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Conserved domains on  [gi|1958806621|ref|XP_038955394|]
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transcriptional regulator ATRX isoform X7 [Rattus norvegicus]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12975182)

DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1499-1742 1.76e-160

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: 494.79  E-value: 1.76e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKL-DFSTALVVCPLNTALNWMNEF 1577
Cdd:cd18068      1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1578 EKWQEGLNDAEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 1656
Cdd:cd18068     81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1657 CDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 1736
Cdd:cd18068    161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240

                   ....*.
gi 1958806621 1737 RVMKKR 1742
Cdd:cd18068    241 RVMKKR 246
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1482-2131 2.99e-85

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 295.60  E-value: 2.99e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1482 EETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTA 1561
Cdd:COG0553    225 RRLREALESLPAGLKATLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PV 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1562 LVVCPLNTALNWMNEFEKWQEGLNdaeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklke 1641
Cdd:COG0553    294 LIVAPTSLVGNWQRELAKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE----------- 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1642 ifnkALVDPGPDFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFIN 1721
Cdd:COG0553    353 ----LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFAR 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1722 PIQNGQcadstmvdvrvmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTAIQCKLYQYYLDHLTGVGNSTD 1801
Cdd:COG0553    429 PIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAE 496
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1802 GGRGKagAKLFQDFQMLSRIWTHPwclqldyiskenkgyfdedsmdefiasdsdetsmslssdeyakkkktkgkkgrkds 1881
Cdd:COG0553    497 GIRRR--GLILAALTRLRQICSHP-------------------------------------------------------- 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1882 sssgsgsdndvevikvwnsrsrgggegnveetgnnpsvSLKLDESKTTStsnpsspapdwykdfvtdadaevlEHSGKMV 1961
Cdd:COG0553    519 --------------------------------------ALLLEEGAELS------------------------GRSAKLE 536
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1962 LLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTNAQSRKKWAEE 2041
Cdd:COG0553    537 ALLELLEELLAEGEKVLVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDR 594
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 2042 FNDETNVrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVT 2121
Cdd:COG0553    595 FQEGPEA--PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEE 672
                          650
                   ....*....|
gi 1958806621 2122 KQSLSFRVVD 2131
Cdd:COG0553    673 KRALAESVLG 682
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
127-230 6.45e-57

ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a PHD-like zinc finger domain of ATRX, which belongs to the SNF2 family of chromatin remodeling proteins. ATRX is a large chromatin-associated nuclear protein with two domains, ADDz_ATRX at the N-terminus, followed by a C-terminal ATPase/helicase domain. The ADDz_ATRX domain recognizes a specific methylated histone, and this interaction is required for heterochromatin localization of the ATRX protein. Missense mutations in either of the two ATRX domains lead to the X-linked alpha-thalassemia and mental retardation syndrome; however the mutations in the ADDz_ATRX domain produce a more severe disease phenotype that may also relate to disturbing unknown functions or interaction sites of this domain. The ADDz domain is also present in chromatin-associated proteins cytosine-5-methyltransferase 3 (Dnmt3); it is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


:

Pssm-ID: 277252 [Multi-domain]  Cd Length: 102  Bit Score: 192.52  E-value: 6.45e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  127 GIVSCTACGQQVNHFqKDSIYRHPSLKVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILR 206
Cdd:cd11726      1 RRVRCTACGEQLNHF-SKEVHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICCDFCPNVFCKKCIKR 79
                           90       100
                   ....*....|....*....|....
gi 1958806621  207 NLGRKELStIMDENNQWYCYICQP 230
Cdd:cd11726     80 NLGRAELS-RIEESDKWKCFVCDP 102
 
Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1499-1742 1.76e-160

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: 494.79  E-value: 1.76e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKL-DFSTALVVCPLNTALNWMNEF 1577
Cdd:cd18068      1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1578 EKWQEGLNDAEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 1656
Cdd:cd18068     81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1657 CDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 1736
Cdd:cd18068    161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240

                   ....*.
gi 1958806621 1737 RVMKKR 1742
Cdd:cd18068    241 RVMKKR 246
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1502-1828 2.35e-106

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: 341.97  E-value: 2.35e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1502 HQVDGVQFMWDCCCEsvkktkksPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQ 1581
Cdd:pfam00176    1 YQIEGVNWMLSLENN--------LGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1582 EglndAEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGH 1661
Cdd:pfam00176   73 S----PPALRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLR-----------KHKELLKKV----HWHRIVLDEGH 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1662 ILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvrvMKK 1741
Cdd:pfam00176  134 RLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKK 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1742 RAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTAIQCKLYQ-YYLDHLTGVGNSTDGGRGKAgAKLFQDFQMLSR 1820
Cdd:pfam00176  203 GVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIK-ASLLNILMRLRK 281

                   ....*...
gi 1958806621 1821 IWTHPWCL 1828
Cdd:pfam00176  282 ICNHPGLI 289
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1482-2131 2.99e-85

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 295.60  E-value: 2.99e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1482 EETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTA 1561
Cdd:COG0553    225 RRLREALESLPAGLKATLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PV 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1562 LVVCPLNTALNWMNEFEKWQEGLNdaeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklke 1641
Cdd:COG0553    294 LIVAPTSLVGNWQRELAKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE----------- 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1642 ifnkALVDPGPDFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFIN 1721
Cdd:COG0553    353 ----LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFAR 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1722 PIQNGQcadstmvdvrvmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTAIQCKLYQYYLDHLTGVGNSTD 1801
Cdd:COG0553    429 PIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAE 496
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1802 GGRGKagAKLFQDFQMLSRIWTHPwclqldyiskenkgyfdedsmdefiasdsdetsmslssdeyakkkktkgkkgrkds 1881
Cdd:COG0553    497 GIRRR--GLILAALTRLRQICSHP-------------------------------------------------------- 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1882 sssgsgsdndvevikvwnsrsrgggegnveetgnnpsvSLKLDESKTTStsnpsspapdwykdfvtdadaevlEHSGKMV 1961
Cdd:COG0553    519 --------------------------------------ALLLEEGAELS------------------------GRSAKLE 536
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1962 LLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTNAQSRKKWAEE 2041
Cdd:COG0553    537 ALLELLEELLAEGEKVLVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDR 594
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 2042 FNDETNVrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVT 2121
Cdd:COG0553    595 FQEGPEA--PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEE 672
                          650
                   ....*....|
gi 1958806621 2122 KQSLSFRVVD 2131
Cdd:COG0553    673 KRALAESVLG 682
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
127-230 6.45e-57

ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a PHD-like zinc finger domain of ATRX, which belongs to the SNF2 family of chromatin remodeling proteins. ATRX is a large chromatin-associated nuclear protein with two domains, ADDz_ATRX at the N-terminus, followed by a C-terminal ATPase/helicase domain. The ADDz_ATRX domain recognizes a specific methylated histone, and this interaction is required for heterochromatin localization of the ATRX protein. Missense mutations in either of the two ATRX domains lead to the X-linked alpha-thalassemia and mental retardation syndrome; however the mutations in the ADDz_ATRX domain produce a more severe disease phenotype that may also relate to disturbing unknown functions or interaction sites of this domain. The ADDz domain is also present in chromatin-associated proteins cytosine-5-methyltransferase 3 (Dnmt3); it is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


Pssm-ID: 277252 [Multi-domain]  Cd Length: 102  Bit Score: 192.52  E-value: 6.45e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  127 GIVSCTACGQQVNHFqKDSIYRHPSLKVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILR 206
Cdd:cd11726      1 RRVRCTACGEQLNHF-SKEVHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICCDFCPNVFCKKCIKR 79
                           90       100
                   ....*....|....*....|....
gi 1958806621  207 NLGRKELStIMDENNQWYCYICQP 230
Cdd:cd11726     80 NLGRAELS-RIEESDKWKCFVCDP 102
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1956-2106 2.02e-51

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: 178.05  E-value: 2.02e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1956 HSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELasrektedkdkpliykgegkwlRNIDYYRLDGSTNAQSR 2035
Cdd:cd18793      9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRE----------------------RGIKYLRLDGSTSSKER 66
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958806621 2036 KKWAEEFNDETNVRgrLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFL 2106
Cdd:cd18793     67 QKLVDRFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1530-2143 8.53e-41

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 165.74  E-value: 8.53e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1530 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWqeglndaekleVSELATVK---RPQERSY 1606
Cdd:PLN03142   192 ILADEMGLGKTLQTISLLGYLHEYRGIT-GPHMVVAPKSTLGNWMNEIRRF-----------CPVLRAVKfhgNPEERAH 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1607 MLQRWQEDGG--VMIIGYEMyrnlaqgrnvksrKLKEifNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIKSRRRII 1684
Cdd:PLN03142   260 QREELLVAGKfdVCVTSFEM-------------AIKE--KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLL 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1685 LTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdVRVMKKrahiLYEMLAGCVQRKDYTALTK 1764
Cdd:PLN03142   325 ITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ--------QEVVQQ----LHKVLRPFLLRRLKSDVEK 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1765 FLPPKHEYVLAVRMTAIQCKLYQYYLDHLTGVGNStdggrGKAGAKLFQDFQMLSRIWTHPWCLQldyiskenkgyfded 1844
Cdd:PLN03142   393 GLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNA-----GGERKRLLNIAMQLRKCCNHPYLFQ--------------- 452
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1845 smdefiasdsdetsmslssdeyakkkktkgkkgrkdssssgsgsdndvevikvwnsrsrgGGEgnveetgnnpsvslkld 1924
Cdd:PLN03142   453 ------------------------------------------------------------GAE----------------- 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1925 eskttstsnpssPAPDWYkdfvtdADAEVLEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLelasrekted 2004
Cdd:PLN03142   456 ------------PGPPYT------TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYL---------- 507
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 2005 kdkplIYKGEGkwlrnidYYRLDGSTNAQSRKKWAEEFNDEtNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYD 2084
Cdd:PLN03142   508 -----MYRGYQ-------YCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVD 574
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958806621 2085 IQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMNE 2143
Cdd:PLN03142   575 LQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNK 633
ADD_ATRX pfam17981
Cysteine Rich ADD domain; This is a cysteine-rich domain termed ADD (ATRX-DNMT3-DNMT3L, ...
118-173 9.84e-28

Cysteine Rich ADD domain; This is a cysteine-rich domain termed ADD (ATRX-DNMT3-DNMT3L, AD-DATRX) found in ATRX proteins. Chromatin-associated human protein ATRX was originally identified because mutations in the ATRX gene cause a severe form of syndromal X-linked mental retardation called ATR-X syndrome. Mutations or knockdown of ATRX expression cause diverse effects, including altered patterns of DNA methylation, a telomere-dysfunction phenotype, aberrant chromosome segregation, premature sister chromatid separation and changes in gene expression. ATRX localizes predominantly to large, tandemly repeated regions (such as telomeres, centromeres and ribosomal DNA) associated with heterochromatin, and studies show that it directs H3.3 deposition to pericentric and telomeric heterochromatin. The ADD domain of ATRX, in which most syndrome-causing mutations occur, engages the N-terminal tail of histone H3 through two rigidly oriented binding pockets, one for unmodified Lys4 and the other for di- or trimethylated Lys9. Mutations in the ATRX ADD domain cause mislocalization of ATRX protein to heterochromatin, and this may contribute to understanding the underlying etiology of ATRX syndrome. Structure analysis of the ADD domain of ATRX revealed that it contains a PHD zinc-finger domain packed against a GATA-like zinc finger. Same structure is also found in the DNMT3 DNA methyltransferases and DNMT3L.


Pssm-ID: 465604  Cd Length: 56  Bit Score: 107.52  E-value: 9.84e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806621  118 KKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLKVLICKNCFKYYMSDDISRDS 173
Cdd:pfam17981    1 KRRGDAELSSIVNCTACGQQVNHFQRDSIYQHPVLKVLICKSCFKYYMSDDISKDE 56
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1958-2095 8.06e-18

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: 81.10  E-value: 8.06e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1958 GKMVLLFEILRmaEEIGDKVLVFSQSLISLDliEDFLelasrektedkdkpliykgegKWLRNIDYYRLDGSTNAQSRKK 2037
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE--AELL---------------------LEKEGIKVARLHGDLSQEEREE 55
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806621 2038 WAEEFNDETnvrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 2095
Cdd:pfam00271   56 ILEDFRKGK----IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
2019-2095 4.14e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 78.02  E-value: 4.14e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806621  2019 RNIDYYRLDGSTNAQSRKKWAEEFNDETNVrgrlFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 2095
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
1497-1692 5.42e-16

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 78.69  E-value: 5.42e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  1497 IKLKPHQVDGVQFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKldFSTALVVCPL-NTALNWMN 1575
Cdd:smart00487    7 EPLRPYQKEAIEALLSG------------LRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTrELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  1576 EFEKWQEGLNDAEKLEVSELATVKRpqersymLQRWQEDGGVMIIG-YEMYrnlaqgrnvksrkLKEIFNKALVDPGPDF 1654
Cdd:smart00487   73 ELKKLGPSLGLKVVGLYGGDSKREQ-------LRKLESGKTDILVTtPGRL-------------LDLLENDKLSLSNVDL 132
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 1958806621  1655 VVCDEGHILKNE--ASAVSKAMNSI-KSRRRIILTGTPLQN 1692
Cdd:smart00487  133 VILDEAHRLLDGgfGDQLEKLLKLLpKNVQLLLLSATPPEE 173
 
Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1499-1742 1.76e-160

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: 494.79  E-value: 1.76e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKL-DFSTALVVCPLNTALNWMNEF 1577
Cdd:cd18068      1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1578 EKWQEGLNDAEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 1656
Cdd:cd18068     81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1657 CDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 1736
Cdd:cd18068    161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240

                   ....*.
gi 1958806621 1737 RVMKKR 1742
Cdd:cd18068    241 RVMKKR 246
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
1499-1742 2.10e-115

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: 365.85  E-value: 2.10e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCCESvkKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKlDFSTALVVCPLNTALNWMNEFE 1578
Cdd:cd18007      1 LKPHQVEGVRFLWSNLVGT--DVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAP-RRSRPLVLCPASTLYNWEDEFK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1579 KWQEGLNDAEKLEVSeLATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNvKSRKLKEIFNKALVDPGPDFVVCD 1658
Cdd:cd18007     78 KWLPPDLRPLLVLVS-LSASKRADARLRKINKWHKEGGVLLIGYELFRNLASNAT-TDPRLKQEFIAALLDPGPDLLVLD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1659 EGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDVRV 1738
Cdd:cd18007    156 EGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRL 235

                   ....
gi 1958806621 1739 MKKR 1742
Cdd:cd18007    236 MLKR 239
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1502-1828 2.35e-106

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: 341.97  E-value: 2.35e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1502 HQVDGVQFMWDCCCEsvkktkksPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQ 1581
Cdd:pfam00176    1 YQIEGVNWMLSLENN--------LGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1582 EglndAEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGH 1661
Cdd:pfam00176   73 S----PPALRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLR-----------KHKELLKKV----HWHRIVLDEGH 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1662 ILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvrvMKK 1741
Cdd:pfam00176  134 RLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKK 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1742 RAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTAIQCKLYQ-YYLDHLTGVGNSTDGGRGKAgAKLFQDFQMLSR 1820
Cdd:pfam00176  203 GVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIK-ASLLNILMRLRK 281

                   ....*...
gi 1958806621 1821 IWTHPWCL 1828
Cdd:pfam00176  282 ICNHPGLI 289
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1482-2131 2.99e-85

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 295.60  E-value: 2.99e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1482 EETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTA 1561
Cdd:COG0553    225 RRLREALESLPAGLKATLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PV 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1562 LVVCPLNTALNWMNEFEKWQEGLNdaeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklke 1641
Cdd:COG0553    294 LIVAPTSLVGNWQRELAKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE----------- 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1642 ifnkALVDPGPDFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFIN 1721
Cdd:COG0553    353 ----LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFAR 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1722 PIQNGQcadstmvdvrvmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTAIQCKLYQYYLDHLTGVGNSTD 1801
Cdd:COG0553    429 PIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAE 496
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1802 GGRGKagAKLFQDFQMLSRIWTHPwclqldyiskenkgyfdedsmdefiasdsdetsmslssdeyakkkktkgkkgrkds 1881
Cdd:COG0553    497 GIRRR--GLILAALTRLRQICSHP-------------------------------------------------------- 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1882 sssgsgsdndvevikvwnsrsrgggegnveetgnnpsvSLKLDESKTTStsnpsspapdwykdfvtdadaevlEHSGKMV 1961
Cdd:COG0553    519 --------------------------------------ALLLEEGAELS------------------------GRSAKLE 536
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1962 LLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTNAQSRKKWAEE 2041
Cdd:COG0553    537 ALLELLEELLAEGEKVLVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDR 594
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 2042 FNDETNVrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVT 2121
Cdd:COG0553    595 FQEGPEA--PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEE 672
                          650
                   ....*....|
gi 1958806621 2122 KQSLSFRVVD 2131
Cdd:COG0553    673 KRALAESVLG 682
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
1499-1742 1.78e-84

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: 276.70  E-value: 1.78e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLdfSTALVVCPLNTALNWMNEFE 1578
Cdd:cd18069      1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGA--KTVLAIVPVNTLQNWLSEFN 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1579 KW-----QEGLNDAEKLEVSELATVKRP-QERSYMLQRWQEDGGVMIIGYEMYRNlaqgrnvksrklkeifnkalvDPGP 1652
Cdd:cd18069     79 KWlpppeALPNVRPRPFKVFILNDEHKTtAARAKVIEDWVKDGGVLLMGYEMFRL---------------------RPGP 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1653 DFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADST 1732
Cdd:cd18069    138 DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDST 217
                          250
                   ....*....|
gi 1958806621 1733 MVDVRVMKKR 1742
Cdd:cd18069    218 PQDVKLMRYR 227
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
1499-1757 8.30e-62

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: 212.15  E-value: 8.30e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCccesVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVL---LCDKLDFSTALVVCPLNTALNWMN 1575
Cdd:cd18004      1 LRPHQREGVQFLYDC----LTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLkqgPYGKPTAKKALIVCPSSLVGNWKA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1576 EFEKWqegLNDaEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSRklkeifnkalvdpgPDFV 1655
Cdd:cd18004     77 EFDKW---LGL-RRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKIS--------------IDLL 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1656 VCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVD 1735
Cdd:cd18004    139 ICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEED 218
                          250       260
                   ....*....|....*....|..
gi 1958806621 1736 VRVMKKRAHILYEMLAGCVQRK 1757
Cdd:cd18004    219 KELGAERSQELSELTSRFILRR 240
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
1499-1704 1.85e-59

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: 202.80  E-value: 1.85e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCCesvkktkksPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMNEFE 1578
Cdd:cd17919      1 LRPYQLEGLNFLLELYE---------NGPGGILADEMGLGKTLQAIAFLAY-LLKEGKERGPVLVVCPLSVLENWEREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1579 KWQEGLNdaeklevseLATVKRPQERSYMLQ--RWQEDGGVMIIGYEMYRNLAQgrnvksrklkeifnkALVDPGPDFVV 1656
Cdd:cd17919     71 KWTPDLR---------VVVYHGSQRERAQIRakEKLDKFDVVLTTYETLRRDKA---------------SLRKFRWDLVV 126
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958806621 1657 CDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFI 1704
Cdd:cd17919    127 VDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFL 174
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
127-230 6.45e-57

ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a PHD-like zinc finger domain of ATRX, which belongs to the SNF2 family of chromatin remodeling proteins. ATRX is a large chromatin-associated nuclear protein with two domains, ADDz_ATRX at the N-terminus, followed by a C-terminal ATPase/helicase domain. The ADDz_ATRX domain recognizes a specific methylated histone, and this interaction is required for heterochromatin localization of the ATRX protein. Missense mutations in either of the two ATRX domains lead to the X-linked alpha-thalassemia and mental retardation syndrome; however the mutations in the ADDz_ATRX domain produce a more severe disease phenotype that may also relate to disturbing unknown functions or interaction sites of this domain. The ADDz domain is also present in chromatin-associated proteins cytosine-5-methyltransferase 3 (Dnmt3); it is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


Pssm-ID: 277252 [Multi-domain]  Cd Length: 102  Bit Score: 192.52  E-value: 6.45e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  127 GIVSCTACGQQVNHFqKDSIYRHPSLKVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILR 206
Cdd:cd11726      1 RRVRCTACGEQLNHF-SKEVHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICCDFCPNVFCKKCIKR 79
                           90       100
                   ....*....|....*....|....
gi 1958806621  207 NLGRKELStIMDENNQWYCYICQP 230
Cdd:cd11726     80 NLGRAELS-RIEESDKWKCFVCDP 102
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1956-2106 2.02e-51

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: 178.05  E-value: 2.02e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1956 HSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELasrektedkdkpliykgegkwlRNIDYYRLDGSTNAQSR 2035
Cdd:cd18793      9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRE----------------------RGIKYLRLDGSTSSKER 66
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958806621 2036 KKWAEEFNDETNVRgrLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFL 2106
Cdd:cd18793     67 QKLVDRFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
ADDz cd11672
ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz); The ADDz zinc finger domain is ...
127-230 2.35e-51

ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz); The ADDz zinc finger domain is present in the chromatin-associated proteins cytosine-5-methyltransferase 3 (Dnmt3) and ATRX, a SNF2 type transcription factor protein. The Dnmt3 family includes two active DNA methyltransferases, Dnmt3a and -3b, and one regulatory factor Dnmt3l. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The ADDz domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


Pssm-ID: 277250 [Multi-domain]  Cd Length: 99  Bit Score: 176.60  E-value: 2.35e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  127 GIVSCTACGQQVnhfqkdSIYRHPSLKVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCD--FCHNAFCKKCI 204
Cdd:cd11672      1 IEDICIACGSLV------VIYRHPLFQGGICKNCKKYFLSDDISYDDDGYQSYCRICCEGGNLLCCGnnFCHRCFCKECV 74
                           90       100
                   ....*....|....*....|....*.
gi 1958806621  205 LRNLGRKELSTiMDENNQWYCYICQP 230
Cdd:cd11672     75 DRLVGPGELST-MDENNQWYCYICHP 99
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
1499-1757 7.62e-47

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: 169.19  E-value: 7.62e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCcesvkKTKKSPGS-GCILAHCMGLGKTLQVVSFLHTVL----LCdKLDFSTALVVCPLNTALNW 1573
Cdd:cd18067      1 LRPHQREGVKFLYRCV-----TGRRIRGShGCIMADEMGLGKTLQCITLMWTLLrqspQC-KPEIDKAIVVSPSSLVKNW 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1574 MNEFEKWQEGlndaeklEVSELATV-KRPQERSYMLQRWQEDGG------VMIIGYEMYRNLAqgrnvksrklkEIFNKA 1646
Cdd:cd18067     75 ANELGKWLGG-------RLQPLAIDgGSKKEIDRKLVQWASQQGrrvstpVLIISYETFRLHV-----------EVLQKG 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1647 LVDpgpdFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNG 1726
Cdd:cd18067    137 EVG----LVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKG 212
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1958806621 1727 QCADSTMVDVRVMKKRAHILYEMLAGCVQRK 1757
Cdd:cd18067    213 RDADASEKERQLGEEKLQELISIVNRCIIRR 243
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
1499-1732 1.45e-44

DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint helicase (ERCC6L, also known as RAD26L) is an essential component of the mitotic spindle assembly checkpoint, by acting as a tension sensor that associates with catenated DNA which is stretched under tension until it is resolved during anaphase. ERCC6L is proposed to stimulate cancer cell proliferation by promoting cell cycle through a way of RAB31-MAPK-CDK2. ERCC6L is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350759 [Multi-domain]  Cd Length: 232  Bit Score: 162.16  E-value: 1.45e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWdcccesvkkTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTALVVCPLNTALNWMNEFE 1578
Cdd:cd18001      1 LYPHQREGVAWLW---------SLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIK--SVLVVMPTSLIPHWVKEFA 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1579 KWQEGLNdaekleVSELATVkRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEIFNKALVdpgPDFVVCD 1658
Cdd:cd18001     70 KWTPGLR------VKVFHGT-SKKERERNLERIQRGGGVLLTTYGMVLSNTE-------QLSADDHDEFK---WDYVILD 132
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806621 1659 EGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFI-KENLLGSIKEFRNRFINPIQNGQCADST 1732
Cdd:cd18001    133 EGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFAcNGSLLGTRKTFKMEFENPITRGRDKDAT 207
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
1499-1742 8.57e-42

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: 154.84  E-value: 8.57e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVL----------------LCDKLDFS--- 1559
Cdd:cd18005      1 LRDYQREGVEFMYDLYKN---------GRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrprfKKKPPASSakk 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1560 TALVVCPLNTALNWMNEFEKWQEglndaekLEVSELATVKRPQERSYMLQRWQEDggVMIIGYEMYRNLAQGrnvksrkL 1639
Cdd:cd18005     72 PVLIVAPLSVLYNWKDELDTWGH-------FEVGVYHGSRKDDELEGRLKAGRLE--VVVTTYDTLRRCIDS-------L 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1640 KEIfnkalvdpGPDFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1719
Cdd:cd18005    136 NSI--------NWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHF 207
                          250       260
                   ....*....|....*....|...
gi 1958806621 1720 INPIQNGQCADSTMVDVRVMKKR 1742
Cdd:cd18005    208 SEPIKRGQRHTATARELRLGRKR 230
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1530-2143 8.53e-41

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 165.74  E-value: 8.53e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1530 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWqeglndaekleVSELATVK---RPQERSY 1606
Cdd:PLN03142   192 ILADEMGLGKTLQTISLLGYLHEYRGIT-GPHMVVAPKSTLGNWMNEIRRF-----------CPVLRAVKfhgNPEERAH 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1607 MLQRWQEDGG--VMIIGYEMyrnlaqgrnvksrKLKEifNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIKSRRRII 1684
Cdd:PLN03142   260 QREELLVAGKfdVCVTSFEM-------------AIKE--KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLL 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1685 LTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdVRVMKKrahiLYEMLAGCVQRKDYTALTK 1764
Cdd:PLN03142   325 ITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ--------QEVVQQ----LHKVLRPFLLRRLKSDVEK 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1765 FLPPKHEYVLAVRMTAIQCKLYQYYLDHLTGVGNStdggrGKAGAKLFQDFQMLSRIWTHPWCLQldyiskenkgyfded 1844
Cdd:PLN03142   393 GLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNA-----GGERKRLLNIAMQLRKCCNHPYLFQ--------------- 452
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1845 smdefiasdsdetsmslssdeyakkkktkgkkgrkdssssgsgsdndvevikvwnsrsrgGGEgnveetgnnpsvslkld 1924
Cdd:PLN03142   453 ------------------------------------------------------------GAE----------------- 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1925 eskttstsnpssPAPDWYkdfvtdADAEVLEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLelasrekted 2004
Cdd:PLN03142   456 ------------PGPPYT------TGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYL---------- 507
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 2005 kdkplIYKGEGkwlrnidYYRLDGSTNAQSRKKWAEEFNDEtNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYD 2084
Cdd:PLN03142   508 -----MYRGYQ-------YCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVD 574
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958806621 2085 IQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMNE 2143
Cdd:PLN03142   575 LQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNK 633
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
1499-1757 3.07e-37

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: 141.14  E-value: 3.07e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCccesVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLD-----FSTALVVCPLNTALNW 1573
Cdd:cd18066      1 LRPHQREGIEFLYEC----VMGMRVNERFGAILADEMGLGKTLQCISLIWT-LLRQGPYggkpvIKRALIVTPGSLVKNW 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1574 MNEFEKWQeglnDAEKLEVSELATVKRPQE--RSYMLQrwqedggVMIIGYEMY-RNLAQGRNVKSrklkeifnkalvdp 1650
Cdd:cd18066     76 KKEFQKWL----GSERIKVFTVDQDHKVEEfiASPLYS-------VLIISYEMLlRSLDQISKLNF-------------- 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1651 gpDFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCAD 1730
Cdd:cd18066    131 --DLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPT 208
                          250       260
                   ....*....|....*....|....*..
gi 1958806621 1731 STMVDVRVMKKRAHILYEMLAGCVQRK 1757
Cdd:cd18066    209 ATPEEKKLGEARAAELTRLTGLFILRR 235
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
1499-1731 1.36e-32

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: 127.30  E-value: 1.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGV---QFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTALVVCPLNTALNWMN 1575
Cdd:cd18012      5 LRPYQKEGFnwlSFLRHY------------GLGGILADDMGLGKTLQTLALLLSRKEEGRKG--PSLVVAPTSLIYNWEE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1576 EFEKWQEGLNdaeklevselATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEI-FNkalvdpgpdF 1654
Cdd:cd18012     71 EAAKFAPELK----------VLVIHGTKRKREKLRALEDYDLVITSYGLLRRDIE-------LLKEVkFH---------Y 124
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806621 1655 VVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADS 1731
Cdd:cd18012    125 LVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEA 201
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
1499-1705 4.04e-31

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: 122.05  E-value: 4.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCCESVkktkkspgsGCILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEFE 1578
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRV---------GGILGDEMGLGKTIQIIAFL-AALHHSKLGLGPSLIVCPATVLKQWVKEFH 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1579 KWqeglndAEKLEVSEL----ATVKRPQERSYMLQRWQ------EDGGVMIIGYEMYRnlaqgrnvksrklkeIFNKALV 1648
Cdd:cd18000     71 RW------WPPFRVVVLhssgSGTGSEEKLGSIERKSQlirkvvGDGGILITTYEGFR---------------KHKDLLL 129
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806621 1649 DPGPDFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIK 1705
Cdd:cd18000    130 NHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVF 186
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
1498-1719 4.40e-28

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: 114.79  E-value: 4.40e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1498 KLKPHQVDGVQFMwdcccesvkKTKKSPGSGCILAHCMGLGKTLQVVSFLhtVLLCDKLDFSTALVVCPLNTALNWMNEF 1577
Cdd:cd18009      3 VMRPYQLEGMEWL---------RMLWENGINGILADEMGLGKTIQTIALL--AHLRERGVWGPFLVIAPLSTLPNWVNEF 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1578 EKWQEGLN----DAEKLEVSELATVKRPQERSYMlqrwqeDGGVMIIGYEMYRNLAqgrnvksrklkeifnKALVDPGPD 1653
Cdd:cd18009     72 ARFTPSVPvllyHGTKEERERLRKKIMKREGTLQ------DFPVVVTSYEIAMRDR---------------KALQHYAWK 130
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806621 1654 FVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1719
Cdd:cd18009    131 YLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWF 196
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1499-1723 6.88e-28

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: 114.37  E-value: 6.88e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWdcccesvkKTKKSPGSGcILAHCMGLGKTLQVVSFLHTVLLCDKLDFST----ALVVCPLNTALNWM 1574
Cdd:cd17999      1 LRPYQQEGINWLA--------FLNKYNLHG-ILCDDMGLGKTLQTLCILASDHHKRANSFNSenlpSLVVCPPTLVGHWV 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1575 NEFEKW--QEGLNdaeklevsELATVKRPQERSyMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEI-FNkalvdpg 1651
Cdd:cd17999     72 AEIKKYfpNAFLK--------PLAYVGPPQERR-RLREQGEKHNVIVASYDVLRNDIE-------VLTKIeWN------- 128
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806621 1652 pdFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI 1723
Cdd:cd17999    129 --YCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPI 198
ADD_ATRX pfam17981
Cysteine Rich ADD domain; This is a cysteine-rich domain termed ADD (ATRX-DNMT3-DNMT3L, ...
118-173 9.84e-28

Cysteine Rich ADD domain; This is a cysteine-rich domain termed ADD (ATRX-DNMT3-DNMT3L, AD-DATRX) found in ATRX proteins. Chromatin-associated human protein ATRX was originally identified because mutations in the ATRX gene cause a severe form of syndromal X-linked mental retardation called ATR-X syndrome. Mutations or knockdown of ATRX expression cause diverse effects, including altered patterns of DNA methylation, a telomere-dysfunction phenotype, aberrant chromosome segregation, premature sister chromatid separation and changes in gene expression. ATRX localizes predominantly to large, tandemly repeated regions (such as telomeres, centromeres and ribosomal DNA) associated with heterochromatin, and studies show that it directs H3.3 deposition to pericentric and telomeric heterochromatin. The ADD domain of ATRX, in which most syndrome-causing mutations occur, engages the N-terminal tail of histone H3 through two rigidly oriented binding pockets, one for unmodified Lys4 and the other for di- or trimethylated Lys9. Mutations in the ATRX ADD domain cause mislocalization of ATRX protein to heterochromatin, and this may contribute to understanding the underlying etiology of ATRX syndrome. Structure analysis of the ADD domain of ATRX revealed that it contains a PHD zinc-finger domain packed against a GATA-like zinc finger. Same structure is also found in the DNMT3 DNA methyltransferases and DNMT3L.


Pssm-ID: 465604  Cd Length: 56  Bit Score: 107.52  E-value: 9.84e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958806621  118 KKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLKVLICKNCFKYYMSDDISRDS 173
Cdd:pfam17981    1 KRRGDAELSSIVNCTACGQQVNHFQRDSIYQHPVLKVLICKSCFKYYMSDDISKDE 56
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
1499-1719 1.30e-27

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: 113.11  E-value: 1.30e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFE 1578
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYN---------RRNCILADEMGLGKTIQSIAFLEHLYQVEGIR-GPFLVIAPLSTIPNWQREFE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1579 KWQEgLNdaeklevselATVKRPQERSYMlqrwqedggvMIIGYEMYRNLAQGRnVKSRKLK--------EIFNK---AL 1647
Cdd:cd17995     71 TWTD-MN----------VVVYHGSGESRQ----------IIQQYEMYFKDAQGR-KKKGVYKfdvlittyEMVIAdaeEL 128
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806621 1648 VDPGPDFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1719
Cdd:cd17995    129 RKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
1498-1725 7.35e-26

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: 108.23  E-value: 7.35e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1498 KLKPHQVDGVQFMWdccceSVKKTKKSPgsgcILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEF 1577
Cdd:cd17996      3 TLKEYQLKGLQWMV-----SLYNNNLNG----ILADEMGLGKTIQTISLI-TYLMEKKKNNGPYLVIVPLSTLSNWVSEF 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1578 EKWQEglndaeklEVSELATVKRPQERSyMLQRWQEDG--GVMIIGYEMYrnlaqgrnVKSR-KLKEIFNKalvdpgpdF 1654
Cdd:cd17996     73 EKWAP--------SVSKIVYKGTPDVRK-KLQSQIRAGkfNVLLTTYEYI--------IKDKpLLSKIKWK--------Y 127
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806621 1655 VVCDEGHILKNEASAVSKAMNS-IKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQN 1725
Cdd:cd17996    128 MIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFAN 199
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
1499-1704 7.52e-25

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: 104.00  E-value: 7.52e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMwdcccESVKKTKKSpgsgCILAHCMGLGKTLQVVSFLhtVLLCDKLDFSTALVVCPLNTALNWMNEFE 1578
Cdd:cd17998      1 LKDYQLIGLNWL-----NLLYQKKLS----GILADEMGLGKTIQVIAFL--AYLKEIGIPGPHLVVVPSSTLDNWLREFK 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1579 KWQEGLndaeKLEVSELATVKRPQERsYMLQRWQEDGGVMIIGYemyrNLAQGrNVKSRKLKEIFNKalvdpgpDFVVCD 1658
Cdd:cd17998     70 RWCPSL----KVEPYYGSQEERKHLR-YDILKGLEDFDVIVTTY----NLATS-NPDDRSFFKRLKL-------NYVVYD 132
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1958806621 1659 EGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFI 1704
Cdd:cd17998    133 EGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFI 178
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
1498-1715 6.48e-24

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: 102.43  E-value: 6.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1498 KLKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEF 1577
Cdd:cd17993      1 ELRDYQLTGLNWLAHSWCK---------GNNGILADEMGLGKTVQTISFL-SYLFHSQQQYGPFLVVVPLSTMPAWQREF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1578 EKWQEGLNdaeklEVSELATVKRPQersymlqrwqedggvMIIGYEMYRNlaqgrnvKSRKLK--------EIFNKALVD 1649
Cdd:cd17993     71 AKWAPDMN-----VIVYLGDIKSRD---------------TIREYEFYFS-------QTKKLKfnvllttyEIILKDKAF 123
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958806621 1650 PGP---DFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEF 1715
Cdd:cd17993    124 LGSikwQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF 192
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
1530-1715 6.80e-24

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: 102.40  E-value: 6.80e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1530 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLNdAEKLEVSElatvkrpQERSYMLQ 1609
Cdd:cd17997     26 ILADEMGLGKTLQTISLLGYLKHYKNIN-GPHLIIVPKSTLDNWMREFKRWCPSLR-VVVLIGDK-------EERADIIR 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1610 RWQEDG--GVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTG 1687
Cdd:cd17997     97 DVLLPGkfDVCITSYEMVI-----------KEKTVLKKF----NWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161
                          170       180
                   ....*....|....*....|....*...
gi 1958806621 1688 TPLQNNLIEYHCMVNFIKENLLGSIKEF 1715
Cdd:cd17997    162 TPLQNNLHELWALLNFLLPDVFTSSEDF 189
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
1530-1723 9.36e-24

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: 102.05  E-value: 9.36e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1530 ILAHCMGLGKTLQVVSFL-HtvLLCDKLDFSTALVVCPLNTALNWMNEFEKWQEGLndaeKLevseLATVKRPQERSYML 1608
Cdd:cd18003     23 ILADEMGLGKTIQTIALLaH--LACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGF----KI----LTYYGSAKERKLKR 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1609 QRWQEDGG--VMIIGYEMyrnLAQGRNV-KSRKLKeifnkalvdpgpdFVVCDEGHILKNEASAVSKAMNSIKSRRRIIL 1685
Cdd:cd18003     93 QGWMKPNSfhVCITSYQL---VVQDHQVfKRKKWK-------------YLILDEAHNIKNFKSQRWQTLLNFNTQRRLLL 156
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958806621 1686 TGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI 1723
Cdd:cd18003    157 TGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL 194
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
1499-1727 1.13e-21

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: 96.59  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMwdCCCesvkktkkspgsGCILAHCMGLGKTLQVVSFLHTVLLCD---------------KLDFSTA-L 1562
Cdd:cd18008      1 LLPYQKQGLAWM--LPR------------GGILADEMGLGKTIQALALILATRPQDpkipeeleenssdpkKLYLSKTtL 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1563 VVCPLNTALNWMNEFEK--WQEGLN-----DAEKLEVSELAtvkrpqeRSYMlqrwqedggVMIIGYEMYRNLAQGRNVK 1635
Cdd:cd18008     67 IVVPLSLLSQWKDEIEKhtKPGSLKvyvyhGSKRIKSIEEL-------SDYD---------IVITTYGTLASEFPKNKKG 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1636 SRKLKEifnkaLVDPGPDF------VVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLL 1709
Cdd:cd18008    131 GGRDSK-----EKEASPLHrirwyrVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPF 205
                          250
                   ....*....|....*...
gi 1958806621 1710 GSIKEFRNRFINPIQNGQ 1727
Cdd:cd18008    206 GDYPWFNSDISKPFSKND 223
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
1499-1721 1.31e-21

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: 95.58  E-value: 1.31e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEFE 1578
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAE---------QHGCILGDEMGLGKTCQTISLL-WYLAGRLKLLGPFLVLCPLSVLDNWKEELN 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1579 KWQEGLN----DAEKLEVSELatvkrpQERSYMLQRWQedggVMIIGYEMYrnLAQGRNVKSRKLKeifnkalvdpgpdF 1654
Cdd:cd18006     71 RFAPDLSvityMGDKEKRLDL------QQDIKSTNRFH----VLLTTYEIC--LKDASFLKSFPWA-------------S 125
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806621 1655 VVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGsiKEFRNRFIN 1721
Cdd:cd18006    126 LVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFP--KDKLDDFIK 190
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
1499-1730 2.65e-20

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: 91.50  E-value: 2.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFmwdccceSVKKtkkspGSGCILAHCMGLGKTLQVVsflhTVLLCDKLDFStALVVCPLNTALNWMNEFE 1578
Cdd:cd18010      1 LLPFQREGVCF-------ALRR-----GGRVLIADEMGLGKTVQAI----AIAAYYREEWP-LLIVCPSSLRLTWADEIE 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1579 KWqegLNDaekLEVSELATVKRPQERSYMLqrwqeDGGVMIIGYEMyrnlaqgrnvkSRKLKEIFNKAlvdpGPDFVVCD 1658
Cdd:cd18010     64 RW---LPS---LPPDDIQVIVKSKDGLRDG-----DAKVVIVSYDL-----------LRRLEKQLLAR----KFKVVICD 117
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958806621 1659 EGHILKNEASAVSKAMNSI--KSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCAD 1730
Cdd:cd18010    118 ESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWD 191
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
1497-1726 5.39e-20

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: 91.61  E-value: 5.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1497 IKLKPHQVDGVQFM---WdCCCESVkktkkspgsgcILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNW 1573
Cdd:cd18054     19 LELRDYQLEGLNWLahsW-CKNNSV-----------ILADEMGLGKTIQTISFL-SYLFHQHQLYGPFLLVVPLSTLTSW 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1574 MNEFEKWQEGLNDAekLEVSELATVKRPQERSYMLQRWQE-DGGVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgp 1652
Cdd:cd18054     86 QREFEIWAPEINVV--VYIGDLMSRNTIREYEWIHSQTKRlKFNALITTYEIL--------LKDKTVLGSINWA------ 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958806621 1653 dFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNG 1726
Cdd:cd18054    150 -FLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG 222
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1958-2095 8.06e-18

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: 81.10  E-value: 8.06e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1958 GKMVLLFEILRmaEEIGDKVLVFSQSLISLDliEDFLelasrektedkdkpliykgegKWLRNIDYYRLDGSTNAQSRKK 2037
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE--AELL---------------------LEKEGIKVARLHGDLSQEEREE 55
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806621 2038 WAEEFNDETnvrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 2095
Cdd:pfam00271   56 ILEDFRKGK----IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
1497-1715 1.23e-17

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: 84.72  E-value: 1.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1497 IKLKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLdFSTALVVCPLNTALNWMNE 1576
Cdd:cd18053     19 LELRDYQLNGLNWLAHSWCK---------GNSCILADEMGLGKTIQTISFLNYLFHEHQL-YGPFLLVVPLSTLTSWQRE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1577 FEKWQEGLNDAEKL-EVSELATVK-----RPQERSYMLQrwqedggVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdp 1650
Cdd:cd18053     89 IQTWAPQMNAVVYLgDINSRNMIRthewmHPQTKRLKFN-------ILLTTYEIL--------LKDKSFLGGLNWA---- 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958806621 1651 gpdFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEF 1715
Cdd:cd18053    150 ---FIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDF 211
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
1499-1719 1.88e-17

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: 82.87  E-value: 1.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMN 1575
Cdd:cd17994      1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTIQTIVFLYS-LYKEGHSKGPFLVSAPLSTIINWER 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1576 EFEKWqeglndAEKLEVSelatvkrpqerSYMLQRwqedggVMIIGYEMYrnlaqgrNVKSRKLKEIFNKALVdpgpdfv 1655
Cdd:cd17994     68 EFEMW------APDFYVV-----------TYVGDH------VLLTSYELI-------SIDQAILGSIDWAVLV------- 110
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958806621 1656 vCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1719
Cdd:cd17994    111 -VDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEF 173
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
1499-1715 3.82e-17

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: 83.19  E-value: 3.82e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMN 1575
Cdd:cd18057      1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTVQTIVFLYS-LYKEGHSKGPYLVSAPLSTIINWER 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1576 EFEKWQEGLNDAEKLEVSELATVKRPQERSYmlqrwqEDGGVMIiGYEMYRnLAQGRNVKSRKLKEIFNKALVDPGP--- 1652
Cdd:cd18057     68 EFEMWAPDFYVVTYTGDKESRSVIRENEFSF------EDNAIRS-GKKVFR-MKKEAQIKFHVLLTSYELITIDQAIlgs 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1653 ---DFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIK----ENLLGSIKEF 1715
Cdd:cd18057    140 iewACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTperfNNLEGFLEEF 209
HELICc smart00490
helicase superfamily c-terminal domain;
2019-2095 4.14e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 78.02  E-value: 4.14e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806621  2019 RNIDYYRLDGSTNAQSRKKWAEEFNDETNVrgrlFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 2095
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
1498-1769 9.54e-17

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: 82.02  E-value: 9.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1498 KLKPHQVDGVQFMWdcccesvkkTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEF 1577
Cdd:cd18064     15 KLRDYQVRGLNWLI---------SLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIP-GPHMVLVPKSTLHNWMAEF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1578 EKWQEGLNdaeklevsELATVKRPQERSYMLQRWQEDG--GVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgpdFV 1655
Cdd:cd18064     85 KRWVPTLR--------AVCLIGDKDQRAAFVRDVLLPGewDVCVTSYEML--------IKEKSVFKKFNWR-------YL 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1656 VCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINpiqNGQCADSTMVD 1735
Cdd:cd18064    142 VIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT---NNCLGDQKLVE 218
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1958806621 1736 VRVMKKRAHILyemlagcvqRKDYTALTKFLPPK 1769
Cdd:cd18064    219 RLHMVLRPFLL---------RRIKADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
1526-1719 4.74e-16

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: 80.06  E-value: 4.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1526 GSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLndaeklevSELATVKRPQERS 1605
Cdd:cd18065     34 GVNGILADEMGLGKTLQTIALLGYLKHYRNIP-GPHMVLVPKSTLHNWMNEFKRWVPSL--------RAVCLIGDKDARA 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1606 YMLQRWQEDG--GVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgpdFVVCDEGHILKNEASAVSKAMNSIKSRRRI 1683
Cdd:cd18065    105 AFIRDVMMPGewDVCVTSYEMV--------IKEKSVFKKFNWR-------YLVIDEAHRIKNEKSKLSEIVREFKTTNRL 169
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958806621 1684 ILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1719
Cdd:cd18065    170 LLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF 205
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
1529-1719 5.32e-16

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: 79.31  E-value: 5.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1529 CILAHCMGLGKTLQVVSFLHTVLLcdKLDFSTALVVCPLNTALNWMNEFEKWQEgLNdaeklevseLATVKRPQERSYML 1608
Cdd:cd18059     22 CILADEMGLGKTIQSITFLYEIYL--KGIHGPFLVIAPLSTIPNWEREFRTWTE-LN---------VVVYHGSQASRRTI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1609 QrwqedggvmiiGYEMYRNLAQGRNVK-SRKLKEI---FNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 1677
Cdd:cd18059     90 Q-----------LYEMYFKDPQGRVIKgSYKFHAIittFEMILTD-CPELrnipwrcVVIDEAHRLKNRNCKLLEGLKMM 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958806621 1678 KSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1719
Cdd:cd18059    158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
DEXDc smart00487
DEAD-like helicases superfamily;
1497-1692 5.42e-16

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 78.69  E-value: 5.42e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  1497 IKLKPHQVDGVQFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKldFSTALVVCPL-NTALNWMN 1575
Cdd:smart00487    7 EPLRPYQKEAIEALLSG------------LRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTrELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  1576 EFEKWQEGLNDAEKLEVSELATVKRpqersymLQRWQEDGGVMIIG-YEMYrnlaqgrnvksrkLKEIFNKALVDPGPDF 1654
Cdd:smart00487   73 ELKKLGPSLGLKVVGLYGGDSKREQ-------LRKLESGKTDILVTtPGRL-------------LDLLENDKLSLSNVDL 132
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 1958806621  1655 VVCDEGHILKNE--ASAVSKAMNSI-KSRRRIILTGTPLQN 1692
Cdd:smart00487  133 VILDEAHRLLDGgfGDQLEKLLKLLpKNVQLLLLSATPPEE 173
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
1529-1719 7.51e-16

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: 78.93  E-value: 7.51e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1529 CILAHCMGLGKTLQVVSFLHTVLLCDKldFSTALVVCPLNTALNWMNEFEKWQEgLNDAekleVSELATVKRPqersyml 1608
Cdd:cd18058     22 CILADEMGLGKTIQSITFLSEIFLMGI--RGPFLIIAPLSTITNWEREFRTWTE-MNAI----VYHGSQISRQ------- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1609 qrwqedggvMIIGYEMYRNLAQGRNV----KSRKLKEIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 1677
Cdd:cd18058     88 ---------MIQQYEMYYRDEQGNPLsgifKFQVVITTFEMILAD-CPELkkinwscVIIDEAHRLKNRNCKLLEGLKLM 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958806621 1678 KSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1719
Cdd:cd18058    158 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
ADDz_Dnmt3 cd11725
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de ...
131-233 1.55e-15

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de novo DNA methyltransferase family that includes two active enzymes Dnmt3a and -3b and one regulatory factor Dnmt3l. The ADDz domain of Dnmt3 is located in the C-terminal region of Dnmt3, which is an active catalytic domain in Dnmt3a and -b, but lacks some residues for enzymatic activity in Dnmt3l. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


Pssm-ID: 277251 [Multi-domain]  Cd Length: 108  Bit Score: 74.35  E-value: 1.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  131 CTACGQQVNhfqkDSIYRHPSLKVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCD--FCHNAFCKKCILRNL 208
Cdd:cd11725      5 CLACGSLEV----SETSDHPFFEGGLCKNCKERFLECIFLFDDDGYQMYCTICGGGGEVVLCDnpDCTRVYCTECLDLLL 80
                           90       100
                   ....*....|....*....|....*
gi 1958806621  209 GRKELSTIMDENNqWYCYICQPEPL 233
Cdd:cd11725     81 GPGAVAKILESDP-WFCFLCSPESN 104
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
1526-1719 1.84e-15

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: 78.13  E-value: 1.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1526 GSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMNEFEKWQEGLNDAEKLEVSELATVKRPQERS 1605
Cdd:cd18055     19 GTDTILADEMGLGKTIQTIVFLYS-LYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVTYTGDKDSRAIIRENEFS 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1606 YmlqrwqeDGGVMIIGYEMYRNLAQGRN-----VKSRKLKEIFNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIKSR 1680
Cdd:cd18055     98 F-------DDNAVKGGKKAFKMKREAQVkfhvlLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKID 170
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958806621 1681 RRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1719
Cdd:cd18055    171 HKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
1499-1724 1.86e-15

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: 77.78  E-value: 1.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMwdcccesvkktKKSPGSGCILAhcMGLGKTLQVVSFLHTVLLCDKLdfSTALVVCPLNTALN-WMNEF 1577
Cdd:cd18013      1 PHPYQKVAINFI-----------IEHPYCGLFLD--MGLGKTVTTLTALSDLQLDDFT--RRVLVIAPLRVARStWPDEV 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1578 EKWqEGLNDaekLEVSelATVKRPQERSYMLQRwqeDGGVMIIGYEmyrnlaqgrNVKsrKLKEIFNkalvDPGP-DFVV 1656
Cdd:cd18013     66 EKW-NHLRN---LTVS--VAVGTERQRSKAANT---PADLYVINRE---------NLK--WLVNKSG----DPWPfDMVV 121
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958806621 1657 CDEGHILKNEASAVSKAMNSIKSR-RRII-LTGTPLQNNLIEYHCMVNFIK--ENLLGSIKEFRNRFINPIQ 1724
Cdd:cd18013    122 IDELSSFKSPRSKRFKALRKVRPViKRLIgLTGTPSPNGLMDLWAQIALLDqgERLGRSITAYRERWFDPDK 193
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
1499-1715 1.97e-15

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: 78.18  E-value: 1.97e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMN 1575
Cdd:cd18056      1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTVQTAVFLYS-LYKEGHSKGPFLVSAPLSTIINWER 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1576 EFEKWQEGLNDAEKLEVSELATVKRPQERSYmlqrwqEDGGVMiiGYEMYRNLAQGRNVKSRKLKEIFNKALVDPGP--- 1652
Cdd:cd18056     68 EFEMWAPDMYVVTYVGDKDSRAIIRENEFSF------EDNAIR--GGKKASRMKKEASVKFHVLLTSYELITIDMAIlgs 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1653 -DF--VVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIK----ENLLGSIKEF 1715
Cdd:cd18056    140 iDWacLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTperfHNLEGFLEEF 209
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
1530-1744 4.08e-15

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: 77.41  E-value: 4.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1530 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLndaEKLEVSELATVKR---PQERSY 1606
Cdd:cd18063     46 ILADEMGLGKTIQTIALITYLMEHKRLN-GPYLIIVPLSTLSNWTYEFDKWAPSV---VKISYKGTPAMRRslvPQLRSG 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1607 MLQrwqedggVMIIGYEMYrnlaqgrnVKSRKLkeifnkaLVDPGPDFVVCDEGHILKNEASAVSKAMNS-IKSRRRIIL 1685
Cdd:cd18063    122 KFN-------VLLTTYEYI--------IKDKHI-------LAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRILL 179
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1686 TGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI-QNGQCADSTMVDVRVMKKRAH 1744
Cdd:cd18063    180 TGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIRRLH 239
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
1499-1725 6.21e-15

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: 76.39  E-value: 6.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLhtVLLCDKLD-FSTALVVCPLNTALNWMNEF 1577
Cdd:cd18002      1 LKEYQLKGLNWLANL---------YEQGINGILADEMGLGKTVQSIAVL--AHLAEEHNiWGPFLVIAPASTLHNWQQEI 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1578 EKWqeglndAEKLEVseLATVKRPQERSYMLQRWQ------EDGG--VMIIGYEM-YRNLAQGRNVKSRklkeifnkalv 1648
Cdd:cd18002     70 SRF------VPQFKV--LPYWGNPKDRKVLRKFWDrknlytRDAPfhVVITSYQLvVQDEKYFQRVKWQ----------- 130
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806621 1649 dpgpdFVVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQN 1725
Cdd:cd18002    131 -----YMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIES 202
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
1491-1726 2.24e-14

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: 75.20  E-value: 2.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1491 VHRNMVIKLKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSflhtVLLCDKldfstALVVCPLNTA 1570
Cdd:cd18071     13 VSRENSQDLPPFWEEAVGLFLNTITNFSQKKRPELVRGGILADDMGLGKTLTTIS----LILANF-----TLIVCPLSVL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1571 LNWMNEFEKwqeglndaeklevselaTVKRPQERSYMlqrwqedggvmiigyemYRNLAQGRNVKSRKLKEI----FNKA 1646
Cdd:cd18071     84 SNWETQFEE-----------------HVKPGQLKVYT-----------------YHGGERNRDPKLLSKYDIvlttYNTL 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1647 LVDPG--PDF---------VVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIKENLLgSIKEF 1715
Cdd:cd18071    130 ASDFGakGDSplhtinwlrVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPF-SNPEY 208
                          250
                   ....*....|..
gi 1958806621 1716 RNRFI-NPIQNG 1726
Cdd:cd18071    209 WRRLIqRPLTMG 220
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
1530-1744 3.30e-14

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: 75.08  E-value: 3.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1530 ILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQEglndaeklEVSELATVKRPQ-ERSYML 1608
Cdd:cd18062     46 ILADEMGLGKTIQTIALI-TYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAP--------SVVKVSYKGSPAaRRAFVP 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1609 QRWQEDGGVMIIGYEMYrnlaqgrnVKSRKLkeifnkaLVDPGPDFVVCDEGHILKNEASAVSKAMNS-IKSRRRIILTG 1687
Cdd:cd18062    117 QLRSGKFNVLLTTYEYI--------IKDKQI-------LAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLLLTG 181
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806621 1688 TPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI-QNGQCADSTMVDVRVMKKRAH 1744
Cdd:cd18062    182 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLH 239
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
1529-1719 7.62e-14

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: 73.16  E-value: 7.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1529 CILAHCMGLGKTLQVVSFLHTVLLCDKLdfSTALVVCPLNTALNWMNEFEKWQEgLNDAekLEVSELATVKrpqersyml 1608
Cdd:cd18060     22 CILADEMGLGKTIQSIAFLQEVYNVGIH--GPFLVIAPLSTITNWEREFNTWTE-MNTI--VYHGSLASRQ--------- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1609 qrwqedggvMIIGYEMYRNLAQGRNV----KSRKLKEIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 1677
Cdd:cd18060     88 ---------MIQQYEMYCKDSRGRLIpgayKFDALITTFEMILSD-CPELreiewrcVIIDEAHRLKNRNCKLLDSLKHM 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958806621 1678 KSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1719
Cdd:cd18060    158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
1529-1719 1.43e-13

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: 72.35  E-value: 1.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1529 CILAHCMGLGKTLQVVSFLHTVLLCD-KLDFstaLVVCPLNTALNWMNEFEKWQEgLNdaekLEVSELATVKRPqersyM 1607
Cdd:cd18061     22 CILADEMGLGKTIQSITFLYEILLTGiRGPF---LIIAPLSTIANWEREFRTWTD-LN----VVVYHGSLISRQ-----M 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1608 LQRwqedggvmiigYEMYRNLAQGRNVK-SRKLKEIFN--KALVDPGPDF-------VVCDEGHILKNEASAVSKAMNSI 1677
Cdd:cd18061     89 IQQ-----------YEMYFRDSQGRIIRgAYRFQAIITtfEMILGGCPELnaidwrcVIIDEAHRLKNKNCKLLEGLKLM 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958806621 1678 KSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1719
Cdd:cd18061    158 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
1499-1716 2.31e-10

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: 62.69  E-value: 2.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFMWDcccesvkktKKSPGsgCILAHCMGLGKTLQVVSFLHTVLLCDKLDFstALVVCPLNTALNWMneFE 1578
Cdd:cd18011      1 PLPHQIDAVLRALR---------KPPVR--LLLADEVGLGKTIEAGLIIKELLLRGDAKR--VLILCPASLVEQWQ--DE 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1579 KWQEGLNDAEKLEVSELATVKRPQersymlQRWQEDGGVMIIGYEMYRnlaqgRNVKSRKLkeifnkaLVDPGPDFVVCD 1658
Cdd:cd18011     66 LQDKFGLPFLILDRETAAQLRRLI------GNPFEEFPIVIVSLDLLK-----RSEERRGL-------LLSEEWDLVVVD 127
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958806621 1659 EGHILKNEASAVS----KAMNSI--KSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFR 1716
Cdd:cd18011    128 EAHKLRNSGGGKEtkryKLGRLLakRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFL 191
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
1499-1705 7.03e-08

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: 55.95  E-value: 7.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1499 LKPHQVDGVQFM-WdcccesvkKTKKSPgSGCILAHCMGLGKTLQVVSF------------------LHTVLLC-DKLDF 1558
Cdd:cd18072      1 LLLHQKQALAWLlW--------RERQKP-RGGILADDMGLGKTLTMIALilaqkntqnrkeeekekaLTEWESKkDSTLV 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621 1559 STA--LVVCPLNTALNWMNEFEKWQEGlndaEKLEVSELATVKRpQERSYMLQRWQedggVMIIGYemyrnlaqgrNVKS 1636
Cdd:cd18072     72 PSAgtLVVCPASLVHQWKNEVESRVAS----NKLRVCLYHGPNR-ERIGEVLRDYD----IVITTY----------SLVA 132
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958806621 1637 RKLKEIFNKALVDPGPDF----VVCDEGHILKNEASAVSKAMNSIKSRRRIILTGTPLQNNLIEYHCMVNFIK 1705
Cdd:cd18072    133 KEIPTYKEESRSSPLFRIawarIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
ADDz_Dnmt3l cd11727
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l); Dnmt3l ...
131-230 2.89e-07

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l); Dnmt3l is a regulator of DNA methylation, which acts by recognizing unmethylated histone H3 tails and interacting with Dnmt3a to stimulate its de novo DNA methylation activity. The ADDz_Dnmt3l domain is located in the C-terminal region of Dnmt3l that otherwise lacks some residues required for DNA methyltransferase activity. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. Dnmt3l is also associating with HDAC1 and acts as a transcriptional repressor. The ADDz_Dnmt3l domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif.


Pssm-ID: 277253 [Multi-domain]  Cd Length: 123  Bit Score: 51.39  E-value: 2.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  131 CTACGQQVNHFQkdsiyrHPSLKVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCD--FCHNAFCKKCILRNL 208
Cdd:cd11727      7 CICCGSLQIHTQ------HPLFHGGICAPCTEKFLEAFFLYDEDGYQAYCTICCSGETLLMCDdpDCTRCYCFECVDSLV 80
                           90       100
                   ....*....|....*....|..
gi 1958806621  209 GRKELSTIMDENNqWYCYICQP 230
Cdd:cd11727     81 GPGTSEKVKATNN-WVCFLCLP 101
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
130-231 2.24e-06

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b is an active catalytic domain of Dnmt3b. Dnmt3b is a member of the Dnmt3 family and is a de novo DNA methyltransferases that has an N-terminal variable region followed by a conserved PWWP region and the cysteine-rich ADDz domain. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The methyltransferase activity of Dnmt3a is not only responsible for the establishment of DNA methylation pattern, but is also essential for the inheritance of these patterns during mitosis. Dnmt3b is ubiquitously expressed in most adult tissues. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif. A knockout of Dnmt3b has been shown to be lethal in the mouse model.


Pssm-ID: 277254 [Multi-domain]  Cd Length: 120  Bit Score: 48.70  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  130 SCTACGQqvnhfqKDSIYRHPSLKVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCD--FCHNAFCKKCILRN 207
Cdd:cd11728      4 FCLSCGR------SNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGnaSCCRCFCVDCLEVL 77
                           90       100
                   ....*....|....*....|....
gi 1958806621  208 LGRKELSTiMDENNQWYCYICQPE 231
Cdd:cd11728     78 VGPGTAAK-AKEQDPWSCYMCLPQ 100
PHD4_NSD cd15567
PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
180-228 2.64e-05

PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the fourth PHD finger.


Pssm-ID: 277042 [Multi-domain]  Cd Length: 41  Bit Score: 43.39  E-value: 2.64e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958806621  180 CRWCAEGGNLICCDFCHNAFCKKCIlrnlgrkELSTIMDENnqWYCYIC 228
Cdd:cd15567      2 CFICSEGGSLICCESCPASFHPECL-------GLEPPPEGK--FYCEDC 41
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
2053-2105 2.76e-05

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 44.23  E-value: 2.76e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958806621 2053 FIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQtKPVYVYRF 2105
Cdd:cd18785     25 ILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK-DEGEVILF 76
PHD2_CHD_II cd15532
PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD ...
180-228 2.96e-05

PHD finger 2 found in class II Chromodomain-Helicase-DNA binding (CHD) proteins; Class II CHD proteins includes chromodomain-helicase-DNA-binding protein CHD3, CHD4, and CHD5, which are nuclear and ubiquitously expressed chromatin remodelling ATPases generally associated with histone deacetylases (HDACs). They are involved in DNA Double Strand Break (DSB) signaling, DSB repair and/or p53-dependent pathways such as apoptosis and senescence, as well as in the maintenance of genomic stability, and/or cancer prevention. They function as subunits of the Nucleosome Remodelling and Deacetylase (NuRD) complex, which is generally associated with gene repression, heterochromatin formation, and overall chromatin compaction. In contrast to the class I CHD enzymes (CHD1 and CHD2), class II CHD proteins lack identifiable DNA-binding domains, but possess a C-terminal coiled-coil region. Moreover, in addition to the tandem chromodomains and a helicase domain, they all harbor tandem plant homeodomain (PHD) zinc fingers involved in the recognition of methylated histone tails. This model corresponds to the second PHD finger.


Pssm-ID: 277007 [Multi-domain]  Cd Length: 43  Bit Score: 43.04  E-value: 2.96e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958806621  180 CRWCAEGGNLICCDFCHNAFCKKCILRNLgrKELSTimdenNQWYCYIC 228
Cdd:cd15532      2 CRVCKDGGELLCCDGCPSSYHLHCLNPPL--AEIPD-----GDWFCPRC 43
PHD_BS69 cd15537
PHD finger found in protein BS69; Protein BS69, also termed zinc finger MYND domain-containing ...
180-228 7.85e-05

PHD finger found in protein BS69; Protein BS69, also termed zinc finger MYND domain-containing protein 11 (ZMYND11 or ZMY11), is a ubiquitously expressed nuclear protein acting as a transcriptional co-repressor in association with various transcription factors. It was originally identified as an adenovirus 5 E1A-binding protein that inhibits E1A transactivation, as well as c-Myb transcription. It also mediates repression, at least in part, through interaction with the co-repressor N-CoR. Moreover, it interacts with Toll-interleukin 1 receptor domain (TIR)-containing adaptor molecule-1 (TICAM-1, also named TRIF) to facilitate NF-kappaB activation and type I IFN induction. It associates with PIAS1, a SUMO E3 enzyme, and Ubc9, a SUMO E2 enzyme, and plays an inhibitory role in muscle and neuronal differentiation. Moreover, BS69 regulates Epstein-Barr virus (EBV) latent membrane protein 1 (LMP1)/C-terminal activation region 2 (CTAR2)-mediated NF-kappaB activation by interfering with the complex formation between TNFR-associated death domain protein (TRADD) and LMP1/CTAR2. It also cooperates with tumor necrosis factor receptor (TNFR)-associated factor 3 (TRAF3) in the regulation of EBV-derived LMP1/CTAR1-induced NF-kappaB activation. Furthermore, BS69 is involved in the p53-p21Cip1-mediated senescence pathway. BS69 contains a plant homeodomain (PHD) finger, a bromodomain, a proline-tryptophan-tryptophan-proline (PWWP) domain, and a Myeloid translocation protein 8, Nervy and DEAF-1 (MYND) domain.


Pssm-ID: 277012  Cd Length: 43  Bit Score: 41.95  E-value: 7.85e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958806621  180 CRWCAEGGNLICCDFCHNAFCKKCILRNLGRkelstimDENNQWYCYIC 228
Cdd:cd15537      2 CFECHAPGEVLPCSGCFRVYHSDCLSEDFRP-------DSTSHWTCPVC 43
PHD1_AIRE cd15539
PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...
180-228 2.65e-04

PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune polyendocrinopathy candidiasis ectodermal dystrophy (APECED) protein, functions as a regulator of gene transcription in the thymus. It is essential for prevention of autoimmunity. AIRE plays a critical role in the induction of central tolerance. It promotes self-tolerance through tissue-specific antigen (TSA) expression. It also acts as an active regulator of chondrocyte differentiation. AIRE contains a homogeneously-staining region (HSR) or caspase-recruitment domain (CARD), a nuclear localization signal (NLS), a SAND (for Sp100, AIRE, nuclear phosphoprotein 41/75 or NucP41/75, and deformed epidermal auto regulatory factor 1 or Deaf1) domain, two plant homeodomain (PHD) fingers, and four LXXLL (where L stands for leucine) motifs. This model corresponds to the first PHD finger that recognizes the unmethylated tail of histone H3 and targets AIRE-dependent genes.


Pssm-ID: 277014 [Multi-domain]  Cd Length: 43  Bit Score: 40.51  E-value: 2.65e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958806621  180 CRWCAEGGNLICCDFCHNAFCKKCIlrnlgrKELSTIMDENNqWYCYIC 228
Cdd:cd15539      2 CAVCGDGGELLCCDGCPRAFHLACL------VPPLTLIPSGT-WRCSSC 43
PHD4_NSD1 cd15656
PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, ...
180-228 5.52e-04

PHD finger 4 found in nuclear receptor-binding SET domain-containing protein 1 (NSD1); NSD1, also termed H3 Lysine-36 and H4 Lysine-20 specific histone-lysine N-methyltransferase, or androgen receptor coactivator 267 kDa protein, or androgen receptor-associated protein of 267 kDa, or H3-K36-HMTase H4-K20-HMTase, or Lysine N-methyltransferase 3B (KMT3B), or NR-binding SET domain-containing protein, is a lysine methyltransferase that preferentially methylates H3 on Lysine36 (H3-K36) and H4 on Lysine20 (H4-K20), which is primarily associated with active transcription. It plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. It can alter transcription by interacting with the protein NSD1-interacting zinc finger protein 1 (NIZP1). It also mitigates caspase-1 activation by listeriolysin o (LLO) in macrophages, and requires functional LLO for the regulation of IL-1beta secretion. Moreover, NSD1 regulates RNA polymerase II (RNAP II) recruitment to bone morphogenetic protein 4 (BMP4). NSD1 contains a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). The SET domain is responsible for histone methyltransferase activity. The PWWP and PHD fingers are involved in protein-protein interactions. This model corresponds to the fourth PHD finger.


Pssm-ID: 277126  Cd Length: 40  Bit Score: 39.61  E-value: 5.52e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958806621  180 CRWCAEGGNLICCDFCHNAFCKKCilrnlgrkeLSTIMDENNqWYCYIC 228
Cdd:cd15656      2 CFVCSEGGSLLCCESCPAAFHREC---------LNIDMPEGS-WYCNDC 40
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
180-225 6.84e-04

PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The nuclear receptor binding SET domain (NSD) protein is a family of three HMTases, NSD1, NSD2/MMSET/WHSC1, and NSD3/WHSC1L1, that are critical in maintaining chromatin integrity. Reducing NSD activity through specific lysine-HMTase inhibitors appears promising to help suppress cancer growth. NSD proteins have specific mono- and dimethylase activities for H3K36, and they play non-redundant roles during development. NSD1 plays a role in several pathologies, including but not limited to Sotos and Weaver syndromes, acute myeloid leukemia, breast cancer, neuroblastoma, and glioblastoma formation. NSD2 is involved in cancer cell proliferation, survival, and tumor growth, by mediating constitutive NF-kappaB signaling via the cytokine autocrine loop. NSD3 is amplified in human breast cancer cell lines. Moreover, translocation resulting in NUP98 fusion to NSD3 leads to the development of acute myeloid leukemia. NSD proteins contain a catalytic suppressor of variegation, enhancer of zeste and trithorax (SET) domain, two proline-tryptophan-tryptophan-proline (PWWP) domains, five plant homeodomain (PHD) fingers, and an NSD-specific Cys-His rich domain (Cys5HisCysHis). This model corresponds to the fifth PHD finger.


Pssm-ID: 277043 [Multi-domain]  Cd Length: 43  Bit Score: 39.23  E-value: 6.84e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958806621  180 CRWCAEGGNLICCDF--CHNAFCKKCilrnLGRKelstiMDENNQWYC 225
Cdd:cd15568      2 CFRCGDGGDLVLCDFkgCPKVYHLSC----LGLE-----KPPGGKWIC 40
PHD1_PHF12 cd15533
PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is ...
180-228 9.84e-04

PHD finger 1 found in PHD finger protein 12 (PHF12); PHF12, also termed PHD factor 1 (Pf1), is a plant homeodomain (PHD) zinc finger-containing protein that bridges the transducin-like enhancer of split (TLE) corepressor to the mSin3A-histone deacetylase (HDAC)-complex, and further represses transcription at targeted genes. PHF12 also interacts with MRG15 (mortality factor-related genes on chromosome 15), a member of the mortality factor (MORF) family of proteins implicated in regulating cellular senescence. PHF12 contains two plant-homeodomain (PHD) zinc fingers followed by a polybasic region. The PHD fingers function downstream of phosphoinositide signaling triggered by the interaction between polybasic regions and phosphoinositides. This model corresponds to the first PHD finger.


Pssm-ID: 277008 [Multi-domain]  Cd Length: 45  Bit Score: 38.88  E-value: 9.84e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958806621  180 CRWCAEGGNLICCDFCHNAFCKKCIlrnlgRKELSTIMDENNQWYCYIC 228
Cdd:cd15533      2 CDSCGEGGDLLCCDRCPASFHLQCC-----NPPLDEEDLPPGEWLCHRC 45
PHD_TIF1_like cd15541
PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...
180-228 1.33e-03

PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar proteins; The TIF1 family of transcriptional cofactors includes TIF1alpha (TRIM24), TIF1beta (TRIM28), TIF1gamma (TRIM33), and TIF1delta (TRIM66), which are characterized by an N-terminal RING-finger B-box coiled-coil (RBCC/TRIM) motif and plant homeodomain (PHD) finger followed by a bromodomain in the C-terminal region. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha, TIF1beta, and TIF1delta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. TIF1alpha and TIF1beta bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. In contrast, TIF1delta appears to lack nuclear receptor- and KRAB-binding activity. Moreover, TIF1delta is specifically involved in heterochromatin-mediated gene silencing during postmeiotic phases of spermatogenesis. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta, and gamma. It cannot bind to nuclear receptors (NRs). This family also includes Sp100/Sp140 family proteins, the nuclear body SP100 and SP140. Sp110 is a leukocyte-specific component of the nuclear body. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers. SP140 is an interferon inducible nuclear leukocyte-specific protein involved in primary biliary cirrhosis and a risk factor in chronic lymphocytic leukemia. It is also implicated in innate immune response to human immunodeficiency virus type 1 (HIV-1) by binding to the virus viral infectivity factor (Vif) protein. Both Sp110 and Sp140 contain a SAND domain, a plant homeodomain (PHD) finger, and a bromodomain (BRD).


Pssm-ID: 277016 [Multi-domain]  Cd Length: 43  Bit Score: 38.48  E-value: 1.33e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958806621  180 CRWCAEGGNLICCDFCHNAFCKKCILRNLGRKelstimdENNQWYCYIC 228
Cdd:cd15541      2 CAVCQNGGELLCCDKCPRVFHLDCHIPPIPEF-------PSGEWSCSLC 43
PHD1_Rco1 cd15535
PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...
179-228 2.38e-03

PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and similar proteins; Rco1 is a component of the Rpd3S histone deacetylase complex that plays an important role at actively transcribed genes. Rco1 contains two plant homeodomain (PHD) fingers, which are required for the methylation of histone H3 lysine 36 (H3K36) nucleosome recognition by Rpd3S. This model corresponds to the first PHD finger.


Pssm-ID: 277010 [Multi-domain]  Cd Length: 45  Bit Score: 37.78  E-value: 2.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958806621  179 QCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELStimdeNNQWYCYIC 228
Cdd:cd15535      1 FCSACGGYGSFLCCDGCPRSFHFSCLDPPLEEDNLP-----DDEWFCNEC 45
PHD_PRHA_like cd15504
PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and ...
183-228 4.62e-03

PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and similar proteins; PRHA is a homeodomain protein encoded by a single-copy Arabidopsis thaliana homeobox gene, prha. It shows the capacity to bind to TAATTG core sequence elements but requires additional adjacent bases for high-affinity binding. PRHA contains a plant homeodomain (PHD) finger, a homeodomain, peptide repeats and a putative leucine zipper dimerization domain.


Pssm-ID: 276979  Cd Length: 53  Bit Score: 37.41  E-value: 4.62e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958806621  183 CAEGGNLICCD-FCHNAFCKKCILRNLgrkELSTIMDENNQWYCYIC 228
Cdd:cd15504     10 ASPDNDILLCDgGCNRAYHQKCLEPPL---LTEDIPPEDEGWLCPLC 53
ADDz_Dnmt3a cd11729
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a ...
131-228 9.92e-03

ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3a (Dnmt3a); Dnmt3a is a member of the Dnmt3 family and is a protein with de novo DNA methyltransferase activity. Dnmt3 family members are Dnmt3a, Dnmt3b, and Dnmt3l the non-enzymatic regulatory factor. Dnmt3a is recruited by Dnmt3l to unmethylated histone H3 and methylates the target. Dnmt3a has a variable region at the N-terminus, followed by a conserved PWWP region and the cysteine-rich ADDz domain. ADDz_Dnmt3a is an active catalytic domain of Dnmt3a. DNA methylation is an important epigenetic mechanism involved in diverse biological processes such as embryonic development, gene expression, and genomic imprinting. The methyltransferase activity of Dnmt3a is not only responsible for the establishment of DNA methylation pattern, but is also essential for the inheritance of these patterns during mitosis. The ADDz_Dnmt3 domain is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger. PHD zinc finger domains have been identified in more than 40 proteins that are mainly involved in chromatin mediated transcriptional control; the classical PHD zinc finger has a C4-H-C3 motif that spans about 50-80 amino acids. In ADDz, the conserved histidine residue of the PHD finger is replaced by a cysteine, and an additional zinc finger C2-C2 like motif is located about twenty residues upstream of the C4-C-C3 motif. A knockout of Dnmt3a has been shown to be lethal in the mouse model.


Pssm-ID: 277255 [Multi-domain]  Cd Length: 128  Bit Score: 38.45  E-value: 9.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806621  131 CTACGqqvnhfqkdSIY---RHPSLKVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICC--DFCHNAFCKKCIL 205
Cdd:cd11729      8 CISCG---------SLNvtlEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCgnNNCCRCFCVECVD 78
                           90       100
                   ....*....|....*....|...
gi 1958806621  206 RNLGRKELSTIMDEnNQWYCYIC 228
Cdd:cd11729     79 LLVGPGAAQAAIKE-DPWNCYMC 100
 
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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