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Conserved domains on  [gi|578838415|ref|XP_005262213|]
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transcriptional regulator ATRX isoform X5 [Homo sapiens]

Protein Classification

DEAD/DEAH box helicase( domain architecture ID 12975241)

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 ...
1505-1748 3.88e-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: 493.64  E-value: 3.88e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKL-DFSTALVVCPLNTALNWMNEF 1583
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1584 EKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 1662
Cdd:cd18068    81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1663 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 1742
Cdd:cd18068   161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240

                  ....*.
gi 578838415 1743 RVMKKR 1748
Cdd:cd18068   241 RVMKKR 246
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1488-2136 5.79e-86

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 297.52  E-value: 5.79e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1488 EETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTA 1567
Cdd:COG0553   225 RRLREALESLPAGLKATLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PV 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1568 LVVCPLNTALNWMNEFEKWQEGLKddeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklke 1647
Cdd:COG0553   294 LIVAPTSLVGNWQRELAKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE----------- 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1648 ifnkALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFIN 1727
Cdd:COG0553   353 ----LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFAR 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1728 PIQNGQcadstmvdvrvmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTSIQCKLYQYYLDHLTGVGNNSE 1807
Cdd:COG0553   429 PIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAE 496
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1808 GGRGKagAKLFQDFQMLSRIWTHPwclqldyiskenkgyfdedsmdefiasdsdetsmslssddytkkkkkgkkgkkdss 1887
Cdd:COG0553   497 GIRRR--GLILAALTRLRQICSHP-------------------------------------------------------- 518
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1888 ssgsgsdndvevikvwnsrsrgggegnvdetgnnpsvSLKLEESKATSssnpsspapdwykdfvtdadaevlEHSGKMVL 1967
Cdd:COG0553   519 -------------------------------------ALLLEEGAELS------------------------GRSAKLEA 537
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1968 LFEILRMAEEIGDKVLVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTTAQSRKKWAEEF 2047
Cdd:COG0553   538 LLELLEELLAEGEKVLVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDRF 595
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 2048 NDETNVrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTK 2127
Cdd:COG0553   596 QEGPEA--PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEK 673

                  ....*....
gi 578838415 2128 QSLSFRVVD 2136
Cdd:COG0553   674 RALAESVLG 682
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
112-215 9.34e-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: 192.14  E-value: 9.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  112 GIVSCTACGQQVNHFqKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILR 191
Cdd:cd11726     1 RRVRCTACGEQLNHF-SKEVHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICCDFCPNVFCKKCIKR 79
                          90       100
                  ....*....|....*....|....
gi 578838415  192 NLGRKELStIMDENNQWYCYICHP 215
Cdd:cd11726    80 NLGRAELS-RIEESDKWKCFVCDP 102
PTZ00121 super family cl31754
MAEBL; Provisional
736-1383 1.96e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  736 DTKKGKSAKSSIISKKKRQT--QSESSNYDSELEKEIKSMSKIGAARTTKKRIPNTKDFDSSEDEKHSKKGMDNQGHKNL 813
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEakKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK 1301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  814 KTSQEGSSDDAERKQERETFSSAEGTVDKdttimelRDRLPKKQQASASTDGVDKlsgKEESFTSLEVRKvAETKEKSKH 893
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKAEEAKKK-------ADAAKKKAEEAKKAAEAAK---AEAEAAADEAEA-AEEKAEAAE 1370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  894 LKTKTCKKVQDGLSDIAEKFLKKDQSDETSEDDKKQS---KKGTEEKKKPSDFKKKVIKMEQQYESSSDGTEKlPEREEI 970
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA-KKADEA 1449
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  971 CHFPKGIKQIKNGTTDGEKKSK----KIRDKTSKKKDELSDYAEKSTGKGDSCDSSED--KKSKNGAYGREKKRCKLLGK 1044
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKadeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKK 1529
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1045 SSRKRQDCSSSDTEKYSmKEDGCNSSDKRLKRIELR---------ERRNLSSKR-------NTKEIQSGSSSSDAEESSE 1108
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKK-KADELKKAEELKKAEEKKkaeeakkaeEDKNMALRKaeeakkaEEARIEEVMKLYEEEKKMK 1608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1109 DNKKKKQRTSSKKKAVIVKEKKRNSLRTSTKRKQADITSSSSSDIEDDDQNSI--GEGSSDEQKIKPVTENLVLSSHTgf 1186
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaAEEAKKAEEDKKKAEEAKKAEED-- 1686
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1187 cQSSGDEALSKsvpvtvddDDDDNDPENRIAKKMLLEEIKANLSSDEDGSSDDEPEEGKKRT---GKQNEENPGDEEAKN 1263
Cdd:PTZ00121 1687 -EKKAAEALKK--------EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAeedKKKAEEAKKDEEEKK 1757
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1264 QVNSESDSDSEESKKPRY-RHRLLRHKLTVSDGESGEEKKTKPKEHKE-----VKGRNRRKVSSEDSEDSDfqeSGVSEE 1337
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKeKEAVIEEELDEEDEKRRMEVDKKIKDIFDnfaniIEGGKEGNLVINDSKEME---DSAIKE 1834
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 578838415 1338 VSESEDEQRPRTRSAKKAELEENQRSykqkkkrrrikvQEDSSSEN 1383
Cdd:PTZ00121 1835 VADSKNMQLEEADAFEKHKFNKNNEN------------GEDGNKEA 1868
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
587-802 3.15e-03

DNA topoisomerase 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00108:

Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 43.11  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  587 NEVSLLLEESDLRRSPRVKTTPLRRPTETNPVTSNsdeecnetvkEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSKQ 666
Cdd:PTZ00108 1170 RKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSD----------EKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSS 1239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  667 SETVDQNSDSDEMLAILKEVSRMSHSSSSDTDINEIHTNHKTLY---DLKTQAGKDDKGKRKRKSSTSGSDFDTKKGKSA 743
Cdd:PTZ00108 1240 VKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYsppPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLA 1319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578838415  744 KSSIiSKKKRQTQSESSNYDSELEKeiksmSKIGAARTTKKRIPNTKDFDSSEDEKHSK 802
Cdd:PTZ00108 1320 ALKK-KKKSEKKTARKKKSKTRVKQ-----ASASQSSRLLRRPRKKKSDSSSEDDDDSE 1372
 
Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1505-1748 3.88e-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: 493.64  E-value: 3.88e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKL-DFSTALVVCPLNTALNWMNEF 1583
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1584 EKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 1662
Cdd:cd18068    81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1663 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 1742
Cdd:cd18068   161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240

                  ....*.
gi 578838415 1743 RVMKKR 1748
Cdd:cd18068   241 RVMKKR 246
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1508-1834 9.32e-107

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: 343.13  E-value: 9.32e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  1508 HQVDGVQFMWDCCCEsvkktkksPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQ 1587
Cdd:pfam00176    1 YQIEGVNWMLSLENN--------LGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  1588 EglkdDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGH 1667
Cdd:pfam00176   73 S----PPALRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLR-----------KHKELLKKV----HWHRIVLDEGH 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  1668 ILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvrvMKK 1747
Cdd:pfam00176  134 RLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKK 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  1748 RAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTSIQCKLYQ-YYLDHLTGVGNNSEGGRGKAgAKLFQDFQMLSR 1826
Cdd:pfam00176  203 GVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIK-ASLLNILMRLRK 281

                   ....*...
gi 578838415  1827 IWTHPWCL 1834
Cdd:pfam00176  282 ICNHPGLI 289
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1488-2136 5.79e-86

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 297.52  E-value: 5.79e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1488 EETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTA 1567
Cdd:COG0553   225 RRLREALESLPAGLKATLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PV 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1568 LVVCPLNTALNWMNEFEKWQEGLKddeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklke 1647
Cdd:COG0553   294 LIVAPTSLVGNWQRELAKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE----------- 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1648 ifnkALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFIN 1727
Cdd:COG0553   353 ----LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFAR 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1728 PIQNGQcadstmvdvrvmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTSIQCKLYQYYLDHLTGVGNNSE 1807
Cdd:COG0553   429 PIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAE 496
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1808 GGRGKagAKLFQDFQMLSRIWTHPwclqldyiskenkgyfdedsmdefiasdsdetsmslssddytkkkkkgkkgkkdss 1887
Cdd:COG0553   497 GIRRR--GLILAALTRLRQICSHP-------------------------------------------------------- 518
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1888 ssgsgsdndvevikvwnsrsrgggegnvdetgnnpsvSLKLEESKATSssnpsspapdwykdfvtdadaevlEHSGKMVL 1967
Cdd:COG0553   519 -------------------------------------ALLLEEGAELS------------------------GRSAKLEA 537
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1968 LFEILRMAEEIGDKVLVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTTAQSRKKWAEEF 2047
Cdd:COG0553   538 LLELLEELLAEGEKVLVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDRF 595
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 2048 NDETNVrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTK 2127
Cdd:COG0553   596 QEGPEA--PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEK 673

                  ....*....
gi 578838415 2128 QSLSFRVVD 2136
Cdd:COG0553   674 RALAESVLG 682
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
112-215 9.34e-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: 192.14  E-value: 9.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  112 GIVSCTACGQQVNHFqKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILR 191
Cdd:cd11726     1 RRVRCTACGEQLNHF-SKEVHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICCDFCPNVFCKKCIKR 79
                          90       100
                  ....*....|....*....|....
gi 578838415  192 NLGRKELStIMDENNQWYCYICHP 215
Cdd:cd11726    80 NLGRAELS-RIEESDKWKCFVCDP 102
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1961-2111 1.12e-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: 178.82  E-value: 1.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1961 HSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELasrektedkdkpliykgegkwlRNIDYYRLDGSTTAQSR 2040
Cdd:cd18793     9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRE----------------------RGIKYLRLDGSTSSKER 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578838415 2041 KKWAEEFNDETNVRgrLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFL 2111
Cdd:cd18793    67 QKLVDRFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1536-2148 1.75e-39

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 161.51  E-value: 1.75e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1536 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLKDDEKLEVSElatvKRPQERSYMLQ 1615
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYLHEYRGIT-GPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPE----ERAHQREELLV 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1616 RWQEDggVMIIGYEMyrnlaqgrnvksrKLKEifNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTP 1695
Cdd:PLN03142  267 AGKFD--VCVTSFEM-------------AIKE--KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTP 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1696 LQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdVRVMKKrahiLYEMLAGCVQRKDYTALTKFLPPK 1775
Cdd:PLN03142  330 LQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ--------QEVVQQ----LHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1776 HEYVLAVRMTSIQCKLYQYYLDHLTGVGNnseggRGKAGAKLFQDFQMLSRIWTHPWCLQldyiskenkgyfdedsmdef 1855
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVN-----AGGERKRLLNIAMQLRKCCNHPYLFQ-------------------- 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1856 iasdsdetsmslssddytkkkkkgkkgkkdssssgsgsdndvevikvwnsrsrGGGEGNVDETGNNpsvslkleeskats 1935
Cdd:PLN03142  453 -----------------------------------------------------GAEPGPPYTTGEH-------------- 465
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1936 ssnpsspapdwykdfvtdadaeVLEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLelasrektedkdkplI 2015
Cdd:PLN03142  466 ----------------------LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYL---------------M 508
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 2016 YKGEGkwlrnidYYRLDGSTTAQSRKKWAEEFNDEtNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFR 2095
Cdd:PLN03142  509 YRGYQ-------YCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDR 580
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578838415 2096 VYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMNE 2148
Cdd:PLN03142  581 AHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNK 633
ADD_ATRX pfam17981
Cysteine Rich ADD domain; This is a cysteine-rich domain termed ADD (ATRX-DNMT3-DNMT3L, ...
103-158 6.14e-27

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: 105.21  E-value: 6.14e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578838415   103 KKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDS 158
Cdd:pfam17981    1 KRRGDAELSSIVNCTACGQQVNHFQRDSIYQHPVLKVLICKSCFKYYMSDDISKDE 56
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1963-2100 5.80e-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: 81.49  E-value: 5.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  1963 GKMVLLFEILRmaEEIGDKVLVFSQSLISLDliEDFLelasrektedkdkpliykgegKWLRNIDYYRLDGSTTAQSRKK 2042
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE--AELL---------------------LEKEGIKVARLHGDLSQEEREE 55
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578838415  2043 WAEEFNDETnvrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 2100
Cdd:pfam00271   56 ILEDFRKGK----IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
2024-2100 2.55e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 78.79  E-value: 2.55e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578838415   2024 RNIDYYRLDGSTTAQSRKKWAEEFNDETNVrgrlFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 2100
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXDc smart00487
DEAD-like helicases superfamily;
1503-1698 1.07e-15

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 77.92  E-value: 1.07e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415   1503 IKLKPHQVDGVQFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKldFSTALVVCPL-NTALNWMN 1581
Cdd:smart00487    7 EPLRPYQKEAIEALLSG------------LRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTrELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415   1582 EFEKWqegLKDDEKLEVSELATVKRPQErsymLQRWQEDGGVMIIG-YEMYrnlaqgrnvksrkLKEIFNKALVDPGPDF 1660
Cdd:smart00487   73 ELKKL---GPSLGLKVVGLYGGDSKREQ----LRKLESGKTDILVTtPGRL-------------LDLLENDKLSLSNVDL 132
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 578838415   1661 VVCDEGHILKNE--ASAVSKAMNSIR-SRRRIILTGTPLQN 1698
Cdd:smart00487  133 VILDEAHRLLDGgfGDQLEKLLKLLPkNVQLLLLSATPPEE 173
PTZ00121 PTZ00121
MAEBL; Provisional
736-1383 1.96e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  736 DTKKGKSAKSSIISKKKRQT--QSESSNYDSELEKEIKSMSKIGAARTTKKRIPNTKDFDSSEDEKHSKKGMDNQGHKNL 813
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEakKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK 1301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  814 KTSQEGSSDDAERKQERETFSSAEGTVDKdttimelRDRLPKKQQASASTDGVDKlsgKEESFTSLEVRKvAETKEKSKH 893
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKAEEAKKK-------ADAAKKKAEEAKKAAEAAK---AEAEAAADEAEA-AEEKAEAAE 1370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  894 LKTKTCKKVQDGLSDIAEKFLKKDQSDETSEDDKKQS---KKGTEEKKKPSDFKKKVIKMEQQYESSSDGTEKlPEREEI 970
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA-KKADEA 1449
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  971 CHFPKGIKQIKNGTTDGEKKSK----KIRDKTSKKKDELSDYAEKSTGKGDSCDSSED--KKSKNGAYGREKKRCKLLGK 1044
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKadeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKK 1529
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1045 SSRKRQDCSSSDTEKYSmKEDGCNSSDKRLKRIELR---------ERRNLSSKR-------NTKEIQSGSSSSDAEESSE 1108
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKK-KADELKKAEELKKAEEKKkaeeakkaeEDKNMALRKaeeakkaEEARIEEVMKLYEEEKKMK 1608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1109 DNKKKKQRTSSKKKAVIVKEKKRNSLRTSTKRKQADITSSSSSDIEDDDQNSI--GEGSSDEQKIKPVTENLVLSSHTgf 1186
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaAEEAKKAEEDKKKAEEAKKAEED-- 1686
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1187 cQSSGDEALSKsvpvtvddDDDDNDPENRIAKKMLLEEIKANLSSDEDGSSDDEPEEGKKRT---GKQNEENPGDEEAKN 1263
Cdd:PTZ00121 1687 -EKKAAEALKK--------EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAeedKKKAEEAKKDEEEKK 1757
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1264 QVNSESDSDSEESKKPRY-RHRLLRHKLTVSDGESGEEKKTKPKEHKE-----VKGRNRRKVSSEDSEDSDfqeSGVSEE 1337
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKeKEAVIEEELDEEDEKRRMEVDKKIKDIFDnfaniIEGGKEGNLVINDSKEME---DSAIKE 1834
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 578838415 1338 VSESEDEQRPRTRSAKKAELEENQRSykqkkkrrrikvQEDSSSEN 1383
Cdd:PTZ00121 1835 VADSKNMQLEEADAFEKHKFNKNNEN------------GEDGNKEA 1868
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
587-802 3.15e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 43.11  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  587 NEVSLLLEESDLRRSPRVKTTPLRRPTETNPVTSNsdeecnetvkEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSKQ 666
Cdd:PTZ00108 1170 RKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSD----------EKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSS 1239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  667 SETVDQNSDSDEMLAILKEVSRMSHSSSSDTDINEIHTNHKTLY---DLKTQAGKDDKGKRKRKSSTSGSDFDTKKGKSA 743
Cdd:PTZ00108 1240 VKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYsppPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLA 1319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578838415  744 KSSIiSKKKRQTQSESSNYDSELEKeiksmSKIGAARTTKKRIPNTKDFDSSEDEKHSK 802
Cdd:PTZ00108 1320 ALKK-KKKSEKKTARKKKSKTRVKQ-----ASASQSSRLLRRPRKKKSDSSSEDDDDSE 1372
 
Name Accession Description Interval E-value
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
1505-1748 3.88e-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: 493.64  E-value: 3.88e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKL-DFSTALVVCPLNTALNWMNEF 1583
Cdd:cd18068     1 LKPHQVDGVQFMWDCCCESLKKTKKSPGSGCILAHCMGLGKTLQVVTFLHTVLLCEKLeNFSRVLVVCPLNTVLNWLNEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1584 EKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSR-KLKEIFNKALVDPGPDFVV 1662
Cdd:cd18068    81 EKWQEGLKDEEKIEVNELATYKRPQERSYKLQRWQEEGGVMIIGYDMYRILAQERNVKSReKLKEIFNKALVDPGPDFVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1663 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDV 1742
Cdd:cd18068   161 CDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVDV 240

                  ....*.
gi 578838415 1743 RVMKKR 1748
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 ...
1505-1748 3.91e-116

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: 367.77  E-value: 3.91e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCCESvkKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKlDFSTALVVCPLNTALNWMNEFE 1584
Cdd:cd18007     1 LKPHQVEGVRFLWSNLVGT--DVGSDEGGGCILAHTMGLGKTLQVITFLHTYLAAAP-RRSRPLVLCPASTLYNWEDEFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1585 KWQEGLKDDEKLEVSeLATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNvKSRKLKEIFNKALVDPGPDFVVCD 1664
Cdd:cd18007    78 KWLPPDLRPLLVLVS-LSASKRADARLRKINKWHKEGGVLLIGYELFRNLASNAT-TDPRLKQEFIAALLDPGPDLLVLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1665 EGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDVRV 1744
Cdd:cd18007   156 EGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRL 235

                  ....
gi 578838415 1745 MKKR 1748
Cdd:cd18007   236 MLKR 239
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
1508-1834 9.32e-107

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: 343.13  E-value: 9.32e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  1508 HQVDGVQFMWDCCCEsvkktkksPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQ 1587
Cdd:pfam00176    1 YQIEGVNWMLSLENN--------LGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGGPTLIVVPLSLLHNWMNEFERWV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  1588 EglkdDEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGH 1667
Cdd:pfam00176   73 S----PPALRVVVLHGNKRPQERWKNDPNFLADFDVVITTYETLR-----------KHKELLKKV----HWHRIVLDEGH 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  1668 ILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdvrvMKK 1747
Cdd:pfam00176  134 RLKNSKSKLSKALKSLKTRNRWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGG-----------GKK 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  1748 RAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTSIQCKLYQ-YYLDHLTGVGNNSEGGRGKAgAKLFQDFQMLSR 1826
Cdd:pfam00176  203 GVSRLHKLLKPFLLRRTKKDVEKSLPPKVEYILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIK-ASLLNILMRLRK 281

                   ....*...
gi 578838415  1827 IWTHPWCL 1834
Cdd:pfam00176  282 ICNHPGLI 289
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
1488-2136 5.79e-86

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 297.52  E-value: 5.79e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1488 EETKEPLVQVHRNMVIKLKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTA 1567
Cdd:COG0553   225 RRLREALESLPAGLKATLRPYQLEGAAWLLFL---------RRLGLGGLLADDMGLGKTIQALALLLELKERGLAR--PV 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1568 LVVCPLNTALNWMNEFEKWQEGLKddeklevseLATVKRPQERSYMLQRWqEDGGVMIIGYEMYRNLAQgrnvksrklke 1647
Cdd:COG0553   294 LIVAPTSLVGNWQRELAKFAPGLR---------VLVLDGTRERAKGANPF-EDADLVITSYGLLRRDIE----------- 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1648 ifnkALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFIN 1727
Cdd:COG0553   353 ----LLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFAR 428
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1728 PIQNGQcadstmvdvrvmKKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTSIQCKLYQYYLDHLTGVGNNSE 1807
Cdd:COG0553   429 PIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGAE 496
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1808 GGRGKagAKLFQDFQMLSRIWTHPwclqldyiskenkgyfdedsmdefiasdsdetsmslssddytkkkkkgkkgkkdss 1887
Cdd:COG0553   497 GIRRR--GLILAALTRLRQICSHP-------------------------------------------------------- 518
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1888 ssgsgsdndvevikvwnsrsrgggegnvdetgnnpsvSLKLEESKATSssnpsspapdwykdfvtdadaevlEHSGKMVL 1967
Cdd:COG0553   519 -------------------------------------ALLLEEGAELS------------------------GRSAKLEA 537
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1968 LFEILRMAEEIGDKVLVFSQSLISLDLIEDFLElasrektedkdkpliykgegkwLRNIDYYRLDGSTTAQSRKKWAEEF 2047
Cdd:COG0553   538 LLELLEELLAEGEKVLVFSQFTDTLDLLEERLE----------------------ERGIEYAYLHGGTSAEERDELVDRF 595
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 2048 NDETNVrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTK 2127
Cdd:COG0553   596 QEGPEA--PVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGTIEEKILELLEEK 673

                  ....*....
gi 578838415 2128 QSLSFRVVD 2136
Cdd:COG0553   674 RALAESVLG 682
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
1505-1748 1.18e-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: 277.08  E-value: 1.18e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLdfSTALVVCPLNTALNWMNEFE 1584
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIESLERYKGSSGFGCILAHSMGLGKTLQVISFLDVLLRHTGA--KTVLAIVPVNTLQNWLSEFN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1585 KWQEGLKDDEKLEVSELAT------VKRPQERSYMLQRWQEDGGVMIIGYEMYRNlaqgrnvksrklkeifnkalvDPGP 1658
Cdd:cd18069    79 KWLPPPEALPNVRPRPFKVfilndeHKTTAARAKVIEDWVKDGGVLLMGYEMFRL---------------------RPGP 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1659 DFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADST 1738
Cdd:cd18069   138 DVVICDEGHRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQCVDST 217
                         250
                  ....*....|
gi 578838415 1739 MVDVRVMKKR 1748
Cdd:cd18069   218 PQDVKLMRYR 227
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
1505-1763 1.26e-61

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: 211.38  E-value: 1.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCccesVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVL---LCDKLDFSTALVVCPLNTALNWMN 1581
Cdd:cd18004     1 LRPHQREGVQFLYDC----LTGRRGYGGGGAILADEMGLGKTLQAIALVWTLLkqgPYGKPTAKKALIVCPSSLVGNWKA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1582 EFEKWqegLKDdEKLEVSELATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQGRNVKSRklkeifnkalvdpgPDFV 1661
Cdd:cd18004    77 EFDKW---LGL-RRIKVVTADGNAKDVKASLDFFSSASTYPVLIISYETLRRHAEKLSKKIS--------------IDLL 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1662 VCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVD 1741
Cdd:cd18004   139 ICDEGHRLKNSESKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEED 218
                         250       260
                  ....*....|....*....|..
gi 578838415 1742 VRVMKKRAHILYEMLAGCVQRK 1763
Cdd:cd18004   219 KELGAERSQELSELTSRFILRR 240
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
1505-1710 1.12e-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: 203.57  E-value: 1.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCCesvkktkksPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMNEFE 1584
Cdd:cd17919     1 LRPYQLEGLNFLLELYE---------NGPGGILADEMGLGKTLQAIAFLAY-LLKEGKERGPVLVVCPLSVLENWEREFE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1585 KWQEGLKddeklevseLATVKRPQERSYMLQ--RWQEDGGVMIIGYEMYRNLAQgrnvksrklkeifnkALVDPGPDFVV 1662
Cdd:cd17919    71 KWTPDLR---------VVVYHGSQRERAQIRakEKLDKFDVVLTTYETLRRDKA---------------SLRKFRWDLVV 126
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578838415 1663 CDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFI 1710
Cdd:cd17919   127 VDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPLQNNLEELWALLDFL 174
ADDz_ATRX cd11726
ADDz domain found in ATRX (alpha-thalassemia/mental retardation, X-linked); ADDz_ATRX is a ...
112-215 9.34e-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: 192.14  E-value: 9.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  112 GIVSCTACGQQVNHFqKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFCKKCILR 191
Cdd:cd11726     1 RRVRCTACGEQLNHF-SKEVHRHPVLKVLICKSCLKFYNSGEFSKDEDGSDEYCRWCGQGGDLICCDFCPNVFCKKCIKR 79
                          90       100
                  ....*....|....*....|....
gi 578838415  192 NLGRKELStIMDENNQWYCYICHP 215
Cdd:cd11726    80 NLGRAELS-RIEESDKWKCFVCDP 102
ADDz cd11672
ATRX, Dnmt3 and Dnmt3l PHD-like zinc finger domain (ADDz); The ADDz zinc finger domain is ...
112-215 5.37e-53

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: 181.22  E-value: 5.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  112 GIVSCTACGQQVnhfqkdSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCD--FCHNAFCKKCI 189
Cdd:cd11672     1 IEDICIACGSLV------VIYRHPLFQGGICKNCKKYFLSDDISYDDDGYQSYCRICCEGGNLLCCGnnFCHRCFCKECV 74
                          90       100
                  ....*....|....*....|....*.
gi 578838415  190 LRNLGRKELSTiMDENNQWYCYICHP 215
Cdd:cd11672    75 DRLVGPGELST-MDENNQWYCYICHP 99
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1961-2111 1.12e-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: 178.82  E-value: 1.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1961 HSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLELasrektedkdkpliykgegkwlRNIDYYRLDGSTTAQSR 2040
Cdd:cd18793     9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRE----------------------RGIKYLRLDGSTSSKER 66
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578838415 2041 KKWAEEFNDETNVRgrLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPVYVYRFL 2111
Cdd:cd18793    67 QKLVDRFNEDPDIR--VFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
1505-1763 2.45e-46

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: 167.65  E-value: 2.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCcesvkKTKKSPGS-GCILAHCMGLGKTLQVVSFLHTVL----LCdKLDFSTALVVCPLNTALNW 1579
Cdd:cd18067     1 LRPHQREGVKFLYRCV-----TGRRIRGShGCIMADEMGLGKTLQCITLMWTLLrqspQC-KPEIDKAIVVSPSSLVKNW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1580 MNEFEKWQEGlkddeklEVSELATV-KRPQERSYMLQRWQEDGG------VMIIGYEMYRNLAqgrnvksrklkEIFNKA 1652
Cdd:cd18067    75 ANELGKWLGG-------RLQPLAIDgGSKKEIDRKLVQWASQQGrrvstpVLIISYETFRLHV-----------EVLQKG 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1653 LVDpgpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNG 1732
Cdd:cd18067   137 EVG----LVICDEGHRLKNSDNQTYQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKG 212
                         250       260       270
                  ....*....|....*....|....*....|.
gi 578838415 1733 QCADSTMVDVRVMKKRAHILYEMLAGCVQRK 1763
Cdd:cd18067   213 RDADASEKERQLGEEKLQELISIVNRCIIRR 243
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
1505-1738 7.21e-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: 160.23  E-value: 7.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWdcccesvkkTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTALVVCPLNTALNWMNEFE 1584
Cdd:cd18001     1 LYPHQREGVAWLW---------SLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIK--SVLVVMPTSLIPHWVKEFA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1585 KWQEGLkddeklevselaTVK-----RPQERSYMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEIFNKALVdpgPD 1659
Cdd:cd18001    70 KWTPGL------------RVKvfhgtSKKERERNLERIQRGGGVLLTTYGMVLSNTE-------QLSADDHDEFK---WD 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1660 FVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFI-KENLLGSIKEFRNRFINPIQNGQCADST 1738
Cdd:cd18001   128 YVILDEGHKIKNSKTKSAKSLREIPAKNRIILTGTPIQNNLKELWALFDFAcNGSLLGTRKTFKMEFENPITRGRDKDAT 207
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
1505-1748 9.02e-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: 9.02e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVL----------------LCDKLDFS--- 1565
Cdd:cd18005     1 LRDYQREGVEFMYDLYKN---------GRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrdrennrprfKKKPPASSakk 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1566 TALVVCPLNTALNWMNEFEKWQEglkddekLEVSELATVKRPQERSYMLQRWQEDggVMIIGYEMYRNLAQGrnvksrkL 1645
Cdd:cd18005    72 PVLIVAPLSVLYNWKDELDTWGH-------FEVGVYHGSRKDDELEGRLKAGRLE--VVVTTYDTLRRCIDS-------L 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1646 KEIfnkalvdpGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1725
Cdd:cd18005   136 NSI--------NWSAVIADEAHRIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHF 207
                         250       260
                  ....*....|....*....|...
gi 578838415 1726 INPIQNGQCADSTMVDVRVMKKR 1748
Cdd:cd18005   208 SEPIKRGQRHTATARELRLGRKR 230
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
1536-2148 1.75e-39

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 161.51  E-value: 1.75e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1536 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLKDDEKLEVSElatvKRPQERSYMLQ 1615
Cdd:PLN03142  192 ILADEMGLGKTLQTISLLGYLHEYRGIT-GPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPE----ERAHQREELLV 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1616 RWQEDggVMIIGYEMyrnlaqgrnvksrKLKEifNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTP 1695
Cdd:PLN03142  267 AGKFD--VCVTSFEM-------------AIKE--KTALKRFSWRYIIIDEAHRIKNENSLLSKTMRLFSTNYRLLITGTP 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1696 LQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQcadstmvdVRVMKKrahiLYEMLAGCVQRKDYTALTKFLPPK 1775
Cdd:PLN03142  330 LQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ--------QEVVQQ----LHKVLRPFLLRRLKSDVEKGLPPK 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1776 HEYVLAVRMTSIQCKLYQYYLDHLTGVGNnseggRGKAGAKLFQDFQMLSRIWTHPWCLQldyiskenkgyfdedsmdef 1855
Cdd:PLN03142  398 KETILKVGMSQMQKQYYKALLQKDLDVVN-----AGGERKRLLNIAMQLRKCCNHPYLFQ-------------------- 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1856 iasdsdetsmslssddytkkkkkgkkgkkdssssgsgsdndvevikvwnsrsrGGGEGNVDETGNNpsvslkleeskats 1935
Cdd:PLN03142  453 -----------------------------------------------------GAEPGPPYTTGEH-------------- 465
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1936 ssnpsspapdwykdfvtdadaeVLEHSGKMVLLFEILRMAEEIGDKVLVFSQSLISLDLIEDFLelasrektedkdkplI 2015
Cdd:PLN03142  466 ----------------------LVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYL---------------M 508
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 2016 YKGEGkwlrnidYYRLDGSTTAQSRKKWAEEFNDEtNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFR 2095
Cdd:PLN03142  509 YRGYQ-------YCRIDGNTGGEDRDASIDAFNKP-GSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDR 580
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578838415 2096 VYRFGQTKPVYVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMNE 2148
Cdd:PLN03142  581 AHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGRLAEQKTVNK 633
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
1505-1763 1.66e-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: 141.91  E-value: 1.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCccesVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLD-----FSTALVVCPLNTALNW 1579
Cdd:cd18066     1 LRPHQREGIEFLYEC----VMGMRVNERFGAILADEMGLGKTLQCISLIWT-LLRQGPYggkpvIKRALIVTPGSLVKNW 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1580 MNEFEKWQeglkDDEKLEVSELATVKRPQE--RSYMLQrwqedggVMIIGYEMY-RNLAQGRNVKSrklkeifnkalvdp 1656
Cdd:cd18066    76 KKEFQKWL----GSERIKVFTVDQDHKVEEfiASPLYS-------VLIISYEMLlRSLDQISKLNF-------------- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1657 gpDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCAD 1736
Cdd:cd18066   131 --DLVICDEGHRLKNTSIKTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPT 208
                         250       260
                  ....*....|....*....|....*..
gi 578838415 1737 STMVDVRVMKKRAHILYEMLAGCVQRK 1763
Cdd:cd18066   209 ATPEEKKLGEARAAELTRLTGLFILRR 235
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
1505-1737 1.69e-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: 126.91  E-value: 1.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGV---QFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfsTALVVCPLNTALNWMN 1581
Cdd:cd18012     5 LRPYQKEGFnwlSFLRHY------------GLGGILADDMGLGKTLQTLALLLSRKEEGRKG--PSLVVAPTSLIYNWEE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1582 EFEKWQEGLKddeklevselATVKRPQERSYMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEI-FNkalvdpgpdF 1660
Cdd:cd18012    71 EAAKFAPELK----------VLVIHGTKRKREKLRALEDYDLVITSYGLLRRDIE-------LLKEVkFH---------Y 124
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578838415 1661 VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADS 1737
Cdd:cd18012   125 LVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGDEEA 201
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
1505-1711 1.68e-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: 123.20  E-value: 1.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCCESVkktkkspgsGCILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEFE 1584
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRV---------GGILGDEMGLGKTIQIIAFL-AALHHSKLGLGPSLIVCPATVLKQWVKEFH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1585 KW------------QEGLKDDEKLEVSELATVKRPQERsymlqrwqEDGGVMIIGYEMYRnlaqgrnvksrklkeIFNKA 1652
Cdd:cd18000    71 RWwppfrvvvlhssGSGTGSEEKLGSIERKSQLIRKVV--------GDGGILITTYEGFR---------------KHKDL 127
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578838415 1653 LVDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK 1711
Cdd:cd18000   128 LLNHNWQYVILDEGHKIRNPDAEITLACKQLRTPHRLILSGTPIQNNLKELWSLFDFVF 186
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
1505-1729 3.53e-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: 115.14  E-value: 3.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWdcccesvkKTKKSPGSGcILAHCMGLGKTLQVVSFLHTVLLCDKLDFST----ALVVCPLNTALNWM 1580
Cdd:cd17999     1 LRPYQQEGINWLA--------FLNKYNLHG-ILCDDMGLGKTLQTLCILASDHHKRANSFNSenlpSLVVCPPTLVGHWV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1581 NEFEKWqeglKDDEKLEVseLATVKRPQERSyMLQRWQEDGGVMIIGYEMYRNLAQgrnvksrKLKEI-FNkalvdpgpd 1659
Cdd:cd17999    72 AEIKKY----FPNAFLKP--LAYVGPPQERR-RLREQGEKHNVIVASYDVLRNDIE-------VLTKIeWN--------- 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1660 FVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI 1729
Cdd:cd17999   129 YCVLDEGHIIKNSKTKLSKAVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPI 198
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
1504-1725 9.05e-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: 114.02  E-value: 9.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1504 KLKPHQVDGVQFMwdcccesvkKTKKSPGSGCILAHCMGLGKTLQVVSFLhtVLLCDKLDFSTALVVCPLNTALNWMNEF 1583
Cdd:cd18009     3 VMRPYQLEGMEWL---------RMLWENGINGILADEMGLGKTIQTIALL--AHLRERGVWGPFLVIAPLSTLPNWVNEF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1584 EKWQ--------EGLKDDEKlevsELATVKRPQERSYMlqrwqeDGGVMIIGYEMYRNLAqgrnvksrklkeifnKALVD 1655
Cdd:cd18009    72 ARFTpsvpvllyHGTKEERE----RLRKKIMKREGTLQ------DFPVVVTSYEIAMRDR---------------KALQH 126
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1656 PGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1725
Cdd:cd18009   127 YAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWF 196
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
1505-1725 3.11e-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: 111.96  E-value: 3.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFE 1584
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYN---------RRNCILADEMGLGKTIQSIAFLEHLYQVEGIR-GPFLVIAPLSTIPNWQREFE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1585 KWqeglkddeklevSELATVkrpqersymLQRWQEDGGVMIIGYEMYRNLAQGRnVKSRKLK--------EIFNK---AL 1653
Cdd:cd17995    71 TW------------TDMNVV---------VYHGSGESRQIIQQYEMYFKDAQGR-KKKGVYKfdvlittyEMVIAdaeEL 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578838415 1654 VDPGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1725
Cdd:cd17995   129 RKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEF 200
ADD_ATRX pfam17981
Cysteine Rich ADD domain; This is a cysteine-rich domain termed ADD (ATRX-DNMT3-DNMT3L, ...
103-158 6.14e-27

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: 105.21  E-value: 6.14e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 578838415   103 KKRGEDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSDDISRDS 158
Cdd:pfam17981    1 KRRGDAELSSIVNCTACGQQVNHFQRDSIYQHPVLKVLICKSCFKYYMSDDISKDE 56
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
1504-1731 3.49e-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: 109.38  E-value: 3.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1504 KLKPHQVDGVQFMWdccceSVKKTKKSPgsgcILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEF 1583
Cdd:cd17996     3 TLKEYQLKGLQWMV-----SLYNNNLNG----ILADEMGLGKTIQTISLI-TYLMEKKKNNGPYLVIVPLSTLSNWVSEF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1584 EKWQEglkddeklEVSELATVKRPQERSyMLQRWQEDG--GVMIIGYEMYrnlaqgrnVKSR-KLKEIFNKalvdpgpdF 1660
Cdd:cd17996    73 EKWAP--------SVSKIVYKGTPDVRK-KLQSQIRAGkfNVLLTTYEYI--------IKDKpLLSKIKWK--------Y 127
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578838415 1661 VVCDEGHILKNEASAVSKAMNS-IRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQN 1731
Cdd:cd17996   128 MIIDEGHRMKNAQSKLTQTLNTyYHARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFAN 199
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
1505-1710 4.70e-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: 104.39  E-value: 4.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMwdcccESVKKTKKSpgsgCILAHCMGLGKTLQVVSFLhtVLLCDKLDFSTALVVCPLNTALNWMNEFE 1584
Cdd:cd17998     1 LKDYQLIGLNWL-----NLLYQKKLS----GILADEMGLGKTIQVIAFL--AYLKEIGIPGPHLVVVPSSTLDNWLREFK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1585 KWQEGLKddekLEVSELATVKRPQERsYMLQRWQEDGGVMIIGYemyrNLAQGrNVKSRKLKEIFNKalvdpgpDFVVCD 1664
Cdd:cd17998    70 RWCPSLK----VEPYYGSQEERKHLR-YDILKGLEDFDVIVTTY----NLATS-NPDDRSFFKRLKL-------NYVVYD 132
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578838415 1665 EGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFI 1710
Cdd:cd17998   133 EGHMLKNMTSERYRHLMTINANFRLLLTGTPLQNNLLELMSLLNFI 178
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
1536-1729 1.43e-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: 104.36  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1536 ILAHCMGLGKTLQVVSFL-HtvLLCDKLDFSTALVVCPLNTALNWMNEFEKWQEGLKddeklevsELATVKRPQERSYML 1614
Cdd:cd18003    23 ILADEMGLGKTIQTIALLaH--LACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFK--------ILTYYGSAKERKLKR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1615 QRWQEDGG--VMIIGYEMyrnLAQGRNV-KSRKLKeifnkalvdpgpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIIL 1691
Cdd:cd18003    93 QGWMKPNSfhVCITSYQL---VVQDHQVfKRKKWK-------------YLILDEAHNIKNFKSQRWQTLLNFNTQRRLLL 156
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 578838415 1692 TGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI 1729
Cdd:cd18003   157 TGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPL 194
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
1536-1721 1.34e-22

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: 98.55  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1536 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLKddekleVSELATVKrpQERSYMLQ 1615
Cdd:cd17997    26 ILADEMGLGKTLQTISLLGYLKHYKNIN-GPHLIIVPKSTLDNWMREFKRWCPSLR------VVVLIGDK--EERADIIR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1616 RWQEDG--GVMIIGYEMYRnlaqgrnvksrKLKEIFNKAlvdpGPDFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTG 1693
Cdd:cd17997    97 DVLLPGkfDVCITSYEMVI-----------KEKTVLKKF----NWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTG 161
                         170       180
                  ....*....|....*....|....*...
gi 578838415 1694 TPLQNNLIEYHCMVNFIKENLLGSIKEF 1721
Cdd:cd17997   162 TPLQNNLHELWALLNFLLPDVFTSSEDF 189
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
1504-1721 2.41e-22

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: 97.81  E-value: 2.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1504 KLKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEF 1583
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCK---------GNNGILADEMGLGKTVQTISFL-SYLFHSQQQYGPFLVVVPLSTMPAWQREF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1584 EKWQEGLKddeklEVSELATVKRPQersymlqrwqedggvMIIGYEMYRNlaqgrnvKSRKLK--------EIFNKALVD 1655
Cdd:cd17993    71 AKWAPDMN-----VIVYLGDIKSRD---------------TIREYEFYFS-------QTKKLKfnvllttyEIILKDKAF 123
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578838415 1656 PGP---DFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEF 1721
Cdd:cd17993   124 LGSikwQYLAVDEAHRLKNDESLLYEALKEFKTNNRLLITGTPLQNSLKELWALLHFLMPGKFDIWEEF 192
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
1505-1733 1.18e-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: 96.20  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMwdCCCesvkktkkspgsGCILAHCMGLGKTLQVVSFLHTVLLCD---------------KLDFSTA-L 1568
Cdd:cd18008     1 LLPYQKQGLAWM--LPR------------GGILADEMGLGKTIQALALILATRPQDpkipeeleenssdpkKLYLSKTtL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1569 VVCPLNTALNWMNEFEK-------------WQEGLKDDEKLEvselatvkrpqerSYMlqrwqedggVMIIGYEMYRNLA 1635
Cdd:cd18008    67 IVVPLSLLSQWKDEIEKhtkpgslkvyvyhGSKRIKSIEELS-------------DYD---------IVITTYGTLASEF 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1636 QGRNVKSRKLKEifnkaLVDPGPDF------VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNF 1709
Cdd:cd18008   125 PKNKKGGGRDSK-----EKEASPLHrirwyrVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRF 199
                         250       260
                  ....*....|....*....|....
gi 578838415 1710 IKENLLGSIKEFRNRFINPIQNGQ 1733
Cdd:cd18008   200 LRVEPFGDYPWFNSDISKPFSKND 223
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
1505-1727 2.26e-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: 94.81  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEFE 1584
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAE---------QHGCILGDEMGLGKTCQTISLL-WYLAGRLKLLGPFLVLCPLSVLDNWKEELN 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1585 KWQEGLK----DDEKLEVSELatvkrpQERSYMLQRWQedggVMIIGYEMYrnLAQGRNVKSRKLKeifnkalvdpgpdF 1660
Cdd:cd18006    71 RFAPDLSvityMGDKEKRLDL------QQDIKSTNRFH----VLLTTYEIC--LKDASFLKSFPWA-------------S 125
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578838415 1661 VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGsiKEFRNRFIN 1727
Cdd:cd18006   126 LVVDEAHRLKNQNSLLHKTLSEFSVDFRLLLTGTPIQNSLQELYALLSFIEPNVFP--KDKLDDFIK 190
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
1505-1736 6.31e-21

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: 93.42  E-value: 6.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFmwdccceSVKKtkkspGSGCILAHCMGLGKTLQVVsflhTVLLCDKLDFStALVVCPLNTALNWMNEFE 1584
Cdd:cd18010     1 LLPFQREGVCF-------ALRR-----GGRVLIADEMGLGKTVQAI----AIAAYYREEWP-LLIVCPSSLRLTWADEIE 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1585 KWqegLKDDEKLEVSELATVKRPQERSymlqrwqeDGGVMIIGYEMyrnlaqgrnvkSRKLKEIFNKAlvdpGPDFVVCD 1664
Cdd:cd18010    64 RW---LPSLPPDDIQVIVKSKDGLRDG--------DAKVVIVSYDL-----------LRRLEKQLLAR----KFKVVICD 117
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578838415 1665 EGHILKNEASAVSKAMNSI--RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCAD 1736
Cdd:cd18010   118 ESHYLKNSKAKRTKAALPLlkRAKRVILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYCAAKQGGFGWD 191
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
1503-1732 3.69e-19

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: 88.91  E-value: 3.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1503 IKLKPHQVDGVQFM---WdCCCESVkktkkspgsgcILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNW 1579
Cdd:cd18054    19 LELRDYQLEGLNWLahsW-CKNNSV-----------ILADEMGLGKTIQTISFL-SYLFHQHQLYGPFLLVVPLSTLTSW 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1580 MNEFEKWQEGLkdDEKLEVSELATVKRPQERSYMLQRWQE-DGGVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgp 1658
Cdd:cd18054    86 QREFEIWAPEI--NVVVYIGDLMSRNTIREYEWIHSQTKRlKFNALITTYEIL--------LKDKTVLGSINWA------ 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578838415 1659 dFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNG 1732
Cdd:cd18054   150 -FLGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDHGKGRENG 222
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1963-2100 5.80e-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: 81.49  E-value: 5.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  1963 GKMVLLFEILRmaEEIGDKVLVFSQSLISLDliEDFLelasrektedkdkpliykgegKWLRNIDYYRLDGSTTAQSRKK 2042
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE--AELL---------------------LEKEGIKVARLHGDLSQEEREE 55
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 578838415  2043 WAEEFNDETnvrgRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 2100
Cdd:pfam00271   56 ILEDFRKGK----IDVLVATDVAERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
HELICc smart00490
helicase superfamily c-terminal domain;
2024-2100 2.55e-17

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 78.79  E-value: 2.55e-17
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578838415   2024 RNIDYYRLDGSTTAQSRKKWAEEFNDETNVrgrlFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFG 2100
Cdd:smart00490   10 LGIKVARLHGGLSQEEREEILDKFNNGKIK----VLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
1504-1775 4.01e-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: 83.18  E-value: 4.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1504 KLKPHQVDGVQFMWdcccesvkkTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEF 1583
Cdd:cd18064    15 KLRDYQVRGLNWLI---------SLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIP-GPHMVLVPKSTLHNWMAEF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1584 EKWQEGLKD-----DEKLEVSELATVKRPQErsymlqrWQedggVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgp 1658
Cdd:cd18064    85 KRWVPTLRAvcligDKDQRAAFVRDVLLPGE-------WD----VCVTSYEML--------IKEKSVFKKFNWR------ 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1659 dFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINpiqNGQCADST 1738
Cdd:cd18064   140 -YLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDT---NNCLGDQK 215
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 578838415 1739 MVDVRVMKKRAHILyemlagcvqRKDYTALTKFLPPK 1775
Cdd:cd18064   216 LVERLHMVLRPFLL---------RRIKADVEKSLPPK 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
1532-1725 1.05e-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: 81.60  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1532 GSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLK-----DDEKLEVSELATVKR 1606
Cdd:cd18065    34 GVNGILADEMGLGKTLQTIALLGYLKHYRNIP-GPHMVLVPKSTLHNWMNEFKRWVPSLRavcliGDKDARAAFIRDVMM 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1607 PQErsymlqrWQedggVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdpgpdFVVCDEGHILKNEASAVSKAMNSIRSR 1686
Cdd:cd18065   113 PGE-------WD----VCVTSYEMV--------IKEKSVFKKFNWR-------YLVIDEAHRIKNEKSKLSEIVREFKTT 166
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 578838415 1687 RRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1725
Cdd:cd18065   167 NRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWF 205
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
1505-1725 1.49e-16

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: 80.18  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMN 1581
Cdd:cd17994     1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTIQTIVFLYS-LYKEGHSKGPFLVSAPLSTIINWER 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1582 EFEKWqeglkddekleVSELATVkrpqerSYMLQRwqedggVMIIGYEMYrnlaqgrNVKSRKLKEIFNKALVdpgpdfv 1661
Cdd:cd17994    68 EFEMW-----------APDFYVV------TYVGDH------VLLTSYELI-------SIDQAILGSIDWAVLV------- 110
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578838415 1662 vCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1725
Cdd:cd17994   111 -VDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEF 173
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
1505-1730 2.13e-16

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: 80.47  E-value: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMwdcccesvkktKKSPGSGCILAhcMGLGKTLQVVSFLHTVLLCDKLdfSTALVVCPLNTALN-WMNEF 1583
Cdd:cd18013     1 PHPYQKVAINFI-----------IEHPYCGLFLD--MGLGKTVTTLTALSDLQLDDFT--RRVLVIAPLRVARStWPDEV 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1584 EKWqEGLKDdekLEVSelATVKRPQERSYMLQRwqeDGGVMIIGYEmyrnlaqgrNVKsrKLKEIFNkalvDPGP-DFVV 1662
Cdd:cd18013    66 EKW-NHLRN---LTVS--VAVGTERQRSKAANT---PADLYVINRE---------NLK--WLVNKSG----DPWPfDMVV 121
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578838415 1663 CDEGHILKNEASAVSKAMNSIRSR-RRII-LTGTPLQNNLIEYHCMVNFIK--ENLLGSIKEFRNRFINPIQ 1730
Cdd:cd18013   122 IDELSSFKSPRSKRFKALRKVRPViKRLIgLTGTPSPNGLMDLWAQIALLDqgERLGRSITAYRERWFDPDK 193
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
1505-1721 3.87e-16

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: 80.11  E-value: 3.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMN 1581
Cdd:cd18057     1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTVQTIVFLYS-LYKEGHSKGPYLVSAPLSTIINWER 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1582 EFEKWQEGLKDDEKLEVSELATVKRPQERSYmlqrwqEDGGVMIiGYEMYRnLAQGRNVKSRKLKEIFNKALVDPGP--- 1658
Cdd:cd18057    68 EFEMWAPDFYVVTYTGDKESRSVIRENEFSF------EDNAIRS-GKKVFR-MKKEAQIKFHVLLTSYELITIDQAIlgs 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1659 ---DFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK----ENLLGSIKEF 1721
Cdd:cd18057   140 iewACLVVDEAHRLKNNQSKFFRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTperfNNLEGFLEEF 209
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
1503-1721 4.89e-16

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: 80.09  E-value: 4.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1503 IKLKPHQVDGVQFMWDCCCEsvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLdFSTALVVCPLNTALNWMNE 1582
Cdd:cd18053    19 LELRDYQLNGLNWLAHSWCK---------GNSCILADEMGLGKTIQTISFLNYLFHEHQL-YGPFLLVVPLSTLTSWQRE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1583 FEKWQEG------LKDDEKLEVSELATVKRPQERSYMLQrwqedggVMIIGYEMYrnlaqgrnVKSRKLKEIFNKAlvdp 1656
Cdd:cd18053    89 IQTWAPQmnavvyLGDINSRNMIRTHEWMHPQTKRLKFN-------ILLTTYEIL--------LKDKSFLGGLNWA---- 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578838415 1657 gpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEF 1721
Cdd:cd18053   150 ---FIGVDEAHRLKNDDSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDF 211
DEXDc smart00487
DEAD-like helicases superfamily;
1503-1698 1.07e-15

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 77.92  E-value: 1.07e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415   1503 IKLKPHQVDGVQFMWDCccesvkktkkspGSGCILAHCMGLGKTLQVVSFLHTVLLCDKldFSTALVVCPL-NTALNWMN 1581
Cdd:smart00487    7 EPLRPYQKEAIEALLSG------------LRDVILAAPTGSGKTLAALLPALEALKRGK--GGRVLVLVPTrELAEQWAE 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415   1582 EFEKWqegLKDDEKLEVSELATVKRPQErsymLQRWQEDGGVMIIG-YEMYrnlaqgrnvksrkLKEIFNKALVDPGPDF 1660
Cdd:smart00487   73 ELKKL---GPSLGLKVVGLYGGDSKREQ----LRKLESGKTDILVTtPGRL-------------LDLLENDKLSLSNVDL 132
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 578838415   1661 VVCDEGHILKNE--ASAVSKAMNSIR-SRRRIILTGTPLQN 1698
Cdd:smart00487  133 VILDEAHRLLDGgfGDQLEKLLKLLPkNVQLLLLSATPPEE 173
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
1535-1725 1.87e-15

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: 77.77  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1535 CILAHCMGLGKTLQVVSFLHTVLLCDKldFSTALVVCPLNTALNWMNEFEKWQEglkddEKLEVSELATVKRPqersyml 1614
Cdd:cd18058    22 CILADEMGLGKTIQSITFLSEIFLMGI--RGPFLIIAPLSTITNWEREFRTWTE-----MNAIVYHGSQISRQ------- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1615 qrwqedggvMIIGYEMYRNLAQGRNV----KSRKLKEIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 1683
Cdd:cd18058    88 ---------MIQQYEMYYRDEQGNPLsgifKFQVVITTFEMILAD-CPELkkinwscVIIDEAHRLKNRNCKLLEGLKLM 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578838415 1684 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1725
Cdd:cd18058   158 ALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEF 199
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
1535-1725 2.03e-15

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: 77.76  E-value: 2.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1535 CILAHCMGLGKTLQVVSFLHTVLLcdKLDFSTALVVCPLNTALNWMNEFEKWqeglkddeklevSELATVkrpqersymL 1614
Cdd:cd18059    22 CILADEMGLGKTIQSITFLYEIYL--KGIHGPFLVIAPLSTIPNWEREFRTW------------TELNVV---------V 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1615 QRWQEDGGVMIIGYEMYRNLAQGRNVK-SRKLKEI---FNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 1683
Cdd:cd18059    79 YHGSQASRRTIQLYEMYFKDPQGRVIKgSYKFHAIittFEMILTD-CPELrnipwrcVVIDEAHRLKNRNCKLLEGLKMM 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578838415 1684 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1725
Cdd:cd18059   158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEF 199
ADDz_Dnmt3 cd11725
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 (Dnmt3); Dnmt3 is a de ...
116-218 4.04e-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: 73.19  E-value: 4.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  116 CTACGQQVNhfqkDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCD--FCHNAFCKKCILRNL 193
Cdd:cd11725     5 CLACGSLEV----SETSDHPFFEGGLCKNCKERFLECIFLFDDDGYQMYCTICGGGGEVVLCDnpDCTRVYCTECLDLLL 80
                          90       100
                  ....*....|....*....|....*
gi 578838415  194 GRKELSTIMDENNqWYCYICHPEPL 218
Cdd:cd11725    81 GPGAVAKILESDP-WFCFLCSPESN 104
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
1536-1750 5.32e-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: 5.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1536 ILAHCMGLGKTLQVVSFLHTVLLCDKLDfSTALVVCPLNTALNWMNEFEKWQEGLKddeKLEVSELATVKR---PQERSY 1612
Cdd:cd18063    46 ILADEMGLGKTIQTIALITYLMEHKRLN-GPYLIIVPLSTLSNWTYEFDKWAPSVV---KISYKGTPAMRRslvPQLRSG 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1613 MLQrwqedggVMIIGYEMYrnlaqgrnVKSRKLkeifnkaLVDPGPDFVVCDEGHILKNEASAVSKAMNS-IRSRRRIIL 1691
Cdd:cd18063   122 KFN-------VLLTTYEYI--------IKDKHI-------LAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRILL 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1692 TGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI-QNGQCADSTMVDVRVMKKRAH 1750
Cdd:cd18063   180 TGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGERVDLNEEETILIIRRLH 239
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
1505-1731 7.59e-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: 7.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDCccesvkktkKSPGSGCILAHCMGLGKTLQVVSFLhtVLLCDKLD-FSTALVVCPLNTALNWMNEF 1583
Cdd:cd18002     1 LKEYQLKGLNWLANL---------YEQGINGILADEMGLGKTVQSIAVL--AHLAEEHNiWGPFLVIAPASTLHNWQQEI 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1584 EKWQEGLKddeklevsELATVKRPQERSYMLQRWQ------EDGG--VMIIGYEMY-RNLAQGRNVKSRklkeifnkalv 1654
Cdd:cd18002    70 SRFVPQFK--------VLPYWGNPKDRKVLRKFWDrknlytRDAPfhVVITSYQLVvQDEKYFQRVKWQ----------- 130
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578838415 1655 dpgpdFVVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQN 1731
Cdd:cd18002   131 -----YMVLDEAQAIKSSSSSRWKTLLSFHCRNRLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIES 202
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
1505-1721 8.16e-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: 76.26  E-value: 8.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGV---QFMWdcccesvkktkkSPGSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMN 1581
Cdd:cd18056     1 LHPYQLEGLnwlRFSW------------AQGTDTILADEMGLGKTVQTAVFLYS-LYKEGHSKGPFLVSAPLSTIINWER 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1582 EFEKWQEGLKDDEKLEVSELATVKRPQERSYmlqrwqEDGGVMiiGYEMYRNLAQGRNVKSRKLKEIFNKALVDPGP--- 1658
Cdd:cd18056    68 EFEMWAPDMYVVTYVGDKDSRAIIRENEFSF------EDNAIR--GGKKASRMKKEASVKFHVLLTSYELITIDMAIlgs 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1659 -DF--VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK----ENLLGSIKEF 1721
Cdd:cd18056   140 iDWacLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTperfHNLEGFLEEF 209
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
1532-1725 8.97e-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: 76.20  E-value: 8.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1532 GSGCILAHCMGLGKTLQVVSFLHTvLLCDKLDFSTALVVCPLNTALNWMNEFEKWQ--------EGLKDDEKL----EVS 1599
Cdd:cd18055    19 GTDTILADEMGLGKTIQTIVFLYS-LYKEGHTKGPFLVSAPLSTIINWEREFQMWApdfyvvtyTGDKDSRAIirenEFS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1600 ELATVKRPQERSYMLQR-WQEDGGVMIIGYEMYrnlaqgrNVKSRKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSK 1678
Cdd:cd18055    98 FDDNAVKGGKKAFKMKReAQVKFHVLLTSYELV-------TIDQAALGSIRWACL--------VVDEAHRLKNNQSKFFR 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578838415 1679 AMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1725
Cdd:cd18055   163 VLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF 209
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
1536-1750 4.55e-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: 74.31  E-value: 4.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1536 ILAHCMGLGKTLQVVSFLhTVLLCDKLDFSTALVVCPLNTALNWMNEFEKWQEglkddeklEVSELATVKRPQ-ERSYML 1614
Cdd:cd18062    46 ILADEMGLGKTIQTIALI-TYLMEHKRINGPFLIIVPLSTLSNWVYEFDKWAP--------SVVKVSYKGSPAaRRAFVP 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1615 QRWQEDGGVMIIGYEMYrnlaqgrnVKSRKLkeifnkaLVDPGPDFVVCDEGHILKNEASAVSKAMNS-IRSRRRIILTG 1693
Cdd:cd18062   117 QLRSGKFNVLLTTYEYI--------IKDKQI-------LAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLLLTG 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578838415 1694 TPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPI-QNGQCADSTMVDVRVMKKRAH 1750
Cdd:cd18062   182 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLH 239
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
1497-1732 5.45e-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: 74.04  E-value: 5.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1497 VHRNMVIKLKPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSflhtVLLCDKldfstALVVCPLNTA 1576
Cdd:cd18071    13 VSRENSQDLPPFWEEAVGLFLNTITNFSQKKRPELVRGGILADDMGLGKTLTTIS----LILANF-----TLIVCPLSVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1577 LNWMNEFEKwqeglkddeklevselaTVKRPQERSYMlqrwqedggvmiigyemYRNLAQGRNVKSRKLKEI----FNKA 1652
Cdd:cd18071    84 SNWETQFEE-----------------HVKPGQLKVYT-----------------YHGGERNRDPKLLSKYDIvlttYNTL 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1653 LVDPG--PDF---------VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIKENLLgSIKEF 1721
Cdd:cd18071   130 ASDFGakGDSplhtinwlrVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLLSFLHLKPF-SNPEY 208
                         250
                  ....*....|..
gi 578838415 1722 RNRFI-NPIQNG 1732
Cdd:cd18071   209 WRRLIqRPLTMG 220
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
1535-1725 1.80e-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: 71.96  E-value: 1.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1535 CILAHCMGLGKTLQVVSFLHTVLLCD-KLDFstaLVVCPLNTALNWMNEFEKWQeglkdDEKLEVSELATVKRPqersyM 1613
Cdd:cd18061    22 CILADEMGLGKTIQSITFLYEILLTGiRGPF---LIIAPLSTIANWEREFRTWT-----DLNVVVYHGSLISRQ-----M 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1614 LQRwqedggvmiigYEMYRNLAQGRNVK-SRKLKEIFN--KALVDPGPDF-------VVCDEGHILKNEASAVSKAMNSI 1683
Cdd:cd18061    89 IQQ-----------YEMYFRDSQGRIIRgAYRFQAIITtfEMILGGCPELnaidwrcVIIDEAHRLKNKNCKLLEGLKLM 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578838415 1684 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1725
Cdd:cd18061   158 NLEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEF 199
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
1535-1725 2.12e-13

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: 72.01  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1535 CILAHCMGLGKTLQVVSFLHTVLLCDKLdfSTALVVCPLNTALNWMNEFEKWQEGlkdDEKLEVSELATVKrpqersyml 1614
Cdd:cd18060    22 CILADEMGLGKTIQSIAFLQEVYNVGIH--GPFLVIAPLSTITNWEREFNTWTEM---NTIVYHGSLASRQ--------- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1615 qrwqedggvMIIGYEMYRNLAQGRNV----KSRKLKEIFNKALVDpGPDF-------VVCDEGHILKNEASAVSKAMNSI 1683
Cdd:cd18060    88 ---------MIQQYEMYCKDSRGRLIpgayKFDALITTFEMILSD-CPELreiewrcVIIDEAHRLKNRNCKLLDSLKHM 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578838415 1684 RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRF 1725
Cdd:cd18060   158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDF 199
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
1505-1722 1.68e-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: 63.08  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFMWDcccesvkktKKSPGsgCILAHCMGLGKTLQVVSFLHTVLLCDKLDFstALVVCPlnTALNwmnefE 1584
Cdd:cd18011     1 PLPHQIDAVLRALR---------KPPVR--LLLADEVGLGKTIEAGLIIKELLLRGDAKR--VLILCP--ASLV-----E 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1585 KWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEdGGVMIIGYEMYRnlaqgRNVKSRKLkeifnkaLVDPGPDFVVCD 1664
Cdd:cd18011    61 QWQDELQDKFGLPFLILDRETAAQLRRLIGNPFEE-FPIVIVSLDLLK-----RSEERRGL-------LLSEEWDLVVVD 127
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578838415 1665 EGHILKNEASAVS----KAMNSI--RSRRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFR 1722
Cdd:cd18011   128 EAHKLRNSGGGKEtkryKLGRLLakRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFL 191
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
1505-1711 1.95e-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: 57.49  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1505 LKPHQVDGVQFM-WdcccesvkKTKKSPgSGCILAHCMGLGKTLQVVSF------------------LHTVLLC-DKLDF 1564
Cdd:cd18072     1 LLLHQKQALAWLlW--------RERQKP-RGGILADDMGLGKTLTMIALilaqkntqnrkeeekekaLTEWESKkDSTLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1565 STA--LVVCPLNTALNWMNEFEKWQEGlkddEKLEVSELATVKRpQERSYMLQRWQedggVMIIGYemyrnlaqgrNVKS 1642
Cdd:cd18072    72 PSAgtLVVCPASLVHQWKNEVESRVAS----NKLRVCLYHGPNR-ERIGEVLRDYD----IVITTY----------SLVA 132
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578838415 1643 RKLKEIFNKALVDPGPDF----VVCDEGHILKNEASAVSKAMNSIRSRRRIILTGTPLQNNLIEYHCMVNFIK 1711
Cdd:cd18072   133 KEIPTYKEESRSSPLFRIawarIILDEAHNIKNPKVQASIAVCKLRAHARWALTGTPIQNNLLDMYSLLKFLR 205
ADDz_Dnmt3l cd11727
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3 like (Dnmt3l); Dnmt3l ...
116-215 2.98e-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: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  116 CTACGQQVNHFQkdsiyrHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCD--FCHNAFCKKCILRNL 193
Cdd:cd11727     7 CICCGSLQIHTQ------HPLFHGGICAPCTEKFLEAFFLYDEDGYQAYCTICCSGETLLMCDdpDCTRCYCFECVDSLV 80
                          90       100
                  ....*....|....*....|..
gi 578838415  194 GRKELSTIMDENNqWYCYICHP 215
Cdd:cd11727    81 GPGTSEKVKATNN-WVCFLCLP 101
ADDz_Dnmt3b cd11728
ADDz domain found in DNA (cytosine-5) methyltransferases (C5-MTases) 3b (Dnmt3b); ADDz_Dnmt3b ...
115-216 2.31e-05

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: 46.00  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  115 SCTACGQqvnhfqKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCD--FCHNAFCKKCILRN 192
Cdd:cd11728     4 FCLSCGR------SNPATFHPLFEGGLCITCKDRFLELFYMYDDDGYQSYCTVCCEGRELLLCGnaSCCRCFCVDCLEVL 77
                          90       100
                  ....*....|....*....|....
gi 578838415  193 LGRKELSTiMDENNQWYCYICHPE 216
Cdd:cd11728    78 VGPGTAAK-AKEQDPWSCYMCLPQ 100
PHD4_NSD cd15567
PHD finger 4 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
165-213 2.65e-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: 2.65e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578838415  165 CRWCAEGGNLICCDFCHNAFCKKCIlrnlgrkELSTIMDENnqWYCYIC 213
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 ...
2058-2110 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 578838415 2058 FIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQtKPVYVYRF 2110
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 ...
165-213 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 578838415  165 CRWCAEGGNLICCDFCHNAFCKKCILRNLgrKELSTimdenNQWYCYIC 213
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 ...
165-213 7.87e-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: 7.87e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578838415  165 CRWCAEGGNLICCDFCHNAFCKKCILRNLGRkelstimDENNQWYCYIC 213
Cdd:cd15537     2 CFECHAPGEVLPCSGCFRVYHSDCLSEDFRP-------DSTSHWTCPVC 43
PHD1_AIRE cd15539
PHD finger 1 found in autoimmune regulator (AIRE); AIRE, also termed autoimmune ...
165-213 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 578838415  165 CRWCAEGGNLICCDFCHNAFCKKCIlrnlgrKELSTIMDENNqWYCYIC 213
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, ...
165-213 5.53e-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: 5.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578838415  165 CRWCAEGGNLICCDFCHNAFCKKCilrnlgrkeLSTIMDENNqWYCYIC 213
Cdd:cd15656     2 CFVCSEGGSLLCCESCPAAFHREC---------LNIDMPEGS-WYCNDC 40
PHD5_NSD cd15568
PHD finger 5 found in nuclear receptor-binding SET domain-containing (NSD) proteins; The ...
165-210 6.85e-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: 6.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578838415  165 CRWCAEGGNLICCDF--CHNAFCKKCilrnLGRKelstiMDENNQWYC 210
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 ...
165-213 9.86e-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: 9.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578838415  165 CRWCAEGGNLICCDFCHNAFCKKCIlrnlgRKELSTIMDENNQWYCYIC 213
Cdd:cd15533     2 CDSCGEGGDLLCCDRCPASFHLQCC-----NPPLDEEDLPPGEWLCHRC 45
PHD_TIF1_like cd15541
PHD finger found in the transcriptional intermediary factor 1 (TIF1) family and similar ...
165-213 1.34e-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: 1.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578838415  165 CRWCAEGGNLICCDFCHNAFCKKCILRNLGRKelstimdENNQWYCYIC 213
Cdd:cd15541     2 CAVCQNGGELLCCDKCPRVFHLDCHIPPIPEF-------PSGEWSCSLC 43
PTZ00121 PTZ00121
MAEBL; Provisional
736-1383 1.96e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  736 DTKKGKSAKSSIISKKKRQT--QSESSNYDSELEKEIKSMSKIGAARTTKKRIPNTKDFDSSEDEKHSKKGMDNQGHKNL 813
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEakKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK 1301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  814 KTSQEGSSDDAERKQERETFSSAEGTVDKdttimelRDRLPKKQQASASTDGVDKlsgKEESFTSLEVRKvAETKEKSKH 893
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKAEEAKKK-------ADAAKKKAEEAKKAAEAAK---AEAEAAADEAEA-AEEKAEAAE 1370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  894 LKTKTCKKVQDGLSDIAEKFLKKDQSDETSEDDKKQS---KKGTEEKKKPSDFKKKVIKMEQQYESSSDGTEKlPEREEI 970
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA-KKADEA 1449
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  971 CHFPKGIKQIKNGTTDGEKKSK----KIRDKTSKKKDELSDYAEKSTGKGDSCDSSED--KKSKNGAYGREKKRCKLLGK 1044
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKadeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakKKADEAKKAEEAKKADEAKK 1529
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1045 SSRKRQDCSSSDTEKYSmKEDGCNSSDKRLKRIELR---------ERRNLSSKR-------NTKEIQSGSSSSDAEESSE 1108
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKK-KADELKKAEELKKAEEKKkaeeakkaeEDKNMALRKaeeakkaEEARIEEVMKLYEEEKKMK 1608
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1109 DNKKKKQRTSSKKKAVIVKEKKRNSLRTSTKRKQADITSSSSSDIEDDDQNSI--GEGSSDEQKIKPVTENLVLSSHTgf 1186
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaAEEAKKAEEDKKKAEEAKKAEED-- 1686
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1187 cQSSGDEALSKsvpvtvddDDDDNDPENRIAKKMLLEEIKANLSSDEDGSSDDEPEEGKKRT---GKQNEENPGDEEAKN 1263
Cdd:PTZ00121 1687 -EKKAAEALKK--------EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAeedKKKAEEAKKDEEEKK 1757
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415 1264 QVNSESDSDSEESKKPRY-RHRLLRHKLTVSDGESGEEKKTKPKEHKE-----VKGRNRRKVSSEDSEDSDfqeSGVSEE 1337
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKeKEAVIEEELDEEDEKRRMEVDKKIKDIFDnfaniIEGGKEGNLVINDSKEME---DSAIKE 1834
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 578838415 1338 VSESEDEQRPRTRSAKKAELEENQRSykqkkkrrrikvQEDSSSEN 1383
Cdd:PTZ00121 1835 VADSKNMQLEEADAFEKHKFNKNNEN------------GEDGNKEA 1868
PHD1_Rco1 cd15535
PHD finger 1 found in Saccharomyces cerevisiae transcriptional regulatory protein Rco1 and ...
164-213 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 578838415  164 QCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELStimdeNNQWYCYIC 213
Cdd:cd15535     1 FCSACGGYGSFLCCDGCPRSFHFSCLDPPLEEDNLP-----DDEWFCNEC 45
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
587-802 3.15e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 43.11  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  587 NEVSLLLEESDLRRSPRVKTTPLRRPTETNPVTSNsdeecnetvkEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSKQ 666
Cdd:PTZ00108 1170 RKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSD----------EKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSS 1239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578838415  667 SETVDQNSDSDEMLAILKEVSRMSHSSSSDTDINEIHTNHKTLY---DLKTQAGKDDKGKRKRKSSTSGSDFDTKKGKSA 743
Cdd:PTZ00108 1240 VKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYsppPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLA 1319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578838415  744 KSSIiSKKKRQTQSESSNYDSELEKeiksmSKIGAARTTKKRIPNTKDFDSSEDEKHSK 802
Cdd:PTZ00108 1320 ALKK-KKKSEKKTARKKKSKTRVKQ-----ASASQSSRLLRRPRKKKSDSSSEDDDDSE 1372
PHD_PRHA_like cd15504
PHD finger found in Arabidopsis thaliana pathogenesis-related homeodomain protein (PRHA) and ...
168-213 4.63e-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: 4.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 578838415  168 CAEGGNLICCD-FCHNAFCKKCILRNLgrkELSTIMDENNQWYCYIC 213
Cdd:cd15504    10 ASPDNDILLCDgGCNRAYHQKCLEPPL---LTEDIPPEDEGWLCPLC 53
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
164-214 5.61e-03

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 37.13  E-value: 5.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 578838415  164 QCRWCAEGGNLIC----CDFCHNAFCKKCILRnlgRKELSTIMDENNQWYCYICH 214
Cdd:cd00065     1 RCMLCGKKFSLFRrrhhCRRCGRVFCSKCSSK---KLPLPSFGSGKPVRVCDSCY 52
 
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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