSDN 719
CDH1_2_SANT_HL1 pfam18375
CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays ...
866-950 5.93e-43

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: 151.35  E-value: 5.93e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   866 KGFTDQEIRRFVKSYKKFSAPLKHLDSIACDAELQEKPLAELKRLGEILQERCKAVLSETAEPSEQNEGRKNNRK----- 940
Cdd:pfam18375    1 KGFTDAEIRRFVKSYKKFSAPLKRLDAIACDAELQEKPLSDLRRLGELLKERCDEAMEEYTEKEDENPGADGGKKrirgp 80
                           90
                   ....*....|
gi 164448642   941 TFKLGGVPVN 950
Cdd:pfam18375   81 SFKLGGVSVN 90
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
2-76 3.64e-36

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: 131.64  E-value: 3.64e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164448642    2 RRGKKGVTGNVTTIYYIEEHGDPNEGCDPNDEDsTEPQYLIKWKGWSHIHNTWESEKTINDQKVKGLKKLENFIK 76
Cdd:cd18666    12 RIGRKGATGASTTIYAVEADGDPNAGFDPEDEE-TEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKLENYKK 85
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1175-1264 1.18e-25

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: 101.95  E-value: 1.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  1175 DLDPSVFEE-CKEKMRPVKKALKALDNPDQSLSETEQVSRTRACLTQIGTQIDLCVEAYPDSQKVEWRSNLWYFVSKFTN 1253
Cdd:pfam13907    1 DEYESMDEEeCKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEETKKEKKEKLRKHLWSFVSKFWP 80
                           90
                   ....*....|...
gi 164448642  1254 --FDAKQLYKLYK 1264
Cdd:pfam13907   81 nkVSGKKLKEMYK 93
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
110-166 2.22e-15

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: 71.45  E-value: 2.22e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 164448642  110 YNNVERIIAEqnRELEGGGTahEYFCKWESLPYADATWEDAVLIEKRWPVEVEHFKS 166
Cdd:cd18659     2 YTIVERIIAH--REDDEGVT--EYLVKWKGLPYDECTWESEEDISDIFQEAIDEYKK 54
 
Name Accession Description Interval E-value
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
204-421 9.72e-154

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: 462.21  E-value: 9.72e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  204 HLRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVV 283
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  284 TYIGDVSSRDIIRQFEWSFSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRL 363
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164448642  364 LVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKGYEKLHKQLEPFILRR 421
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKGIADLHKELEPFILRR 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
205-779 8.46e-150

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 481.22  E-value: 8.46e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWckDNSV--ILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINV 282
Cdd:PLN03142  170 MRDYQLAGLNWLIRLY--ENGIngILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  283 VTYIGDVSSRDIIRQfewsfSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHR 362
Cdd:PLN03142  248 VKFHGNPEERAHQRE-----ELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYR 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  363 LLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEK----DHEDAATKGYEKLHKQLEPFILRRQKKDVEKSLPAKVEQIL 438
Cdd:PLN03142  323 LLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEwfqiSGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETIL 402
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  439 RVEMTSIQKQYYKWILTKNYSALRKGvkGSINTFINIVIELKKCCNHALLtkpedFESRASLATSDAVEKLLRGSGKLLL 518
Cdd:PLN03142  403 KVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYL-----FQGAEPGPPYTTGEHLVENSGKMVL 475
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  519 LDKLLCRLKETGHRVLIFSQMVRMLDILAEYLQRRHFPFQRLDGSIKGELRKQALDHFNAEGSQDFCFLLSTRAGGLGIN 598
Cdd:PLN03142  476 LDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGIN 555
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  599 LATADTVIIFDSDWNPQNDLQAQARAHRIGQKNQVNIYRLVTARSVEEDIVERAKRKMVLDHLVIQRmdttGKTVLNKRd 678
Cdd:PLN03142  556 LATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ----GRLAEQKT- 630
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  679 asgttannpFNKEDLNAILKFGAEELFKDDEENDEDPvcDIDEILQRAEtrdEGPAMVgDELLSAF--KVASFTFDEEKA 756
Cdd:PLN03142  631 ---------VNKDELLQMVRYGAEMVFSSKDSTITDE--DIDRIIAKGE---EATAEL-DAKMKKFteDAIKFKMDDTAE 695
                         570       580
                  ....*....|....*....|....
gi 164448642  757 VNELK-KDNADEEPKDWDDIIPEN 779
Cdd:PLN03142  696 LYDFDdEDDKDENKLDFKKIVSDN 719
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
137-658 3.34e-125

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.22  E-value: 3.34e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  137 WESLPYADATWEDAVLIEKRWPVEVEHFKSREAAKSTPSRHCPVLKRRPKFHQIKEQPEYVGKDssyhLRDYQMDGLNWL 216
Cdd:COG0553   178 LGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKAT----LRPYQLEGAAWL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  217 IHSWCKDNSVILADEMGLGKTIQTICFLYYLfKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVTYIGDVSSRDIIR 296
Cdd:COG0553   254 LFLRRLGLGGLLADDMGLGKTIQALALLLEL-KERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGAN 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  297 QFEwsfssskrlKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKE 376
Cdd:COG0553   333 PFE---------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEE 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  377 LWALLHFIMPYKFESWEDFEKDHEDAATKG----YEKLHKQLEPFILRRQKKDVEKSLPAKVEQILRVEMTSIQKQYYKW 452
Cdd:COG0553   404 LWSLLDFLNPGLLGSLKAFRERFARPIEKGdeeaLERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEA 483
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  453 IL--TKNYSALRKGVKGSINTFInIVIELKKCCNHALLTKPEDFESRASLATSDAVEKLLRgsgklllldkllcRLKETG 530
Cdd:COG0553   484 VLeyLRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLLEEGAELSGRSAKLEALLELLE-------------ELLAEG 549
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  531 HRVLIFSQMVRMLDILAEYLQRRHFPFQRLDGSIKGELRKQALDHFNAEGSQDFcFLLSTRAGGLGINLATADTVIIFDS 610
Cdd:COG0553   550 EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPV-FLISLKAGGEGLNLTAADHVIHYDL 628
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 164448642  611 DWNPQNDLQAQARAHRIGQKNQVNIYRLVTARSVEEDIVERAKRKMVL 658
Cdd:COG0553   629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
208-485 3.80e-93

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: 301.91  E-value: 3.80e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   208 YQMDGLNWLIHSWCKD-NSVILADEMGLGKTIQTICFLYYLFKSQHLYG-PFLCVVPLSTMTAWQREFQQWA--PDINVV 283
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   284 TYIGDVSSRDIIRQFEwsfssSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRL 363
Cdd:pfam00176   81 VLHGNKRPQERWKNDP-----NFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   364 LVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHE-----DAATKGYEKLHKQLEPFILRRQKKDVEKSLPAKVEQIL 438
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpierGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYIL 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 164448642   439 RVEMTSIQKQYYK-WILTKNYSALRKGVKGS--INTFINIVIELKKCCNH 485
Cdd:pfam00176  236 FCRLSKLQRKLYQtFLLKKDLNAIKTGEGGReiKASLLNILMRLRKICNH 285
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
528-639 1.01e-52

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: 181.14  E-value: 1.01e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  528 ETGHRVLIFSQMVRMLDILAEYLQRRHFPFQRLDGSIKGELRKQALDHFNaEGSQDFCFLLSTRAGGLGINLATADTVII 607
Cdd:cd18793    25 EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFN-EDPDIRVFLLSTKAGGVGLNLTAANRVIL 103
                          90       100       110
                  ....*....|....*....|....*....|..
gi 164448642  608 FDSDWNPQNDLQAQARAHRIGQKNQVNIYRLV 639
Cdd:cd18793   104 YDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
CDH1_2_SANT_HL1 pfam18375
CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays ...
866-950 5.93e-43

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: 151.35  E-value: 5.93e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   866 KGFTDQEIRRFVKSYKKFSAPLKHLDSIACDAELQEKPLAELKRLGEILQERCKAVLSETAEPSEQNEGRKNNRK----- 940
Cdd:pfam18375    1 KGFTDAEIRRFVKSYKKFSAPLKRLDAIACDAELQEKPLSDLRRLGELLKERCDEAMEEYTEKEDENPGADGGKKrirgp 80
                           90
                   ....*....|
gi 164448642   941 TFKLGGVPVN 950
Cdd:pfam18375   81 SFKLGGVSVN 90
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
2-76 3.64e-36

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: 131.64  E-value: 3.64e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164448642    2 RRGKKGVTGNVTTIYYIEEHGDPNEGCDPNDEDsTEPQYLIKWKGWSHIHNTWESEKTINDQKVKGLKKLENFIK 76
Cdd:cd18666    12 RIGRKGATGASTTIYAVEADGDPNAGFDPEDEE-TEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKLENYKK 85
DEXDc smart00487
DEAD-like helicases superfamily;
203-396 1.30e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.29  E-value: 1.30e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642    203 YHLRDYQMDGLNWLIHSWckdNSVILADEMGLGKTIQTICFLYYLFKSQHlYGPFLCVVPL-STMTAWQREFQQWAPD-- 279
Cdd:smart00487    7 EPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTrELAEQWAEELKKLGPSlg 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642    280 INVVTYIGDVSSRDIIRQFEWSfssskrlKFNAILTTYEILLKD--RQFLRSFSWACLLVDEAHRLKNDD--SLLYKALK 355
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESG-------KTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLK 155
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 164448642    356 EFDTN-HRLLVTGTP---LQNSLKELWALLHFIMPyKFESWEDFE 396
Cdd:smart00487  156 LLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDV-GFTPLEPIE 199
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
528-628 7.38e-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: 106.14  E-value: 7.38e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   528 ETGHRVLIFSQMVRMLDilAEYL-QRRHFPFQRLDGSIKGELRKQALDHFNAEgsqDFCFLLSTRAGGLGINLATADTVI 606
Cdd:pfam00271   13 ERGGKVLIFSQTKKTLE--AELLlEKEGIKVARLHGDLSQEEREEILEDFRKG---KIDVLVATDVAERGLDLPDVDLVI 87
                           90       100
                   ....*....|....*....|..
gi 164448642   607 IFDSDWNPQNDLQAQARAHRIG 628
Cdd:pfam00271   88 NYDLPWNPASYIQRIGRAGRAG 109
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1175-1264 1.18e-25

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: 101.95  E-value: 1.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  1175 DLDPSVFEE-CKEKMRPVKKALKALDNPDQSLSETEQVSRTRACLTQIGTQIDLCVEAYPDSQKVEWRSNLWYFVSKFTN 1253
Cdd:pfam13907    1 DEYESMDEEeCKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEETKKEKKEKLRKHLWSFVSKFWP 80
                           90
                   ....*....|...
gi 164448642  1254 --FDAKQLYKLYK 1264
Cdd:pfam13907   81 nkVSGKKLKEMYK 93
HELICc smart00490
helicase superfamily c-terminal domain;
544-628 2.33e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.97  E-value: 2.33e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642    544 DILAEYLQRRHFPFQRLDGSIKGELRKQALDHFNaegSQDFCFLLSTRAGGLGINLATADTVIIFDSDWNPQNDLQAQAR 623
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 164448642    624 AHRIG 628
Cdd:smart00490   78 AGRAG 82
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
110-166 2.22e-15

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: 71.45  E-value: 2.22e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 164448642  110 YNNVERIIAEqnRELEGGGTahEYFCKWESLPYADATWEDAVLIEKRWPVEVEHFKS 166
Cdd:cd18659     2 YTIVERIIAH--REDDEGVT--EYLVKWKGLPYDECTWESEEDISDIFQEAIDEYKK 54
DpdE NF041062
protein DpdE;
228-397 1.45e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 59.60  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  228 LADEMGLGKTIQTiCFLYylfkSQHLY-GPFLCV---VPLSTMTAWQRE----FqqwapdinvvtYIGDVSSRDIirqfe 299
Cdd:NF041062  175 LADEVGLGKTIEA-GLVI----RQHLLdNPDARVlvlVPDALVRQWRRElrdkF-----------FLDDFPGARV----- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  300 wsfssskrlkfnaILTTYEILLKDRQFLRSFSwacLLV-DEAHRL-------KNDDSLLYKALKEF-DTNHRLLV-TGTP 369
Cdd:NF041062  234 -------------RVLSHEEPERWEPLLDAPD---LLVvDEAHQLarlawsgDPPERARYRELAALaHAAPRLLLlSATP 297
                         170       180       190
                  ....*....|....*....|....*....|
gi 164448642  370 LQNSLKELWALLHFIMP--YKFESWEDFEK 397
Cdd:NF041062  298 VLGNEETFLALLHLLDPdlYPLDDLEAFRE 327
CHROMO smart00298
Chromatin organization modifier domain;
37-78 3.47e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 48.36  E-value: 3.47e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 164448642     37 EPQYLIKWKGWSHIHNTWESEKTIndqkVKGLKKLENFIKKE 78
Cdd:smart00298   17 ELEYLVKWKGYSYSEDTWEPEENL----LNCSKKLDNYKKKE 54
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
113-167 3.57e-07

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 47.96  E-value: 3.57e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 164448642   113 VERIIAEQNREleggGTAHEYFCKWESLPYADATWEDAVLIEKRwPVEVEHFKSR 167
Cdd:pfam00385    3 VERILDHRKDK----GGKEEYLVKWKGYPYDENTWEPEENLSKC-PELIEEFKDR 52
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
34-77 4.99e-06

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 44.88  E-value: 4.99e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 164448642    34 DSTEPQYLIKWKGWSHIHNTWESEKTINDQKvkglKKLENFIKK 77
Cdd:pfam00385   13 KGGKEEYLVKWKGYPYDENTWEPEENLSKCP----ELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
113-169 1.56e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.96  E-value: 1.56e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 164448642    113 VERIIAEqnRELEGGGTahEYFCKWESLPYADATWEDAVLIEKrWPVEVEHFKSREA 169
Cdd:smart00298    4 VEKILDH--RWKKKGEL--EYLVKWKGYSYSEDTWEPEENLLN-CSKKLDNYKKKER 55
 
Name Accession Description Interval E-value
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
204-421 9.72e-154

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: 462.21  E-value: 9.72e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  204 HLRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVV 283
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  284 TYIGDVSSRDIIRQFEWSFSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRL 363
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164448642  364 LVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKGYEKLHKQLEPFILRR 421
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEHDEEQEKGIADLHKELEPFILRR 218
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
205-779 8.46e-150

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 481.22  E-value: 8.46e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWckDNSV--ILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINV 282
Cdd:PLN03142  170 MRDYQLAGLNWLIRLY--ENGIngILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVLRA 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  283 VTYIGDVSSRDIIRQfewsfSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHR 362
Cdd:PLN03142  248 VKFHGNPEERAHQRE-----ELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYR 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  363 LLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEK----DHEDAATKGYEKLHKQLEPFILRRQKKDVEKSLPAKVEQIL 438
Cdd:PLN03142  323 LLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEwfqiSGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPKKETIL 402
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  439 RVEMTSIQKQYYKWILTKNYSALRKGvkGSINTFINIVIELKKCCNHALLtkpedFESRASLATSDAVEKLLRGSGKLLL 518
Cdd:PLN03142  403 KVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYL-----FQGAEPGPPYTTGEHLVENSGKMVL 475
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  519 LDKLLCRLKETGHRVLIFSQMVRMLDILAEYLQRRHFPFQRLDGSIKGELRKQALDHFNAEGSQDFCFLLSTRAGGLGIN 598
Cdd:PLN03142  476 LDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGIN 555
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  599 LATADTVIIFDSDWNPQNDLQAQARAHRIGQKNQVNIYRLVTARSVEEDIVERAKRKMVLDHLVIQRmdttGKTVLNKRd 678
Cdd:PLN03142  556 LATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQ----GRLAEQKT- 630
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  679 asgttannpFNKEDLNAILKFGAEELFKDDEENDEDPvcDIDEILQRAEtrdEGPAMVgDELLSAF--KVASFTFDEEKA 756
Cdd:PLN03142  631 ---------VNKDELLQMVRYGAEMVFSSKDSTITDE--DIDRIIAKGE---EATAEL-DAKMKKFteDAIKFKMDDTAE 695
                         570       580
                  ....*....|....*....|....
gi 164448642  757 VNELK-KDNADEEPKDWDDIIPEN 779
Cdd:PLN03142  696 LYDFDdEDDKDENKLDFKKIVSDN 719
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
184-421 1.57e-133

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: 409.39  E-value: 1.57e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  184 RPKFHQIKEQPEYVGKDSsYHLRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPL 263
Cdd:cd18054     1 RPRFVALKKQPSYIGGEN-LELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  264 STMTAWQREFQQWAPDINVVTYIGDVSSRDIIRQFEWSFSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRL 343
Cdd:cd18054    80 STLTSWQREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164448642  344 KNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKGYEKLHKQLEPFILRR 421
Cdd:cd18054   160 KNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENGYQSLHKVLEPFLLRR 237
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
137-658 3.34e-125

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 404.22  E-value: 3.34e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  137 WESLPYADATWEDAVLIEKRWPVEVEHFKSREAAKSTPSRHCPVLKRRPKFHQIKEQPEYVGKDssyhLRDYQMDGLNWL 216
Cdd:COG0553   178 LGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGLKAT----LRPYQLEGAAWL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  217 IHSWCKDNSVILADEMGLGKTIQTICFLYYLfKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVTYIGDVSSRDIIR 296
Cdd:COG0553   254 LFLRRLGLGGLLADDMGLGKTIQALALLLEL-KERGLARPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGAN 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  297 QFEwsfssskrlKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKE 376
Cdd:COG0553   333 PFE---------DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEE 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  377 LWALLHFIMPYKFESWEDFEKDHEDAATKG----YEKLHKQLEPFILRRQKKDVEKSLPAKVEQILRVEMTSIQKQYYKW 452
Cdd:COG0553   404 LWSLLDFLNPGLLGSLKAFRERFARPIEKGdeeaLERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEA 483
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  453 IL--TKNYSALRKGVKGSINTFInIVIELKKCCNHALLTKPEDFESRASLATSDAVEKLLRgsgklllldkllcRLKETG 530
Cdd:COG0553   484 VLeyLRRELEGAEGIRRRGLILA-ALTRLRQICSHPALLLEEGAELSGRSAKLEALLELLE-------------ELLAEG 549
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  531 HRVLIFSQMVRMLDILAEYLQRRHFPFQRLDGSIKGELRKQALDHFNAEGSQDFcFLLSTRAGGLGINLATADTVIIFDS 610
Cdd:COG0553   550 EKVLVFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPV-FLISLKAGGEGLNLTAADHVIHYDL 628
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 164448642  611 DWNPQNDLQAQARAHRIGQKNQVNIYRLVTARSVEEDIVERAKRKMVL 658
Cdd:COG0553   629 WWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
185-421 5.92e-113

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: 354.36  E-value: 5.92e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  185 PKFHQIKEQPEYVGKDSSYHLRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLS 264
Cdd:cd18053     1 PRFVALKKQPSYIGGHEGLELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  265 TMTAWQREFQQWAPDINVVTYIGDVSSRDIIRQFEWSFSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLK 344
Cdd:cd18053    81 TLTSWQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164448642  345 NDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKGYEKLHKQLEPFILRR 421
Cdd:cd18053   161 NDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYGYASLHKELEPFLLRR 237
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
208-485 3.80e-93

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: 301.91  E-value: 3.80e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   208 YQMDGLNWLIHSWCKD-NSVILADEMGLGKTIQTICFLYYLFKSQHLYG-PFLCVVPLSTMTAWQREFQQWA--PDINVV 283
Cdd:pfam00176    1 YQIEGVNWMLSLENNLgRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   284 TYIGDVSSRDIIRQFEwsfssSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRL 363
Cdd:pfam00176   81 VLHGNKRPQERWKNDP-----NFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRW 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   364 LVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHE-----DAATKGYEKLHKQLEPFILRRQKKDVEKSLPAKVEQIL 438
Cdd:pfam00176  156 ILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpierGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYIL 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 164448642   439 RVEMTSIQKQYYK-WILTKNYSALRKGVKGS--INTFINIVIELKKCCNH 485
Cdd:pfam00176  236 FCRLSKLQRKLYQtFLLKKDLNAIKTGEGGReiKASLLNILMRLRKICNH 285
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
205-421 2.80e-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: 291.46  E-value: 2.80e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWApDINVVT 284
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWT-DMNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSF------SSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFD 358
Cdd:cd17995    80 YHGSGESRQIIQQYEMYFkdaqgrKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164448642  359 TNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKG-YEKLHKQLEPFILRR 421
Cdd:cd17995   160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEqVEKLQALLKPYMLRR 223
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
205-421 2.15e-83

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: 270.21  E-value: 2.15e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWsfssskRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLL 364
Cdd:cd17919    81 YHGSQRERAQIRAKEK------LDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 164448642  365 VTGTPLQNSLKELWALLHFIMPykfeswedfekdhedaatkgyeklhkqlePFILRR 421
Cdd:cd17919   155 LTGTPLQNNLEELWALLDFLDP-----------------------------PFLLRR 182
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
205-421 2.22e-74

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: 246.20  E-value: 2.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSFSsskrlKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLL 364
Cdd:cd18006    81 YMGDKEKRLDLQQDIKSTN-----RFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164448642  365 VTGTPLQNSLKELWALLHFIMPYKF--ESWEDFEKDHEDAAT--KGYEKLHKQLEPFILRR 421
Cdd:cd18006   156 LTGTPIQNSLQELYALLSFIEPNVFpkDKLDDFIKAYSETDDesETVEELHLLLQPFLLRR 216
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
205-423 1.54e-72

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: 241.07  E-value: 1.54e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd17997     4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLRVVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSR-DIIRQFewsfssSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRL 363
Cdd:cd17997    84 LIGDKEERaDIIRDV------LLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164448642  364 LVTGTPLQNSLKELWALLHFIMPYKFESWEDFEK-----DHEDAATKGYEKLHKQLEPFILRRQK 423
Cdd:cd17997   158 LLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEwfnvnNCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
205-421 6.47e-72

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: 238.49  E-value: 6.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDvssrdiirqfewsfssskrlkfNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLL 364
Cdd:cd17994    81 YVGD----------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLL 138
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164448642  365 VTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKG-YEKLHKQLEPFILRR 421
Cdd:cd17994   139 LTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDqIKKLHDLLGPHMLRR 196
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
205-423 2.22e-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: 235.74  E-value: 2.22e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLfKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18009     4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHL-RERGVWGPFLVIAPLSTLPNWVNEFARFTPSVPVLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSFSSSKRlKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLL 364
Cdd:cd18009    83 YHGTKEERERLRKKIMKREGTLQ-DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164448642  365 VTGTPLQNSLKELWALLHFIMP------YKFESWEDFEKDHEDAATKGYE----------KLHKQLEPFILRRQK 423
Cdd:cd18009   162 LTGTPLQNNLSELWSLLNFLLPdvfddlSSFESWFDFSSLSDNAADISNLseereqnivhMLHAILKPFLLRRLK 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
205-423 4.23e-69

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: 231.87  E-value: 4.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd17996     4 LKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVSKIV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGdvsSRDIIRQFewsFSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKE-FDTNHRL 363
Cdd:cd17996    84 YKG---TPDVRKKL---QSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTyYHARYRL 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164448642  364 LVTGTPLQNSLKELWALLHFIMPYKFESWEDFEK--DHEDAATKGYEK--------------LHKQLEPFILRRQK 423
Cdd:cd17996   158 LLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQwfNTPFANTGEQVKielneeetlliirrLHKVLRPFLLRRLK 233
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
205-421 2.67e-67

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: 226.82  E-value: 2.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSFSSS--------------KRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLL 350
Cdd:cd18055    81 YTGDKDSRAIIRENEFSFDDNavkggkkafkmkreAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164448642  351 YKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKG-YEKLHKQLEPFILRR 421
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDqIKKLHDLLGPHMLRR 232
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
205-421 1.09e-66

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: 224.54  E-value: 1.09e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQfEWSFSSSkrlkFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLL 364
Cdd:cd18003    81 YYGSAKERKLKRQ-GWMKPNS----FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164448642  365 VTGTPLQNSLKELWALLHFIMPYKFESWEDFE---KDHEDAATKGYE--------KLHKQLEPFILRR 421
Cdd:cd18003   156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKewfSNPLTAMSEGSQeeneelvrRLHKVLRPFLLRR 223
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
205-421 1.24e-66

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: 224.94  E-value: 1.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSFSSS--------------KRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLL 350
Cdd:cd18056    81 YVGDKDSRAIIRENEFSFEDNairggkkasrmkkeASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164448642  351 YKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKG-YEKLHKQLEPFILRR 421
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDqIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
205-421 5.97e-65

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: 219.94  E-value: 5.97e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSFSSS--------------KRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLL 350
Cdd:cd18057    81 YTGDKESRSVIRENEFSFEDNairsgkkvfrmkkeAQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164448642  351 YKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKG-YEKLHKQLEPFILRR 421
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDqIKKLHDLLGPHMLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
205-421 1.30e-62

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: 212.99  E-value: 1.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFkSQHLYGPFLCVVPLSTMTAWQREFQQWApDINVVT 284
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-NVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSFSSSK-RL-----KFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFD 358
Cdd:cd18060    79 YHGSLASRQMIQQYEMYCKDSRgRLipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164448642  359 TNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAAT-KGYEKLHKQLEPFILRR 421
Cdd:cd18060   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTeEQVQKLQAILKPMMLRR 222
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
205-421 4.14e-59

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: 202.96  E-value: 4.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFkSQHLYGPFLCVVPLSTMTAWQREFQQWApDINVVT 284
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIF-LMGIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSFSS------SKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFD 358
Cdd:cd18058    79 YHGSQISRQMIQQYEMYYRDeqgnplSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164448642  359 TNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAAT-KGYEKLHKQLEPFILRR 421
Cdd:cd18058   159 LEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTeEQVKKLQSILKPMMLRR 222
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
205-423 4.63e-59

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: 202.41  E-value: 4.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLihSWCKDNSV--ILADEMGLGKTIQTICFLYYlFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINV 282
Cdd:cd18012     5 LRPYQKEGFNWL--SFLRHYGLggILADDMGLGKTLQTLALLLS-RKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPELKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  283 VTYIGDVSSRDIIRQFEwsfssskrlKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHR 362
Cdd:cd18012    82 LVIHGTKRKREKLRALE---------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHR 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164448642  363 LLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHE-----DAATKGYEKLHKQLEPFILRRQK 423
Cdd:cd18012   153 LALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkpiekDGDEEALEELKKLISPFILRRLK 218
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
205-421 1.19e-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: 1.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFeWsfsSSKRLK-----FNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDT 359
Cdd:cd18002    81 YWGNPKDRKVLRKF-W---DRKNLYtrdapFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHC 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164448642  360 NHRLLVTGTPLQNSLKELWALLHFIMPYKFESWED----FEKDHEDAATKG-------YEKLHKQLEPFILRR 421
Cdd:cd18002   157 RNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEfnewFSKDIESHAENKtglnehqLKRLHMILKPFMLRR 229
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
205-421 1.84e-58

DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1 (SMARCAD1, also known as ATP-dependent helicase 1 or Hel1) possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for both DNA repair and heterochromatin organization. SMARCAD1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 199.53  E-value: 1.84e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHlYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEwsfsSSKRLKFNAILTTYEILL---KDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNH 361
Cdd:cd17998    80 YYGSQEERKHLRYDI----LKGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINANF 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  362 RLLVTGTPLQNSLKELWALLHFIMPykfeswedfekdhedaatkgyeklhkqlEPFILRR 421
Cdd:cd17998   156 RLLLTGTPLQNNLLELMSLLNFIMP----------------------------KPFILRR 187
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
205-421 2.12e-58

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: 201.03  E-value: 2.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFkSQHLYGPFLCVVPLSTMTAWQREFQQWApDINVVT 284
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIY-LKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSFSSSK------RLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFD 358
Cdd:cd18059    79 YHGSQASRRTIQLYEMYFKDPQgrvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164448642  359 TNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAAT-KGYEKLHKQLEPFILRR 421
Cdd:cd18059   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTeEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
205-421 7.79e-58

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: 199.08  E-value: 7.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQhLYGPFLCVVPLSTMTAWQREFQQWApDINVVT 284
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTG-IRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSFSSSK------RLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFD 358
Cdd:cd18061    79 YHGSLISRQMIQQYEMYFRDSQgriirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164448642  359 TNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAAT-KGYEKLHKQLEPFILRR 421
Cdd:cd18061   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTeEQVQKLQAILKPMMLRR 222
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
189-433 1.03e-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: 199.89  E-value: 1.03e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  189 QIKEQPEYV--GKdssyhLRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTM 266
Cdd:cd18064     3 RFEDSPSYVkwGK-----LRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  267 TAWQREFQQWAPDINVVTYIGDVSSR-----DIIRQFEWsfssskrlkfNAILTTYEILLKDRQFLRSFSWACLLVDEAH 341
Cdd:cd18064    78 HNWMAEFKRWVPTLRAVCLIGDKDQRaafvrDVLLPGEW----------DVCVTSYEMLIKEKSVFKKFNWRYLVIDEAH 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  342 RLKNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKG----YEKLHKQLEPF 417
Cdd:cd18064   148 RIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGdqklVERLHMVLRPF 227
                         250
                  ....*....|....*.
gi 164448642  418 ILRRQKKDVEKSLPAK 433
Cdd:cd18064   228 LLRRIKADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
189-423 8.92e-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: 187.92  E-value: 8.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  189 QIKEQPEYVGKDSsyhLRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTA 268
Cdd:cd18065     3 RFEESPSYVKGGT---LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  269 WQREFQQWAPDINVVTYIGDVSSR-----DIIRQFEWsfssskrlkfNAILTTYEILLKDRQFLRSFSWACLLVDEAHRL 343
Cdd:cd18065    80 WMNEFKRWVPSLRAVCLIGDKDARaafirDVMMPGEW----------DVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  344 KNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKG----YEKLHKQLEPFIL 419
Cdd:cd18065   150 KNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGdqklVERLHAVLKPFLL 229

                  ....
gi 164448642  420 RRQK 423
Cdd:cd18065   230 RRIK 233
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
528-639 1.01e-52

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: 181.14  E-value: 1.01e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  528 ETGHRVLIFSQMVRMLDILAEYLQRRHFPFQRLDGSIKGELRKQALDHFNaEGSQDFCFLLSTRAGGLGINLATADTVII 607
Cdd:cd18793    25 EPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFN-EDPDIRVFLLSTKAGGVGLNLTAANRVIL 103
                          90       100       110
                  ....*....|....*....|....*....|..
gi 164448642  608 FDSDWNPQNDLQAQARAHRIGQKNQVNIYRLV 639
Cdd:cd18793   104 YDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
195-423 9.88e-52

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: 182.94  E-value: 9.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  195 EYVGKDSSY----HLRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQ 270
Cdd:cd18062    10 EKVEKQSSLlvngVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  271 REFQQWAPDINVVTYIGDVSSRdiiRQFEWSFSSSkrlKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLL 350
Cdd:cd18062    90 YEFDKWAPSVVKVSYKGSPAAR---RAFVPQLRSG---KFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  351 YKALK-EFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEK--------------DHEDAATKGYEKLHKQLE 415
Cdd:cd18062   164 TQVLNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfamtgekvdLNEEETILIIRRLHKVLR 243

                  ....*...
gi 164448642  416 PFILRRQK 423
Cdd:cd18062   244 PFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
205-423 1.69e-50

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: 179.10  E-value: 1.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18063    24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPLSTLSNWTYEFDKWAPSVVKIS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVS-SRDIIRQFewsfsssKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALK-EFDTNHR 362
Cdd:cd18063   104 YKGTPAmRRSLVPQL-------RSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRR 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164448642  363 LLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEK--------------DHEDAATKGYEKLHKQLEPFILRRQK 423
Cdd:cd18063   177 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfamtgervdLNEEETILIIRRLHKVLRPFLLRRLK 251
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
205-386 3.05e-47

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: 167.50  E-value: 3.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFEWSFSSSKRLKFNA-----ILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDT 359
Cdd:cd18000    81 LHSSGSGTGSEEKLGSIERKSQLIRKVVgdggiLITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
                         170       180
                  ....*....|....*....|....*..
gi 164448642  360 NHRLLVTGTPLQNSLKELWALLHFIMP 386
Cdd:cd18000   161 PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
205-421 1.69e-45

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: 164.06  E-value: 1.69e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWL-------IHSwckdnsvILADEMGLGKTIQTICFLY-------YLFKSQHLygPFLCVVPLSTMTAWQ 270
Cdd:cd17999     1 LRPYQQEGINWLaflnkynLHG-------ILCDDMGLGKTLQTLCILAsdhhkraNSFNSENL--PSLVVCPPTLVGHWV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  271 REFQQWAPD--INVVTYIGDVSSRDIIRQFEwsfssskrLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDS 348
Cdd:cd17999    72 AEIKKYFPNafLKPLAYVGPPQERRRLREQG--------EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKT 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  349 LLYKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDF-----------------EKDHEdAATKGYEKLH 411
Cdd:cd17999   144 KLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFqrrflkpilasrdskasAKEQE-AGALALEALH 222
                         250
                  ....*....|
gi 164448642  412 KQLEPFILRR 421
Cdd:cd17999   223 KQVLPFLLRR 232
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
205-421 2.83e-43

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: 157.92  E-value: 2.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSVILADEMGLGKTIQTICFLYYLFKSQHLYGPfLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGdVSSRDIIRQFEWSFSsskrlKFNAILTTYEILLKDRQFLRS-----FSWACLLVDEAHRLKNDDSLLYKALKEFDT 359
Cdd:cd18001    80 FHG-TSKKERERNLERIQR-----GGGVLLTTYGMVLSNTEQLSAddhdeFKWDYVILDEGHKIKNSKTKSAKSLREIPA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164448642  360 NHRLLVTGTPLQNSLKELWALLHFIMP---------YKFESWEDFEKDHEDAATKG--------YEKLHKQLEPFILRR 421
Cdd:cd18001   154 KNRIILTGTPIQNNLKELWALFDFACNgsllgtrktFKMEFENPITRGRDKDATQGekalgsevAENLRQIIKPYFLRR 232
CDH1_2_SANT_HL1 pfam18375
CDH1/2 SANT-Helical linker 1; CDH1 is an ATP-dependent chromatin-remodelling factor and plays ...
866-950 5.93e-43

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: 151.35  E-value: 5.93e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   866 KGFTDQEIRRFVKSYKKFSAPLKHLDSIACDAELQEKPLAELKRLGEILQERCKAVLSETAEPSEQNEGRKNNRK----- 940
Cdd:pfam18375    1 KGFTDAEIRRFVKSYKKFSAPLKRLDAIACDAELQEKPLSDLRRLGELLKERCDEAMEEYTEKEDENPGADGGKKrirgp 80
                           90
                   ....*....|
gi 164448642   941 TFKLGGVPVN 950
Cdd:pfam18375   81 SFKLGGVSVN 90
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
205-421 4.06e-41

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: 152.15  E-value: 4.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLiHSWCKDN-SVILADEMGLGKTIQTICFLYYLFK--------------------SQHLYGPFLCVVPL 263
Cdd:cd18005     1 LRDYQREGVEFM-YDLYKNGrGGILGDDMGLGKTVQVIAFLAAVLGktgtrrdrennrprfkkkppASSAKKPVLIVAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  264 STMTAWQREFQQWApDINVVTYIGDVSSRDIIrqfewsfSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRL 343
Cdd:cd18005    80 SVLYNWKDELDTWG-HFEVGVYHGSRKDDELE-------GRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  344 KNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHED--------AAT--------KGY 407
Cdd:cd18005   152 KNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhTATarelrlgrKRK 231
                         250
                  ....*....|....
gi 164448642  408 EKLHKQLEPFILRR 421
Cdd:cd18005   232 QELAVKLSKFFLRR 245
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
205-421 1.93e-37

DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 141.27  E-value: 1.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLI-----HSWCKDNSVILADEMGLGKTIQTICFLYYLFKsQHLYGPFLC-----VVPLSTMTAWQREFQ 274
Cdd:cd18004     1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVWTLLK-QGPYGKPTAkkaliVCPSSLVGNWKAEFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  275 QWAPD--INVVTYIGDVSSRDIIRQFEWSFSSSKRLkfnaiLTTYEILLK-DRQFLRSFSWACLLVDEAHRLKNDDSLLY 351
Cdd:cd18004    80 KWLGLrrIKVVTADGNAKDVKASLDFFSSASTYPVL-----IISYETLRRhAEKLSKKISIDLLICDEGHRLKNSESKTT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  352 KALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKGYEK----------------LHKQLE 415
Cdd:cd18004   155 KALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPdaseedkelgaersqeLSELTS 234

                  ....*.
gi 164448642  416 PFILRR 421
Cdd:cd18004   235 RFILRR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
205-421 2.65e-36

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: 137.80  E-value: 2.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHswckdNSVILADEMGLGKTIQTICFLY------------YLFKSQHLYGPFLC-----VVPLSTMT 267
Cdd:cd18008     1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQALALILatrpqdpkipeeLEENSSDPKKLYLSkttliVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  268 AWQREFQQ--WAPDINVVTYIGdvSSRDIirqfewsfSSSKRLKFNAILTTYEILLKD----------------RQFLRS 329
Cdd:cd18008    76 QWKDEIEKhtKPGSLKVYVYHG--SKRIK--------SIEELSDYDIVITTYGTLASEfpknkkgggrdskekeASPLHR 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  330 FSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKD----HEDAATK 405
Cdd:cd18008   146 IRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDiskpFSKNDRK 225
                         250
                  ....*....|....*.
gi 164448642  406 GYEKLHKQLEPFILRR 421
Cdd:cd18008   226 ALERLQALLKPILLRR 241
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
2-76 3.64e-36

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: 131.64  E-value: 3.64e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164448642    2 RRGKKGVTGNVTTIYYIEEHGDPNEGCDPNDEDsTEPQYLIKWKGWSHIHNTWESEKTINDQKVKGLKKLENFIK 76
Cdd:cd18666    12 RIGRKGATGASTTIYAVEADGDPNAGFDPEDEE-TEIQYLIKWKGWSHIHNTWESEESLKDQNVKGMKKLENYKK 85
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
227-397 5.69e-35

DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350765 [Multi-domain]  Cd Length: 239  Bit Score: 133.96  E-value: 5.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  227 ILADEMGLGKTIQTICFLYYLFKSQHLYGPFLCVVPLSTMTAWQREFQQWAPDINVVTYIGDVSSR--------DIIRQf 298
Cdd:cd18007    30 ILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWLPPDLRPLLVLVSLSAskradarlRKINK- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  299 eWSFSSSkrlkfnAILTTYEILLK--------DRQFLRSFSWAC-----LLV-DEAHRLKNDDSLLYKALKEFDTNHRLL 364
Cdd:cd18007   109 -WHKEGG------VLLIGYELFRNlasnattdPRLKQEFIAALLdpgpdLLVlDEGHRLKNEKSQLSKALSKVKTKRRIL 181
                         170       180       190
                  ....*....|....*....|....*....|...
gi 164448642  365 VTGTPLQNSLKELWALLHFIMPYKFESWEDFEK 397
Cdd:cd18007   182 LTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKK 214
DEXDc smart00487
DEAD-like helicases superfamily;
203-396 1.30e-30

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 120.29  E-value: 1.30e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642    203 YHLRDYQMDGLNWLIHSWckdNSVILADEMGLGKTIQTICFLYYLFKSQHlYGPFLCVVPL-STMTAWQREFQQWAPD-- 279
Cdd:smart00487    7 EPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGK-GGRVLVLVPTrELAEQWAEELKKLGPSlg 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642    280 INVVTYIGDVSSRDIIRQFEWSfssskrlKFNAILTTYEILLKD--RQFLRSFSWACLLVDEAHRLKNDD--SLLYKALK 355
Cdd:smart00487   83 LKVVGLYGGDSKREQLRKLESG-------KTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGGfgDQLEKLLK 155
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*
gi 164448642    356 EFDTN-HRLLVTGTP---LQNSLKELWALLHFIMPyKFESWEDFE 396
Cdd:smart00487  156 LLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDV-GFTPLEPIE 199
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
205-421 2.01e-28

DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a like 1, also known as HARP) is recruited to stalled replication forks to promote repair and helps restart replication. It plays a role in DNA repair, telomere maintenance and replication fork stability in response to DNA replication stress. Mutations cause Schimke Immunoosseous Dysplasia. SMARCAL1 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 114.22  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHswcKDNSVILADEMGLGKTIQTICFLYYLFKSqhlyGPFLCVVPLSTMTAWQREFQQWAP-----D 279
Cdd:cd18010     1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPslppdD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  280 INVVtyigdVSSRDIIRqfewsfssSKRLKFNaiLTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEF-- 357
Cdd:cd18010    74 IQVI-----VKSKDGLR--------DGDAKVV--IVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLlk 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164448642  358 DTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKGY----------EKLHKQLEP-FILRR 421
Cdd:cd18010   139 RAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFgwdysgssnlEELHLLLLAtIMIRR 213
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
224-421 8.03e-28

DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as RAD54L or RAD54, plays a role in homologous recombination related repair of DNA double-strand breaks. RAD54A is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 113.72  E-value: 8.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  224 NSVILADEMGLGKTIQTICFLYYLFKSQHLYGPFL--CVV--PLSTMTAWQREFQQW-APDINVVTYIGDVSSRDIIRQF 298
Cdd:cd18067    25 HGCIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkAIVvsPSSLVKNWANELGKWlGGRLQPLAIDGGSKKEIDRKLV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  299 EWSFSSSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELW 378
Cdd:cd18067   105 QWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYF 184
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 164448642  379 ALLHFIMPYKFESWEDFEKDHE-------DAA------TKGYEKLHK---QLEPFILRR 421
Cdd:cd18067   185 SLVNFVNPGILGTAAEFKKNFElpilkgrDADasekerQLGEEKLQElisIVNRCIIRR 243
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
528-628 7.38e-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: 106.14  E-value: 7.38e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   528 ETGHRVLIFSQMVRMLDilAEYL-QRRHFPFQRLDGSIKGELRKQALDHFNAEgsqDFCFLLSTRAGGLGINLATADTVI 606
Cdd:pfam00271   13 ERGGKVLIFSQTKKTLE--AELLlEKEGIKVARLHGDLSQEEREEILEDFRKG---KIDVLVATDVAERGLDLPDVDLVI 87
                           90       100
                   ....*....|....*....|..
gi 164448642   607 IFDSDWNPQNDLQAQARAHRIG 628
Cdd:pfam00271   88 NYDLPWNPASYIQRIGRAGRAG 109
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1175-1264 1.18e-25

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: 101.95  E-value: 1.18e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  1175 DLDPSVFEE-CKEKMRPVKKALKALDNPDQSLSETEQVSRTRACLTQIGTQIDLCVEAYPDSQKVEWRSNLWYFVSKFTN 1253
Cdd:pfam13907    1 DEYESMDEEeCKELMRPVKKSLKRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEETKKEKKEKLRKHLWSFVSKFWP 80
                           90
                   ....*....|...
gi 164448642  1254 --FDAKQLYKLYK 1264
Cdd:pfam13907   81 nkVSGKKLKEMYK 93
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
205-421 1.36e-23

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: 101.08  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKDNSV-----ILADEMGLGKTIQTICFLYYLFKSQHlYGP------FLCVVPLSTMTAWQREF 273
Cdd:cd18066     1 LRPHQREGIEFLYECVMGMRVNerfgaILADEMGLGKTLQCISLIWTLLRQGP-YGGkpvikrALIVTPGSLVKNWKKEF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  274 QQW--APDINVVTYIGDVSSRDIIrqfewsfsssKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLKNDDSLLY 351
Cdd:cd18066    80 QKWlgSERIKVFTVDQDHKVEEFI----------ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  352 KALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHED--------AATKGYEKLHKQ--------LE 415
Cdd:cd18066   150 TALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEpivrsrepTATPEEKKLGEAraaeltrlTG 229

                  ....*.
gi 164448642  416 PFILRR 421
Cdd:cd18066   230 LFILRR 235
HELICc smart00490
helicase superfamily c-terminal domain;
544-628 2.33e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 94.97  E-value: 2.33e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642    544 DILAEYLQRRHFPFQRLDGSIKGELRKQALDHFNaegSQDFCFLLSTRAGGLGINLATADTVIIFDSDWNPQNDLQAQAR 623
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 164448642    624 AHRIG 628
Cdd:smart00490   78 AGRAG 82
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
227-392 4.69e-23

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: 99.47  E-value: 4.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  227 ILADEMGLGKTIQTICFLyylfksqhLYGPFLCVVPLSTMTAWQREFQQWAPD--INVVTYIGDVSSRDIirqfewsfss 304
Cdd:cd18071    52 ILADDMGLGKTLTTISLI--------LANFTLIVCPLSVLSNWETQFEEHVKPgqLKVYTYHGGERNRDP---------- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  305 SKRLKFNAILTTYEILL-----KDRQFLRSFSWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELWA 379
Cdd:cd18071   114 KLLSKYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGS 193
                         170
                  ....*....|....*
gi 164448642  380 LLHF--IMPYKFESW 392
Cdd:cd18071   194 LLSFlhLKPFSNPEY 208
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
227-386 1.27e-19

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: 89.49  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  227 ILADEMGLGKTIQTICFLYYLFKSQHLyGPFLCVVPLSTMTAWQREFQQWAPDInvvtyigDVSSRDIIRQFEWSF--SS 304
Cdd:cd18069    32 ILAHSMGLGKTLQVISFLDVLLRHTGA-KTVLAIVPVNTLQNWLSEFNKWLPPP-------EALPNVRPRPFKVFIlnDE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  305 SKRLKFNAIL-----TTYEILLKDRQFLRSFSWACLLV-DEAHRLKNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELW 378
Cdd:cd18069   104 HKTTAARAKViedwvKDGGVLLMGYEMFRLRPGPDVVIcDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYW 183

                  ....*...
gi 164448642  379 ALLHFIMP 386
Cdd:cd18069   184 CMVDFVRP 191
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
205-395 4.92e-19

DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) is involved in transcriptional regulation and chromatin remodeling. Mutations in humans cause mental retardation, X-linked, syndromic, with hypotonic facies 1 (MRXSHF1) and alpha-thalassemia myelodysplasia syndrome (ATMDS). ATRX is part of the a DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 88.02  E-value: 4.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSWCKD---------NSVILADEMGLGKTIQTICFLYYLFKSQHLYG--PFLCVVPLSTMTAWQREF 273
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCESlkktkkspgSGCILAHCMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  274 QQWAPDINVVTYIgDVSSRDIIRQFEwsfssSKRLKFNAILTT----------YEILLKDR-------------QFLRSF 330
Cdd:cd18068    81 EKWQEGLKDEEKI-EVNELATYKRPQ-----ERSYKLQRWQEEggvmiigydmYRILAQERnvksreklkeifnKALVDP 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164448642  331 SWACLLVDEAHRLKNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDF 395
Cdd:cd18068   155 GPDFVVCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEF 219
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
226-421 4.29e-18

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: 84.26  E-value: 4.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  226 VILADEMGLGKTIQTICFLYYLfKSQHLYGPFLCVVPLSTMTAWQREFQQwapDINVVTYIGDVSSRDIIRQFEWSFsss 305
Cdd:cd18011    20 LLLADEVGLGKTIEAGLIIKEL-LLRGDAKRVLILCPASLVEQWQDELQD---KFGLPFLILDRETAAQLRRLIGNP--- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  306 kRLKFNAILTTYEiLLKD----RQFLRSFSWACLLVDEAHRLKN----DDSLLYKALKEF--DTNHRLLVTGTPLQNSLK 375
Cdd:cd18011    93 -FEEFPIVIVSLD-LLKRseerRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLakRARHVLLLTATPHNGKEE 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 164448642  376 ELWALLHFIMPYKFESWEDFEKDhedaatkgyEKLHKQLEPFILRR 421
Cdd:cd18011   171 DFRALLSLLDPGRFAVLGRFLRL---------DGLREVLAKVLLRR 207
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
110-166 2.22e-15

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: 71.45  E-value: 2.22e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 164448642  110 YNNVERIIAEqnRELEGGGTahEYFCKWESLPYADATWEDAVLIEKRWPVEVEHFKS 166
Cdd:cd18659     2 YTIVERIIAH--REDDEGVT--EYLVKWKGLPYDECTWESEEDISDIFQEAIDEYKK 54
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
31-76 1.31e-13

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: 67.00  E-value: 1.31e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 164448642   31 NDEDSTEPQYLIKWKGWSHIHNTWESEKTIndQKVKGLKKLENFIK 76
Cdd:cd18660    27 PDEPWDEREFLVKWKGKSYLHCTWVTEETL--EQLRGKKKLKNYIK 70
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
110-167 5.72e-13

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: 64.63  E-value: 5.72e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164448642  110 YNNVERIIAEQNRElEGGGTAHEYFCKWESLPYADATWEDAVLIEKRWPVEVEHFKSR 167
Cdd:cd18661     2 YQIVERIIAHSPQK-SAASGYPDYLCKWQGLPYSECTWEDGALISKKFQACIDEYHSR 58
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
139-804 1.87e-12

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 71.59  E-value: 1.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  139 SLPYADATWEDAVLIEKRWPVEVEHFKSREAAKSTPSRHCPVLKRRPKFHQIKEQPEYVGKDSSYHLRDYQMDGLNWLIH 218
Cdd:COG1061    15 RSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALEALLA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  219 SWCKDNS---VILAdeMGLGKTIqTICFLYylfKSQHLYGPFLCVVP-LSTMTAWQREFQQWAPDINVVtyigdvssrdi 294
Cdd:COG1061    95 ALERGGGrglVVAP--TGTGKTV-LALALA---AELLRGKRVLVLVPrRELLEQWAEELRRFLGDPLAG----------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  295 irqfewsfSSSKRLKFNAILTTYEILLKdRQFLRSFS--WACLLVDEAHRLKNDdsLLYKALKEFDTNHRLLVTGTPLQN 372
Cdd:COG1061   158 --------GGKKDSDAPITVATYQSLAR-RAHLDELGdrFGLVIIDEAHHAGAP--SYRRILEAFPAAYRLGLTATPFRS 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  373 SLKELwallhfimpyKFESWED--FEKDHEDAATKGYeklhkqLEPFILRrqkkdvekslpakveqILRVEMTSIQKQYy 450
Cdd:COG1061   227 DGREI----------LLFLFDGivYEYSLKEAIEDGY------LAPPEYY----------------GIRVDLTDERAEY- 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  451 kwiltknysalrkgvkgsintfinivIELKKCCNHALLTKPEdfesraslATSDAVEKLLRGSGKlllldkllcrlketG 530
Cdd:COG1061   274 --------------------------DALSERLREALAADAE--------RKDKILRELLREHPD--------------D 305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  531 HRVLIFSQMVRMLDILAEYLQRRHFPFQRLDGSIKGELRKQALDHFnAEGSQDfcFLLSTRAGGLGINLATADTVIIFDS 610
Cdd:COG1061   306 RKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAF-RDGELR--ILVTVDVLNEGVDVPRLDVAILLRP 382
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  611 DWNPQNDLQAQARAHRIGQ-KNQVNIYRLVTarsVEEDIVERAKRKmvldhlviQRMDTTGKTVLNKRDASGTTANNPFN 689
Cdd:COG1061   383 TGSPREFIQRLGRGLRPAPgKEDALVYDFVG---NDVPVLEELAKD--------LRDLAGYRVEFLDEEESEELALLIAV 451
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  690 KEDLNAILKFGAEELFKDDEENDEDPVCDIDEILQRAETRDEGPAMVGDEllsAFKVASFTFDEEKAVNELKKDNADEEP 769
Cdd:COG1061   452 KPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKA---EGKAEEEEEEKELLLLLALAKLLKLLL 528
                         650       660       670
                  ....*....|....*....|....*....|....*
gi 164448642  770 KDWDDIIPENVRKTIAEAEKLKEMEDIYLPPRRKN 804
Cdd:COG1061   529 LLLLLLLLELLELLAALLRLEELAALLLKELLRAA 563
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
110-167 2.28e-12

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: 63.06  E-value: 2.28e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164448642  110 YNNVERIIAEQNRELEGGGTAHEYFCKWESLPYADATWEDAVLIEKRWPVEVEHFKSR 167
Cdd:cd18664     2 FHVVERIIASQRASLEDGTSQLQYLVKWRRLNYDECTWEDATLIAKLAPEQVDHFQNR 59
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
227-421 4.51e-12

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: 67.51  E-value: 4.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  227 ILADEMGLGKTIQTICFLYY--------------------LFKSQHLY--GPFLCVVPLSTMTAWQREFQQWAPDINVVT 284
Cdd:cd18072    24 ILADDMGLGKTLTMIALILAqkntqnrkeeekekalteweSKKDSTLVpsAGTLVVCPASLVHQWKNEVESRVASNKLRV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  285 YIGDVSSRDIIRQFewsFSSskrlkFNAILTTYEILLK----DRQFLRS-----FSWACLLVDEAHRLKNDDSLLYKALK 355
Cdd:cd18072   104 CLYHGPNRERIGEV---LRD-----YDIVITTYSLVAKeiptYKEESRSsplfrIAWARIILDEAHNIKNPKVQASIAVC 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164448642  356 EFDTNHRLLVTGTPLQNSLKELWALLHFIMPYKFESWEDFEKDHEDAATKGYEKLHKQLEPFILRR 421
Cdd:cd18072   176 KLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGERLNILTKSLLLRR 241
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
205-420 1.04e-11

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 66.60  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSwckdnSVILADEMGLGKTIQTI------------------------CFLYYLFKSQHLY-GPFLC 259
Cdd:cd18070     1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLalillhprpdndldaadddsdemvCCPDCLVAETPVSsKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  260 VVPlSTMTAwqrefqQWAPDIN--------VVTYIGDVSSRDIIRQFEWSFSSskrlkFNAILTTYEILLKDRQFLRSFS 331
Cdd:cd18070    76 VCP-SAILA------QWLDEINrhvpsslkVLTYQGVKKDGALASPAPEILAE-----YDIVVTTYDVLRTELHYAEANR 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  332 ----------------------WACLLVDEAHRLKNDDSLLYKALKEFDTNHRLLVTGTPLQNSLKELWALLHFIM--PY 387
Cdd:cd18070   144 snrrrrrqkryeappsplvlveWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGvePF 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 164448642  388 KFESWEDFEKDHEDAATKGYEKLHKQLEPFILR 420
Cdd:cd18070   224 CDSDWWARVLIRPQGRNKAREPLAALLKELLWR 256
ResIII pfam04851
Type III restriction enzyme, res subunit;
203-369 3.07e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 63.07  E-value: 3.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   203 YHLRDYQMDGL-NWLIHSWCKDNSVILADEMGLGKTIqTICFLYYLFKSQHLYGPFLCVVP-LSTMTAWQREFQQWAPdi 280
Cdd:pfam04851    2 LELRPYQIEAIeNLLESIKNGQKRGLIVMATGSGKTL-TAAKLIARLFKKGPIKKVLFLVPrKDLLEQALEEFKKFLP-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   281 NVVTYIGDVSSRDIIRQFEwsfssSKRLKFNAILTTYEILLKDRQFLRSFSWACLLVDEAHRLkNDDSllYKALKE-FDT 359
Cdd:pfam04851   79 NYVEIGEIISGDKKDESVD-----DNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAHRS-GASS--YRNILEyFKP 150
                          170
                   ....*....|
gi 164448642   360 NHRLLVTGTP 369
Cdd:pfam04851  151 AFLLGLTATP 160
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
25-76 1.88e-10

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: 57.78  E-value: 1.88e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 164448642   25 NEGCDPNDED--STEPQYLIKWKGWSHIHNTWESEKTIndQKVKGLKKLENFIK 76
Cdd:cd18665    14 KEGLEEGELDdpKENYEFLIKWTDESHLHNTWETYESL--KQVRGLKKVDNYIK 65
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
205-384 2.42e-09

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: 58.90  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGLNWLIHSwckDNSVILADeMGLGKTIQTICFLYYLFkSQHLYGPFLCVVPL----STmtaWQREFQQWA--P 278
Cdd:cd18013     1 PHPYQKVAINFIIEH---PYCGLFLD-MGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLrvarST---WPDEVEKWNhlR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  279 DINVVTYIGDVSSRdiirqfewsfssSKRLKFNAILTTYEI-LLKD--RQFLRSFSWACLLVDEAHRLKNDDSLLYKALK 355
Cdd:cd18013    73 NLTVSVAVGTERQR------------SKAANTPADLYVINReNLKWlvNKSGDPWPFDMVVIDELSSFKSPRSKRFKALR 140
                         170       180       190
                  ....*....|....*....|....*....|.
gi 164448642  356 E--FDTNHRLLVTGTPLQNSLKELWALLHFI 384
Cdd:cd18013   141 KvrPVIKRLIGLTGTPSPNGLMDLWAQIALL 171
DpdE NF041062
protein DpdE;
228-397 1.45e-08

protein DpdE;


Pssm-ID: 468989 [Multi-domain]  Cd Length: 1048  Bit Score: 59.60  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  228 LADEMGLGKTIQTiCFLYylfkSQHLY-GPFLCV---VPLSTMTAWQRE----FqqwapdinvvtYIGDVSSRDIirqfe 299
Cdd:NF041062  175 LADEVGLGKTIEA-GLVI----RQHLLdNPDARVlvlVPDALVRQWRRElrdkF-----------FLDDFPGARV----- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  300 wsfssskrlkfnaILTTYEILLKDRQFLRSFSwacLLV-DEAHRL-------KNDDSLLYKALKEF-DTNHRLLV-TGTP 369
Cdd:NF041062  234 -------------RVLSHEEPERWEPLLDAPD---LLVvDEAHQLarlawsgDPPERARYRELAALaHAAPRLLLlSATP 297
                         170       180       190
                  ....*....|....*....|....*....|
gi 164448642  370 LQNSLKELWALLHFIMP--YKFESWEDFEK 397
Cdd:NF041062  298 VLGNEETFLALLHLLDPdlYPLDDLEAFRE 327
CHROMO smart00298
Chromatin organization modifier domain;
37-78 3.47e-07

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 48.36  E-value: 3.47e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 164448642     37 EPQYLIKWKGWSHIHNTWESEKTIndqkVKGLKKLENFIKKE 78
Cdd:smart00298   17 ELEYLVKWKGYSYSEDTWEPEENL----LNCSKKLDNYKKKE 54
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
113-167 3.57e-07

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 47.96  E-value: 3.57e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 164448642   113 VERIIAEQNREleggGTAHEYFCKWESLPYADATWEDAVLIEKRwPVEVEHFKSR 167
Cdd:pfam00385    3 VERILDHRKDK----GGKEEYLVKWKGYPYDENTWEPEENLSKC-PELIEEFKDR 52
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
205-369 6.64e-07

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 50.38  E-value: 6.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  205 LRDYQMDGL-NWLIHSWCKDNSVILAdeMGLGKTIQTICFLYYLFKsqhlyGPFLCVVP-LSTMTAWQREFQQWAPDInV 282
Cdd:cd17926     1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTLTALALIAYLKE-----LRTLIVVPtDALLDQWKERFEDFLGDS-S 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  283 VTYIGDVSSRDIIrqfewsfssskrlKFNAILTTYEIL---LKDRQFLRSFsWACLLVDEAHRLkndDSLLYKA-LKEFD 358
Cdd:cd17926    73 IGLIGGGKKKDFD-------------DANVVVATYQSLsnlAEEEKDLFDQ-FGLLIVDEAHHL---PAKTFSEiLKELN 135
                         170
                  ....*....|.
gi 164448642  359 TNHRLLVTGTP 369
Cdd:cd17926   136 AKYRLGLTATP 146
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
38-78 1.52e-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: 46.30  E-value: 1.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 164448642   38 PQYLIKWKGWSHIHNTWESEKTINDQKVkglkkLENFIKKE 78
Cdd:cd18644    19 VEYLVKWKGWSNKHNTWEPEENILDRRL-----IEIFERTN 54
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
442-645 2.02e-06

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 51.17  E-value: 2.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   442 MTSIQKQYYKWILTKNYSALRKGV-----KGSINTFINIVIELKKCCNHAllTKP----EDFESRaSLATSDAVEKLLRG 512
Cdd:pfam11496   12 MTSYQKELTEQIVSLHYSDILKYCetsdsKEDISLIKSMTLCLENLSLVA--THPyllvDHYMPK-SLLLKDEPEKLAYT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   513 SGKLLL-----LDKLLCRLKETGHrVLIFSQMVRMLDILAEYLQRRHFPFQRLDG-SIKGELRKQALDHFNAEGSQDFCF 586
Cdd:pfam11496   89 SGKFLVlndlvNLLIERDRKEPIN-VAIVARSGKTLDLVEALLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHL 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164448642   587 LLSTR-----AGGLGINlaTADTVIIFDSDWNPQNDLQAQARAHRIGQKNQVNIYRLVTARSVE 645
Cdd:pfam11496  168 LSSTGqltndDSLLENY--KFDLIIAFDSSVDTSSPSVEHLRTQNRRKGNLAPIIRLVVINSIE 229
CD_polycomb_like cd18627
chromodomain of polycomb and chromobox family proteins; CHRomatin Organization Modifier ...
39-64 4.28e-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: 45.07  E-value: 4.28e-06
                          10        20
                  ....*....|....*....|....*.
gi 164448642   39 QYLIKWKGWSHIHNTWESEKTINDQK 64
Cdd:cd18627    17 EYLVKWKGWSQKYNTWEPEENILDPR 42
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
34-77 4.99e-06

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 44.88  E-value: 4.99e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 164448642    34 DSTEPQYLIKWKGWSHIHNTWESEKTINDQKvkglKKLENFIKK 77
Cdd:pfam00385   13 KGGKEEYLVKWKGYPYDENTWEPEENLSKCP----ELIEEFKDR 52
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
226-368 5.79e-06

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 47.40  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  226 VILADEMGLGKTIQTICFLYYLFKSQHlyGPFLCVVPLSTMT-AWQREFQQWAPDINVVTYIGdvssrdiirqfewSFSS 304
Cdd:cd00046     4 VLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALAlQTAERLRELFGPGIRVAVLV-------------GGSS 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164448642  305 SKRLKFNA------ILTTYEILLKDRQFLRSFS---WACLLVDEAHR-LKNDDSLLYKAL----KEFDTNHRLLVTGT 368
Cdd:cd00046    69 AEEREKNKlgdadiIIATPDMLLNLLLREDRLFlkdLKLIIVDEAHAlLIDSRGALILDLavrkAGLKNAQVILLSAT 146
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
37-62 1.31e-05

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: 43.62  E-value: 1.31e-05
                          10        20
                  ....*....|....*....|....*.
gi 164448642   37 EPQYLIKWKGWSHIHNTWESEKTIND 62
Cdd:cd00024    15 KLEYLVKWKGYPPEENTWEPEENLTN 40
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
531-631 1.50e-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: 44.23  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  531 HRVLIFSQMVRMLDILAEYLQrrhfpfqrldgsikgelrkqaldhfnaegsqdfcFLLSTRAGGLGINLATADTVIIFDS 610
Cdd:cd18785     4 VKIIVFTNSIEHAEEIASSLE----------------------------------ILVATNVLGEGIDVPSLDTVIFFDP 49
                          90       100
                  ....*....|....*....|.
gi 164448642  611 DWNPQNDLQAQARAHRIGQKN 631
Cdd:cd18785    50 PSSAASYIQRVGRAGRGGKDE 70
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
39-62 5.33e-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: 42.33  E-value: 5.33e-05
                          10        20
                  ....*....|....*....|....
gi 164448642   39 QYLIKWKGWSHIHNTWESEKTIND 62
Cdd:cd18968    24 KYLVKWAGYPDEENTWEPEESFDG 47
CD_Cbx2 cd18647
chromodomain of chromobox homolog 2; CHRomatin Organization Modifier (chromo) domain of ...
39-65 1.88e-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: 1.88e-04
                          10        20
                  ....*....|....*....|....*..
gi 164448642   39 QYLIKWKGWSHIHNTWESEKTINDQKV 65
Cdd:cd18647    20 EYLVKWRGWSSKHNSWEPEENILDPRL 46
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
110-168 6.89e-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: 39.19  E-value: 6.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642  110 YNNVERIIAEQNRELEGGGTAHEYF-CKWESLPYADATWEdavLIEKRWPVEVEHFKSRE 168
Cdd:cd18663     3 YVEVDRILDVSVSTDPNTGEPVTHYlVKWCSLPYEDSTWE---LEEDVDPAKIEEFEKLR 59
CD_Cbx8 cd18649
chromodomain of chromobox homolog 8; CHRomatin Organization Modifier (chromo) domain of ...
39-65 1.41e-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: 38.16  E-value: 1.41e-03
                          10        20
                  ....*....|....*....|....*..
gi 164448642   39 QYLIKWKGWSHIHNTWESEKTINDQKV 65
Cdd:cd18649    21 EYLVKWKGWSQKYSTWEPEENILDARL 47
CHROMO smart00298
Chromatin organization modifier domain;
113-169 1.56e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.96  E-value: 1.56e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 164448642    113 VERIIAEqnRELEGGGTahEYFCKWESLPYADATWEDAVLIEKrWPVEVEHFKSREA 169
Cdd:smart00298    4 VEKILDH--RWKKKGEL--EYLVKWKGYSYSEDTWEPEENLLN-CSKKLDNYKKKER 55
CD_Cbx4 cd18645
chromodomain of chromobox homolog 4; CHRomatin Organization Modifier (chromo) domain of ...
39-65 1.67e-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: 38.11  E-value: 1.67e-03
                          10        20
                  ....*....|....*....|....*..
gi 164448642   39 QYLIKWKGWSHIHNTWESEKTINDQKV 65
Cdd:cd18645    20 EYLVKWRGWSPKYNTWEPEENILDPRL 46
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
32-63 1.96e-03

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: 37.56  E-value: 1.96e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 164448642   32 DEDSTEPQYLIKWKGWSHIHNTWESEKTINDQ 63
Cdd:cd18659    13 EDDEGVTEYLVKWKGLPYDECTWESEEDISDI 44
CD_HP1alpha_Cbx5 cd18651
chromodomain of heterochromatin protein 1 homolog alpha; CHRomatin Organization Modifier ...
39-61 2.08e-03

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: 37.66  E-value: 2.08e-03
                          10        20
                  ....*....|....*....|...
gi 164448642   39 QYLIKWKGWSHIHNTWESEKTIN 61
Cdd:cd18651    18 EYLLKWKGFSEEHNTWEPEKNLD 40
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
39-65 3.76e-03

chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in the polyprotein from the MarY1 Ty3/Gypsy long terminal repeat (LTR) retroelement from the from the Ectomycorrhizal Basidiomycete Tricholoma matsutake. The pol gene in TY3/gypsy elements generally encodes domains in the following order: prt-reverse transcriptase-RNase H-integrase, in marY1 POL the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and 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: 349331  Cd Length: 49  Bit Score: 36.75  E-value: 3.76e-03
                          10        20
                  ....*....|....*....|....*..
gi 164448642   39 QYLIKWKGWSHIHNTWESEKTINDQKV 65
Cdd:cd18975    17 QYLIQWKGYPLEEASWELEDNIKNPRL 43
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
217-369 4.97e-03

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 39.15  E-value: 4.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   217 IHSWCKDNSVILADEMGLGKTIqtiCFLYYLFK--SQHLYGP-FLCVVPLSTMtAWQ--REFQQWA--PDINVVTYIGDV 289
Cdd:pfam00270    8 IPAILEGRDVLVQAPTGSGKTL---AFLLPALEalDKLDNGPqALVLAPTREL-AEQiyEELKKLGkgLGLKVASLLGGD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164448642   290 SSRDIIRQFewsfsssKRLKFnaILTTYEIL---LKDRQFLRSFSWacLLVDEAHRLKNDD--SLLYKALKEFDTNHR-L 363
Cdd:pfam00270   84 SRKEQLEKL-------KGPDI--LVGTPGRLldlLQERKLLKNLKL--LVLDEAHRLLDMGfgPDLEEILRRLPKKRQiL 152

                   ....*.
gi 164448642   364 LVTGTP 369
Cdd:pfam00270  153 LLSATL 158
CD_DDE_transposase_like cd18978
chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This ...
39-62 6.91e-03

chromodomain of Rhizopus microsporus putative DDE transposases, and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Rhizopus microsporus putative DDE transposases, and similar proteins. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and 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: 349334  Cd Length: 52  Bit Score: 36.14  E-value: 6.91e-03
                          10        20
                  ....*....|....*....|....
gi 164448642   39 QYLIKWKGWSHIHNTWESEKTIND 62
Cdd:cd18978    20 KYLVKWKGYDDTDNSWVTQEDFND 43
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
38-61 9.88e-03

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: 349321  Cd Length: 53  Bit Score: 35.53  E-value: 9.88e-03
                          10        20
                  ....*....|....*....|....
gi 164448642   38 PQYLIKWKGWSHIHNTWESEKTIN 61
Cdd:cd18965    16 LEYLVKWHGLPESENTWEREKDIK 39
 
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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