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Conserved domains on  [gi|1907105093|ref|XP_011243467|]
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chromodomain-helicase-DNA-binding protein 8 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEAD-like_helicase_N super family cl28899
N-terminal helicase domain of the DEAD-box helicase superfamily; The DEAD-like helicase ...
813-1034 1.08e-153

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


The actual alignment was detected with superfamily member cd18060:

Pssm-ID: 475120 [Multi-domain]  Cd Length: 222  Bit Score: 474.16  E-value: 1.08e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 892
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  893 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 972
Cdd:cd18060     81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  973 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18060    161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
812-1411 2.62e-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: 496.25  E-value: 2.62e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  812 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTEM-NTI 889
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYrGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQYemyckdsrgRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 969
Cdd:PLN03142   249 KFHGNPEERAHQREE---------LLVAG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  970 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPK 1046
Cdd:PLN03142   318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1047 QETIIEVELTNIQKKYYRAILEKNFSFLSKGAGHTNmpnLLNTMMELRKCCNHPYLINGAEEKilmefreachiiPQDFH 1126
Cdd:PLN03142   398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPYTT 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1127 LQAMVRSAGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFV 1206
Cdd:PLN03142   463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1207 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQs 1286
Cdd:PLN03142   543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ- 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1287 mSGRdgnitgIQQFSKKEIEDLLRKGAYAAIMEEDDEGSKFCEEDIDQILLR-RTTTITIESEGKGSTfakasfvasENR 1365
Cdd:PLN03142   622 -QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFT---------EDA 685
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907105093 1366 TDISLDDPN----FWQKWAKKAD-LDMDLLNSKNnlVIDTPRvRKQTRHFS 1411
Cdd:PLN03142   686 IKFKMDDTAelydFDDEDDKDENkLDFKKIVSDN--WIDPPK-RERKRNYS 733
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
723-781 7.50e-36

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: 130.49  E-value: 7.50e-36
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907105093  723 PDYVEVDRILDESHSVDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQ 781
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
640-705 1.39e-29

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


:

Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 113.20  E-value: 1.39e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907105093  640 EEDAAIVDKVLSMRVVKKELPSG-QYTEAEEFFVKYKNYSYLHCEWATISQLEK-DKRIHQKLKRFKT 705
Cdd:cd18668      1 EEDTMIIEKILASRKKKKEKEEGaEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
2319-2362 6.93e-15

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


:

Pssm-ID: 462196  Cd Length: 44  Bit Score: 70.23  E-value: 6.93e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907105093 2319 LDLETRIPVINKVDGTLLVGDEAPRRAELEMWLQGHPEFAVDPR 2362
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
SP1-4_N super family cl41773
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
61-421 6.67e-05

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


The actual alignment was detected with superfamily member cd22540:

Pssm-ID: 425404 [Multi-domain]  Cd Length: 511  Bit Score: 48.00  E-value: 6.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   61 SSASDLVP-PPEETAST---------ELPKESTAPapesltlhdytTQPTSQEQPAQPVLQTSTPTAGllqvsKSQEILS 130
Cdd:cd22540     17 STTQDSQPsPLALLAATcskigppavEAAVTPPAP-----------PQPTPRKLVPIKPAPLPLGPGK-----NSIGFLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  131 -QGNPFMGVSATGVSPSNTGGQPSQSAPKIVILKAPPNSSVTGTH---VAQIQAQGITS-TAQPLVAGTANGGKVTFTKV 205
Cdd:cd22540     81 aKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGSQTRSSTNQQyqiSPQIQAAGQINnSGQIQIIPGTNQAIITPVQV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  206 LTGT-------PLRPGVSIVSGNTVLATKVPGNQaavqrIVQPSRPVKQLVLqPVKGSAPAGNPGA----AGPPLKPAVT 274
Cdd:cd22540    161 LQQPqqahkpvPIKPAPLQTSNTNSASLQVPGNV-----IKLQSGGNVALTL-PVNNLVGTQDGATqlqlAAAPSKPSKK 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  275 LTSTPTQGESKRITlVLQQPQSggpqghrhVVLGSLPGKIVLQGNQLaaLTQAKNAQGQPAkvvtiqlqvqqpqqkiqiv 354
Cdd:cd22540    235 IRKKSAQAAQPAVT-VAEQVET--------VLIETTADNIIQAGNNL--LIVQSPGTGQPA------------------- 284
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907105093  355 pqppssqpqpqpqpppsaqplTLSSVQQAQimgPGQNPG--QRLSVPLKMVlqpqagssQGASSGLSVV 421
Cdd:cd22540    285 ---------------------VLQQVQVLQ---PKQEQQvvQIPQQALRVV--------QAASATLPTV 321
PTZ00121 super family cl31754
MAEBL; Provisional
449-624 4.12e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 4.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  449 EENRRLEHQKKQEKANRIVAEAIARARARgEQNIPRVLNEDELPSVRPEEEGEKKRRKKSSGERLKEEKPKKSKTAAASK 528
Cdd:PTZ00121  1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEE-KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  529 TKGKsklntitpvvgKKRKRNTSSDNSDVEVMPAQSPREDEESSIQK----RRSNRQVKRK----KYTEDLDIKITDDEE 600
Cdd:PTZ00121  1696 KEAE-----------EAKKAEELKKKEAEEKKKAEELKKAEEENKIKaeeaKKEAEEDKKKaeeaKKDEEEKKKIAHLKK 1764
                          170       180
                   ....*....|....*....|....*
gi 1907105093  601 EEEVDVTGPIK-PEPILPEPVQEPD 624
Cdd:PTZ00121  1765 EEEKKAEEIRKeKEAVIEEELDEED 1789
 
Name Accession Description Interval E-value
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
813-1034 1.08e-153

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: 474.16  E-value: 1.08e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 892
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  893 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 972
Cdd:cd18060     81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  973 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18060    161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
812-1411 2.62e-150

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 496.25  E-value: 2.62e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  812 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTEM-NTI 889
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYrGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQYemyckdsrgRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 969
Cdd:PLN03142   249 KFHGNPEERAHQREE---------LLVAG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  970 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPK 1046
Cdd:PLN03142   318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1047 QETIIEVELTNIQKKYYRAILEKNFSFLSKGAGHTNmpnLLNTMMELRKCCNHPYLINGAEEKilmefreachiiPQDFH 1126
Cdd:PLN03142   398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPYTT 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1127 LQAMVRSAGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFV 1206
Cdd:PLN03142   463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1207 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQs 1286
Cdd:PLN03142   543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ- 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1287 mSGRdgnitgIQQFSKKEIEDLLRKGAYAAIMEEDDEGSKFCEEDIDQILLR-RTTTITIESEGKGSTfakasfvasENR 1365
Cdd:PLN03142   622 -QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFT---------EDA 685
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907105093 1366 TDISLDDPN----FWQKWAKKAD-LDMDLLNSKNnlVIDTPRvRKQTRHFS 1411
Cdd:PLN03142   686 IKFKMDDTAelydFDDEDDKDENkLDFKKIVSDN--WIDPPK-RERKRNYS 733
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
683-1271 6.83e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 408.07  E-value: 6.83e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  683 EWATISQLEKDKRIHQKLKRFKTKMAQMRHFFHEDEEPFNPDYVEVDRILDESHSVDKDNGEPVIYYLVKWCSLPYEDST 762
Cdd:COG0553    110 LLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLAL 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  763 WELKEDVDEGKIREFKRIQSRHPELRRVnRPQANAWKKLELSHEYKNRN---QLREYQLEGVNWLLFNWYNRQNCILADE 839
Cdd:COG0553    190 LELALLAAEAELLLLLELLLELELLAEA-AVDAFRLRRLREALESLPAGlkaTLRPYQLEGAAWLLFLRRLGLGGLLADD 268
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  840 MGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVYHGSLASRQMIQQYEmyckdsrgrlipg 918
Cdd:COG0553    269 MGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLVLDGTRERAKGANPFE------------- 335
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  919 ayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEP 998
Cdd:COG0553    336 --DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNP 413
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  999 SQFPSESEFLKDFGDLKT---EEQVQKLQAILKPMMLRRLKEDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLS 1075
Cdd:COG0553    414 GLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELE 493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1076 KGAGHTNMPNLLNTMMELRKCCNHPYLINGAEEKILmefreachiipqdfhlqamVRSaGKLVLIDKLLPKLKAGGHKVL 1155
Cdd:COG0553    494 GAEGIRRRGLILAALTRLRQICSHPALLLEEGAELS-------------------GRS-AKLEALLELLEELLAEGEKVL 553
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1156 IFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKpDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNP 1235
Cdd:COG0553    554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1907105093 1236 QNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFD 1271
Cdd:COG0553    633 AVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
816-1103 2.05e-88

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: 290.35  E-value: 2.05e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  816 YQLEGVNWLLFNWYNRQ-NCILADEMGLGKTIQSIAFLQEVYNVGI--HGPFLVIAPLSTITNWEREFNTWT---EMNTI 889
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVsppALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQYEMYckdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 969
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNF-----------LADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  970 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----DLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAP 1045
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1046 KQETIIEVELTNIQKKYY-RAILEKNFSFLSKG-AGHTNMPNLLNTMMELRKCCNHPYLI 1103
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1135-1260 4.54e-57

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 194.23  E-value: 4.54e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1135 GKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDrFVFLLCTRAG 1214
Cdd:cd18793     11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907105093 1215 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 1260
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
723-781 7.50e-36

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: 130.49  E-value: 7.50e-36
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907105093  723 PDYVEVDRILDESHSVDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQ 781
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
640-705 1.39e-29

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


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 113.20  E-value: 1.39e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907105093  640 EEDAAIVDKVLSMRVVKKELPSG-QYTEAEEFFVKYKNYSYLHCEWATISQLEK-DKRIHQKLKRFKT 705
Cdd:cd18668      1 EEDTMIIEKILASRKKKKEKEEGaEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
DEXDc smart00487
DEAD-like helicases superfamily;
806-1004 5.48e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 116.44  E-value: 5.48e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   806 EYKNRNQLREYQLEGVNWLLFNWynrQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTIT-NWEREFNTWT 884
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   885 E---MNTIVYHGSLASRQMIQQYEMYCkdsrgrlipgaykFDALITTFEMILSDCPE--LREIEWRCVIIDEAHRLKN-- 957
Cdd:smart00487   79 PslgLKVVGLYGGDSKREQLRKLESGK-------------TDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDgg 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1907105093   958 RNCKLLDSLKHMDLE-HKVLLTGTP---LQNTVEELFSLLHFLEPSQFPSE 1004
Cdd:smart00487  146 FGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1135-1249 7.98e-26

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: 103.83  E-value: 7.98e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1135 GKLVLIDKLLPKLKagGHKVLIFSQMVRCLDilEDYLIQRR-YLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRA 1213
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907105093 1214 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 1249
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
1165-1249 1.31e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.04  E-value: 1.31e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  1165 DILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 1244
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1907105093  1245 CHRIG 1249
Cdd:smart00490   78 AGRAG 82
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
835-1283 1.58e-20

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 99.37  E-value: 1.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  835 ILADEMGLGKTIQSIAFLQEVYNVGIHgPFLVIAPLSTITNWEREFNTWTEMNTIVyhgslASRQMIQQYemycKDSRGR 914
Cdd:NF038318    51 ILADEVGLGKTIEAGLVLKYVLESGAK-KILIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKD----AKKWNK 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  915 LIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKN--RNCKLLDSLkhMDLEH---KVLLTGTPLQNTVEEL 989
Cdd:NF038318   121 RLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNL--YELTKgipKILLTATPLQNSLLDL 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  990 FSLLHFLEPSQFPSESEFLK------DFGDLKTEeqvqklqaiLKPMMLRRLKEDVEKNLAPKQETII---------EVE 1054
Cdd:NF038318   199 YGLVSFIDPRIFGSEKVFSKryikdeDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdEIE 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1055 LTN-----IQKKYYRAILEKN----FSFLSKGAGHTNMP---------NLLNTMMELRKCCNHPYLIN------------ 1104
Cdd:NF038318   270 LYVrvnnfLKRDILYSIPTSNrtliILVIRKLLASSSFAlaetfevlkKRLEKLKEGTRSANAQEGFDlfwsfvedeide 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1105 -GAEEK-----------ILMEFREACHIIpqdfHLQAMVRSAGKLVLIDKLLPK-----LKAG-GHKVLIFSQMVRCLDI 1166
Cdd:NF038318   350 sGFEEKqdelytrqkefIQHEIDEVDAII----DVAKRIKTNAKVTALKTALEIafeyqREEGiAQKVVVFTESKRTQKY 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1167 LEDYLIQRRYLYERI---DG--------------RVR--GN--------LRQAAIDRFSkpdsDRFVFLLCTRAGGLGIN 1219
Cdd:NF038318   426 IAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYFK----NNAKILIVTDAGSEGLN 501
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093 1220 LTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGLDKAV 1283
Cdd:NF038318   502 LQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELFEGV 566
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
2319-2362 6.93e-15

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


Pssm-ID: 462196  Cd Length: 44  Bit Score: 70.23  E-value: 6.93e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907105093 2319 LDLETRIPVINKVDGTLLVGDEAPRRAELEMWLQGHPEFAVDPR 2362
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
BRK smart00592
domain in transcription and CHROMO domain helicases;
2320-2364 2.02e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 69.30  E-value: 2.02e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1907105093  2320 DLETRIPVINKVDGTLLVGDEAPRRAELEMWLQGHPEFAVDPRFL 2364
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
727-779 1.10e-10

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 58.74  E-value: 1.10e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093  727 EVDRILDesHSVDKDNGEpviYYLVKWCSLPYEDSTWELKEDVDEGK--IREFKR 779
Cdd:pfam00385    2 EVERILD--HRKDKGGKE---EYLVKWKGYPYDENTWEPEENLSKCPelIEEFKD 51
CHROMO smart00298
Chromatin organization modifier domain;
646-706 1.47e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 52.99  E-value: 1.47e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907105093   646 VDKVLSMRVVKKelpsGQYteaeEFFVKYKNYSYLHCEWATISQLEKDKRihqKLKRFKTK 706
Cdd:smart00298    4 VEKILDHRWKKK----GEL----EYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKK 53
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
645-706 4.70e-07

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 48.34  E-value: 4.70e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  645 IVDKVLSMRVVKKELpsgqyteaEEFFVKYKNYSYLHCEWATISQLEKDKRIhqkLKRFKTK 706
Cdd:pfam00385    2 EVERILDHRKDKGGK--------EEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
727-779 2.53e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 43.74  E-value: 2.53e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093   727 EVDRILDesHSVDKDNGEpviYYLVKWCSLPYEDSTWELKEDVDEG--KIREFKR 779
Cdd:smart00298    3 EVEKILD--HRWKKKGEL---EYLVKWKGYSYSEDTWEPEENLLNCskKLDNYKK 52
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
61-421 6.67e-05

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 48.00  E-value: 6.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   61 SSASDLVP-PPEETAST---------ELPKESTAPapesltlhdytTQPTSQEQPAQPVLQTSTPTAGllqvsKSQEILS 130
Cdd:cd22540     17 STTQDSQPsPLALLAATcskigppavEAAVTPPAP-----------PQPTPRKLVPIKPAPLPLGPGK-----NSIGFLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  131 -QGNPFMGVSATGVSPSNTGGQPSQSAPKIVILKAPPNSSVTGTH---VAQIQAQGITS-TAQPLVAGTANGGKVTFTKV 205
Cdd:cd22540     81 aKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGSQTRSSTNQQyqiSPQIQAAGQINnSGQIQIIPGTNQAIITPVQV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  206 LTGT-------PLRPGVSIVSGNTVLATKVPGNQaavqrIVQPSRPVKQLVLqPVKGSAPAGNPGA----AGPPLKPAVT 274
Cdd:cd22540    161 LQQPqqahkpvPIKPAPLQTSNTNSASLQVPGNV-----IKLQSGGNVALTL-PVNNLVGTQDGATqlqlAAAPSKPSKK 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  275 LTSTPTQGESKRITlVLQQPQSggpqghrhVVLGSLPGKIVLQGNQLaaLTQAKNAQGQPAkvvtiqlqvqqpqqkiqiv 354
Cdd:cd22540    235 IRKKSAQAAQPAVT-VAEQVET--------VLIETTADNIIQAGNNL--LIVQSPGTGQPA------------------- 284
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907105093  355 pqppssqpqpqpqpppsaqplTLSSVQQAQimgPGQNPG--QRLSVPLKMVlqpqagssQGASSGLSVV 421
Cdd:cd22540    285 ---------------------VLQQVQVLQ---PKQEQQvvQIPQQALRVV--------QAASATLPTV 321
PHA03247 PHA03247
large tegument protein UL36; Provisional
68-280 1.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   68 PPPEETASTELPKESTAPAPESLTLHDYTTQPTSQEQPAQPVLQTSTPTAGLLQVSKSQEILSQGNPfMGVSATGVSPSN 147
Cdd:PHA03247  2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA-AQASSPPQRPRR 2685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  148 TGGQPS-----------------QSAPKIVIlKAPPNSSVTGTHVAQIQAQGITSTAQPLVAGTANGGKVT--FTKVLTG 208
Cdd:PHA03247  2686 RAARPTvgsltsladpppppptpEPAPHALV-SATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArpARPPTTA 2764
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907105093  209 TPLRPG--VSIVSGNTVLATKVPGNQAAVQRIVQPSRPVKQLVLQPVKGSAPAGNPGAAGPPLKPAVTlTSTPT 280
Cdd:PHA03247  2765 GPPAPAppAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT-SAQPT 2837
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
56-445 2.83e-03

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


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 42.64  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   56 GDVGNSSASDLVPPPEETASTELPKEST--APAPESLT-----LHDYTTQPTSQEQPAQPvlQTSTP-TAGLLQVSKSQE 127
Cdd:pfam17823   36 GAGKQNASGDAVPRADNKSSEQ*NFCAAtaAPAPVTLTkgtsaAHLNSTEVTAEHTPHGT--DLSEPaTREGAADGAASR 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  128 ILSQGNPFMGVSATGVSPSNTGGQPSQ--SAPKIVILKAP-------PNSSVTGTHVAQ---IQAQGITSTAQPLVAGTA 195
Cdd:pfam17823  114 ALAAAASSSPSSAAQSLPAAIAALPSEafSAPRAAACRANasaapraAIAAASAPHAASpapRTAASSTTAASSTTAASS 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  196 NGGKVTFTKVLTGTPLRPGVSIVSG------NTVLA-----TKVPGNQAAVQRIVQPSrPVKQLV--LQPVKGSAPAGN- 261
Cdd:pfam17823  194 APTTAASSAPATLTPARGISTAATAtghpaaGTALAavgnsSPAAGTVTAAVGTVTPA-ALATLAaaAGTVASAAGTINm 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  262 --PGAAGP-PLK--PAVTLTSTP-------TQGESKRITLvlQQP---QSGGPQGHRHVVLGSLPGKIVLQGNQLAALT- 325
Cdd:pfam17823  273 gdPHARRLsPAKhmPSDTMARNPaapmgaqAQGPIIQVST--DQPvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTt 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  326 ---QAKNAQGQPAKVvtiqlqvqqpqqkiqivpqPPSSQPQPQPQPPPSAQPLTLSSVQQAQimGPGQnpgqrLSVPLKM 402
Cdd:pfam17823  351 tkaQAKEPSASPVPV-------------------LHTSMIPEVEATSPTTQPSPLLPTQGAA--GPGI-----LLAPEQV 404
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1907105093  403 VLQPQAGS-SQGASSGLS-VVKVLSAsevaalsspASCAPHTAGK 445
Cdd:pfam17823  405 ATEATAGTaSAGPTPRSSgDPKTLAM---------ASCQLSTQGQ 440
PTZ00121 PTZ00121
MAEBL; Provisional
449-624 4.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 4.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  449 EENRRLEHQKKQEKANRIVAEAIARARARgEQNIPRVLNEDELPSVRPEEEGEKKRRKKSSGERLKEEKPKKSKTAAASK 528
Cdd:PTZ00121  1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEE-KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  529 TKGKsklntitpvvgKKRKRNTSSDNSDVEVMPAQSPREDEESSIQK----RRSNRQVKRK----KYTEDLDIKITDDEE 600
Cdd:PTZ00121  1696 KEAE-----------EAKKAEELKKKEAEEKKKAEELKKAEEENKIKaeeaKKEAEEDKKKaeeaKKDEEEKKKIAHLKK 1764
                          170       180
                   ....*....|....*....|....*
gi 1907105093  601 EEEVDVTGPIK-PEPILPEPVQEPD 624
Cdd:PTZ00121  1765 EEEKKAEEIRKeKEAVIEEELDEED 1789
 
Name Accession Description Interval E-value
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
813-1034 1.08e-153

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: 474.16  E-value: 1.08e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 892
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  893 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 972
Cdd:cd18060     81 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  973 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18060    161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 222
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
812-1411 2.62e-150

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 496.25  E-value: 2.62e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  812 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTEM-NTI 889
Cdd:PLN03142   169 KMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYrGITGPHMVVAPKSTLGNWMNEIRRFCPVlRAV 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQYemyckdsrgRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 969
Cdd:PLN03142   249 KFHGNPEERAHQREE---------LLVAG--KFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLF 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  970 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---GDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPK 1046
Cdd:PLN03142   318 STNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFqisGENDQQEVVQQLHKVLRPFLLRRLKSDVEKGLPPK 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1047 QETIIEVELTNIQKKYYRAILEKNFSFLSKGAGHTNmpnLLNTMMELRKCCNHPYLINGAEEKilmefreachiiPQDFH 1126
Cdd:PLN03142   398 KETILKVGMSQMQKQYYKALLQKDLDVVNAGGERKR---LLNIAMQLRKCCNHPYLFQGAEPG------------PPYTT 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1127 LQAMVRSAGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFV 1206
Cdd:PLN03142   463 GEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFV 542
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1207 FLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQs 1286
Cdd:PLN03142   543 FLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQ- 621
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1287 mSGRdgnitgIQQFSKKEIEDLLRKGAYAAIMEEDDEGSKFCEEDIDQILLR-RTTTITIESEGKGSTfakasfvasENR 1365
Cdd:PLN03142   622 -QGR------LAEQKTVNKDELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKgEEATAELDAKMKKFT---------EDA 685
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907105093 1366 TDISLDDPN----FWQKWAKKAD-LDMDLLNSKNnlVIDTPRvRKQTRHFS 1411
Cdd:PLN03142   686 IKFKMDDTAelydFDDEDDKDENkLDFKKIVSDN--WIDPPK-RERKRNYS 733
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
813-1034 2.49e-146

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: 453.24  E-value: 2.49e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWTEMNTIVY 891
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVeGIRGPFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  892 HGSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDL 971
Cdd:cd17995     81 HGSGESRQIIQQYEMYFKDAQGRKKKGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907105093  972 EHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd17995    161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQVEKLQALLKPYMLRR 223
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
813-1034 4.95e-134

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: 418.29  E-value: 4.95e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 892
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLMGIRGPFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  893 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 972
Cdd:cd18058     81 GSQISRQMIQQYEMYYRDEQGNPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  973 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKTEEQVKKLQSILKPMMLRR 222
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
813-1034 4.97e-128

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: 401.33  E-value: 4.97e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 892
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFLYEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  893 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 972
Cdd:cd18059     81 GSQASRRTIQLYEMYFKDPQGRVIKGSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  973 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18059    161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
813-1034 9.77e-128

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: 400.54  E-value: 9.77e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYH 892
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTGIRGPFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  893 GSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 972
Cdd:cd18061     81 GSLISRQMIQQYEMYFRDSQGRIIRGAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  973 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18061    161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKTEEQVQKLQAILKPMMLRR 222
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
683-1271 6.83e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 408.07  E-value: 6.83e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  683 EWATISQLEKDKRIHQKLKRFKTKMAQMRHFFHEDEEPFNPDYVEVDRILDESHSVDKDNGEPVIYYLVKWCSLPYEDST 762
Cdd:COG0553    110 LLALLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLAL 189
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  763 WELKEDVDEGKIREFKRIQSRHPELRRVnRPQANAWKKLELSHEYKNRN---QLREYQLEGVNWLLFNWYNRQNCILADE 839
Cdd:COG0553    190 LELALLAAEAELLLLLELLLELELLAEA-AVDAFRLRRLREALESLPAGlkaTLRPYQLEGAAWLLFLRRLGLGGLLADD 268
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  840 MGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVYHGSLASRQMIQQYEmyckdsrgrlipg 918
Cdd:COG0553    269 MGLGKTIQALALLLELKERGLARPVLIVAPTSLVGNWQRELAKFApGLRVLVLDGTRERAKGANPFE------------- 335
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  919 ayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEP 998
Cdd:COG0553    336 --DADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNP 413
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  999 SQFPSESEFLKDFGDLKT---EEQVQKLQAILKPMMLRRLKEDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLS 1075
Cdd:COG0553    414 GLLGSLKAFRERFARPIEkgdEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELE 493
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1076 KGAGHTNMPNLLNTMMELRKCCNHPYLINGAEEKILmefreachiipqdfhlqamVRSaGKLVLIDKLLPKLKAGGHKVL 1155
Cdd:COG0553    494 GAEGIRRRGLILAALTRLRQICSHPALLLEEGAELS-------------------GRS-AKLEALLELLEELLAEGEKVL 553
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1156 IFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKpDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNP 1235
Cdd:COG0553    554 VFSQFTDTLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNP 632
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1907105093 1236 QNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFD 1271
Cdd:COG0553    633 AVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
816-1103 2.05e-88

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: 290.35  E-value: 2.05e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  816 YQLEGVNWLLFNWYNRQ-NCILADEMGLGKTIQSIAFLQEVYNVGI--HGPFLVIAPLSTITNWEREFNTWT---EMNTI 889
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKHVDKnwGGPTLIVVPLSLLHNWMNEFERWVsppALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQYEMYckdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 969
Cdd:pfam00176   81 VLHGNKRPQERWKNDPNF-----------LADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  970 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----DLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAP 1045
Cdd:pfam00176  150 KTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDrpieRGGGKKGVSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1046 KQETIIEVELTNIQKKYY-RAILEKNFSFLSKG-AGHTNMPNLLNTMMELRKCCNHPYLI 1103
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGeGGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
812-1034 4.10e-86

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: 280.78  E-value: 4.10e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  812 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWT-EMNTI 889
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSqQQYGPFLVVVPLSTMPAWQREFAKWApDMNVI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQYEMYcKDSRGRLipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 969
Cdd:cd17993     81 VYLGDIKSRDTIREYEFY-FSQTKKL-----KFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEF 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093  970 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFgDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd17993    155 KTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEEEH-DEEQEKGIADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
813-998 2.02e-75

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: 248.63  E-value: 2.02e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 890
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLlKEGKERGPVLVVCPLSVLENWEREFEKWTpDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  891 YHGSLASRQMIQQYEMYCKdsrgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 970
Cdd:cd17919     81 YHGSQRERAQIRAKEKLDK------------FDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR 148
                          170       180
                   ....*....|....*....|....*...
gi 1907105093  971 LEHKVLLTGTPLQNTVEELFSLLHFLEP 998
Cdd:cd17919    149 AKRRLLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
812-1036 9.36e-73

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: 243.45  E-value: 9.36e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  812 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 890
Cdd:cd18009      3 VMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERGVWGPFLVIAPLSTLPNWVNEFARFTpSVPVLL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  891 YHGSLASRQMIQQYEMYCKDSRGrlipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 970
Cdd:cd18009     83 YHGTKEERERLRKKIMKREGTLQ-------DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFN 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  971 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLK--DFGDLK---------TEEQ----VQKLQAILKPMMLRRL 1035
Cdd:cd18009    156 SDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESwfDFSSLSdnaadisnlSEEReqniVHMLHAILKPFLLRRL 235

                   .
gi 1907105093 1036 K 1036
Cdd:cd18009    236 K 236
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
812-1036 1.64e-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: 233.80  E-value: 1.64e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  812 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWT-EMNTI 889
Cdd:cd17996      3 TLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKkKNNGPYLVIVPLSTLSNWVSEFEKWApSVSKI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQYEMYCKdsrgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 969
Cdd:cd17996     83 VYKGTPDVRKKLQSQIRAGK------------FNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTY 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  970 -DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEF------------LKDFGDLKTEEQV---QKLQAILKPMMLR 1033
Cdd:cd17996    151 yHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFeqwfntpfantgEQVKIELNEEETLliiRRLHKVLRPFLLR 230

                   ...
gi 1907105093 1034 RLK 1036
Cdd:cd17996    231 RLK 233
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
813-1034 1.66e-68

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: 229.63  E-value: 1.66e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 890
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  891 YHGSlasrqmiqqyemyckdsrgrlipgaykfDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 970
Cdd:cd17994     81 YVGD----------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYK 132
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907105093  971 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd17994    133 IGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADISKEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
812-1034 4.49e-67

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: 227.20  E-value: 4.49e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  812 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTI 889
Cdd:cd18054     20 ELRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHqLYGPFLLVVPLSTLTSWQREFEIWApEINVV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQYEMYCKDSRgRLipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 969
Cdd:cd18054    100 VYIGDLMSRNTIREYEWIHSQTK-RL-----KFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDF 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093  970 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKtEEQVQKLQAILKPMMLRR 1034
Cdd:cd18054    174 KSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGR-ENGYQSLHKVLEPFLLRR 237
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
812-1036 2.12e-65

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: 221.81  E-value: 2.12e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  812 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWT-EMNTI 889
Cdd:cd17997      3 TMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYkNINGPHLIIVPKSTLDNWMREFKRWCpSLRVV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIqqyemyckdSRGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHM 969
Cdd:cd17997     83 VLIGDKEERADI---------IRDVLLPG--KFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLF 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907105093  970 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF----GDLKTEEQVQKLQAILKPMMLRRLK 1036
Cdd:cd17997    152 NSRNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFnvnnCDDDNQEVVQRLHKVLRPFLLRRIK 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
813-1034 1.92e-63

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: 216.42  E-value: 1.92e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 890
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGhTKGPFLVSAPLSTIINWEREFQMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  891 YHGSLASRQMIQQYEMYCKDSRGRLIPGAYK--------FDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 962
Cdd:cd18055     81 YTGDKDSRAIIRENEFSFDDNAVKGGKKAFKmkreaqvkFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  963 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
810-1036 6.90e-63

DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging to SNF2 family of DNA dependent ATPases are important members of the chromatin remodeling complexes that are implicated in epigenetic control of gene expression. The Snf2 family comprises a large group of ATP-hydrolyzing proteins that are ubiquitous in eukaryotes, but also present in eubacteria and archaea. Archaeal SWI2 and SNF2 are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350770 [Multi-domain]  Cd Length: 218  Bit Score: 214.35  E-value: 6.90e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  810 RNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNT 888
Cdd:cd18012      2 KATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLSRKEEGRKGPSLVVAPTSLIYNWEEEAAKFApELKV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  889 IVYHGSLASRQMIQQYEmyckdsrgrlipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKH 968
Cdd:cd18012     82 LVIHGTKRKREKLRALE---------------DYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKA 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  969 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----DLKTEEQVQKLQAILKPMMLRRLK 1036
Cdd:cd18012    147 LKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAkpieKDGDEEALEELKKLISPFILRRLK 218
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
813-1034 2.74e-62

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: 213.00  E-value: 2.74e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 890
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGhSKGPFLVSAPLSTIINWEREFEMWApDMYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  891 YHGSLASRQMIQQYEMYCKDS--RG-----RLIPGA-YKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 962
Cdd:cd18056     81 YVGDKDSRAIIRENEFSFEDNaiRGgkkasRMKKEAsVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  963 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
813-1034 5.50e-62

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: 212.23  E-value: 5.50e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 890
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGhSKGPYLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  891 YHGSLASRQMIQQYEMYCKDSRGRLIPGAY--------KFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 962
Cdd:cd18057     81 YTGDKESRSVIRENEFSFEDNAIRSGKKVFrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  963 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
813-1034 4.18e-57

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: 197.66  E-value: 4.18e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 890
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLaGRLKLLGPFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  891 YHGSLASRQMIQQyEMYcKDSRgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 970
Cdd:cd18006     81 YMGDKEKRLDLQQ-DIK-STNR---------FHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907105093  971 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSES--EFLKDFGDLKTE-EQVQKLQAILKPMMLRR 1034
Cdd:cd18006    150 VDFRLLLTGTPIQNSLQELYALLSFIEPNVFPKDKldDFIKAYSETDDEsETVEELHLLLQPFLLRR 216
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1135-1260 4.54e-57

C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 194.23  E-value: 4.54e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1135 GKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDrFVFLLCTRAG 1214
Cdd:cd18793     11 GKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDI-RVFLLSTKAG 89
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1907105093 1215 GLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI 1260
Cdd:cd18793     90 GVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
813-1034 1.76e-55

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: 193.34  E-value: 1.76e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEV-YNVGIHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 890
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLaCEKGNWGPHLIVVPTSVMLNWEMEFKRWCPgFKILT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  891 YHGSLASRQMIQQyEMYCKDSrgrlipgaykFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 970
Cdd:cd18003     81 YYGSAKERKLKRQ-GWMKPNS----------FHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFN 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907105093  971 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKT----------EEQVQKLQAILKPMMLRR 1034
Cdd:cd18003    150 TQRRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLTamsegsqeenEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
812-1034 1.17e-54

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: 191.42  E-value: 1.17e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  812 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWEREFNTWT-EMNTI 889
Cdd:cd18053     20 ELRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEhQLYGPFLLVVPLSTLTSWQREIQTWApQMNAV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQYE-MYCKDSRgrlipgaYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKH 968
Cdd:cd18053    100 VYLGDINSRNMIRTHEwMHPQTKR-------LKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLID 172
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907105093  969 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKtEEQVQKLQAILKPMMLRR 1034
Cdd:cd18053    173 FKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGR-EYGYASLHKELEPFLLRR 237
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
813-1001 1.79e-53

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: 186.05  E-value: 1.79e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIVY 891
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGIPGPHLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  892 HGSLASRqmiqqyemycKDSRGRLIPGAYKFDALITTFEMILSDCPE---LREIEWRCVIIDEAHRLKNRNCKLLDSLKH 968
Cdd:cd17998     81 YGSQEER----------KHLRYDILKGLEDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSERYRHLMT 150
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907105093  969 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQF 1001
Cdd:cd17998    151 INANFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
813-1034 3.59e-52

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: 184.50  E-value: 3.59e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLlFNWY-NRQNCILADEMGLGKTIQSIAFLQEVY-----------------------NVGihGPFLVIA 868
Cdd:cd18005      1 LRDYQREGVEFM-YDLYkNGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrprfkkkppasSAK--KPVLIVA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  869 PLSTITNWEREFNTWTEMNTIVYHGSLASRQMIqqyemyckdsrGRLIPGAYkfDALITTFEMILSDCPELREIEWRCVI 948
Cdd:cd18005     78 PLSVLYNWKDELDTWGHFEVGVYHGSRKDDELE-----------GRLKAGRL--EVVVTTYDTLRRCIDSLNSINWSAVI 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  949 IDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD--------------- 1013
Cdd:cd18005    145 ADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEpikrgqrhtatarel 224
                          250       260
                   ....*....|....*....|.
gi 1907105093 1014 LKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18005    225 RLGRKRKQELAVKLSKFFLRR 245
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
813-1034 9.12e-52

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: 182.70  E-value: 9.12e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLfNWYNRQ-NCILADEMGLGKTIQSIAF---LQEVYNvgIHGPFLVIAPLSTITNWEREFNTWT-EMN 887
Cdd:cd18002      1 LKEYQLKGLNWLA-NLYEQGiNGILADEMGLGKTVQSIAVlahLAEEHN--IWGPFLVIAPASTLHNWQQEISRFVpQFK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  888 TIVYHGSLASRQMIQQY----EMYCKDSrgrlipgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLL 963
Cdd:cd18002     78 VLPYWGNPKDRKVLRKFwdrkNLYTRDA---------PFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRW 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  964 DSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-DLKT---------EEQVQKLQAILKPMMLR 1033
Cdd:cd18002    149 KTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSkDIEShaenktglnEHQLKRLHMILKPFMLR 228

                   .
gi 1907105093 1034 R 1034
Cdd:cd18002    229 R 229
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
800-1047 2.00e-49

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: 176.78  E-value: 2.00e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  800 KLELSHEYKNRNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWER 878
Cdd:cd18064      3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYrNIPGPHMVLVPKSTLHNWMA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  879 EFNTWTEmntivyhgSLASRQMIQQYEMYCKDSRGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 958
Cdd:cd18064     83 EFKRWVP--------TLRAVCLIGDKDQRAAFVRDVLLPG--EWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  959 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---LKTEEQVQKLQAILKPMMLRRL 1035
Cdd:cd18064    153 KSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTnncLGDQKLVERLHMVLRPFLLRRI 232
                          250
                   ....*....|..
gi 1907105093 1036 KEDVEKNLAPKQ 1047
Cdd:cd18064    233 KADVEKSLPPKK 244
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
812-1036 9.28e-47

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: 169.45  E-value: 9.28e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  812 QLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWT-EMNTI 889
Cdd:cd18062     23 VLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKrINGPFLIIVPLSTLSNWVYEFDKWApSVVKV 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQyemyckdsrgrlIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK-H 968
Cdd:cd18062    103 SYKGSPAARRAFVP------------QLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtH 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  969 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRRL 1035
Cdd:cd18062    171 YVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRRL 250

                   .
gi 1907105093 1036 K 1036
Cdd:cd18062    251 K 251
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
813-1034 4.88e-46

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: 166.69  E-value: 4.88e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFnwynrqnC--ILADEMGLGKTIQSIA--------FLQEVYNVGIHGPF----------LVIAPLST 872
Cdd:cd18008      1 LLPYQKQGLAWMLP-------RggILADEMGLGKTIQALAlilatrpqDPKIPEELEENSSDpkklylskttLIVVPLSL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  873 ITNWEREFNTWTE---MNTIVYHGSlasrqmiqqyemyckdSRGRLIPGAYKFDALITTFEMILSDCPE----------- 938
Cdd:cd18008     74 LSQWKDEIEKHTKpgsLKVYVYHGS----------------KRIKSIEELSDYDIVITTYGTLASEFPKnkkgggrdske 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  939 -----LREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD 1013
Cdd:cd18008    138 keaspLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISK 217
                          250       260
                   ....*....|....*....|....
gi 1907105093 1014 LKTE---EQVQKLQAILKPMMLRR 1034
Cdd:cd18008    218 PFSKndrKALERLQALLKPILLRR 241
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
813-1036 5.82e-46

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: 167.16  E-value: 5.82e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVY-NVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 890
Cdd:cd18063     24 LKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMeHKRLNGPYLIIVPLSTLSNWTYEFDKWApSVVKIS 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  891 YHGSLASRQmiqqyemyckdsrgRLIPG--AYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK- 967
Cdd:cd18063    104 YKGTPAMRR--------------SLVPQlrSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  968 HMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 1034
Cdd:cd18063    170 HYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgervDLNEEETiliIRRLHKVLRPFLLRR 249

                   ..
gi 1907105093 1035 LK 1036
Cdd:cd18063    250 LK 251
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
800-1036 1.35e-44

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: 162.49  E-value: 1.35e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  800 KLELSHEYKNRNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNV-GIHGPFLVIAPLSTITNWER 878
Cdd:cd18065      3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYrNIPGPHMVLVPKSTLHNWMN 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  879 EFNTWTEmntivyhgSLASRQMIQQYEMYCKDSRGRLIPGayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 958
Cdd:cd18065     83 EFKRWVP--------SLRAVCLIGDKDARAAFIRDVMMPG--EWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNE 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  959 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD---LKTEEQVQKLQAILKPMMLRRL 1035
Cdd:cd18065    153 KSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTkncLGDQKLVERLHAVLKPFLLRRI 232

                   .
gi 1907105093 1036 K 1036
Cdd:cd18065    233 K 233
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
813-1034 2.20e-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: 158.69  E-value: 2.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTE-MNTIVY 891
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSVLVVMPTSLIPHWVKEFAKWTPgLRVKVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  892 HG-SLASRQMIQqyeMYCKDSRGrlipgaykfdALITTFEMILSDCPEL-----REIEWRCVIIDEAHRLKNRNCKLLDS 965
Cdd:cd18001     81 HGtSKKERERNL---ERIQRGGG----------VLLTTYGMVLSNTEQLsaddhDEFKWDYVILDEGHKIKNSKTKSAKS 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  966 LKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQ-FPSESEFLKDF------GDLKTEEQVQK---------LQAILKP 1029
Cdd:cd18001    148 LREIPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFenpitrGRDKDATQGEKalgsevaenLRQIIKP 227

                   ....*
gi 1907105093 1030 MMLRR 1034
Cdd:cd18001    228 YFLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
813-1034 2.25e-39

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


Pssm-ID: 350762 [Multi-domain]  Cd Length: 240  Bit Score: 147.43  E-value: 2.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLL-----FNWYNRQNCILADEMGLGKTIQSIAFL-----QEVYNVGIHGPFLVIAPLSTITNWEREFNT 882
Cdd:cd18004      1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAIALVwtllkQGPYGKPTAKKALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  883 WT-EMNTIVYhgSLASRQMIQQYEMYCKDSRGRlipgaykFDALITTFEMILSDCPELREIEwRC--VIIDEAHRLKNRN 959
Cdd:cd18004     81 WLgLRRIKVV--TADGNAKDVKASLDFFSSAST-------YPVLIISYETLRRHAEKLSKKI-SIdlLICDEGHRLKNSE 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  960 CKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD--LK------TEEQV-------QKLQ 1024
Cdd:cd18004    151 SKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEpiLRsrdpdaSEEDKelgaersQELS 230
                          250
                   ....*....|
gi 1907105093 1025 AILKPMMLRR 1034
Cdd:cd18004    231 ELTSRFILRR 240
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
813-1034 6.95e-39

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: 145.96  E-value: 6.95e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLF-NWYNRQNcILADEMGLGKTIQSIAFL-------QEVYNVgIHGPFLVIAPLSTITNWEREFNTWT 884
Cdd:cd17999      1 LRPYQQEGINWLAFlNKYNLHG-ILCDDMGLGKTLQTLCILasdhhkrANSFNS-ENLPSLVVCPPTLVGHWVAEIKKYF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  885 E---MNTIVYHGSLASRQmiqqyemyckdsrgRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCK 961
Cdd:cd17999     79 PnafLKPLAYVGPPQERR--------------RLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  962 LLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG-------DLK-----TEEQVQKLQAILK- 1028
Cdd:cd17999    145 LSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLkpilasrDSKasakeQEAGALALEALHKq 224

                   ....*...
gi 1907105093 1029 --PMMLRR 1034
Cdd:cd17999    225 vlPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
813-998 2.16e-37

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: 140.15  E-value: 2.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLfnWYNRQNC--ILADEMGLGKTIQSIAFLQevynvGIH------GPFLVIAPLSTITNWEREFNTW- 883
Cdd:cd18000      1 LFKYQQTGVQWLW--ELHCQRVggILGDEMGLGKTIQIIAFLA-----ALHhsklglGPSLIVCPATVLKQWVKEFHRWw 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  884 TEMNTIVYHGSLASrqMIQQYEMYCKDSRGRLIPGAYK-FDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 962
Cdd:cd18000     74 PPFRVVVLHSSGSG--TGSEEKLGSIERKSQLIRKVVGdGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEI 151
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907105093  963 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEP 998
Cdd:cd18000    152 TLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
723-781 7.50e-36

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: 130.49  E-value: 7.50e-36
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907105093  723 PDYVEVDRILDESHSVDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQ 781
Cdd:cd18663      1 PDYVEVDRILDVSVSTDPNTGEPVTHYLVKWCSLPYEDSTWELEEDVDPAKIEEFEKLR 59
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
813-1011 1.52e-31

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: 125.10  E-value: 1.52e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVN--W--LLFNWYNRQN---CILADEMGLGKTIQSIAFLQeVYNvgIHGP----FLVIAPLSTITNWEREFN 881
Cdd:cd18007      1 LKPHQVEGVRflWsnLVGTDVGSDEgggCILAHTMGLGKTLQVITFLH-TYL--AAAPrrsrPLVLCPASTLYNWEDEFK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  882 TWTEMNTIVYHGSLASRQ---------MIQQ-----------YEMY-----CKDSRGRLIPGAYKFDALITtfemilsdc 936
Cdd:cd18007     78 KWLPPDLRPLLVLVSLSAskradarlrKINKwhkeggvlligYELFrnlasNATTDPRLKQEFIAALLDPG--------- 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093  937 PELreiewrcVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 1011
Cdd:cd18007    149 PDL-------LVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKF 216
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
640-705 1.39e-29

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


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 113.20  E-value: 1.39e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907105093  640 EEDAAIVDKVLSMRVVKKELPSG-QYTEAEEFFVKYKNYSYLHCEWATISQLEK-DKRIHQKLKRFKT 705
Cdd:cd18668      1 EEDTMIIEKILASRKKKKEKEEGaEEIEVEEYLVKYKNFSYLHCEWKTEEELEKgDKRIKQKIKRFKQ 68
DEXDc smart00487
DEAD-like helicases superfamily;
806-1004 5.48e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 116.44  E-value: 5.48e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   806 EYKNRNQLREYQLEGVNWLLFNWynrQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTIT-NWEREFNTWT 884
Cdd:smart00487    2 EKFGFEPLRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAeQWAEELKKLG 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   885 E---MNTIVYHGSLASRQMIQQYEMYCkdsrgrlipgaykFDALITTFEMILSDCPE--LREIEWRCVIIDEAHRLKN-- 957
Cdd:smart00487   79 PslgLKVVGLYGGDSKREQLRKLESGK-------------TDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDgg 145
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1907105093   958 RNCKLLDSLKHMDLE-HKVLLTGTP---LQNTVEELFSLLHFLEPSQFPSE 1004
Cdd:smart00487  146 FGDQLEKLLKLLPKNvQLLLLSATPpeeIENLLELFLNDPVFIDVGFTPLE 196
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
813-1011 5.04e-28

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: 114.56  E-value: 5.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVnwlLFNWY--------NRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGP------FLVIAPLSTITNWER 878
Cdd:cd18066      1 LRPHQREGI---EFLYEcvmgmrvnERFGAILADEMGLGKTLQCISLIWTLLRQGPYGGkpvikrALIVTPGSLVKNWKK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  879 EFNTWTemntivyhgslaSRQMIQQYEMYcKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNR 958
Cdd:cd18066     78 EFQKWL------------GSERIKVFTVD-QDHKVEEFIASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNT 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907105093  959 NCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 1011
Cdd:cd18066    145 SIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVY 197
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
813-1034 1.73e-27

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


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 112.30  E-value: 1.73e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLfnwynRQN--CILADEMGLGKTIQSIAFLQEVYNvgiHGPFLVIAPLSTITNWEREFNTW------T 884
Cdd:cd18010      1 LLPFQREGVCFAL-----RRGgrVLIADEMGLGKTVQAIAIAAYYRE---EWPLLIVCPSSLRLTWADEIERWlpslppD 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  885 EMNTIVyhgslasrqmiqqyemyckDSRGRLIPGAYKFdaLITTFEMILSDCPELREIEWRCVIIDEAHRLKNRN----- 959
Cdd:cd18010     73 DIQVIV-------------------KSKDGLRDGDAKV--VIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKakrtk 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  960 --CKLLDSLKhmdleHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEF---------LKDFGDLKTEEQVQKLQAIL- 1027
Cdd:cd18010    132 aaLPLLKRAK-----RVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgrrycaakqGGFGWDYSGSSNLEELHLLLl 206

                   ....*..
gi 1907105093 1028 KPMMLRR 1034
Cdd:cd18010    207 ATIMIRR 213
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
813-1034 7.32e-26

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


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 108.71  E-value: 7.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLL-----FNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGP-----FLVIAPLSTITNWEREFNT 882
Cdd:cd18067      1 LRPHQREGVKFLYrcvtgRRIRGSHGCIMADEMGLGKTLQCITLMWTLLRQSPQCKpeidkAIVVSPSSLVKNWANELGK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  883 WTEMNTIVYHGSLASRQMIQQYEMYCKDSRGRLIPGAykfdALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKL 962
Cdd:cd18067     81 WLGGRLQPLAIDGGSKKEIDRKLVQWASQQGRRVSTP----VLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  963 LDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF---------GD------LKTEEQVQKLQAIL 1027
Cdd:cd18067    157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFelpilkgrdADasekerQLGEEKLQELISIV 236

                   ....*..
gi 1907105093 1028 KPMMLRR 1034
Cdd:cd18067    237 NRCIIRR 243
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1135-1249 7.98e-26

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: 103.83  E-value: 7.98e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1135 GKLVLIDKLLPKLKagGHKVLIFSQMVRCLDilEDYLIQRR-YLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRA 1213
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKKTLE--AELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKID---VLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1907105093 1214 GGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIG 1249
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
828-1034 4.72e-24

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: 103.32  E-value: 4.72e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  828 WYN-----RQNC--------ILADEMGLGKTIQSIAFLqevynvgIHGPFLVIAPLSTITNWEREFNTWTE---MNTIVY 891
Cdd:cd18071     32 FLNtitnfSQKKrpelvrggILADDMGLGKTLTTISLI-------LANFTLIVCPLSVLSNWETQFEEHVKpgqLKVYTY 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  892 HGSlasrqmiqqyemyckdSRGRLIPGAYKFDALITTFEMILSD-----CPELREIEWRCVIIDEAHRLKNRNCKLLDSL 966
Cdd:cd18071    105 HGG----------------ERNRDPKLLSKYDIVLTTYNTLASDfgakgDSPLHTINWLRVVLDEGHQIRNPNAQQTKAV 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907105093  967 KHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG---DLKTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18071    169 LNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQrplTMGDPTGLKRLQVLMKQITLRR 239
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
813-1034 9.12e-23

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: 98.52  E-value: 9.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLFNWYNRqnCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREfntwtemntivyh 892
Cdd:cd18011      1 PLPHQIDAVLRALRKPPVR--LLLADEVGLGKTIEAGLIIKELLLRGDAKRVLILCPASLVEQWQDE------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  893 gsLASRQMIQQYEMYcKDSRGRLIPGAYK----FDALITTFEMILSDcPELRE----IEWRCVIIDEAHRLKNRNC---- 960
Cdd:cd18011     66 --LQDKFGLPFLILD-RETAAQLRRLIGNpfeeFPIVIVSLDLLKRS-EERRGlllsEEWDLVVVDEAHKLRNSGGgket 141
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907105093  961 ---KLLDSLKHMDlEHKVLLTGTPLQNTVEELFSLLHFLEPSQFpsesEFLKDFGDLKTEEQVqklqaiLKPMMLRR 1034
Cdd:cd18011    142 kryKLGRLLAKRA-RHVLLLTATPHNGKEEDFRALLSLLDPGRF----AVLGRFLRLDGLREV------LAKVLLRR 207
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
813-1034 1.09e-20

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


Pssm-ID: 350830 [Multi-domain]  Cd Length: 241  Bit Score: 93.70  E-value: 1.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLfnWYNRQNC---ILADEMGLGKTIQSIAF-----------------------LQEVYNVGIHGPFLV 866
Cdd:cd18072      1 LLLHQKQALAWLL--WRERQKPrggILADDMGLGKTLTMIALilaqkntqnrkeeekekalteweSKKDSTLVPSAGTLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  867 IAPLSTITNWEREFNTWTEMNTI---VYHGslASRqmiqqyemyckDSRGRLIPgayKFDALITTFEMILSDCPELRE-- 941
Cdd:cd18072     79 VCPASLVHQWKNEVESRVASNKLrvcLYHG--PNR-----------ERIGEVLR---DYDIVITTYSLVAKEIPTYKEes 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  942 -------IEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFpSESEFLKDFGDL 1014
Cdd:cd18072    143 rssplfrIAWARIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPF-DDLKVWKKQVDN 221
                          250       260
                   ....*....|....*....|
gi 1907105093 1015 KTEEQVQKLQAILKPMMLRR 1034
Cdd:cd18072    222 KSRKGGERLNILTKSLLLRR 241
HELICc smart00490
helicase superfamily c-terminal domain;
1165-1249 1.31e-20

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 88.04  E-value: 1.31e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  1165 DILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDrfvFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQAR 1244
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIK---VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 1907105093  1245 CHRIG 1249
Cdd:smart00490   78 AGRAG 82
DISARM_DrmD_b NF038318
DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component ...
835-1283 1.58e-20

DISARM system SNF2-like helicase DrmD, short form; DrmD, a SNF2-like helicase, is a component of class 1 DISARM (Defence Island System Associated with Restriction Modification), which contains a DNA adenine N6 methyltransferase. This HMM describes a distinct form that is somewhat shorter than the majority of DrmD proteins.


Pssm-ID: 468472 [Multi-domain]  Cd Length: 868  Bit Score: 99.37  E-value: 1.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  835 ILADEMGLGKTIQSIAFLQEVYNVGIHgPFLVIAPLSTITNWEREFNTWTEMNTIVyhgslASRQMIQQYemycKDSRGR 914
Cdd:NF038318    51 ILADEVGLGKTIEAGLVLKYVLESGAK-KILIILPANLRKQWEIELEEKFDLESLI-----LDSLTVEKD----AKKWNK 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  915 LIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKN--RNCKLLDSLkhMDLEH---KVLLTGTPLQNTVEEL 989
Cdd:NF038318   121 RLTDNKKVRIVITSYDYASKLMKRFPKVKWDFIIIDEAHNLRNvhKGGKRAKNL--YELTKgipKILLTATPLQNSLLDL 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  990 FSLLHFLEPSQFPSESEFLK------DFGDLKTEeqvqklqaiLKPMMLRRLKEDVEKNLAPKQETII---------EVE 1054
Cdd:NF038318   199 YGLVSFIDPRIFGSEKVFSKryikdeDYSDLKRE---------LSPVLYRTLRKDVADYMQFKKRKCItvdfelspdEIE 269
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1055 LTN-----IQKKYYRAILEKN----FSFLSKGAGHTNMP---------NLLNTMMELRKCCNHPYLIN------------ 1104
Cdd:NF038318   270 LYVrvnnfLKRDILYSIPTSNrtliILVIRKLLASSSFAlaetfevlkKRLEKLKEGTRSANAQEGFDlfwsfvedeide 349
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1105 -GAEEK-----------ILMEFREACHIIpqdfHLQAMVRSAGKLVLIDKLLPK-----LKAG-GHKVLIFSQMVRCLDI 1166
Cdd:NF038318   350 sGFEEKqdelytrqkefIQHEIDEVDAII----DVAKRIKTNAKVTALKTALEIafeyqREEGiAQKVVVFTESKRTQKY 425
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1167 LEDYLIQRRYLYERI---DG--------------RVR--GN--------LRQAAIDRFSkpdsDRFVFLLCTRAGGLGIN 1219
Cdd:NF038318   426 IAEELRKSGYEGEDIllfNGdfddamtkeiyrawQVKnyGKanygrsveYKHAIVDYFK----NNAKILIVTDAGSEGLN 501
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093 1220 LTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLI-TRNSYEREMFDKASLKLGLDKAV 1283
Cdd:NF038318   502 LQFCNTVINYDLPWNPQKIEQRIGRCHRYGQKNDVVAINLLnTQNVADKRVYEILSEKFELFEGV 566
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
834-1011 2.59e-20

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: 92.64  E-value: 2.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  834 CILADEMGLGKTIQSIAFLQEVY-NVGIHG--PFLVIAPLSTITNWEREFNTW------------TEMNTI--------- 889
Cdd:cd18068     31 CILAHCMGLGKTLQVVTFLHTVLlCEKLENfsRVLVVCPLNTVLNWLNEFEKWqeglkdeekievNELATYkrpqersyk 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  890 VYHGSLASRQMIQQYEMYCKDSRGRLIPGAYKfdaLITTFEMILSD-CPELreiewrcVIIDEAHRLKNRNCKLLDSLKH 968
Cdd:cd18068    111 LQRWQEEGGVMIIGYDMYRILAQERNVKSREK---LKEIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNS 180
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907105093  969 MDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 1011
Cdd:cd18068    181 IRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRF 223
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
834-1011 8.52e-20

DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called RAD54 like 2 or RAD54L2 ) modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. ARIP4 is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 90.64  E-value: 8.52e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  834 CILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWteMNTIVYHGSLASRQM---IQQYEMYCKD 910
Cdd:cd18069     31 CILAHSMGLGKTLQVISFLDVLLRHTGAKTVLAIVPVNTLQNWLSEFNKW--LPPPEALPNVRPRPFkvfILNDEHKTTA 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  911 SRGRLIPG-AYKFDALITTFEMI-LSDCPELreiewrcVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEE 988
Cdd:cd18069    109 ARAKVIEDwVKDGGVLLMGYEMFrLRPGPDV-------VICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIE 181
                          170       180
                   ....*....|....*....|...
gi 1907105093  989 LFSLLHFLEPSQFPSESEFLKDF 1011
Cdd:cd18069    182 YWCMVDFVRPDFLGTRQEFSNMF 204
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
724-779 4.91e-16

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: 74.15  E-value: 4.91e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907105093  724 DYVEVDRILDEShsvdkDNGEPVIYYLVKWCSLPYEDSTWELKEDV---DEGKIREFKR 779
Cdd:cd18659      1 EYTIVERIIAHR-----EDDEGVTEYLVKWKGLPYDECTWESEEDIsdiFQEAIDEYKK 54
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
2319-2362 6.93e-15

BRK domain; The function of this domain is unknown. It is often found associated with helicases and transcription factors.


Pssm-ID: 462196  Cd Length: 44  Bit Score: 70.23  E-value: 6.93e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907105093 2319 LDLETRIPVINKVDGTLLVGDEAPRRAELEMWLQGHPEFAVDPR 2362
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
BRK smart00592
domain in transcription and CHROMO domain helicases;
2320-2364 2.02e-14

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 69.30  E-value: 2.02e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1907105093  2320 DLETRIPVINKVDGTLLVGDEAPRRAELEMWLQGHPEFAVDPRFL 2364
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
642-704 1.88e-11

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: 61.61  E-value: 1.88e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  642 DAAIVDKVLSMRVVK-KELPSGQYTEAE------EFFVKYKNYSYLHCEWATISQLEKDkRIHQKLKRFK 704
Cdd:cd18660      1 DEDKIEKILDHRPKGpVEEASLDLTDPDepwderEFLVKWKGKSYLHCTWVTEETLEQL-RGKKKLKNYI 69
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
813-1000 2.62e-11

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: 65.45  E-value: 2.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLfnwYNRQNCILADeMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITN-WEREFNTWTEMNTIVY 891
Cdd:cd18013      1 PHPYQKVAINFII---EHPYCGLFLD-MGLGKTVTTLTALSDLQLDDFTRRVLVIAPLRVARStWPDEVEKWNHLRNLTV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  892 hgSLAsrqmiqqyemyckDSRGR-LIPGAYK-FDALITTFEMiLSDCPELREIEW--RCVIIDEAHRLKNRNCKLLDSLK 967
Cdd:cd18013     77 --SVA-------------VGTERqRSKAANTpADLYVINREN-LKWLVNKSGDPWpfDMVVIDELSSFKSPRSKRFKALR 140
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1907105093  968 HMD--LEHKVLLTGTPLQNTVEELFSLLHFLEPSQ 1000
Cdd:cd18013    141 KVRpvIKRLIGLTGTPSPNGLMDLWAQIALLDQGE 175
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
813-1033 3.41e-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: 65.83  E-value: 3.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGVNWLLfnwyNRQNcILADEMGLGKTIQSIAFL--------------------------QEVYNVGIHGPFLV 866
Cdd:cd18070      1 LLPYQRRAVNWML----VPGG-ILADEMGLGKTVEVLALIllhprpdndldaadddsdemvccpdcLVAETPVSSKATLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  867 IAPLSTITNWEREFNTWTEMNTIVYHgslasrqmiqqYEMYCKDsrGRLIPGAYKF----DALITTFEMILSD------- 935
Cdd:cd18070     76 VCPSAILAQWLDEINRHVPSSLKVLT-----------YQGVKKD--GALASPAPEIlaeyDIVVTTYDVLRTElhyaean 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  936 ----------------CPeLREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPS 999
Cdd:cd18070    143 rsnrrrrrqkryeappSP-LVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVE 221
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907105093 1000 QFpSESEFLKDFGDLKTEEQ--VQKLQAILKPMMLR 1033
Cdd:cd18070    222 PF-CDSDWWARVLIRPQGRNkaREPLAALLKELLWR 256
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
727-779 1.10e-10

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 58.74  E-value: 1.10e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093  727 EVDRILDesHSVDKDNGEpviYYLVKWCSLPYEDSTWELKEDVDEGK--IREFKR 779
Cdd:pfam00385    2 EVERILD--HRKDKGGKE---EYLVKWKGYPYDENTWEPEENLSKCPelIEEFKD 51
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
723-770 6.31e-10

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


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 56.89  E-value: 6.31e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907105093  723 PDYVEVDRILDesHSVDKDNGepvIYYLVKWCSLPYEDSTWElKEDVD 770
Cdd:cd18662      1 PEWLQIHRIIN--HRVDKDGN---TWYLVKWRDLPYDQSTWE-SEDDD 42
CHROMO smart00298
Chromatin organization modifier domain;
646-706 1.47e-08

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 52.99  E-value: 1.47e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907105093   646 VDKVLSMRVVKKelpsGQYteaeEFFVKYKNYSYLHCEWATISQLEKDKRihqKLKRFKTK 706
Cdd:smart00298    4 VEKILDHRWKKK----GEL----EYLVKWKGYSYSEDTWEPEENLLNCSK---KLDNYKKK 53
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
645-706 4.70e-07

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 48.34  E-value: 4.70e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  645 IVDKVLSMRVVKKELpsgqyteaEEFFVKYKNYSYLHCEWATISQLEKDKRIhqkLKRFKTK 706
Cdd:pfam00385    2 EVERILDHRKDKGGK--------EEYLVKWKGYPYDENTWEPEENLSKCPEL---IEEFKDR 52
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
727-779 3.50e-06

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


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 45.93  E-value: 3.50e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093  727 EVDRILDesHSVDKDngepVIYYLVKWCSLPYEDSTWELKEDVDEGK--IREFKR 779
Cdd:cd00024      2 EVEKILD--HRVRKG----KLEYLVKWKGYPPEENTWEPEENLTNAPelIKEYEK 50
CHROMO smart00298
Chromatin organization modifier domain;
727-779 2.53e-05

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 43.74  E-value: 2.53e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093   727 EVDRILDesHSVDKDNGEpviYYLVKWCSLPYEDSTWELKEDVDEG--KIREFKR 779
Cdd:smart00298    3 EVEKILD--HRWKKKGEL---EYLVKWKGYSYSEDTWEPEENLLNCskKLDNYKK 52
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
813-981 2.76e-05

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 46.14  E-value: 2.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  813 LREYQLEGV-NWLLFNWYNRQNCILAdeMGLGKTIQSIAFLQEVYNvgihGPFLVIAP-LSTITNWEREFNTWTEMNTIV 890
Cdd:cd17926      1 LRPYQEEALeAWLAHKNNRRGILVLP--TGSGKTLTALALIAYLKE----LRTLIVVPtDALLDQWKERFEDFLGDSSIG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  891 YHGSLASrqmiqqyemycKDSRGRLIpgaykfdaLITTFEMILSDCPELREIEWRC--VIIDEAHRLknrNCKLLDSLKH 968
Cdd:cd17926     75 LIGGGKK-----------KDFDDANV--------VVATYQSLSNLAEEEKDLFDQFglLIVDEAHHL---PAKTFSEILK 132
                          170
                   ....*....|....
gi 1907105093  969 MDLEHKVL-LTGTP 981
Cdd:cd17926    133 ELNAKYRLgLTATP 146
CD1_tandem_CHD3-4_like cd18667
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
669-691 2.84e-05

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and 4, 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 CHD3 and CHD4. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. Human CHD3 (also named Mi-2 alpha) and CHD4 (also named Mi-2 beta) are coexpressed in many cell lines and tissues and may act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). The proteins form distinct CHD3- and CHD4-NuRD complexes that repress, as well as activate gene transcription of overlapping and specific target genes. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349314 [Multi-domain]  Cd Length: 79  Bit Score: 44.25  E-value: 2.84e-05
                           10        20
                   ....*....|....*....|...
gi 1907105093  669 EFFVKYKNYSYLHCEWATISQLE 691
Cdd:cd18667     45 EFFVKWHGMSYWHCEWVSELQLE 67
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
833-980 2.98e-05

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: 46.24  E-value: 2.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  833 NCILADEMGLGKTIqsIAFLQ-EVYNVGIHGPFLVIAPLSTITN-WEREFNTWTEMN--TIVYHGSlasrqmiqqyemyc 908
Cdd:cd00046      3 NVLITAPTGSGKTL--AALLAaLLLLLKKGKKVLVLVPTKALALqTAERLRELFGPGirVAVLVGG-------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  909 KDSRGRLIPGAYKFDALITTFEMILSDCPELREI---EWRCVIIDEAHRL----KNRNCKLLDSLKHMDLEHK-VLLTGT 980
Cdd:cd00046     67 SSAEEREKNKLGDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQvILLSAT 146
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
724-783 3.99e-05

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: 43.42  E-value: 3.99e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  724 DYVEVDRILDeSHSVDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQSR 783
Cdd:cd18664      1 EFHVVERIIA-SQRASLEDGTSQLQYLVKWRRLNYDECTWEDATLIAKLAPEQVDHFQNR 59
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
61-421 6.67e-05

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 48.00  E-value: 6.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   61 SSASDLVP-PPEETAST---------ELPKESTAPapesltlhdytTQPTSQEQPAQPVLQTSTPTAGllqvsKSQEILS 130
Cdd:cd22540     17 STTQDSQPsPLALLAATcskigppavEAAVTPPAP-----------PQPTPRKLVPIKPAPLPLGPGK-----NSIGFLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  131 -QGNPFMGVSATGVSPSNTGGQPSQSAPKIVILKAPPNSSVTGTH---VAQIQAQGITS-TAQPLVAGTANGGKVTFTKV 205
Cdd:cd22540     81 aKGNIIQLQGSQLSSSAPGGQQVFAIQNPTMIIKGSQTRSSTNQQyqiSPQIQAAGQINnSGQIQIIPGTNQAIITPVQV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  206 LTGT-------PLRPGVSIVSGNTVLATKVPGNQaavqrIVQPSRPVKQLVLqPVKGSAPAGNPGA----AGPPLKPAVT 274
Cdd:cd22540    161 LQQPqqahkpvPIKPAPLQTSNTNSASLQVPGNV-----IKLQSGGNVALTL-PVNNLVGTQDGATqlqlAAAPSKPSKK 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  275 LTSTPTQGESKRITlVLQQPQSggpqghrhVVLGSLPGKIVLQGNQLaaLTQAKNAQGQPAkvvtiqlqvqqpqqkiqiv 354
Cdd:cd22540    235 IRKKSAQAAQPAVT-VAEQVET--------VLIETTADNIIQAGNNL--LIVQSPGTGQPA------------------- 284
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907105093  355 pqppssqpqpqpqpppsaqplTLSSVQQAQimgPGQNPG--QRLSVPLKMVlqpqagssQGASSGLSVV 421
Cdd:cd22540    285 ---------------------VLQQVQVLQ---PKQEQQvvQIPQQALRVV--------QAASATLPTV 321
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
727-772 4.36e-04

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: 349322  Cd Length: 49  Bit Score: 39.96  E-value: 4.36e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907105093  727 EVDRILDEshsvDKDNGEpvIYYLVKWCSLPYEDSTWELKEDVDEG 772
Cdd:cd18966      2 EVERILAE----RRDDGG--KRYLVKWEGYPLEEATWEPEENIGDE 41
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1202-1254 6.34e-04

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 40.38  E-value: 6.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907105093 1202 SDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAV 1254
Cdd:cd18785     20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDEGE 72
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
1093-1266 6.57e-04

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: 44.24  E-value: 6.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1093 LRKCC---NHPYLIngaeekilmefreACHIIPQDFHLQAM----VRSAGKLV----LIDKLLPKLKAGGHKVLIFSQMV 1161
Cdd:pfam11496   54 LENLSlvaTHPYLL-------------VDHYMPKSLLLKDEpeklAYTSGKFLvlndLVNLLIERDRKEPINVAIVARSG 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093 1162 RCLDILEDYLIQRRYLYERIDG-RVRGNLRQAAIDRFSKPDSDRFVFL----LCTRAGGLGINlTAADTCIIFDSDWNPQ 1236
Cdd:pfam11496  121 KTLDLVEALLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTCHLLsstgQLTNDDSLLEN-YKFDLIIAFDSSVDTS 199
                          170       180       190
                   ....*....|....*....|....*....|
gi 1907105093 1237 NDLQAQARCHRIGQSKAVKVYRLITRNSYE 1266
Cdd:pfam11496  200 SPSVEHLRTQNRRKGNLAPIIRLVVINSIE 229
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
725-764 1.13e-03

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: 39.21  E-value: 1.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1907105093  725 YVEVDRILDESHSVDKDNGEPviYYLVKWCSLPYEDSTWE 764
Cdd:cd18661      2 YQIVERIIAHSPQKSAASGYP--DYLCKWQGLPYSECTWE 39
PHA03247 PHA03247
large tegument protein UL36; Provisional
68-280 1.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   68 PPPEETASTELPKESTAPAPESLTLHDYTTQPTSQEQPAQPVLQTSTPTAGLLQVSKSQEILSQGNPfMGVSATGVSPSN 147
Cdd:PHA03247  2607 DPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA-AQASSPPQRPRR 2685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  148 TGGQPS-----------------QSAPKIVIlKAPPNSSVTGTHVAQIQAQGITSTAQPLVAGTANGGKVT--FTKVLTG 208
Cdd:PHA03247  2686 RAARPTvgsltsladpppppptpEPAPHALV-SATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPArpARPPTTA 2764
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907105093  209 TPLRPG--VSIVSGNTVLATKVPGNQAAVQRIVQPSRPVKQLVLQPVKGSAPAGNPGAAGPPLKPAVTlTSTPT 280
Cdd:PHA03247  2765 GPPAPAppAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT-SAQPT 2837
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
814-989 1.92e-03

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 41.46  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  814 REYQLEGVNWLLfnwyNRQNCILADEMGLGKT-IQSIAFLQEVYNVGIHGPFLVIAPLSTITN-WEREFNTWTEMNTIVY 891
Cdd:pfam00270    1 TPIQAEAIPAIL----EGRDVLVQAPTGSGKTlAFLLPALEALDKLDNGPQALVLAPTRELAEqIYEELKKLGKGLGLKV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  892 HGSLASRQMIQQYEMYCKdsrgrlipgaykFDALITTFEMILSDCPE---LREIewRCVIIDEAHRL--KNRNCKLLDSL 966
Cdd:pfam00270   77 ASLLGGDSRKEQLEKLKG------------PDILVGTPGRLLDLLQErklLKNL--KLLVLDEAHRLldMGFGPDLEEIL 142
                          170       180
                   ....*....|....*....|....
gi 1907105093  967 KHMDLEHK-VLLTGTPLQNtVEEL 989
Cdd:pfam00270  143 RRLPKKRQiLLLSATLPRN-LEDL 165
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
56-445 2.83e-03

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


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 42.64  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093   56 GDVGNSSASDLVPPPEETASTELPKEST--APAPESLT-----LHDYTTQPTSQEQPAQPvlQTSTP-TAGLLQVSKSQE 127
Cdd:pfam17823   36 GAGKQNASGDAVPRADNKSSEQ*NFCAAtaAPAPVTLTkgtsaAHLNSTEVTAEHTPHGT--DLSEPaTREGAADGAASR 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  128 ILSQGNPFMGVSATGVSPSNTGGQPSQ--SAPKIVILKAP-------PNSSVTGTHVAQ---IQAQGITSTAQPLVAGTA 195
Cdd:pfam17823  114 ALAAAASSSPSSAAQSLPAAIAALPSEafSAPRAAACRANasaapraAIAAASAPHAASpapRTAASSTTAASSTTAASS 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  196 NGGKVTFTKVLTGTPLRPGVSIVSG------NTVLA-----TKVPGNQAAVQRIVQPSrPVKQLV--LQPVKGSAPAGN- 261
Cdd:pfam17823  194 APTTAASSAPATLTPARGISTAATAtghpaaGTALAavgnsSPAAGTVTAAVGTVTPA-ALATLAaaAGTVASAAGTINm 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  262 --PGAAGP-PLK--PAVTLTSTP-------TQGESKRITLvlQQP---QSGGPQGHRHVVLGSLPGKIVLQGNQLAALT- 325
Cdd:pfam17823  273 gdPHARRLsPAKhmPSDTMARNPaapmgaqAQGPIIQVST--DQPvhnTAGEPTPSPSNTTLEPNTPKSVASTNLAVVTt 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  326 ---QAKNAQGQPAKVvtiqlqvqqpqqkiqivpqPPSSQPQPQPQPPPSAQPLTLSSVQQAQimGPGQnpgqrLSVPLKM 402
Cdd:pfam17823  351 tkaQAKEPSASPVPV-------------------LHTSMIPEVEATSPTTQPSPLLPTQGAA--GPGI-----LLAPEQV 404
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1907105093  403 VLQPQAGS-SQGASSGLS-VVKVLSAsevaalsspASCAPHTAGK 445
Cdd:pfam17823  405 ATEATAGTaSAGPTPRSSgDPKTLAM---------ASCQLSTQGQ 440
PTZ00121 PTZ00121
MAEBL; Provisional
449-624 4.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 4.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  449 EENRRLEHQKKQEKANRIVAEAIARARARgEQNIPRVLNEDELPSVRPEEEGEKKRRKKSSGERLKEEKPKKSKTAAASK 528
Cdd:PTZ00121  1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEE-KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907105093  529 TKGKsklntitpvvgKKRKRNTSSDNSDVEVMPAQSPREDEESSIQK----RRSNRQVKRK----KYTEDLDIKITDDEE 600
Cdd:PTZ00121  1696 KEAE-----------EAKKAEELKKKEAEEKKKAEELKKAEEENKIKaeeaKKEAEEDKKKaeeaKKDEEEKKKIAHLKK 1764
                          170       180
                   ....*....|....*....|....*
gi 1907105093  601 EEEVDVTGPIK-PEPILPEPVQEPD 624
Cdd:PTZ00121  1765 EEEKKAEEIRKeKEAVIEEELDEED 1789
CD_CMT3_like cd18635
chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier ...
727-777 6.91e-03

chromodomain of chromomethylase 3, and similar proteins; CHRomatin Organization Modifier (chromo) domain of DNA (cytosine-5)-methyltransferase chromomethylase 3 (CMT3, EC:2.1.1.37), and similar proteins. CMT3 is primarily a CHG (where H is either A, T or C) methyltransferase and is predominantly expressed in actively replicating cells. The protein is involved in preferentially methylating transposon-related sequences, reducing their mobility. Studies suggest that in order to target DNA methylation, CMT3 associates with H3K9me2-containing nucleosomes through binding of its BAH- and chromo-domains to H3K9me2. 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: 349285  Cd Length: 57  Bit Score: 36.91  E-value: 6.91e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907105093  727 EVDRILDESHSVDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVD--EGKIREF 777
Cdd:cd18635      3 EVEKLVGICYGDPKKTGERGLYFKVRWKGYGPEEDTWEPIEGLSncPEKIKEF 55
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
739-777 7.18e-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: 349320  Cd Length: 54  Bit Score: 36.93  E-value: 7.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907105093  739 DKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGK--IREF 777
Cdd:cd18964     12 SARDGPGKFLWLVKWDGYPIEDATWEPPENLGEHAklIEDF 52
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
645-694 8.00e-03

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: 36.98  E-value: 8.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907105093  645 IVDKVLSMRVVKKELPSGQYTEAE--EFFVKYKNYSYLHCEWATISQLEKDK 694
Cdd:cd18665      4 GIDIVLDHRLKEGLEEGELDDPKEnyEFLIKWTDESHLHNTWETYESLKQVR 55
CD_MarY1_POL_like cd18975
chromodomain of Tricholoma matsutake polyprotein, and similar proteins; This subgroup includes ...
727-779 8.50e-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: 36.37  E-value: 8.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907105093  727 EVDRILDESHSVDKdngepvIYYLVKWCSLPYEDSTWELKEDVDEGK-IREFKR 779
Cdd:cd18975      2 EVESILNSRLHRGK------LQYLIQWKGYPLEEASWELEDNIKNPRlIEEFHK 49
CD_POL_like cd18974
chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the ...
727-779 9.30e-03

chromodomain of Penicillium solitum protein PENSOL_c198G03123; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Penicillium solitum protein PENSOL_c198G03123 a putative polyprotein from a Ty3/Gypsy long terminal repeat (LTR) retroelement. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here 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: 349330  Cd Length: 50  Bit Score: 36.30  E-value: 9.30e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907105093  727 EVDRILDESHSVDKdngepvIYYLVKWCSLPYEDSTWELKEDVDEGK--IREFKR 779
Cdd:cd18974      2 EVEEIVDEKMIDDE------LHYLVKWKGWPAEYNQWEPEDDMENAPkaIQSYEK 50
 
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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