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Conserved domains on  [gi|1039744333|ref|XP_017171122|]
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DNA excision repair protein ERCC-6-like 2 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
51-609 1.17e-123

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


:

Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 401.91  E-value: 1.17e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333   51 AVVLYPDFQEKTIPLQRLQEVKSTKDYSRSLIFDDKDLEKPYFPDRKIPSLASAfQLSEDGDSIPYTINRYLRDYQREGA 130
Cdd:COG0553    172 LEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR-RLREALESLPAGLKATLRPYQLEGA 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  131 QFLYRHYIEGRGCILGDDMGLGKTIQM---------------FLIVAPLSVLYNWKDELDTWGY-FRVTVLHGSKKDNEL 194
Cdd:COG0553    251 AWLLFLRRLGLGGLLADDMGLGKTIQAlalllelkerglarpVLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKG 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  195 LRLkQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMD 274
Cdd:COG0553    331 ANP-FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLD 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  275 WAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGWFLRRTKTLIKGQLPKKEDRMVYCSLTDFQ 354
Cdd:COG0553    410 FLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQ 477
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  355 KAVYQTVLETEDVALiltssqpctcgsgqkrrkccykTNSRGDTVRTLCLSYLTVLQKVANHVALLQAastskhqetvik 434
Cdd:COG0553    478 RALYEAVLEYLRREL----------------------EGAEGIRRRGLILAALTRLRQICSHPALLLE------------ 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  435 ricdrvfsrfpdfvqkskdaafETLSDPKYSGKMKVLQQLLNHFRKQRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDG 514
Cdd:COG0553    524 ----------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHG 581
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  515 STKSEERLKIVKEFNSSQDVNICLVSTMAGGLGLNFVGANVVILFDPTWNPANDLQAVDRAYRIGQCRDVKVLRLISLGT 594
Cdd:COG0553    582 GTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGT 661
                          570
                   ....*....|....*
gi 1039744333  595 VEEIMYLRQVYKQQL 609
Cdd:COG0553    662 IEEKILELLEEKRAL 676
Tudor_SF super family cl02573
Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally ...
17-72 6.09e-17

Tudor domain superfamily; The Tudor domain is a conserved structural domain, originally identified in the Tudor protein of Drosophila, that adopts a beta-barrel-like core structure containing four short beta-strands followed by an alpha-helical region. It binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions. Tudor domain-containing proteins may mediate protein-protein interactions required for various DNA-templated biological processes, such as RNA metabolism, as well as histone modification and the DNA damage response. Members of this superfamily contain one or more copies of the Tudor domain.


The actual alignment was detected with superfamily member cd20400:

Pssm-ID: 470623  Cd Length: 59  Bit Score: 76.21  E-value: 6.09e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039744333   17 WCPGERCLAPSLDNKKLCEASIKSITVDGNGKPFAVVL---YPDFQEKTIPLQRLQEVK 72
Cdd:cd20400      1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKflgYESDEDEKVPVSKLQKVK 59
VIGSSK super family cl20696
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
1068-1091 8.25e-03

Helicase-associated putative binding domain, C-terminal; The function of this short, serine-rich C-terminal region is not known. However, as it is frequently found at the very C-terminus of P-loop containing nucleoside triphosphate hydrolases, it might possibly be a binding domain.


The actual alignment was detected with superfamily member pfam14773:

Pssm-ID: 464308  Cd Length: 62  Bit Score: 36.04  E-value: 8.25e-03
                           10        20
                   ....*....|....*....|....
gi 1039744333 1068 VAYIHSNQNVIGSSRAENHMSRWA 1091
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRA 61
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
51-609 1.17e-123

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 401.91  E-value: 1.17e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333   51 AVVLYPDFQEKTIPLQRLQEVKSTKDYSRSLIFDDKDLEKPYFPDRKIPSLASAfQLSEDGDSIPYTINRYLRDYQREGA 130
Cdd:COG0553    172 LEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR-RLREALESLPAGLKATLRPYQLEGA 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  131 QFLYRHYIEGRGCILGDDMGLGKTIQM---------------FLIVAPLSVLYNWKDELDTWGY-FRVTVLHGSKKDNEL 194
Cdd:COG0553    251 AWLLFLRRLGLGGLLADDMGLGKTIQAlalllelkerglarpVLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKG 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  195 LRLkQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMD 274
Cdd:COG0553    331 ANP-FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLD 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  275 WAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGWFLRRTKTLIKGQLPKKEDRMVYCSLTDFQ 354
Cdd:COG0553    410 FLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQ 477
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  355 KAVYQTVLETEDVALiltssqpctcgsgqkrrkccykTNSRGDTVRTLCLSYLTVLQKVANHVALLQAastskhqetvik 434
Cdd:COG0553    478 RALYEAVLEYLRREL----------------------EGAEGIRRRGLILAALTRLRQICSHPALLLE------------ 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  435 ricdrvfsrfpdfvqkskdaafETLSDPKYSGKMKVLQQLLNHFRKQRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDG 514
Cdd:COG0553    524 ----------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHG 581
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  515 STKSEERLKIVKEFNSSQDVNICLVSTMAGGLGLNFVGANVVILFDPTWNPANDLQAVDRAYRIGQCRDVKVLRLISLGT 594
Cdd:COG0553    582 GTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGT 661
                          570
                   ....*....|....*
gi 1039744333  595 VEEIMYLRQVYKQQL 609
Cdd:COG0553    662 IEEKILELLEEKRAL 676
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
122-329 2.24e-121

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: 379.03  E-value: 2.24e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQ------------------------------------MFLIVAPLS 165
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQviaflaavlgktgtrrdrennrprfkkkppassakkPVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  166 VLYNWKDELDTWGYFRVTVLHGSKKDNEL-LRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTE 244
Cdd:cd18005     81 VLYNWKDELDTWGHFEVGVYHGSRKDDELeGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLTQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  245 VMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAKKMSG 324
Cdd:cd18005    161 AMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAVKLSK 240

                   ....*
gi 1039744333  325 WFLRR 329
Cdd:cd18005    241 FFLRR 245
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
115-614 1.98e-67

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 248.56  E-value: 1.98e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  115 PYTINRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQMF----------------LIVAPLSVLYNWKDELDTW- 177
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTIsllgylheyrgitgphMVVAPKSTLGNWMNEIRRFc 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  178 GYFRVTVLHGSKKDNELLR---LKQRKCEIALTTYEtlrLCLEELNSLE---WSAIIVDEAHRIKNPKARVTEVMKAVKC 251
Cdd:PLN03142   243 PVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRYIIIDEAHRIKNENSLLSKTMRLFST 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  252 KVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGWFLRRTK 331
Cdd:PLN03142   320 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ------------QEVVQQLHKVLRPFLLRRLK 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  332 TLIKGQLPKKEDRMVYCSLTDFQKAVYQTVLEtEDVALIltssqpctcgsgqkrrkccyktNSRGDtvRTLCLSYLTVLQ 411
Cdd:PLN03142   388 SDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV----------------------NAGGE--RKRLLNIAMQLR 442
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  412 KVANHVALLQAASTSkhqetvikricdrvfsrfPDFVqkSKDAAFETlsdpkySGKMKVLQQLLNHFRKQRDKVLLFSFS 491
Cdd:PLN03142   443 KCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SGKMVLLDKLLPKLKERDSRVLIFSQM 496
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  492 TKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNIC-LVSTMAGGLGLNFVGANVVILFDPTWNPANDLQ 570
Cdd:PLN03142   497 TRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGGLGINLATADIVILYDSDWNPQVDLQ 576
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1039744333  571 AVDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQVYKQQLHCVVV 614
Cdd:PLN03142   577 AQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
125-420 9.83e-65

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: 221.79  E-value: 9.83e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  125 YQREGAQFLY-RHYIEGRGCILGDDMGLGKTIQM-----------------FLIVAPLSVLYNWKDELDTW---GYFRVT 183
Cdd:pfam00176    1 YQIEGVNWMLsLENNLGRGGILADEMGLGKTLQTislllylkhvdknwggpTLIVVPLSLLHNWMNEFERWvspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  184 VLHGSKKDNELLRLKQ---RKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGT 260
Cdd:pfam00176   81 VLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  261 VLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVehgQRHTATKRelatgrkaMHRLAKKMSGWFLRRTKTLIKGQLPK 340
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  341 KEDRMVYCSLTDFQKAVYQTVLETEDVALILTSSQpctcgsgqkrrkccyktnsrGDTVRTLCLSYLTVLQKVANHVALL 420
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEG--------------------GREIKASLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
122-270 2.06e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 105.27  E-value: 2.06e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333   122 LRDYQREGAQFLYRHYiegRGCILGDDMGLGKTIQM---------------FLIVAPLSVL-YNWKDELDTWGYF----R 181
Cdd:smart00487    9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAAllpalealkrgkggrVLVLVPTRELaEQWAEELKKLGPSlglkV 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333   182 VTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEE--LNSLEWSAIIVDEAHRIKNPKAR--VTEVMKAV-KCKVRIG 256
Cdd:smart00487   86 VGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDGGFGdqLEKLLKLLpKNVQLLL 165
                           170
                    ....*....|....
gi 1039744333   257 LTGTVLQNNMKELW 270
Cdd:smart00487  166 LSATPPEEIENLLE 179
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
17-72 6.09e-17

Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. ERCC6L2 gene mutations have been associated with bone marrow failure that includes developmental delay and microcephaly. It contains an N-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410471  Cd Length: 59  Bit Score: 76.21  E-value: 6.09e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039744333   17 WCPGERCLAPSLDNKKLCEASIKSITVDGNGKPFAVVL---YPDFQEKTIPLQRLQEVK 72
Cdd:cd20400      1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKflgYESDEDEKVPVSKLQKVK 59
VIGSSK pfam14773
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
1068-1091 8.25e-03

Helicase-associated putative binding domain, C-terminal; The function of this short, serine-rich C-terminal region is not known. However, as it is frequently found at the very C-terminus of P-loop containing nucleoside triphosphate hydrolases, it might possibly be a binding domain.


Pssm-ID: 464308  Cd Length: 62  Bit Score: 36.04  E-value: 8.25e-03
                           10        20
                   ....*....|....*....|....
gi 1039744333 1068 VAYIHSNQNVIGSSRAENHMSRWA 1091
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRA 61
 
Name Accession Description Interval E-value
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
51-609 1.17e-123

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 401.91  E-value: 1.17e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333   51 AVVLYPDFQEKTIPLQRLQEVKSTKDYSRSLIFDDKDLEKPYFPDRKIPSLASAfQLSEDGDSIPYTINRYLRDYQREGA 130
Cdd:COG0553    172 LEALLLLGLLLALALLALLELALLAAEAELLLLLELLLELELLAEAAVDAFRLR-RLREALESLPAGLKATLRPYQLEGA 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  131 QFLYRHYIEGRGCILGDDMGLGKTIQM---------------FLIVAPLSVLYNWKDELDTWGY-FRVTVLHGSKKDNEL 194
Cdd:COG0553    251 AWLLFLRRLGLGGLLADDMGLGKTIQAlalllelkerglarpVLIVAPTSLVGNWQRELAKFAPgLRVLVLDGTRERAKG 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  195 LRLkQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMD 274
Cdd:COG0553    331 ANP-FEDADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLD 409
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  275 WAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGWFLRRTKTLIKGQLPKKEDRMVYCSLTDFQ 354
Cdd:COG0553    410 FLNPGLLGSLKAFRERFARPIEKGD------------EEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQ 477
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  355 KAVYQTVLETEDVALiltssqpctcgsgqkrrkccykTNSRGDTVRTLCLSYLTVLQKVANHVALLQAastskhqetvik 434
Cdd:COG0553    478 RALYEAVLEYLRREL----------------------EGAEGIRRRGLILAALTRLRQICSHPALLLE------------ 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  435 ricdrvfsrfpdfvqkskdaafETLSDPKYSGKMKVLQQLLNHFRKQRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDG 514
Cdd:COG0553    524 ----------------------EGAELSGRSAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEERGIEYAYLHG 581
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  515 STKSEERLKIVKEFNSSQDVNICLVSTMAGGLGLNFVGANVVILFDPTWNPANDLQAVDRAYRIGQCRDVKVLRLISLGT 594
Cdd:COG0553    582 GTSAEERDELVDRFQEGPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDVQVYKLVAEGT 661
                          570
                   ....*....|....*
gi 1039744333  595 VEEIMYLRQVYKQQL 609
Cdd:COG0553    662 IEEKILELLEEKRAL 676
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
122-329 2.24e-121

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: 379.03  E-value: 2.24e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQ------------------------------------MFLIVAPLS 165
Cdd:cd18005      1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQviaflaavlgktgtrrdrennrprfkkkppassakkPVLIVAPLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  166 VLYNWKDELDTWGYFRVTVLHGSKKDNEL-LRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTE 244
Cdd:cd18005     81 VLYNWKDELDTWGHFEVGVYHGSRKDDELeGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSKLTQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  245 VMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAKKMSG 324
Cdd:cd18005    161 AMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIKRGQRHTATARELRLGRKRKQELAVKLSK 240

                   ....*
gi 1039744333  325 WFLRR 329
Cdd:cd18005    241 FFLRR 245
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
115-614 1.98e-67

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 248.56  E-value: 1.98e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  115 PYTINRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQMF----------------LIVAPLSVLYNWKDELDTW- 177
Cdd:PLN03142   163 PSCIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTIsllgylheyrgitgphMVVAPKSTLGNWMNEIRRFc 242
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  178 GYFRVTVLHGSKKDNELLR---LKQRKCEIALTTYEtlrLCLEELNSLE---WSAIIVDEAHRIKNPKARVTEVMKAVKC 251
Cdd:PLN03142   243 PVLRAVKFHGNPEERAHQReelLVAGKFDVCVTSFE---MAIKEKTALKrfsWRYIIIDEAHRIKNENSLLSKTMRLFST 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  252 KVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQrhtatkrelatgRKAMHRLAKKMSGWFLRRTK 331
Cdd:PLN03142   320 NYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQ------------QEVVQQLHKVLRPFLLRRLK 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  332 TLIKGQLPKKEDRMVYCSLTDFQKAVYQTVLEtEDVALIltssqpctcgsgqkrrkccyktNSRGDtvRTLCLSYLTVLQ 411
Cdd:PLN03142   388 SDVEKGLPPKKETILKVGMSQMQKQYYKALLQ-KDLDVV----------------------NAGGE--RKRLLNIAMQLR 442
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  412 KVANHVALLQAASTSkhqetvikricdrvfsrfPDFVqkSKDAAFETlsdpkySGKMKVLQQLLNHFRKQRDKVLLFSFS 491
Cdd:PLN03142   443 KCCNHPYLFQGAEPG------------------PPYT--TGEHLVEN------SGKMVLLDKLLPKLKERDSRVLIFSQM 496
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  492 TKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNIC-LVSTMAGGLGLNFVGANVVILFDPTWNPANDLQ 570
Cdd:PLN03142   497 TRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVfLLSTRAGGLGINLATADIVILYDSDWNPQVDLQ 576
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1039744333  571 AVDRAYRIGQCRDVKVLRLISLGTVEEIMYLRQVYKQQLHCVVV 614
Cdd:PLN03142   577 AQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
122-278 4.66e-66

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: 221.29  E-value: 4.66e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTW-GYFRVTV 184
Cdd:cd17919      1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAiaflayllkegkergpVLVVCPLSVLENWEREFEKWtPDLRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LHGSKKDNELLR--LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVL 262
Cdd:cd17919     81 YHGSQRERAQIRakEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRRLLLTGTPL 160
                          170
                   ....*....|....*.
gi 1039744333  263 QNNMKELWCVMDWAVP 278
Cdd:cd17919    161 QNNLEELWALLDFLDP 176
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
125-420 9.83e-65

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: 221.79  E-value: 9.83e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  125 YQREGAQFLY-RHYIEGRGCILGDDMGLGKTIQM-----------------FLIVAPLSVLYNWKDELDTW---GYFRVT 183
Cdd:pfam00176    1 YQIEGVNWMLsLENNLGRGGILADEMGLGKTLQTislllylkhvdknwggpTLIVVPLSLLHNWMNEFERWvspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  184 VLHGSKKDNELLRLKQ---RKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGT 260
Cdd:pfam00176   81 VLHGNKRPQERWKNDPnflADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRNRWILTGT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  261 VLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVehgQRHTATKRelatgrkaMHRLAKKMSGWFLRRTKTLIKGQLPK 340
Cdd:pfam00176  161 PLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPI---ERGGGKKG--------VSRLHKLLKPFLLRRTKKDVEKSLPP 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  341 KEDRMVYCSLTDFQKAVYQTVLETEDVALILTSSQpctcgsgqkrrkccyktnsrGDTVRTLCLSYLTVLQKVANHVALL 420
Cdd:pfam00176  230 KVEYILFCRLSKLQRKLYQTFLLKKDLNAIKTGEG--------------------GREIKASLLNILMRLRKICNHPGLI 289
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
464-590 2.19e-55

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: 188.84  E-value: 2.19e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  464 YSGKMKVLQQLLNHFRKQRDKVLLFSFSTKLLDVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSQDVNICLVSTMA 543
Cdd:cd18793      9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDPDIRVFLLSTKA 88
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039744333  544 GGLGLNFVGANVVILFDPTWNPANDLQAVDRAYRIGQCRDVKVLRLI 590
Cdd:cd18793     89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
122-329 2.39e-55

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: 192.59  E-value: 2.39e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQ-------MF--------LIVAPLSVLYNWKDELDTWGY-FRVTVL 185
Cdd:cd18001      1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQicaflsgMFdsgliksvLVVMPTSLIPHWVKEFAKWTPgLRVKVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  186 HGSKKD--NELLRLKQRKCEIALTTYETLRLCLEELNSLE-----WSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLT 258
Cdd:cd18001     81 HGTSKKerERNLERIQRGGGVLLTTYGMVLSNTEQLSADDhdefkWDYVILDEGHKIKNSKTKSAKSLREIPAKNRIILT 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039744333  259 GTVLQNNMKELWCVMDWAVPG-LLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAKKMSGWFLRR 329
Cdd:cd18001    161 GTPIQNNLKELWALFDFACNGsLLGTRKTFKMEFENPITRGRDKDATQGEKALGSEVAENLRQIIKPYFLRR 232
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
122-331 3.09e-54

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: 188.93  E-value: 3.09e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLY--RHYieGRGCILGDDMGLGKTIQM---------------FLIVAPLSVLYNWKDELDTWG-YFRVT 183
Cdd:cd18012      5 LRPYQKEGFNWLSflRHY--GLGGILADDMGLGKTLQTlalllsrkeegrkgpSLVVAPTSLIYNWEEEAAKFApELKVL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  184 VLHGSK-KDNELLRLKQRkcEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVL 262
Cdd:cd18012     83 VIHGTKrKREKLRALEDY--DLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKALKADHRLALTGTPI 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039744333  263 QNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRhtatkrelatgRKAMHRLAKKMSGWFLRRTK 331
Cdd:cd18012    161 ENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPIEKDGD-----------EEALEELKKLISPFILRRLK 218
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
122-329 2.19e-51

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: 181.33  E-value: 2.19e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLY-----RHYIEGRGCILGDDMGLGKTIQM--------------------FLIVAPLSVLYNWKDELDT 176
Cdd:cd18004      1 LRPHQREGVQFLYdcltgRRGYGGGGAILADEMGLGKTLQAialvwtllkqgpygkptakkALIVCPSSLVGNWKAEFDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  177 W-GYFRVTVL--HGSKKDNELLRLKQ---RKCEIALTTYETLRLCLEELNSLEWSAIIV-DEAHRIKNPKARVTEVMKAV 249
Cdd:cd18004     81 WlGLRRIKVVtaDGNAKDVKASLDFFssaSTYPVLIISYETLRRHAEKLSKKISIDLLIcDEGHRLKNSESKTTKALNSL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  250 KCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAKKMSGWFLRR 329
Cdd:cd18004    161 PCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDPDASEEDKELGAERSQELSELTSRFILRR 240
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
122-299 5.30e-49

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: 173.97  E-value: 5.30e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWGYFRVTVL 185
Cdd:cd17995      1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSiaflehlyqvegirgpFLVIAPLSTIPNWQREFETWTDMNVVVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  186 HGSKKDNELLRLKQR--------------KCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKC 251
Cdd:cd17995     81 HGSGESRQIIQQYEMyfkdaqgrkkkgvyKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLTL 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1039744333  252 KVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQ 299
Cdd:cd17995    161 EHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKTAEQ 208
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
122-329 4.32e-46

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: 165.99  E-value: 4.32e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQ---FLYRHYIEGrgcILGDDMGLGKTIQMF---------------------LIVAPLSVLYNWKDELDTW 177
Cdd:cd17999      1 LRPYQQEGINwlaFLNKYNLHG---ILCDDMGLGKTLQTLcilasdhhkransfnsenlpsLVVCPPTLVGHWVAEIKKY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  178 ---GYFRVTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVR 254
Cdd:cd17999     78 fpnAFLKPLAYVGPPQERRRLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAVKQLKANHR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039744333  255 IGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAKKMSGWFLRR 329
Cdd:cd17999    158 LILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
122-313 9.60e-42

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: 153.60  E-value: 9.60e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRH-------YIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTW- 177
Cdd:cd18007      1 LKPHQVEGVRFLWSNlvgtdvgSDEGGGCILAHTMGLGKTLQVitflhtylaaaprrsrPLVLCPASTLYNWEDEFKKWl 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  178 --GYFRVTVLHGSKKDN-ELLRLK-----QRKCEIALTTYETLRLCLEELNSLEWSA--------------IIVDEAHRI 235
Cdd:cd18007     81 ppDLRPLLVLVSLSASKrADARLRkinkwHKEGGVLLIGYELFRNLASNATTDPRLKqefiaalldpgpdlLVLDEGHRL 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039744333  236 KNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRK 313
Cdd:cd18007    161 KNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIEAGQCVDSTEEDVRLMLK 238
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
122-281 4.41e-41

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: 150.17  E-value: 4.41e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQMF----------------LIVAPLSVLYNWKDELDTW-GYFRVTV 184
Cdd:cd18000      1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIaflaalhhsklglgpsLIVCPATVLKQWVKEFHRWwPPFRVVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LH--------GSKKDNELLRLKQRKCE-----IALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKC 251
Cdd:cd18000     81 LHssgsgtgsEEKLGSIERKSQLIRKVvgdggILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLACKQLRT 160
                          170       180       190
                   ....*....|....*....|....*....|
gi 1039744333  252 KVRIGLTGTVLQNNMKELWCVMDWAVPGLL 281
Cdd:cd18000    161 PHRLILSGTPIQNNLKELWSLFDFVFPPYL 190
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
122-331 1.81e-38

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: 143.62  E-value: 1.81e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTW-GYFRVTV 184
Cdd:cd17997      4 MRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTisllgylkhykningpHLIIVPKSTLDNWMREFKRWcPSLRVVV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LHGSKK-DNELLR--LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTV 261
Cdd:cd17997     84 LIGDKEeRADIIRdvLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNSRNRLLLTGTP 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  262 LQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKrelatgrkamhRLAKKMSGWFLRRTK 331
Cdd:cd17997    164 LQNNLHELWALLNFLLPDVFTSSEDFDEWFNVNNCDDDNQEVVQ-----------RLHKVLRPFLLRRIK 222
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
122-329 2.57e-37

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: 140.18  E-value: 2.57e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWG-YFRVTV 184
Cdd:cd17993      2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTisflsylfhsqqqygpFLVVVPLSTMPAWQREFAKWApDMNVIV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LHGSKKDNELLR--------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIG 256
Cdd:cd17993     82 YLGDIKSRDTIReyefyfsqTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNNRLL 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039744333  257 LTGTVLQNNMKELWCVMDWAVPGllgsRIHFKKQFSDpvEHGQrhtatKRElatgrKAMHRLAKKMSGWFLRR 329
Cdd:cd17993    162 ITGTPLQNSLKELWALLHFLMPG----KFDIWEEFEE--EHDE-----EQE-----KGIADLHKELEPFILRR 218
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
122-329 4.96e-37

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: 140.30  E-value: 4.96e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRhYIEGR------GCILGDDMGLGKTIQMF--------------------LIVAPLSVLYNWKDELD 175
Cdd:cd18067      1 LRPHQREGVKFLYR-CVTGRrirgshGCIMADEMGLGKTLQCItlmwtllrqspqckpeidkaIVVSPSSLVKNWANELG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  176 TWGYFRVTVL--HGSKKDNELLRLKQRKCE--------IALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEV 245
Cdd:cd18067     80 KWLGGRLQPLaiDGGSKKEIDRKLVQWASQqgrrvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  246 MKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAKKMSGW 325
Cdd:cd18067    160 LDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPILKGRDADASEKERQLGEEKLQELISIVNRC 239

                   ....
gi 1039744333  326 FLRR 329
Cdd:cd18067    240 IIRR 243
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
122-331 1.51e-36

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: 138.67  E-value: 1.51e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM---------------FLIVAPLSVLYNWKDELDTWG-YFRVTVL 185
Cdd:cd18009      4 MRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTiallahlrergvwgpFLVIAPLSTLPNWVNEFARFTpSVPVLLY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  186 HGSKKDNELLRLKQRK-------CEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLT 258
Cdd:cd18009     84 HGTKEERERLRKKIMKregtlqdFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNSDNRLLLT 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039744333  259 GTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFsDPVEHGQRhTATKRELATGRKA--MHRLAKKMSGWFLRRTK 331
Cdd:cd18009    164 GTPLQNNLSELWSLLNFLLPDVFDDLSSFESWF-DFSSLSDN-AADISNLSEEREQniVHMLHAILKPFLLRRLK 236
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
122-329 2.29e-36

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: 138.05  E-value: 2.29e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLY-----RHYIEGRGCILGDDMGLGKTIQMF---------------------LIVAPLSVLYNWKDELD 175
Cdd:cd18066      1 LRPHQREGIEFLYecvmgMRVNERFGAILADEMGLGKTLQCIsliwtllrqgpyggkpvikraLIVTPGSLVKNWKKEFQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  176 TW---GYFRVTVLHGSKKDNELLrlKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCK 252
Cdd:cd18066     81 KWlgsERIKVFTVDQDHKVEEFI--ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTALTSLSCE 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744333  253 VRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRELATGRKAMHRLAKKMSGWFLRR 329
Cdd:cd18066    159 RRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARAAELTRLTGLFILRR 235
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
122-331 9.40e-35

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: 133.26  E-value: 9.40e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQF---LYRHYIEGrgcILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWGYFRV 182
Cdd:cd17996      4 LKEYQLKGLQWmvsLYNNNLNG---ILADEMGLGKTIQTislitylmekkknngpYLVIVPLSTLSNWVSEFEKWAPSVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  183 TVLH-GSKKDNELLRLKQRKCE--IALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKC-KVRIGLT 258
Cdd:cd17996     81 KIVYkGTPDVRKKLQSQIRAGKfnVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHaRYRLLLT 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039744333  259 GTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEH-GQRHtatKRELATGRKAM--HRLAKKMSGWFLRRTK 331
Cdd:cd17996    161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANtGEQV---KIELNEEETLLiiRRLHKVLRPFLLRRLK 233
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
122-293 9.80e-33

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: 127.08  E-value: 9.80e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM---------------FLIVAPLSVLYNWKDELDTWGYFRVTVLH 186
Cdd:cd18058      1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSitflseiflmgirgpFLIIAPLSTITNWEREFRTWTEMNAIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  187 GSKKDNELLRLKQR--------------KCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCK 252
Cdd:cd18058     81 GSQISRQMIQQYEMyyrdeqgnplsgifKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMALE 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039744333  253 VRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 293
Cdd:cd18058    161 HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGD 201
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
122-329 2.10e-32

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: 126.31  E-value: 2.10e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQMF----------------LIVAPLSVLYNWKDELDTW--GyFRVT 183
Cdd:cd18003      1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIallahlacekgnwgphLIVVPTSVMLNWEMEFKRWcpG-FKIL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  184 VLHGSKKDNELLR---LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGT 260
Cdd:cd18003     80 TYYGSAKERKLKRqgwMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQRRLLLTGT 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039744333  261 VLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDP----VEHGQRHTatkrelatgRKAMHRLAKKMSGWFLRR 329
Cdd:cd18003    160 PLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPltamSEGSQEEN---------EELVRRLHKVLRPFLLRR 223
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
122-299 1.26e-31

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: 124.16  E-value: 1.26e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIE---------GRGCILGDDMGLGKTIQMF---------------LIVAPLSVLYNWKDELDTW 177
Cdd:cd18069      1 LKPHQIGGIRFLYDNIIEslerykgssGFGCILAHSMGLGKTLQVIsfldvllrhtgaktvLAIVPVNTLQNWLSEFNKW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  178 ------------GYFRVTVLHGSKKD----NELLRLKQRKCEIALTTYETLRLclEELNSLewsaIIVDEAHRIKNPKAR 241
Cdd:cd18069     81 lpppealpnvrpRPFKVFILNDEHKTtaarAKVIEDWVKDGGVLLMGYEMFRL--RPGPDV----VICDEGHRIKNCHAS 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039744333  242 VTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQ 299
Cdd:cd18069    155 TSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPILNGQ 212
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
122-293 1.31e-31

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: 123.96  E-value: 1.31e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM---------------FLIVAPLSVLYNWKDELDTWGYFRVTVLH 186
Cdd:cd18061      1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSitflyeilltgirgpFLIIAPLSTIANWEREFRTWTDLNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  187 GSKKDNELLRLKQRKC--------------EIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCK 252
Cdd:cd18061     81 GSLISRQMIQQYEMYFrdsqgriirgayrfQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMNLE 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039744333  253 VRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 293
Cdd:cd18061    161 HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGD 201
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
122-293 2.24e-31

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: 123.24  E-value: 2.24e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM---------------FLIVAPLSVLYNWKDELDTWGYFRVTVLH 186
Cdd:cd18060      1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSiaflqevynvgihgpFLVIAPLSTITNWEREFNTWTEMNTIVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  187 GSKKDNELLRLKQRKC--------------EIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCK 252
Cdd:cd18060     81 GSLASRQMIQQYEMYCkdsrgrlipgaykfDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLE 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039744333  253 VRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 293
Cdd:cd18060    161 HKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGD 201
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
122-293 4.08e-31

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: 122.45  E-value: 4.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM---------------FLIVAPLSVLYNWKDELDTWGYFRVTVLH 186
Cdd:cd18059      1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSitflyeiylkgihgpFLVIAPLSTIPNWEREFRTWTELNVVVYH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  187 GSKKDNELLRLKQR--------------KCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCK 252
Cdd:cd18059     81 GSQASRRTIQLYEMyfkdpqgrvikgsyKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMDLE 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039744333  253 VRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 293
Cdd:cd18059    161 HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGD 201
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
122-329 1.82e-29

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: 118.18  E-value: 1.82e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWG-YFRVTV 184
Cdd:cd18054     21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTisflsylfhqhqlygpFLLVVPLSTLTSWQREFEIWApEINVVV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LHGSKKDNELLR--------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIG 256
Cdd:cd18054    101 YIGDLMSRNTIReyewihsqTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTLIDFKSNHRLL 180
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039744333  257 LTGTVLQNNMKELWCVMDWAVPgllgSRIHFKKQFSDpvEHGQrhtatKRElaTGRKAMHRLakkMSGWFLRR 329
Cdd:cd18054    181 ITGTPLQNSLKELWSLLHFIMP----EKFEFWEDFEE--DHGK-----GRE--NGYQSLHKV---LEPFLLRR 237
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
122-270 2.19e-29

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: 118.16  E-value: 2.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRhyiegRGCILGDDMGLGKTIQM---------------------------------FLIVAPLSVLY 168
Cdd:cd18008      1 LLPYQKQGLAWMLP-----RGGILADEMGLGKTIQAlalilatrpqdpkipeeleenssdpkklylsktTLIVVPLSLLS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  169 NWKDELDT---WGYFRVTVLHGSKKDNELLRLKQrkCEIALTTYETLR------------LCLEE----LNSLEWSAIIV 229
Cdd:cd18008     76 QWKDEIEKhtkPGSLKVYVYHGSKRIKSIEELSD--YDIVITTYGTLAsefpknkkgggrDSKEKeaspLHRIRWYRVIL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039744333  230 DEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELW 270
Cdd:cd18008    154 DEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLY 194
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
122-329 2.40e-29

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: 117.15  E-value: 2.40e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWG-YFRVTV 184
Cdd:cd18006      1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTisllwylagrlkllgpFLVLCPLSVLDNWKEELNRFApDLSVIT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LHGSKKDNELLRlKQRKCE----IALTTYEtlrLCLEE---LNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGL 257
Cdd:cd18006     81 YMGDKEKRLDLQ-QDIKSTnrfhVLLTTYE---ICLKDasfLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDFRLLL 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039744333  258 TGTVLQNNMKELWCVMDWAVPGLLGSRI--HFKKQFSDpvehgqrhtaTKRELATGrKAMHRLAKKmsgWFLRR 329
Cdd:cd18006    157 TGTPIQNSLQELYALLSFIEPNVFPKDKldDFIKAYSE----------TDDESETV-EELHLLLQP---FLLRR 216
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
122-329 5.18e-29

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: 116.84  E-value: 5.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTW-GYFRVTV 184
Cdd:cd18002      1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSiavlahlaeehniwgpFLVIAPASTLHNWQQEISRFvPQFKVLP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LHGSKKDNELLR---------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRI 255
Cdd:cd18002     81 YWGNPKDRKVLRkfwdrknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRNRL 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039744333  256 GLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVE-HGQRHTATKRElatgrkAMHRLAKKMSGWFLRR 329
Cdd:cd18002    161 LLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIEsHAENKTGLNEH------QLKRLHMILKPFMLRR 229
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
122-294 6.88e-29

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: 115.77  E-value: 6.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHyiEGRgCILGDDMGLGKTIQM------------FLIVAPLSVLYNWKDELDTW----GYFRVTVL 185
Cdd:cd18010      1 LLPFQREGVCFALRR--GGR-VLIADEMGLGKTVQAiaiaayyreewpLLIVCPSSLRLTWADEIERWlpslPPDDIQVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  186 HGSKkdnELLRLKQRKceIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKA-RVTEVMKAVK-CKVRIGLTGTVLQ 263
Cdd:cd18010     78 VKSK---DGLRDGDAK--VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAkRTKAALPLLKrAKRVILLSGTPAL 152
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039744333  264 NNMKELWCVMDWAVPGLLGSRIHFKKQFSDP 294
Cdd:cd18010    153 SRPIELFTQLDALDPKLFGRFHDFGRRYCAA 183
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
122-293 9.62e-29

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: 114.84  E-value: 9.62e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWG-YFRVTV 184
Cdd:cd17994      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTivflyslykeghskgpFLVSAPLSTIINWEREFEMWApDFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LHGskkDNELLrlkqrkceialTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQN 264
Cdd:cd17994     81 YVG---DHVLL-----------TSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYKLLLTGTPLQN 146
                          170       180
                   ....*....|....*....|....*....
gi 1039744333  265 NMKELWCVMDWAVPGLLGSRIHFKKQFSD 293
Cdd:cd17994    147 NLEELFHLLNFLTPERFNNLQGFLEEFAD 175
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
122-308 3.57e-28

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: 114.38  E-value: 3.57e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWG-YFRVTV 184
Cdd:cd18053     21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTisflnylfhehqlygpFLLVVPLSTLTSWQREIQTWApQMNAVV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LHGSKKDNELLRL--------KQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIG 256
Cdd:cd18053    101 YLGDINSRNMIRThewmhpqtKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTLIDFKSNHRLL 180
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039744333  257 LTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGqrHTATKREL 308
Cdd:cd18053    181 ITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEHGKGREYG--YASLHKEL 230
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
466-579 1.33e-27

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 108.45  E-value: 1.33e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  466 GKMKVLQQLLNhfRKQRDKVLLFSFSTKLLDvLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSSqDVNIcLVSTMAGG 545
Cdd:pfam00271    1 EKLEALLELLK--KERGGKVLIFSQTKKTLE-AELLLEKEGIKVARLHGDLSQEEREEILEDFRKG-KIDV-LVATDVAE 75
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1039744333  546 LGLNFVGANVVILFDPTWNPANDLQAVDRAYRIG 579
Cdd:pfam00271   76 RGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
140-329 4.00e-27

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: 111.41  E-value: 4.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  140 GRGCILGDDMGLGKTIQMF--------LIVAPLSVLYNWKDELD---TWGYFRVTVLHGSKKDNELLRLKqrKCEIALTT 208
Cdd:cd18071     48 VRGGILADDMGLGKTLTTIslilanftLIVCPLSVLSNWETQFEehvKPGQLKVYTYHGGERNRDPKLLS--KYDIVLTT 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  209 YETLrlCLEE-------LNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMdwavpgll 281
Cdd:cd18071    126 YNTL--ASDFgakgdspLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDLGSLL-------- 195
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1039744333  282 gSRIHFKKqFSDPvEHGQRhtATKRELATG-RKAMHRLAKKMSGWFLRR 329
Cdd:cd18071    196 -SFLHLKP-FSNP-EYWRR--LIQRPLTMGdPTGLKRLQVLMKQITLRR 239
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
112-342 2.48e-26

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: 109.37  E-value: 2.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  112 DSIPYTINRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQMF----------------LIVAPLSVLYNWKDELD 175
Cdd:cd18064      6 DSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTIsllgymkhyrnipgphMVLVPKSTLHNWMAEFK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  176 TW-GYFRVTVLHGSKKDNELLR---LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKC 251
Cdd:cd18064     86 RWvPTLRAVCLIGDKDQRAAFVrdvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  252 KVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSdpvehgqrhtatKRELATGRKAMHRLAKKMSGWFLRRTK 331
Cdd:cd18064    166 TNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFD------------TNNCLGDQKLVERLHMVLRPFLLRRIK 233
                          250
                   ....*....|.
gi 1039744333  332 TLIKGQLPKKE 342
Cdd:cd18064    234 ADVEKSLPPKK 244
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
118-331 2.83e-26

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: 109.38  E-value: 2.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  118 INRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWGyfr 181
Cdd:cd18063     20 INGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTialitylmehkrlngpYLIIVPLSTLSNWTYEFDKWA--- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  182 VTVLHGSKKDNELLR------LKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKA-VKCKVR 254
Cdd:cd18063     97 PSVVKISYKGTPAMRrslvpqLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRR 176
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039744333  255 IGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEH-GQRHTATKRELATgrkAMHRLAKKMSGWFLRRTK 331
Cdd:cd18063    177 ILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGERVDLNEEETIL---IIRRLHKVLRPFLLRRLK 251
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
122-293 4.58e-26

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: 108.17  E-value: 4.58e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWG------- 178
Cdd:cd18055      1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTivflyslykeghtkgpFLVSAPLSTIINWEREFQMWApdfyvvt 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  179 ----------------YFRVTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARV 242
Cdd:cd18055     81 ytgdkdsraiirenefSFDDNAVKGGKKAFKMKREAQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039744333  243 TEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSD 293
Cdd:cd18055    161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFAD 211
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
122-299 1.17e-25

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: 107.07  E-value: 1.17e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWGY-FRVTV 184
Cdd:cd18057      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTivflyslykeghskgpYLVSAPLSTIINWEREFEMWAPdFYVVT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LHGSK------KDNE-------------LLRLK---QRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARV 242
Cdd:cd18057     81 YTGDKesrsviRENEfsfednairsgkkVFRMKkeaQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744333  243 TEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQ 299
Cdd:cd18057    161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQ 217
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
122-299 1.35e-25

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: 107.07  E-value: 1.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWG------- 178
Cdd:cd18056      1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTavflyslykeghskgpFLVSAPLSTIINWEREFEMWApdmyvvt 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  179 ----------------YFRVTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARV 242
Cdd:cd18056     81 yvgdkdsraiirenefSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744333  243 TEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQ 299
Cdd:cd18056    161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQ 217
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
118-331 1.85e-25

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: 107.05  E-value: 1.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  118 INRYLRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQM----------------FLIVAPLSVLYNWKDELDTWGYFR 181
Cdd:cd18062     20 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTialitylmehkringpFLIIVPLSTLSNWVYEFDKWAPSV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  182 VTVLH-GSKKDNE--LLRLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKA-VKCKVRIGL 257
Cdd:cd18062    100 VKVSYkGSPAARRafVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLLL 179
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039744333  258 TGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEH-GQRHTATKRELATgrkAMHRLAKKMSGWFLRRTK 331
Cdd:cd18062    180 TGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVDLNEEETIL---IIRRLHKVLRPFLLRRLK 251
DEXDc smart00487
DEAD-like helicases superfamily;
122-270 2.06e-25

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 105.27  E-value: 2.06e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333   122 LRDYQREGAQFLYRHYiegRGCILGDDMGLGKTIQM---------------FLIVAPLSVL-YNWKDELDTWGYF----R 181
Cdd:smart00487    9 LRPYQKEAIEALLSGL---RDVILAAPTGSGKTLAAllpalealkrgkggrVLVLVPTRELaEQWAEELKKLGPSlglkV 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333   182 VTVLHGSKKDNELLRLKQRKCEIALTTYETLRLCLEE--LNSLEWSAIIVDEAHRIKNPKAR--VTEVMKAV-KCKVRIG 256
Cdd:smart00487   86 VGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLLENdkLSLSNVDLVILDEAHRLLDGGFGdqLEKLLKLLpKNVQLLL 165
                           170
                    ....*....|....
gi 1039744333   257 LTGTVLQNNMKELW 270
Cdd:smart00487  166 LSATPPEEIENLLE 179
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
122-308 2.50e-24

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


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 103.81  E-value: 2.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLY---------RHYIEGRGCILGDDMGLGKTIQMF------------------LIVAPLSVLYNWKDEL 174
Cdd:cd18068      1 LKPHQVDGVQFMWdccceslkkTKKSPGSGCILAHCMGLGKTLQVVtflhtvllceklenfsrvLVVCPLNTVLNWLNEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  175 DTWGYF-------RVTVLhGSKKDNELLRLK----QRKCEIALTTYETLRLCLEELN-SLEWSA---------------I 227
Cdd:cd18068     81 EKWQEGlkdeekiEVNEL-ATYKRPQERSYKlqrwQEEGGVMIIGYDMYRILAQERNvKSREKLkeifnkalvdpgpdfV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  228 IVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKELWCVMDWAVPGLLGSRIHFKKQFSDPVEHGQRHTATKRE 307
Cdd:cd18068    160 VCDEGHILKNEASAVSKAMNSIRTKRRIVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQNGQCADSTLVD 239

                   .
gi 1039744333  308 L 308
Cdd:cd18068    240 V 240
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
122-331 3.97e-24

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: 102.79  E-value: 3.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQMF----------------LIVAPLSVLYNWKDELDTW-GYFRVTV 184
Cdd:cd18065     16 LRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIallgylkhyrnipgphMVLVPKSTLHNWMNEFKRWvPSLRAVC 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  185 LHGSKKDNELL---RLKQRKCEIALTTYETLRLCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTV 261
Cdd:cd18065     96 LIGDKDARAAFirdVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVREFKTTNRLLLTGTP 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  262 LQNNMKELWCVMDWAVPGLLGSRIHFKKQFSdpvehgqrhtaTKRELATgRKAMHRLAKKMSGWFLRRTK 331
Cdd:cd18065    176 LQNNLHELWALLNFLLPDVFNSADDFDSWFD-----------TKNCLGD-QKLVERLHAVLKPFLLRRIK 233
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
122-278 3.07e-22

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: 95.92  E-value: 3.07e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCILGDDMGLGKTIQMF---------------LIVAPLSVLYNWKDELDTWG-YFRVTVL 185
Cdd:cd17998      1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIaflaylkeigipgphLVVVPSSTLDNWLREFKRWCpSLKVEPY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  186 HGSKKDNELLR---LKQR-KCEIALTTYETLRLCLEE---LNSLEWSAIIVDEAHRIKNPKA-RVTEVMKaVKCKVRIGL 257
Cdd:cd17998     81 YGSQEERKHLRydiLKGLeDFDVIVTTYNLATSNPDDrsfFKRLKLNYVVYDEGHMLKNMTSeRYRHLMT-INANFRLLL 159
                          170       180
                   ....*....|....*....|.
gi 1039744333  258 TGTVLQNNMKELWCVMDWAVP 278
Cdd:cd17998    160 TGTPLQNNLLELMSLLNFIMP 180
HELICc smart00490
helicase superfamily c-terminal domain;
496-579 7.36e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 91.12  E-value: 7.36e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333   496 DVLQQYCMASGLDYRRLDGSTKSEERLKIVKEFNSsqDVNICLVSTMAGGLGLNFVGANVVILFDPTWNPANDLQAVDRA 575
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNN--GKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 1039744333   576 YRIG 579
Cdd:smart00490   79 GRAG 82
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
122-270 1.88e-17

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: 82.78  E-value: 1.88e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLyrhyIEGRGCILGDDMGLGKT---------IQM------FLIVAPLSVLYN-WKDELDTWGYFR---V 182
Cdd:cd18013      1 PHPYQKVAINFI----IEHPYCGLFLDMGLGKTvttltalsdLQLddftrrVLVIAPLRVARStWPDEVEKWNHLRnltV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  183 TVLHGSKKdnELLRLKQRKCEIALTTYETLR-LCLEELNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVR--IGLTG 259
Cdd:cd18013     77 SVAVGTER--QRSKAANTPADLYVINRENLKwLVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKVRPVIKrlIGLTG 154
                          170
                   ....*....|.
gi 1039744333  260 TVLQNNMKELW 270
Cdd:cd18013    155 TPSPNGLMDLW 165
Tudor_ERCC6L2 cd20400
Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ...
17-72 6.09e-17

Tudor domain found in DNA excision repair protein ERCC-6-like 2 (ERCC6L2) and similar proteins; ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. ERCC6L2 gene mutations have been associated with bone marrow failure that includes developmental delay and microcephaly. It contains an N-terminal Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410471  Cd Length: 59  Bit Score: 76.21  E-value: 6.09e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039744333   17 WCPGERCLAPSLDNKKLCEASIKSITVDGNGKPFAVVL---YPDFQEKTIPLQRLQEVK 72
Cdd:cd20400      1 WHVGDRCLAPYSGDGKLYEAVIKSISTDENGKSFAVVKflgYESDEDEKVPVSKLQKVK 59
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
122-301 7.21e-16

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: 78.10  E-value: 7.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIegRGCILGDDMGLGKTIQM---------------FLIVAPLSVLYNWKDELDTWGYFRVTVLH 186
Cdd:cd18011      1 PLPHQIDAVLRALRKPP--VRLLLADEVGLGKTIEAgliikelllrgdakrVLILCPASLVEQWQDELQDKFGLPFLILD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  187 GSKKDNELLRLKQRKCE--IALTTYETLR---LCLEELNSLEWSAIIVDEAHRIKN----PKARVTEVMKAVKCKVR--I 255
Cdd:cd18011     79 RETAAQLRRLIGNPFEEfpIVIVSLDLLKrseERRGLLLSEEWDLVVVDEAHKLRNsgggKETKRYKLGRLLAKRARhvL 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1039744333  256 GLTGTVLQNNMKELWCVMDWAVPGllgsRIHFKKQFSDPVEHGQRH 301
Cdd:cd18011    159 LLTATPHNGKEEDFRALLSLLDPG----RFAVLGRFLRLDGLREVL 200
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
130-270 4.54e-15

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: 76.36  E-value: 4.54e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  130 AQFLYRHYIEGRGCILGDDMGLGKTIQMF--------------------------------------LIVAPLSVLYNWK 171
Cdd:cd18072     10 AWLLWRERQKPRGGILADDMGLGKTLTMIalilaqkntqnrkeeekekalteweskkdstlvpsagtLVVCPASLVHQWK 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  172 DELDT---WGYFRVTVLHGSKKDNELLRLkqRKCEIALTTYETL---------RLCLEELNSLEWSAIIVDEAHRIKNPK 239
Cdd:cd18072     90 NEVESrvaSNKLRVCLYHGPNRERIGEVL--RDYDIVITTYSLVakeiptykeESRSSPLFRIAWARIILDEAHNIKNPK 167
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039744333  240 ARVTEVMKAVKCKVRIGLTGTVLQNNMKELW 270
Cdd:cd18072    168 VQASIAVCKLRAHARWALTGTPIQNNLLDMY 198
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
79-260 7.94e-13

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 73.14  E-value: 7.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333   79 RSLIFDDKDLEKPYFPDRKIPSLASAFQLSEDGDSIPYTinryLRDYQREGAQFLYRHYIEG--RGCILGDdMGLGKTI- 155
Cdd:COG1061     42 IKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFE----LRPYQQEALEALLAALERGggRGLVVAP-TGTGKTVl 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  156 -----------QMFLIVAPLSVLYN-WKDELDTWgyFRVTVLHGSKKDNEllrlkqrkCEIALTTYETL--RLCLEELNS 221
Cdd:COG1061    117 alalaaellrgKRVLVLVPRRELLEqWAEELRRF--LGDPLAGGGKKDSD--------APITVATYQSLarRAHLDELGD 186
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039744333  222 lEWSAIIVDEAHRIknPKARVTEVMKAVKCKVRIGLTGT 260
Cdd:COG1061    187 -RFGLVIIDEAHHA--GAPSYRRILEAFPAAYRLGLTAT 222
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
122-260 7.97e-13

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


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 67.33  E-value: 7.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEGRGCIlgdDM--GLGKTIQM-----------FLIVAP-LSVLYNWKDELDTWGYFRVTVLHG 187
Cdd:cd17926      1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKTLTAlaliaylkelrTLIVVPtDALLDQWKERFEDFLGDSSIGLIG 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039744333  188 SKKDNellrlKQRKCEIALTTYETLRLCLEELNSL--EWSAIIVDEAHRIKNPKARvtEVMKAVKCKVRIGLTGT 260
Cdd:cd17926     78 GGKKK-----DFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAHHLPAKTFS--EILKELNAKYRLGLTAT 145
ResIII pfam04851
Type III restriction enzyme, res subunit;
122-260 3.17e-11

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 63.07  E-value: 3.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRHYIEG--RGCIlgdDM--GLGKTIQM---------------FLIVAP-LSVLYNWKDELDtwGYFR 181
Cdd:pfam04851    4 LRPYQIEAIENLLESIKNGqkRGLI---VMatGSGKTLTAakliarlfkkgpikkVLFLVPrKDLLEQALEEFK--KFLP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  182 VTVLHGSKKDNELLRLKQRKCEIALTTYETL----RLCLEELNSLEWSAIIVDEAHRIKNPKARvtEVMKAVKCKVRIGL 257
Cdd:pfam04851   79 NYVEIGEIISGDKKDESVDDNKIVVTTIQSLykalELASLELLPDFFDVIIIDEAHRSGASSYR--NILEYFKPAFLLGL 156

                   ...
gi 1039744333  258 TGT 260
Cdd:pfam04851  157 TAT 159
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
122-269 3.89e-09

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


Pssm-ID: 350828 [Multi-domain]  Cd Length: 257  Bit Score: 59.28  E-value: 3.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRhyiegRGCILGDDMGLGKTIQMF-----------------------------------------LI 160
Cdd:cd18070      1 LLPYQRRAVNWMLV-----PGGILADEMGLGKTVEVLalillhprpdndldaadddsdemvccpdclvaetpvsskatLI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  161 VAPLSVLYNWKDELD--TWGYFRVTVLHGSKKDNELL-----RLKQrkCEIALTTYETLR--------------LCLEE- 218
Cdd:cd18070     76 VCPSAILAQWLDEINrhVPSSLKVLTYQGVKKDGALAspapeILAE--YDIVVTTYDVLRtelhyaeanrsnrrRRRQKr 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039744333  219 -------LNSLEWSAIIVDEAHRIKNPKARVTEVMKAVKCKVRIGLTGTVLQNNMKEL 269
Cdd:cd18070    154 yeappspLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDL 211
DEXHc_XPB cd18029
DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription ...
122-262 1.73e-08

DEXH-box helicase domain of TFIIH XPB subunit and similar proteins; TFIIH basal transcription factor complex helicase XPB subunit (also known as DNA excision repair protein ERCC-3 or TFIIH 89 kDa subunit) is the ATP-dependent 3'-5' DNA helicase component of the core-TFIIH basal transcription factor, involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. XPB 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: 350787 [Multi-domain]  Cd Length: 169  Bit Score: 55.39  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  122 LRDYQREGAQFLYRhyiEGRG--------CilgddmGLGKTI----------QMFLIVAPLSV-LYNWKDELDTWGYF-- 180
Cdd:cd18029      9 LRPYQEKALSKMFG---NGRArsgvivlpC------GAGKTLvgitaactikKSTLVLCTSAVsVEQWRRQFLDWTTIdd 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  181 -RVTVLHGSKKDnellrlKQRKCEIALTTYETLR----------LCLEELNSLEWSAIIVDEAHRIKNPKARvtEVMKAV 249
Cdd:cd18029     80 eQIGRFTSDKKE------IFPEAGVTVSTYSMLAntrkrspeseKFMEFITEREWGLIILDEVHVVPAPMFR--RVLTLQ 151
                          170
                   ....*....|...
gi 1039744333  250 KCKVRIGLTGTVL 262
Cdd:cd18029    152 KAHCKLGLTATLV 164
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
140-260 4.65e-08

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


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 53.56  E-value: 4.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  140 GRGCILGDDMGLGKTIQMF--------------LIVAPLSVL-YNWKDELDTWGYF--RVTVLHGSKKDNELLRLKQRKC 202
Cdd:cd00046      1 GENVLITAPTGSGKTLAALlaalllllkkgkkvLVLVPTKALaLQTAERLRELFGPgiRVAVLVGGSSAEEREKNKLGDA 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744333  203 EIALTTYETLRLCLEELNSL---EWSAIIVDEAHRIKnPKARVTEVMKAVKCKV------RIGLTGT 260
Cdd:cd00046     81 DIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALL-IDSRGALILDLAVRKAglknaqVILLSAT 146
MPH1 COG1111
ERCC4-related helicase [Replication, recombination and repair];
462-600 5.05e-06

ERCC4-related helicase [Replication, recombination and repair];


Pssm-ID: 440728 [Multi-domain]  Cd Length: 718  Bit Score: 51.27  E-value: 5.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  462 PKYSGKMKVLQQLLNHFRKqrDKVLLFSFSTKLLDVLQQYCMASGLDYRRL------DGST--KSEERLKIVKEFnSSQD 533
Cdd:COG1111    335 PKLSKLREILKEQLGTNPD--SRIIVFTQYRDTAEMIVEFLSEPGIKAGRFvgqaskEGDKglTQKEQIEILERF-RAGE 411
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039744333  534 VNIcLVSTMAGGLGLNFVGANVVILFDPTWNPANDLQavdRAYRIGQCRDVKVLRLISLGTVEEIMY 600
Cdd:COG1111    412 FNV-LVATSVAEEGLDIPEVDLVIFYEPVPSEIRSIQ---RKGRTGRKREGRVVVLIAKGTRDEAYY 474
Tudor_SMN_SPF30-like cd21182
Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing ...
20-71 3.85e-05

Tudor domain found in survival motor neuron protein (SMN), motor neuron-related-splicing factor 30 (SPF30), and similar proteins; This group contains SMN, SPF30, Tudor domain-containing protein 3 (TDRD3), DNA excision repair protein ERCC-6-like 2 (ERCC6L2), and similar proteins. SMN, also called component of gems 1, or Gemin-1, is part of a multimeric SMN complex that includes spliceosomal Sm core proteins and plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. SPF30, also called 30 kDa splicing factor SMNrp, SMN-related protein, or survival motor neuron domain-containing protein 1 (SMNDC1), is an essential pre-mRNA splicing factor required for assembly of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the spliceosome. TDRD3 is a scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. ERCC6L2, also called DNA repair and recombination protein RAD26-like (RAD26L), may be involved in early DNA damage response. It regulates RNA Pol II-mediated transcription via its interaction with DNA-dependent protein kinase (DNA-PK) to resolve R loops and minimize transcription-associated genome instability. Members of this group contain a single Tudor domain. The Tudor domain binds to proteins with dimethylated arginine or lysine residues, and may also bind methylated histone tails to facilitate protein-protein interactions.


Pssm-ID: 410549  Cd Length: 50  Bit Score: 42.24  E-value: 3.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039744333   20 GERCLAPSLDNKKLCEASIKSITVDGNGkpfAVVLYPDF-QEKTIPLQRLQEV 71
Cdd:cd21182      1 GDKCLAPYSDDGKYYEATIEEITEESDT---ATVVFDGYgNSEEVPLSDLKPL 50
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
538-580 5.35e-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: 43.08  E-value: 5.35e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1039744333  538 LVSTMAGGLGLNFVGANVVILFDPTWNPANDLQAVDRAYRIGQ 580
Cdd:cd18785     26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
138-261 3.90e-04

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 42.61  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  138 IEGRGCILGDDMGLGKT-------IQMF---------LIVAPLSVL----Y-NWKDELDTWGYFRVTVLHGSKKDNELLR 196
Cdd:pfam00270   12 LEGRDVLVQAPTGSGKTlafllpaLEALdkldngpqaLVLAPTRELaeqiYeELKKLGKGLGLKVASLLGGDSRKEQLEK 91
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039744333  197 LKqrKCEIALTTYETLRLCLEE---LNSLEWsaIIVDEAHRI--KNPKARVTEVMKAVKCKVRI-GLTGTV 261
Cdd:pfam00270   92 LK--GPDILVGTPGRLLDLLQErklLKNLKL--LVLDEAHRLldMGFGPDLEEILRRLPKKRQIlLLSATL 158
PRK02250 PRK02250
hypothetical protein; Provisional
285-389 6.69e-03

hypothetical protein; Provisional


Pssm-ID: 179393 [Multi-domain]  Cd Length: 166  Bit Score: 39.09  E-value: 6.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744333  285 IHFKKQFSdpvEHGQRHTATKRElatgrkamhRLAKKMSGWFLrrtktlIKGQLPKKEdrmvycslTDFQKAVYQTVlet 364
Cdd:PRK02250    92 VEFKAYFD---EEGKRYCLEERS---------RFLKENGLWYY------IDGTFPEEE--------PEQDPRLNQSV--- 142
                           90       100
                   ....*....|....*....|....*
gi 1039744333  365 edVALILTSSQPCTCGSGQKRRKCC 389
Cdd:PRK02250   143 --SSLKQGRNDPCICGSGKKFKKCC 165
VIGSSK pfam14773
Helicase-associated putative binding domain, C-terminal; The function of this short, ...
1068-1091 8.25e-03

Helicase-associated putative binding domain, C-terminal; The function of this short, serine-rich C-terminal region is not known. However, as it is frequently found at the very C-terminus of P-loop containing nucleoside triphosphate hydrolases, it might possibly be a binding domain.


Pssm-ID: 464308  Cd Length: 62  Bit Score: 36.04  E-value: 8.25e-03
                           10        20
                   ....*....|....*....|....
gi 1039744333 1068 VAYIHSNQNVIGSSRAENHMSRWA 1091
Cdd:pfam14773   38 VEYTHENSEVIGTSKVEEQLSRRA 61
 
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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