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Conserved domains on  [gi|192807314|ref|NP_001122317|]
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transcription activator BRG1 isoform C [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
731-981 1.88e-173

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: 520.76  E-value: 1.88e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  731 YYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 810
Cdd:cd18062     1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  811 PLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 890
Cdd:cd18062    81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  891 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 970
Cdd:cd18062   161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                         250
                  ....*....|.
gi 192807314  971 VLRPFLLRRLK 981
Cdd:cd18062   241 VLRPFLLRRLK 251
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
750-1232 1.35e-162

Probable chromatin-remodeling complex ATPase chain; Provisional


The actual alignment was detected with superfamily member PLN03142:

Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 520.90  E-value: 1.35e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  750 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSV 829
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  830 VKVSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 905
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  906 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 985
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  986 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQHIEE----SFS 1060
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPgppyTTG 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1061 EHLgftggivqgldlYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLK 1140
Cdd:PLN03142  464 EHL------------VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASID 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1141 TFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKY 1220
Cdd:PLN03142  532 AFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYK 611
                         490
                  ....*....|..
gi 192807314 1221 KLNVDQKVIQAG 1232
Cdd:PLN03142  612 KLALDALVIQQG 623
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1428-1534 5.53e-61

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


:

Pssm-ID: 99947  Cd Length: 107  Bit Score: 203.81  E-value: 5.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1428 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1507
Cdd:cd05516     2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                          90       100
                  ....*....|....*....|....*..
gi 192807314 1508 TFNLEGSLIYEDSIVLQSVFTSVRQKI 1534
Cdd:cd05516    81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1289-1356 2.26e-23

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


:

Pssm-ID: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 95.02  E-value: 2.26e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 192807314  1289 DRRREEARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWL 1356
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
460-532 5.98e-23

domain in helicases and associated with SANT domains;


:

Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 94.00  E-value: 5.98e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 192807314    460 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 532
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
BRK smart00592
domain in transcription and CHROMO domain helicases;
612-656 1.10e-16

domain in transcription and CHROMO domain helicases;


:

Pssm-ID: 197800  Cd Length: 45  Bit Score: 75.08  E-value: 1.10e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 192807314    612 MSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSD 656
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
171-205 1.42e-13

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


:

Pssm-ID: 462622  Cd Length: 35  Bit Score: 65.82  E-value: 1.42e-13
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 192807314   171 PFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 205
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
Med15 super family cl26621
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
42-222 5.71e-08

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


The actual alignment was detected with superfamily member pfam09606:

Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 57.71  E-value: 5.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    42 MMGPSP---GPPSA----------------GHPIPTQGPGGYPQDNMH--------QMHKPMESMHEKGMSDDPryNQMK 94
Cdd:pfam09606   98 MMGPMGpgpGGPMGqqmggpgtasnllaslGRPQMPMGGAGFPSQMSRvgrmqpggQAGGMMQPSSGQPGSGTP--NQMG 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    95 GMGmrsGGHAGMGPPPSPMDQHS--QGYPSPLGGSehaSSPVPASGPSSGPQMSSGPGGAP---LDGADPQ-ALGQQNRG 168
Cdd:pfam09606  176 PNG---GPGQGQAGGMNGGQQGPmgGQMPPQMGVP---GMPGPADAGAQMGQQAQANGGMNpqqMGGAPNQvAMQQQQPQ 249
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 192807314   169 PTPfNQNQLHQLRAQIMAYkmlARGQPLPDHLQMAVQgkrPMPGMQQQMPTLPP 222
Cdd:pfam09606  250 QQG-QQSQLGMGINQMQQM---PQGVGGGAGQGGPGQ---PMGPPGQQPGAMPN 296
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
364-570 5.14e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  364 VEILQEREY-------RLQARIAHRIQELENLPGSLAgdlRTKATIELKALRLLNFQRQLRQEvvvcmrrDTALETALNA 436
Cdd:COG1196   283 LEEAQAEEYellaelaRLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEEL-------EEELEEAEEE 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  437 KAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQK 516
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 192807314  517 KENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRQ 570
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEE 485
 
Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
731-981 1.88e-173

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: 520.76  E-value: 1.88e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  731 YYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 810
Cdd:cd18062     1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  811 PLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 890
Cdd:cd18062    81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  891 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 970
Cdd:cd18062   161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                         250
                  ....*....|.
gi 192807314  971 VLRPFLLRRLK 981
Cdd:cd18062   241 VLRPFLLRRLK 251
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
750-1232 1.35e-162

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 520.90  E-value: 1.35e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  750 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSV 829
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  830 VKVSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 905
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  906 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 985
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  986 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQHIEE----SFS 1060
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPgppyTTG 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1061 EHLgftggivqgldlYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLK 1140
Cdd:PLN03142  464 EHL------------VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASID 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1141 TFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKY 1220
Cdd:PLN03142  532 AFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYK 611
                         490
                  ....*....|..
gi 192807314 1221 KLNVDQKVIQAG 1232
Cdd:PLN03142  612 KLALDALVIQQG 623
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
631-1216 1.12e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 406.53  E-value: 1.12e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  631 TDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENA 710
Cdd:COG0553   121 ALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAE 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  711 KQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALmvNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTI 790
Cdd:COG0553   201 LLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGL--KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQAL 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  791 ALITYLMEHKRInGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPqlrSGKFNVLLTTYEYIIKDKHIL 870
Cdd:COG0553   279 ALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANP---FEDADLVITSYGLLRRDIELL 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  871 AKIRWKYMIVDEGHRMKNHHCKLTQV---LNthyvAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPf 947
Cdd:COG0553   355 AAVDWDLVILDEAQHIKNPATKRAKAvraLK----ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP- 429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  948 amtGEKVDLNEEEtiliirRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMqakgVLLTDGSEKDKK 1027
Cdd:COG0553   430 ---IEKGDEEALE------RLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV----LEYLRRELEGAE 496
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1028 GKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHlgftggivqgldlyraSGKFELLDRILPKLRATNHKVLLFCQMTS 1107
Cdd:COG0553   497 GIRRRGLILAALTRLRQICSHPALLLEEGAELSGR----------------SAKLEALLELLEELLAEGEKVLVFSQFTD 560
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1108 LMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEpGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQ 1187
Cdd:COG0553   561 TLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAI 639
                         570       580
                  ....*....|....*....|....*....
gi 192807314 1188 DRAHRIGQQNEVRVLRLCTVNSVEEKILA 1216
Cdd:COG0553   640 DRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
757-1052 2.22e-114

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: 362.77  E-value: 2.22e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   757 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLME-HKRINGPFLIIVPLSTLSNWAYEFDKWA--PSVVKV 832
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   833 SYKGSPAAR-RAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLTG 911
Cdd:pfam00176   81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   912 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetiLIIRRLHKVLRPFLLRRLKKEVEAQLPEK 991
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 192807314   992 VEYVIKCDMSALQRVLY-RHMQAKGVLLTDGSEkdkKGKGGTKTLMNTIMQLRKICNHPYMF 1052
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1428-1534 5.53e-61

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 203.81  E-value: 5.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1428 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1507
Cdd:cd05516     2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                          90       100
                  ....*....|....*....|....*..
gi 192807314 1508 TFNLEGSLIYEDSIVLQSVFTSVRQKI 1534
Cdd:cd05516    81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1079-1205 7.06e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 193.08  E-value: 7.06e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1079 SGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPgSEYFIFLLSTRA 1158
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 192807314 1159 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1205
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXDc smart00487
DEAD-like helicases superfamily;
754-942 6.18e-32

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 124.14  E-value: 6.18e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    754 LKQYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEHKriNGPFLIIVPLSTL-SNWAYEFDKWAPS-VV 830
Cdd:smart00487    9 LRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlGL 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    831 KVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKD--KHILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYVAPRR 906
Cdd:smart00487   84 KVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQL 163
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 192807314    907 LLLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 942
Cdd:smart00487  164 LLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
BROMO smart00297
bromo domain;
1426-1534 4.18e-31

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 118.54  E-value: 4.18e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   1426 PNLTKKMKKIVDAVIKYKDSssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQN 1505
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS---HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 192807314   1506 AQTFNLEGSLIYEDSIVLQSVFTSVRQKI 1534
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1080-1194 4.64e-28

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: 109.61  E-value: 4.64e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  1080 GKFELLDRILPKLRatNHKVLLFCQMTSlmTIMEDYFAYR-GFKYLRLDGTTKAEDRGMLLKTFNEpgSEYFIfLLSTRA 1158
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRK--GKIDV-LVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 192807314  1159 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIG 1194
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1289-1356 2.26e-23

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


Pssm-ID: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 95.02  E-value: 2.26e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 192807314  1289 DRRREEARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWL 1356
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
460-532 5.98e-23

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 94.00  E-value: 5.98e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 192807314    460 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 532
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
HELICc smart00490
helicase superfamily c-terminal domain;
1111-1194 8.95e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 8.95e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   1111 IMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSeyfIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRA 1190
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI---KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 192807314   1191 HRIG 1194
Cdd:smart00490   79 GRAG 82
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
461-527 4.25e-20

HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.


Pssm-ID: 462194 [Multi-domain]  Cd Length: 67  Bit Score: 85.32  E-value: 4.25e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 192807314   461 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERM 527
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1432-1520 1.46e-19

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 84.67  E-value: 1.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  1432 MKKIVDAVIKykdsssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNL 1511
Cdd:pfam00439    1 CLEILDKLME-------HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73

                   ....*....
gi 192807314  1512 EGSLIYEDS 1520
Cdd:pfam00439   74 PGSVIYKAA 82
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1403-1536 3.94e-17

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 85.24  E-value: 3.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1403 KDDESKKQKKRGRPPAEKLSPNPPN--LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKI 1480
Cdd:COG5076   116 SGLGSLLMAHLKTSVKKRKTPKIEDelLYADNKAIAKFKKQLFLRD-GRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTI 194
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 192807314 1481 KERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEK 1536
Cdd:COG5076   195 QKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPE 250
BRK smart00592
domain in transcription and CHROMO domain helicases;
612-656 1.10e-16

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 75.08  E-value: 1.10e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 192807314    612 MSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSD 656
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
611-654 2.98e-16

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


Pssm-ID: 462196  Cd Length: 44  Bit Score: 73.70  E-value: 2.98e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 192807314   611 QMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPR 654
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
171-205 1.42e-13

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


Pssm-ID: 462622  Cd Length: 35  Bit Score: 65.82  E-value: 1.42e-13
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 192807314   171 PFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 205
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
171-204 6.65e-11

QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.


Pssm-ID: 214931  Cd Length: 36  Bit Score: 58.31  E-value: 6.65e-11
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 192807314    171 PFNQNQLHQLRAQIMAYK-MLARGQPLPDHLQMAV 204
Cdd:smart00951    2 PFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
42-222 5.71e-08

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 57.71  E-value: 5.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    42 MMGPSP---GPPSA----------------GHPIPTQGPGGYPQDNMH--------QMHKPMESMHEKGMSDDPryNQMK 94
Cdd:pfam09606   98 MMGPMGpgpGGPMGqqmggpgtasnllaslGRPQMPMGGAGFPSQMSRvgrmqpggQAGGMMQPSSGQPGSGTP--NQMG 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    95 GMGmrsGGHAGMGPPPSPMDQHS--QGYPSPLGGSehaSSPVPASGPSSGPQMSSGPGGAP---LDGADPQ-ALGQQNRG 168
Cdd:pfam09606  176 PNG---GPGQGQAGGMNGGQQGPmgGQMPPQMGVP---GMPGPADAGAQMGQQAQANGGMNpqqMGGAPNQvAMQQQQPQ 249
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 192807314   169 PTPfNQNQLHQLRAQIMAYkmlARGQPLPDHLQMAVQgkrPMPGMQQQMPTLPP 222
Cdd:pfam09606  250 QQG-QQSQLGMGINQMQQM---PQGVGGGAGQGGPGQ---PMGPPGQQPGAMPN 296
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
695-913 5.04e-07

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 54.26  E-value: 5.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  695 SDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNG--------VLKQYQIKGLE-WL 765
Cdd:COG1061    14 LRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGdeasgtsfELRPYQQEALEaLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  766 VSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRIngpfLIIVPLSTLSN-WAYEFDKWAPSVVKVSYKgspaarraf 844
Cdd:COG1061    94 AALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGDPLAGGGK--------- 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 192807314  845 vpqlRSGKFNVLLTTYEYIIKDKHiLAKI--RWKYMIVDEGHrmknhHC---KLTQVLNtHYVAPRRLLLTGTP 913
Cdd:COG1061   161 ----KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEAH-----HAgapSYRRILE-AFPAAYRLGLTATP 223
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
364-570 5.14e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  364 VEILQEREY-------RLQARIAHRIQELENLPGSLAgdlRTKATIELKALRLLNFQRQLRQEvvvcmrrDTALETALNA 436
Cdd:COG1196   283 LEEAQAEEYellaelaRLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEEL-------EEELEEAEEE 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  437 KAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQK 516
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 192807314  517 KENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRQ 570
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEE 485
PTZ00121 PTZ00121
MAEBL; Provisional
437-548 7.95e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  437 KAYKRSKRQSLREARITEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHAntEREQK 516
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614
                          90       100       110
                  ....*....|....*....|....*....|..
gi 192807314  517 KENERIEKERMRRlmaedEEGYRKLIDQKKDK 548
Cdd:PTZ00121 1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
45-227 1.57e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   45 PSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYNqMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPL 124
Cdd:PRK07764  619 AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG-GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAA 697
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  125 GGSEHA-SSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQnqlhqlraqimaykmLARGQPLPDHLQMA 203
Cdd:PRK07764  698 PAQPAPaPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP---------------PDPAGAPAQPPPPP 762
                         170       180
                  ....*....|....*....|....
gi 192807314  204 VQGKRPMPGMQQQMPTLPPPSVSA 227
Cdd:PRK07764  763 APAPAAAPAAAPPPSPPSEEEEMA 786
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
357-547 7.03e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 7.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   357 KPRGLDPVEILQEREY-------RLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTA 429
Cdd:TIGR02169  669 SRSEPAELQRLRERLEglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   430 LETALNAK-----------AYKRSKRQSLREA-----------RITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFK 487
Cdd:TIGR02169  749 LEQEIENVkselkeleariEELEEDLHKLEEAlndlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 192807314   488 EYHRSvtgKIQKLTKAVATYHAN-TEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKD 547
Cdd:TIGR02169  829 EYLEK---EIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
413-559 8.89e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 8.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   413 QRQLRQEVvvcMRRDTALETALNAKAYKRSKRQSLREARITEklEKQQKIEQERKRRQKHQEYLNSILQHAKdfkEYHRS 492
Cdd:pfam15709  360 QRRLQQEQ---LERAEKMREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQLQAAQERARQQQE---EFRRK 431
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 192807314   493 VTgKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEgyrklidqkkdKRLAYLLQQTDE 559
Cdd:pfam15709  432 LQ-ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE-----------ERLEYQRQKQEA 486
 
Name Accession Description Interval E-value
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
731-981 1.88e-173

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: 520.76  E-value: 1.88e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  731 YYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 810
Cdd:cd18062     1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  811 PLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 890
Cdd:cd18062    81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  891 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 970
Cdd:cd18062   161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                         250
                  ....*....|.
gi 192807314  971 VLRPFLLRRLK 981
Cdd:cd18062   241 VLRPFLLRRLK 251
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
751-981 1.80e-167

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: 504.21  E-value: 1.80e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  751 NGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVV 830
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  831 KVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLT 910
Cdd:cd17996    81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 192807314  911 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKV--DLNEEETILIIRRLHKVLRPFLLRRLK 981
Cdd:cd17996   161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
750-1232 1.35e-162

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 520.90  E-value: 1.35e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  750 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSV 829
Cdd:PLN03142  166 IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMNEIRRFCPVL 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  830 VKVSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvapr 905
Cdd:PLN03142  246 RAVKFHGNPEERAHQREElLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSLLSKTMrlfSTNY---- 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  906 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfAMTGEkvdlNEEETIliIRRLHKVLRPFLLRRLKKEVE 985
Cdd:PLN03142  322 RLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----NDQQEV--VQQLHKVLRPFLLRRLKSDVE 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  986 AQLPEKVEYVIKCDMSALQRVLYRHMQAKGV-LLTDGSEKDKkgkggtktLMNTIMQLRKICNHPYMFQHIEE----SFS 1060
Cdd:PLN03142  392 KGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLNIAMQLRKCCNHPYLFQGAEPgppyTTG 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1061 EHLgftggivqgldlYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLK 1140
Cdd:PLN03142  464 EHL------------VENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASID 531
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1141 TFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKY 1220
Cdd:PLN03142  532 AFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYK 611
                         490
                  ....*....|..
gi 192807314 1221 KLNVDQKVIQAG 1232
Cdd:PLN03142  612 KLALDALVIQQG 623
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
731-981 2.19e-162

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: 491.50  E-value: 2.19e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  731 YYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 810
Cdd:cd18063     1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  811 PLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 890
Cdd:cd18063    81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  891 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 970
Cdd:cd18063   161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240
                         250
                  ....*....|.
gi 192807314  971 VLRPFLLRRLK 981
Cdd:cd18063   241 VLRPFLLRRLK 251
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
631-1216 1.12e-124

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 406.53  E-value: 1.12e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  631 TDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENA 710
Cdd:COG0553   121 ALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAE 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  711 KQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALmvNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTI 790
Cdd:COG0553   201 LLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGL--KATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQAL 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  791 ALITYLMEHKRInGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPqlrSGKFNVLLTTYEYIIKDKHIL 870
Cdd:COG0553   279 ALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRERAKGANP---FEDADLVITSYGLLRRDIELL 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  871 AKIRWKYMIVDEGHRMKNHHCKLTQV---LNthyvAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPf 947
Cdd:COG0553   355 AAVDWDLVILDEAQHIKNPATKRAKAvraLK----ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP- 429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  948 amtGEKVDLNEEEtiliirRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMqakgVLLTDGSEKDKK 1027
Cdd:COG0553   430 ---IEKGDEEALE------RLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV----LEYLRRELEGAE 496
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1028 GKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHlgftggivqgldlyraSGKFELLDRILPKLRATNHKVLLFCQMTS 1107
Cdd:COG0553   497 GIRRRGLILAALTRLRQICSHPALLLEEGAELSGR----------------SAKLEALLELLEELLAEGEKVLVFSQFTD 560
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1108 LMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEpGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQ 1187
Cdd:COG0553   561 TLDLLEERLEERGIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAI 639
                         570       580
                  ....*....|....*....|....*....
gi 192807314 1188 DRAHRIGQQNEVRVLRLCTVNSVEEKILA 1216
Cdd:COG0553   640 DRAHRIGQTRDVQVYKLVAEGTIEEKILE 668
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
757-1052 2.22e-114

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: 362.77  E-value: 2.22e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   757 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTIALITYLME-HKRINGPFLIIVPLSTLSNWAYEFDKWA--PSVVKV 832
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHvDKNWGGPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   833 SYKGSPAAR-RAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLTG 911
Cdd:pfam00176   81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   912 TPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetiLIIRRLHKVLRPFLLRRLKKEVEAQLPEK 991
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 192807314   992 VEYVIKCDMSALQRVLY-RHMQAKGVLLTDGSEkdkKGKGGTKTLMNTIMQLRKICNHPYMF 1052
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYqTFLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
751-981 2.80e-93

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: 300.78  E-value: 2.80e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  751 NGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVV 830
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  831 KVSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL---NTHYvaprR 906
Cdd:cd17997    81 VVVLIGDKEERADIIrDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVrlfNSRN----R 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 192807314  907 LLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNApfamtgEKVDLNEEEtilIIRRLHKVLRPFLLRRLK 981
Cdd:cd17997   157 LLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNV------NNCDDDNQE---VVQRLHKVLRPFLLRRIK 222
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
751-981 5.58e-92

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: 297.76  E-value: 5.58e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  751 NGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKrINGPFLIIVPLSTLSNWAYEFDKWAPSVV 830
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRERG-VWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  831 KVSYKGSPAARRAFVPQLRS-----GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPR 905
Cdd:cd18009    80 VLLYHGTKEERERLRKKIMKregtlQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELK-TFNSDN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 192807314  906 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFN--APFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLK 981
Cdd:cd18009   159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
754-979 1.31e-82

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: 270.38  E-value: 1.31e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARRAfvpqLRSG-----KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRLL 908
Cdd:cd18003    81 YYGSAKERKL----KRQGwmkpnSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 192807314  909 LTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF-AMTGEKVDLNEEetilIIRRLHKVLRPFLLRR 979
Cdd:cd18003   156 LTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLtAMSEGSQEENEE----LVRRLHKVLRPFLLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
754-979 1.10e-80

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: 264.60  E-value: 1.10e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd17993     2 LRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARRA------FVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAPRRL 907
Cdd:cd17993    82 YLGDIKSRDTireyefYFSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-FKTNNRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 192807314  908 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEqwfnapfamtgekVDLNEEETILiIRRLHKVLRPFLLRR 979
Cdd:cd17993   161 LITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-------------EEHDEEQEKG-IADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
754-930 2.92e-80

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: 262.12  E-value: 2.92e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYvAPRRLLLTGTP 913
Cdd:cd17919    81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR-AKRRLLLTGTP 159
                         170
                  ....*....|....*..
gi 192807314  914 LQNKLPELWALLNFLLP 930
Cdd:cd17919   160 LQNNLEELWALLDFLDP 176
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
754-979 1.20e-75

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: 250.63  E-value: 1.20e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVkVS 833
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDMNV-VV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARR------AFVPQL------RSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHY 901
Cdd:cd17995    80 YHGSGESRQiiqqyeMYFKDAqgrkkkGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK-KL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 192807314  902 VAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 979
Cdd:cd17995   159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG----------DLKTAEQ---VEKLQALLKPYMLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
752-991 1.63e-72

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: 242.65  E-value: 1.63e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  752 GVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVK 831
Cdd:cd18064    14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  832 VSYKGSPAARRAFVPQ-LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNtHYVAPRRLLLT 910
Cdd:cd18064    94 VCLIGDKDQRAAFVRDvLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR-EFKTTNRLLLT 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  911 GTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRRLKKEVEAQLPE 990
Cdd:cd18064   173 GTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQK----------LVERLHMVLRPFLLRRIKADVEKSLPP 242

                  .
gi 192807314  991 K 991
Cdd:cd18064   243 K 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
741-981 1.10e-71

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: 239.53  E-value: 1.10e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  741 RVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAY 820
Cdd:cd18065     3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  821 EFDKWAPSVVKVSYKGSPAARRAFV-PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 899
Cdd:cd18065    83 EFKRWVPSLRAVCLIGDKDARAAFIrDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  900 HYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvdlneeetilIIRRLHKVLRPFLLRR 979
Cdd:cd18065   162 EFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRR 231

                  ..
gi 192807314  980 LK 981
Cdd:cd18065   232 IK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
754-979 2.71e-66

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: 223.92  E-value: 2.71e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAAR---RAFVPQ----LRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRR 906
Cdd:cd18002    81 YWGNPKDRkvlRKFWDRknlyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL-LSFHCRNR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 192807314  907 LLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGE-KVDLNEEEtiliIRRLHKVLRPFLLRR 979
Cdd:cd18002   160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAEnKTGLNEHQ----LKRLHMILKPFMLRR 229
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
754-979 3.72e-63

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: 215.25  E-value: 3.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd18054    21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARRAFV------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRL 907
Cdd:cd18054   101 YIGDLMSRNTIReyewihSQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 192807314  908 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLRPFLLRR 979
Cdd:cd18054   180 LITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE-------DHGKGRENGYQS-------LHKVLEPFLLRR 237
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
750-981 5.18e-62

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: 211.27  E-value: 5.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  750 VNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYlMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSV 829
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTLALLLS-RKEEGRKGPSLVVAPTSLIYNWEEEAAKFAPEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  830 VKVSYKGSPAARRAfvpQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHYvaprR 906
Cdd:cd18012    80 KVLVIHGTKRKREK---LRALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAvkaLKADH----R 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 192807314  907 LLLTGTPLQNKLPELWALLNFLLPTIFKScstfEQWFNAPFAMTGEKvDLNEEEtiliIRRLHKVLRPFLLRRLK 981
Cdd:cd18012   153 LALTGTPIENHLGELWSIFDFLNPGLLGS----YKRFKKRFAKPIEK-DGDEEA----LEELKKLISPFILRRLK 218
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1428-1534 5.53e-61

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 203.81  E-value: 5.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1428 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1507
Cdd:cd05516     2 LTKKMNKIVDVVIKYKDSD-GRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                          90       100
                  ....*....|....*....|....*..
gi 192807314 1508 TFNLEGSLIYEDSIVLQSVFTSVRQKI 1534
Cdd:cd05516    81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
754-979 3.88e-60

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: 205.75  E-value: 3.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARRAFVPQLRS-GKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVaPRRLLLTGT 912
Cdd:cd18006    81 YMGDKEKRLDLQQDIKStNRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV-DFRLLLTGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 192807314  913 PLQNKLPELWALLNFLLPTIFkSCSTFEQWFNApFAMTGEKVDLNEEetiliirrLHKVLRPFLLRR 979
Cdd:cd18006   160 PIQNSLQELYALLSFIEPNVF-PKDKLDDFIKA-YSETDDESETVEE--------LHLLLQPFLLRR 216
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
754-979 7.60e-58

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: 198.43  E-value: 7.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSpaarrafvpqlrsgkfNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVApRRLLLTGTP 913
Cdd:cd17994    81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIG-YKLLLTGTP 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 192807314  914 LQNKLPELWALLNFLLPTIFKSCSTFeqwfnapfamTGEKVDLNEEETiliIRRLHKVLRPFLLRR 979
Cdd:cd17994   144 LQNNLEELFHLLNFLTPERFNNLQGF----------LEEFADISKEDQ---IKKLHDLLGPHMLRR 196
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1079-1205 7.06e-57

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


Pssm-ID: 350180 [Multi-domain]  Cd Length: 135  Bit Score: 193.08  E-value: 7.06e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1079 SGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPgSEYFIFLLSTRA 1158
Cdd:cd18793    10 SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDIRVFLLSTKA 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 192807314 1159 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLC 1205
Cdd:cd18793    89 GGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
754-933 1.47e-53

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


Pssm-ID: 350756 [Multi-domain]  Cd Length: 187  Bit Score: 185.67  E-value: 1.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEhKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARRafvpQLR------SGKFNVLLTTYEYII---KDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNThYVAP 904
Cdd:cd17998    80 YYGSQEERK----HLRydilkgLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INAN 154
                         170       180
                  ....*....|....*....|....*....
gi 192807314  905 RRLLLTGTPLQNKLPELWALLNFLLPTIF 933
Cdd:cd17998   155 FRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
754-979 9.56e-51

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: 179.86  E-value: 9.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd18053    21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARRAFV------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPRRL 907
Cdd:cd18053   101 YLGDINSRNMIRthewmhPQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 192807314  908 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQwfnapfaMTGEKVDLNEEEtiliirrLHKVLRPFLLRR 979
Cdd:cd18053   180 LITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE-------EHGKGREYGYAS-------LHKELEPFLLRR 237
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
754-979 2.70e-49

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: 175.23  E-value: 2.70e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKR------INGPFLIIVPLSTLSNWAYEFDKWAP 827
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRansfnsENLPSLVVCPPTLVGHWVAEIKKYFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  828 SVVK--VSYKGSPAARRAFVPQLrsGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYVAPR 905
Cdd:cd17999    80 NAFLkpLAYVGPPQERRRLREQG--EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV-KQLKANH 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 192807314  906 RLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVD--LNEEETILIIRRLHKVLRPFLLRR 979
Cdd:cd17999   157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASRDSKAsaKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
754-930 3.04e-49

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: 173.66  E-value: 3.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAP------ 827
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPpfrvvv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  828 ------SVVKVSYKGSPAARRAFVPQLRsGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LN 898
Cdd:cd18000    81 lhssgsGTGSEEKLGSIERKSQLIRKVV-GDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAckqLR 159
                         170       180       190
                  ....*....|....*....|....*....|..
gi 192807314  899 ThyvaPRRLLLTGTPLQNKLPELWALLNFLLP 930
Cdd:cd18000   160 T----PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
754-979 5.08e-49

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: 174.07  E-value: 5.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT--YLMEhkrINGPFLIIVPLSTLSNWAYEFDKWAPSVVK 831
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSeiFLMG---IRGPFLIIAPLSTITNWEREFRTWTEMNAI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  832 VsYKGSPAARRAFV------------PQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNT 899
Cdd:cd18058    78 V-YHGSQISRQMIQqyemyyrdeqgnPLSGIFKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  900 HYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 979
Cdd:cd18058   157 MALE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG----------DLKTEEQ---VKKLQSILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
754-979 1.01e-48

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: 173.66  E-value: 1.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAAR-------------------RAFVPQLRSG-KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 893
Cdd:cd18055    81 YTGDKDSRaiirenefsfddnavkggkKAFKMKREAQvKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  894 TQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 973
Cdd:cd18055   161 FRVLNG-YKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226

                  ....*.
gi 192807314  974 PFLLRR 979
Cdd:cd18055   227 PHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
754-979 4.86e-48

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: 171.79  E-value: 4.86e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARRAFVPQ--------LRSG------------KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKL 893
Cdd:cd18057    81 YTGDKESRSVIRENefsfednaIRSGkkvfrmkkeaqiKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  894 TQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVLR 973
Cdd:cd18057   161 FRVLNS-YKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226

                  ....*.
gi 192807314  974 PFLLRR 979
Cdd:cd18057   227 PHMLRR 232
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
754-979 1.69e-47

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: 169.85  E-value: 1.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYlMEHKRINGPFLIIVPLSTLSNWAYEFDKWApSVVKVS 833
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQE-VYNVGIHGPFLVIAPLSTITNWEREFNTWT-EMNTIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARRA--------------FVPQlrSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNt 899
Cdd:cd18060    79 YHGSLASRQMiqqyemyckdsrgrLIPG--AYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  900 HYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 979
Cdd:cd18060   156 HMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
754-979 1.91e-47

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: 170.64  E-value: 1.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALIT-----------------YLMEHKRIN---GPFLIIVPLS 813
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAavlgktgtrrdrennrpRFKKKPPASsakKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  814 TLSNWAYEFDKWAPSVVKVsYKGSpaaRRAFVPQLR--SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHC 891
Cdd:cd18005    81 VLYNWKDELDTWGHFEVGV-YHGS---RKDDELEGRlkAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  892 KLTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPF----AMTGEKVDLNEEETilIIRR 967
Cdd:cd18005   157 KLTQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgqRHTATARELRLGRK--RKQE 233
                         250
                  ....*....|..
gi 192807314  968 LHKVLRPFLLRR 979
Cdd:cd18005   234 LAVKLSKFFLRR 245
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
754-979 2.21e-47

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: 169.86  E-value: 2.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPfLIIVPLSTLSNWAYEFDKWAPSV-VKV 832
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLIKSV-LVVMPTSLIPHWVKEFAKWTPGLrVKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  833 SYKGSPAARRAfvpQLRS--GKFNVLLTTYEYIIKDKHILA-----KIRWKYMIVDEGHRMKNHHCKLTQVLntHYV-AP 904
Cdd:cd18001    80 FHGTSKKERER---NLERiqRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSL--REIpAK 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 192807314  905 RRLLLTGTPLQNKLPELWALLNFLLP-TIFKSCSTFEQWFNAPFAMTGEKVDLNEEETI--LIIRRLHKVLRPFLLRR 979
Cdd:cd18001   155 NRIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPITRGRDKDATQGEKALgsEVAENLRQIIKPYFLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
754-979 6.02e-47

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: 168.29  E-value: 6.02e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALItYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVkVS 833
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTELNV-VV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAARRAFV--------PQLR----SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHY 901
Cdd:cd18059    79 YHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 192807314  902 VApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 979
Cdd:cd18059   159 LE-HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
754-979 1.47e-45

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: 164.47  E-value: 1.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVS 833
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  834 YKGSPAArRAFVPQ---------LRSG------------KFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCK 892
Cdd:cd18056    81 YVGDKDS-RAIIREnefsfednaIRGGkkasrmkkeasvKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  893 LTQVLNThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFnapfamtgekVDLNEEETiliIRRLHKVL 972
Cdd:cd18056   160 FFRVLNG-YSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF----------ADIAKEDQ---IKKLHDML 225

                  ....*..
gi 192807314  973 RPFLLRR 979
Cdd:cd18056   226 GPHMLRR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
754-979 1.79e-43

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: 158.99  E-value: 1.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVS--LYNNNLNG---ILADEMGLGKTIQTIALITYLMEHKRINGP----FLIIVPLSTLSNWAYEFDK 824
Cdd:cd18004     1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  825 WAPSVVK--VSYKGSPAARRAFVPQLRSGK-FNVLLTTYE-YIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTh 900
Cdd:cd18004    81 WLGLRRIkvVTADGNAKDVKASLDFFSSAStYPVLIISYEtLRRHAEKLSKKISIDLLICDEGHRLKNSESKTTKALNS- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  901 YVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvDLNEEETILIIRRLH---KVLRPFLL 977
Cdd:cd18004   160 LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDP-DASEEDKELGAERSQelsELTSRFIL 238

                  ..
gi 192807314  978 RR 979
Cdd:cd18004   239 RR 240
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
754-979 3.02e-42

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: 154.78  E-value: 3.02e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTialITYLMEHKR--INGPFLIIVPLSTLSNWAYEFDKWAPSVVk 831
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQS---ITFLYEILLtgIRGPFLIIAPLSTIANWEREFRTWTDLNV- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  832 VSYKGSPAARRAFV--------PQLR----SGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNT 899
Cdd:cd18061    77 VVYHGSLISRQMIQqyemyfrdSQGRiirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  900 HYVApRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNapfamtgekvDLNEEETiliIRRLHKVLRPFLLRR 979
Cdd:cd18061   157 MNLE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
754-979 3.33e-40

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: 149.36  E-value: 3.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLynnnlNGILADEMGLGKTIQTIALI-------TYLMEHKRINGPF----------LIIVPLSTLS 816
Cdd:cd18008     1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdPKIPEELEENSSDpkklylskttLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  817 NWAYEFDK-WAPSVVKVS-YKGSPAARRAFVPQlrsgKFNVLLTTY-----EY-----------IIKDKHILAKIRWKYM 878
Cdd:cd18008    76 QWKDEIEKhTKPGSLKVYvYHGSKRIKSIEELS----DYDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIRWYRV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  879 IVDEGHRMKNHHCKLTQV---LNTHyvapRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKvd 955
Cdd:cd18008   152 ILDEAHNIKNRSTKTSRAvcaLKAE----RRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK-- 225
                         250       260
                  ....*....|....*....|....
gi 192807314  956 lneeetilIIRRLHKVLRPFLLRR 979
Cdd:cd18008   226 --------ALERLQALLKPILLRR 241
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
754-967 1.13e-36

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: 139.35  E-value: 1.13e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLE--W--LVSLYNNNLNG---ILADEMGLGKTIQTIALI-TYLMEHKRINGPfLIIVPLSTLSNWAYEFDKW 825
Cdd:cd18007     1 LKPHQVEGVRflWsnLVGTDVGSDEGggcILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEFKKW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  826 APSVVkVSYKGSPAARRAFVPQLRSGKFN-------VLLTTYEY---IIKDKHILAKIRWKYM-----------IVDEGH 884
Cdd:cd18007    80 LPPDL-RPLLVLVSLSASKRADARLRKINkwhkeggVLLIGYELfrnLASNATTDPRLKQEFIaalldpgpdllVLDEGH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  885 RMKNHHCKLTQVLNTHYvAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGEKVDLNEEETILI 964
Cdd:cd18007   159 RLKNEKSQLSKALSKVK-TKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKPIE-AGQCVDSTEEDVRLM 236

                  ...
gi 192807314  965 IRR 967
Cdd:cd18007   237 LKR 239
DEXDc smart00487
DEAD-like helicases superfamily;
754-942 6.18e-32

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 124.14  E-value: 6.18e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    754 LKQYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TIALITYLMEHKriNGPFLIIVPLSTL-SNWAYEFDKWAPS-VV 830
Cdd:smart00487    9 LRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGK--GGRVLVLVPTRELaEQWAEELKKLGPSlGL 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    831 KVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKD--KHILAKIRWKYMIVDEGHRMKN--HHCKLTQVLNTHYVAPRR 906
Cdd:smart00487   84 KVVGLYGGDSKREQLRKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKNVQL 163
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 192807314    907 LLLTGTPLQNKLPELWALLN--FLLPTIFKSCSTFEQW 942
Cdd:smart00487  164 LLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
754-979 3.30e-31

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: 123.35  E-value: 3.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNL-----------------------------NGILADEMGLGKTIQTIALItylmehkrING 804
Cdd:cd18071     1 LLPHQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLI--------LAN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  805 PFLIIVPLSTLSNWAYEF-DKWAPSVVKV-SYKGspAARRAFVPQLrsGKFNVLLTTY-----EYIIKDKHILAKIRWKY 877
Cdd:cd18071    73 FTLIVCPLSVLSNWETQFeEHVKPGQLKVyTYHG--GERNRDPKLL--SKYDIVLTTYntlasDFGAKGDSPLHTINWLR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  878 MIVDEGHRMKNHHCKLTQ-VLNTHyvAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMtGEKVDL 956
Cdd:cd18071   149 VVLDEGHQIRNPNAQQTKaVLNLS--SERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPLTM-GDPTGL 225
                         250       260
                  ....*....|....*....|...
gi 192807314  957 neeetiliiRRLHKVLRPFLLRR 979
Cdd:cd18071   226 ---------KRLQVLMKQITLRR 239
BROMO smart00297
bromo domain;
1426-1534 4.18e-31

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 118.54  E-value: 4.18e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   1426 PNLTKKMKKIVDAVIKYKDSssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQN 1505
Cdd:smart00297    2 PKLQKKLQELLKAVLDKLDS---HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSN 78
                            90       100
                    ....*....|....*....|....*....
gi 192807314   1506 AQTFNLEGSLIYEDSIVLQSVFTSVRQKI 1534
Cdd:smart00297   79 ARTYNGPDSEVYKDAKKLEKFFEKKLREL 107
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1428-1532 8.80e-30

Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99946  Cd Length: 105  Bit Score: 114.32  E-value: 8.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1428 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1507
Cdd:cd05515     1 MQQKLWELYNAVKNYTDGR-GRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNAC 79
                          90       100
                  ....*....|....*....|....*
gi 192807314 1508 TFNLEGSLIYEDSIVLQSVFTSVRQ 1532
Cdd:cd05515    80 KYNEPDSQIYKDALTLQKVLLETKR 104
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
754-979 1.12e-29

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: 118.79  E-value: 1.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSL-----YNNNLNGILADEMGLGKTIQTIALITYLMEH-----KRINGPFLIIVPLSTLSNWAYEFD 823
Cdd:cd18066     1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRQgpyggKPVIKRALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  824 KWAPSV-VKVSYKGSPAARRAFVpqlRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLnTHYV 902
Cdd:cd18066    81 KWLGSErIKVFTVDQDHKVEEFI---ASPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL-TSLS 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 192807314  903 APRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIR--RLHKVLRPFLLRR 979
Cdd:cd18066   157 CERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARaaELTRLTGLFILRR 235
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1080-1194 4.64e-28

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: 109.61  E-value: 4.64e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  1080 GKFELLDRILPKLRatNHKVLLFCQMTSlmTIMEDYFAYR-GFKYLRLDGTTKAEDRGMLLKTFNEpgSEYFIfLLSTRA 1158
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKeGIKVARLHGDLSQEEREEILEDFRK--GKIDV-LVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 192807314  1159 GGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIG 1194
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1428-1530 7.76e-28

Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99950  Cd Length: 103  Bit Score: 108.97  E-value: 7.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1428 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1507
Cdd:cd05519     1 LKAAMLEIYDAVLNCEDET-GRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANAR 79
                          90       100
                  ....*....|....*....|...
gi 192807314 1508 TFNLEGSLIYEDSIVLQSVFTSV 1530
Cdd:cd05519    80 TYNQEGSIVYEDAVEMEKAFKKK 102
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1428-1527 7.78e-28

Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 108.61  E-value: 7.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1428 LTKKMKKIVDAVIKYKdsssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1507
Cdd:cd04369     1 LKKKLRSLLDALKKLK-----RDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAK 75
                          90       100
                  ....*....|....*....|
gi 192807314 1508 TFNLEGSLIYEDSIVLQSVF 1527
Cdd:cd04369    76 TYNGPGSPIYKDAKKLEKLF 95
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
754-979 1.27e-27

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


Pssm-ID: 350825 [Multi-domain]  Cd Length: 243  Bit Score: 113.33  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWL----VSLYNNNLNG-ILADEMGLGKTIQTIALITYLMEHKRINGPFL----IIVPLSTLSNWAYEFDK 824
Cdd:cd18067     1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  825 W-----APSVV--KVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVL 897
Cdd:cd18067    81 WlggrlQPLAIdgGSKKEIDRKLVQWASQQGRRVSTPVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  898 NThYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRRLHK---VLRP 974
Cdd:cd18067   161 DS-LNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPI-LKGRDADASEKERQLGEEKLQElisIVNR 238

                  ....*
gi 192807314  975 FLLRR 979
Cdd:cd18067   239 CIIRR 243
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
754-967 1.43e-27

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


Pssm-ID: 350768 [Multi-domain]  Cd Length: 213  Bit Score: 111.91  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSlynNNLNGILADEMGLGKTIQTIALITYLmehkRINGPFLIIVPLSTLSNWAYEFDKWAPSV---- 829
Cdd:cd18010     1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYY----REEWPLLIVCPSSLRLTWADEIERWLPSLppdd 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  830 VKVSYKGSPAARRafvpqlRSGKFNVllTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQV---LNTHyvAPRR 906
Cdd:cd18010    74 IQVIVKSKDGLRD------GDAKVVI--VSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAalpLLKR--AKRV 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  907 LLLTGTPLQNKLPELWALLNFLLPTIFKSCSTF-EQWFNA----PFAMTGEKVDLNEEETILI----IRR 967
Cdd:cd18010   144 ILLSGTPALSRPIELFTQLDALDPKLFGRFHDFgRRYCAAkqggFGWDYSGSSNLEELHLLLLatimIRR 213
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
754-967 2.45e-25

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: 106.05  E-value: 2.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTIALITYLMEHKRINgPFLIIVPLSTLSNWAYE 821
Cdd:cd18069     1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLLRHTGAK-TVLAIVPVNTLQNWLSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  822 FDKWAPSVV----------KVSYKGSPAARRAFVPQLRS---GKFNVLLTTYE-YIIKDKHILakirwkyMIVDEGHRMK 887
Cdd:cd18069    77 FNKWLPPPEalpnvrprpfKVFILNDEHKTTAARAKVIEdwvKDGGVLLMGYEmFRLRPGPDV-------VICDEGHRIK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  888 NHHCKLTQVLNtHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFaMTGEKVDLNEEETILIIRR 967
Cdd:cd18069   150 NCHASTSQALK-NIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERPI-LNGQCVDSTPQDVKLMRYR 227
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1430-1526 3.22e-24

Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99949 [Multi-domain]  Cd Length: 103  Bit Score: 98.67  E-value: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1430 KKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTF 1509
Cdd:cd05518     3 KRMLALFLYVLEYREGS-GRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHY 81
                          90
                  ....*....|....*..
gi 192807314 1510 NLEGSLIYEDSIVLQSV 1526
Cdd:cd05518    82 NEEGSQVYEDANILEKV 98
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1289-1356 2.26e-23

Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role in chromatin remodelling for yeast SWI/SNF. It binds histones. It is required for mobilising nucleosomes and lies within the catalytic subunit of the yeast SWI/SNF. It is found to be universally conserved.


Pssm-ID: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 95.02  E-value: 2.26e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 192807314  1289 DRRREEARNPK-RKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWL 1356
Cdd:pfam14619    1 ERRREEAEQLPpLPSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
HSA smart00573
domain in helicases and associated with SANT domains;
460-532 5.98e-23

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 94.00  E-value: 5.98e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 192807314    460 QKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMA 532
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1435-1528 7.46e-23

Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99948  Cd Length: 103  Bit Score: 94.81  E-value: 7.46e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1435 IVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGS 1514
Cdd:cd05517     8 LLEAVMTATDPS-GRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFNEPGS 86
                          90
                  ....*....|....
gi 192807314 1515 LIYEDSIVLQSVFT 1528
Cdd:cd05517    87 QVYKDANAIKKIFT 100
HELICc smart00490
helicase superfamily c-terminal domain;
1111-1194 8.95e-22

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 90.73  E-value: 8.95e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   1111 IMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSeyfIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRA 1190
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKI---KVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 192807314   1191 HRIG 1194
Cdd:smart00490   79 GRAG 82
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1435-1534 1.21e-21

Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99954 [Multi-domain]  Cd Length: 113  Bit Score: 91.63  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1435 IVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGS 1514
Cdd:cd05524    10 LYDTIRNYKSED-GRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDS 88
                          90       100
                  ....*....|....*....|
gi 192807314 1515 LIYEDSIVLQSVFTSVRQKI 1534
Cdd:cd05524    89 PEHKDACKLWELFLSARNEV 108
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
754-979 3.35e-21

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: 94.47  E-value: 3.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSLYNNNLNG-ILADEMGLGKTIQTIALI------------------TYLMEHKRIN----GPFLIIV 810
Cdd:cd18072     1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALIlaqkntqnrkeeekekalTEWESKKDSTlvpsAGTLVVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  811 PLSTLSNWAYEFD-KWAPSVVKV-SYKGSPAARRAFVpqLRSgkFNVLLTTYEYIIKD---------KHILAKIRWKYMI 879
Cdd:cd18072    81 PASLVHQWKNEVEsRVASNKLRVcLYHGPNRERIGEV--LRD--YDIVITTYSLVAKEiptykeesrSSPLFRIAWARII 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  880 VDEGHRMKNHH-------CKltqvLNTHYvaprRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGE 952
Cdd:cd18072   157 LDEAHNIKNPKvqasiavCK----LRAHA----RWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSRKGGE 228
                         250       260
                  ....*....|....*....|....*..
gi 192807314  953 kvdlneeetiliirRLHKVLRPFLLRR 979
Cdd:cd18072   229 --------------RLNILTKSLLLRR 241
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
775-967 5.73e-21

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: 94.18  E-value: 5.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  775 GILADEMGLGKTIQTIALITYLMEHKRING--PFLIIVPLSTLSNWAYEFDKWA-----PSVVKV----SYKGSPaaRRA 843
Cdd:cd18068    31 CILAHCMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEFEKWQeglkdEEKIEVnelaTYKRPQ--ERS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  844 FVPQLRSGKFNVLLTTYE-YII----KDKHILAKIRWKYM-----------IVDEGHRMKNHHCKLTQVLNThYVAPRRL 907
Cdd:cd18068   109 YKLQRWQEEGGVMIIGYDmYRIlaqeRNVKSREKLKEIFNkalvdpgpdfvVCDEGHILKNEASAVSKAMNS-IRTKRRI 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  908 LLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAmTGEKVDLNEEETILIIRR 967
Cdd:cd18068   188 VLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPIQ-NGQCADSTLVDVRVMKKR 246
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
776-933 1.31e-20

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: 91.97  E-value: 1.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  776 ILADEMGLGKTIQTIALITYLM---EHKRIngpfLIIVPLSTLSNWAYEF--DKWAPSVVKVSYKGSPAARRAFVPQLRs 850
Cdd:cd18011    21 LLADEVGLGKTIEAGLIIKELLlrgDAKRV----LILCPASLVEQWQDELqdKFGLPFLILDRETAAQLRRLIGNPFEE- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  851 gkFNVLLTTYEYI---IKDKHILAKIRWKYMIVDEGHRMKNHHC-------KLTQVLNTHyvAPRRLLLTGTPLQNKLPE 920
Cdd:cd18011    96 --FPIVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKR--ARHVLLLTATPHNGKEED 171
                         170
                  ....*....|...
gi 192807314  921 LWALLNFLLPTIF 933
Cdd:cd18011   172 FRALLSLLDPGRF 184
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1447-1529 2.10e-20

Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99951  Cd Length: 103  Bit Score: 87.78  E-value: 2.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1447 SGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSV 1526
Cdd:cd05520    19 QGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKLQKL 98

                  ...
gi 192807314 1527 FTS 1529
Cdd:cd05520    99 MQA 101
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
461-527 4.25e-20

HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. This region does not form a compact domain in the known structures.


Pssm-ID: 462194 [Multi-domain]  Cd Length: 67  Bit Score: 85.32  E-value: 4.25e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 192807314   461 KIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERM 527
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1432-1520 1.46e-19

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 84.67  E-value: 1.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  1432 MKKIVDAVIKykdsssgRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNL 1511
Cdd:pfam00439    1 CLEILDKLME-------HPIAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73

                   ....*....
gi 192807314  1512 EGSLIYEDS 1520
Cdd:pfam00439   74 PGSVIYKAA 82
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1403-1536 3.94e-17

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 85.24  E-value: 3.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1403 KDDESKKQKKRGRPPAEKLSPNPPN--LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKI 1480
Cdd:COG5076   116 SGLGSLLMAHLKTSVKKRKTPKIEDelLYADNKAIAKFKKQLFLRD-GRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTI 194
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 192807314 1481 KERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEK 1536
Cdd:COG5076   195 QKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFLKLIEEIPE 250
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1428-1525 1.04e-16

Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99952  Cd Length: 106  Bit Score: 77.36  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1428 LTKKMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNhkYRSLNDLEKDVMLLCQNAQ 1507
Cdd:cd05521     2 LSKKLKPLYDGIYTLKEEN-GIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLPH--YTNAQEFVNDLAQIPWNAR 78
                          90
                  ....*....|....*...
gi 192807314 1508 TFNLEGSLIYEDSIVLQS 1525
Cdd:cd05521    79 LYNTKGSVIYKYALILEK 96
BRK smart00592
domain in transcription and CHROMO domain helicases;
612-656 1.10e-16

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 75.08  E-value: 1.10e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 192807314    612 MSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSD 656
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
611-654 2.98e-16

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


Pssm-ID: 462196  Cd Length: 44  Bit Score: 73.70  E-value: 2.98e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 192807314   611 QMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPR 654
Cdd:pfam07533    1 LTGDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1431-1530 1.08e-15

Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99953 [Multi-domain]  Cd Length: 104  Bit Score: 74.20  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1431 KMKKIVDAVIKYKDSSsGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1510
Cdd:cd05522     5 RIKNILKGLRKERDEN-GRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYN 83
                          90       100
                  ....*....|....*....|
gi 192807314 1511 LEGSLIYEDSIVLQSVFTSV 1530
Cdd:cd05522    84 ENDSQEYKDAVLLEKEARLL 103
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
754-928 1.44e-14

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: 75.46  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVslynnNLNGILADEMGLGKTIQTIALItylMEHKRIN----------------------------GP 805
Cdd:cd18070     1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLALI---LLHPRPDndldaadddsdemvccpdclvaetpvssKA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  806 FLIIVPLSTLSNWAYEFDKWAPSVVKVS-YKGspaARRAFVPQLRSGKF----NVLLTTYEYIIKDKHI----------- 869
Cdd:cd18070    73 TLIVCPSAILAQWLDEINRHVPSSLKVLtYQG---VKKDGALASPAPEIlaeyDIVVTTYDVLRTELHYaeanrsnrrrr 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 192807314  870 -----------LAKIRWKYMIVDEghrMKNHHCKLTQVLNTHYVAPR--RLLLTGTPLQNKLPELWALLNFL 928
Cdd:cd18070   150 rqkryeappspLVLVEWWRVCLDE---AQMVESSTSKAAEMARRLPRvnRWCVSGTPIQRGLDDLFGLLSFL 218
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1431-1536 8.65e-14

Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 68.74  E-value: 8.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1431 KMKKIVDAVIKYKDSSSgrqlsevFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1510
Cdd:cd05509     5 QLKKVLDSLKNHKSAWP-------FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYN 77
                          90       100
                  ....*....|....*....|....*.
gi 192807314 1511 LEGSLIYEDSIVLQSVFtsvRQKIEK 1536
Cdd:cd05509    78 GPDTEYYKCANKLEKFF---WKKLKE 100
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
171-205 1.42e-13

QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. This domain has thus been postulated to be involved in mediating protein interactions.


Pssm-ID: 462622  Cd Length: 35  Bit Score: 65.82  E-value: 1.42e-13
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 192807314   171 PFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQ 205
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPELQQAIF 35
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
754-944 2.82e-13

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: 70.84  E-value: 2.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLEWLVSlynNNLNGILADeMGLGKTIQTIALITYLMEHKRInGPFLIIVPLSTLSN-WAYEFDKW-APSVVK 831
Cdd:cd18013     1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQLDDFT-RRVLVIAPLRVARStWPDEVEKWnHLRNLT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  832 VSYK-GSPAARRAfvpqLRSGKFNVLLTTYEyIIKDKHILAKIRWKY--MIVDEGHRMKNHHCKLTQVLNTH-YVAPRRL 907
Cdd:cd18013    76 VSVAvGTERQRSK----AANTPADLYVINRE-NLKWLVNKSGDPWPFdmVVIDELSSFKSPRSKRFKALRKVrPVIKRLI 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 192807314  908 LLTGTPLQNKLPELWALLNFL--LPTIFKSCSTF-EQWFN 944
Cdd:cd18013   151 GLTGTPSPNGLMDLWAQIALLdqGERLGRSITAYrERWFD 190
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1435-1527 5.79e-13

Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was identified as a novel human bromodomain gene by cDNA library screening. The Drosophila homologue, Acf1, is part of the CHRAC (chromatin accessibility complex) and regulates ISWI-induced nucleosome remodeling. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99936  Cd Length: 115  Bit Score: 67.04  E-value: 5.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1435 IVDAVIKYKDSSSgrqlsevFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGS 1514
Cdd:cd05504    20 LLVEIVKHKDSWP-------FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHT 92
                          90
                  ....*....|...
gi 192807314 1515 LIYEDSIVLQSVF 1527
Cdd:cd05504    93 SVYKAGTRLQRFF 105
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1428-1532 1.75e-11

Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99955 [Multi-domain]  Cd Length: 106  Bit Score: 62.41  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1428 LTKKMKKIVDAVIKYKDSSSGrQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1507
Cdd:cd05525     3 LAQVLKEICDAIITYKDSNGQ-SLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAE 81
                          90       100
                  ....*....|....*....|....*
gi 192807314 1508 TFNLEGSLIYEDSIVLQSVFTSVRQ 1532
Cdd:cd05525    82 KYYGRKSPIGRDVCRLRKAYYQAKH 106
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1459-1527 5.21e-11

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99931  Cd Length: 102  Bit Score: 60.76  E-value: 5.21e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 192807314 1459 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1527
Cdd:cd05499    30 PVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVF 98
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
171-204 6.65e-11

QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2/SNF2 protein, which has been shown to be involved in protein-protein interactions. QLQ has been postulated to be involved in mediating protein interactions.


Pssm-ID: 214931  Cd Length: 36  Bit Score: 58.31  E-value: 6.65e-11
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 192807314    171 PFNQNQLHQLRAQIMAYK-MLARGQPLPDHLQMAV 204
Cdd:smart00951    2 PFTPAQLELLRAQILAYKyLLARNQPVPPELLQAI 36
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1463-1510 8.91e-11

Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver


Pssm-ID: 99957  Cd Length: 112  Bit Score: 60.45  E-value: 8.91e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 192807314 1463 ELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1510
Cdd:cd05528    32 EVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1426-1529 6.93e-10

Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99958  Cd Length: 128  Bit Score: 58.50  E-value: 6.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1426 PNLTKKMKKIVDavikykdsSSGRQLSEVFIQ-LPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQ 1504
Cdd:cd05529    27 ERLISGLDKLLL--------SLQLEIAEYFEYpVDLRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILS 98
                          90       100
                  ....*....|....*....|....*
gi 192807314 1505 NAQTFNLEGSLIYEDSIVLQSVFTS 1529
Cdd:cd05529    99 NAETFNEPNSEIAKKAKRLSDWLLR 123
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1459-1528 2.67e-09

Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99930  Cd Length: 102  Bit Score: 56.13  E-value: 2.67e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1459 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFT 1528
Cdd:cd05498    30 PEALGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVFE 99
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1462-1529 3.30e-09

Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99935  Cd Length: 97  Bit Score: 55.46  E-value: 3.30e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 192807314 1462 KELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTS 1529
Cdd:cd05503    28 KLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFFEK 95
ResIII pfam04851
Type III restriction enzyme, res subunit;
753-913 8.61e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 56.14  E-value: 8.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   753 VLKQYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINgPFLIIVP-LSTLSNWAYEFDKWAPSVV 830
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK-KVLFLVPrKDLLEQALEEFKKFLPNYV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   831 KVSYKGSPaarRAFVPQLRSGKfnVLLTTYEYIIKD----KHILAKIRWKYMIVDEGHRM--KNHhcklTQVLNtHYVAP 904
Cdd:pfam04851   82 EIGEIISG---DKKDESVDDNK--IVVTTIQSLYKAlelaSLELLPDFFDVIIIDEAHRSgaSSY----RNILE-YFKPA 151

                   ....*....
gi 192807314   905 RRLLLTGTP 913
Cdd:pfam04851  152 FLLGLTATP 160
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
754-913 1.41e-08

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: 55.39  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  754 LKQYQIKGLE-WLvsLYNNNLNGILADEMGLGKTIQTIALITYLMEHKringpFLIIVP-LSTLSNWAYEFDKWAPSVVk 831
Cdd:cd17926     1 LRPYQEEALEaWL--AHKNNRRGILVLPTGSGKTLTALALIAYLKELR-----TLIVVPtDALLDQWKERFEDFLGDSS- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  832 vsykgspaarrafVPQLRSGK------FNVLLTTYEYIIKDKHILAKI--RWKYMIVDEGHrmknHHC--KLTQVLnTHY 901
Cdd:cd17926    73 -------------IGLIGGGKkkdfddANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAH----HLPakTFSEIL-KEL 134
                         170
                  ....*....|..
gi 192807314  902 VAPRRLLLTGTP 913
Cdd:cd17926   135 NAKYRLGLTATP 146
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1428-1524 1.52e-08

Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein assumed to be a transcriptional regulator. BRD1 has been implicated with brain development and susceptibility to schizophrenia and bipolar affective disorder. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99944  Cd Length: 98  Bit Score: 53.56  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1428 LTKKMKKIVDAViKYKDSSsgrqlsEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQ 1507
Cdd:cd05512     2 LEVLLRKTLDQL-QEKDTA------EIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCL 74
                          90
                  ....*....|....*..
gi 192807314 1508 TFNLEGSLIYEDSIVLQ 1524
Cdd:cd05512    75 AYNAKDTIFYRAAVRLR 91
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1465-1517 1.57e-08

Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown to inhibit cell growth and the progression of the cell cycle by regulating cell-cycle genes at the transcriptional level. BRD7 has been identified as a gene involved in nasopharyngeal carcinoma. The protein interacts with acetylated histone H3 via its bromodomain. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99945  Cd Length: 98  Bit Score: 53.57  E-value: 1.57e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 192807314 1465 PEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIY 1517
Cdd:cd05513    32 PGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNKPDTIYY 84
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1449-1534 2.78e-08

Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99934 [Multi-domain]  Cd Length: 109  Bit Score: 53.45  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1449 RQLSEVFIQLPSR-------KELPEYYELIRKPVDFKKIKERIR----NHkYRSLNDLEKDVMLLCQNAQTFNLEGSLIY 1517
Cdd:cd05502    11 RLLLELYCHELSLpfhepvsPSVPNYYKIIKTPMDLSLIRKKLQpkspQH-YSSPEEFVADVRLMFKNCYKFNEEDSEVA 89
                          90
                  ....*....|....*..
gi 192807314 1518 EDSIVLQSVFTSVRQKI 1534
Cdd:cd05502    90 QAGKELELFFEEQLKEI 106
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
42-222 5.71e-08

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 57.71  E-value: 5.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    42 MMGPSP---GPPSA----------------GHPIPTQGPGGYPQDNMH--------QMHKPMESMHEKGMSDDPryNQMK 94
Cdd:pfam09606   98 MMGPMGpgpGGPMGqqmggpgtasnllaslGRPQMPMGGAGFPSQMSRvgrmqpggQAGGMMQPSSGQPGSGTP--NQMG 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    95 GMGmrsGGHAGMGPPPSPMDQHS--QGYPSPLGGSehaSSPVPASGPSSGPQMSSGPGGAP---LDGADPQ-ALGQQNRG 168
Cdd:pfam09606  176 PNG---GPGQGQAGGMNGGQQGPmgGQMPPQMGVP---GMPGPADAGAQMGQQAQANGGMNpqqMGGAPNQvAMQQQQPQ 249
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 192807314   169 PTPfNQNQLHQLRAQIMAYkmlARGQPLPDHLQMAVQgkrPMPGMQQQMPTLPP 222
Cdd:pfam09606  250 QQG-QQSQLGMGINQMQQM---PQGVGGGAGQGGPGQ---PMGPPGQQPGAMPN 296
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1430-1534 6.43e-08

Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99928  Cd Length: 119  Bit Score: 52.46  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1430 KKMKKIVDAVIKYKDSSSGRQLSEVFiqlpsrkELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTF 1509
Cdd:cd05496     8 KQCKELVNLMWDCEDSEPFRQPVDLL-------KYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSY 80
                          90       100
                  ....*....|....*....|....*.
gi 192807314 1510 NL-EGSLIYEDSIVLQSVFTSVRQKI 1534
Cdd:cd05496    81 TPnKRSRIYSMTLRLSALFEEHIKKI 106
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
774-912 1.44e-07

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: 52.41  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  774 NGILADEMGLGKTIQTIALITYLMEHKRinGPFLIIVPLSTLSN-WAYEFDKWAPSVVKVSY--KGSPAARRAfvpQLRS 850
Cdd:cd00046     3 NVLITAPTGSGKTLAALLAALLLLLKKG--KKVLVLVPTKALALqTAERLRELFGPGIRVAVlvGGSSAEERE---KNKL 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 192807314  851 GKFNVLLTTYEYIIKDKHILAKI---RWKYMIVDEGHRM----KNHHCKLTQVLNTHYVAPRRLLLTGT 912
Cdd:cd00046    78 GDADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILLSAT 146
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1462-1535 2.28e-07

Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99943 [Multi-domain]  Cd Length: 112  Bit Score: 50.73  E-value: 2.28e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 192807314 1462 KELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIyedSIVLQSVFTSVRQKIE 1535
Cdd:cd05511    28 KKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSVY---TKKAKEMLELAEELLA 98
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1459-1527 3.72e-07

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99932  Cd Length: 103  Bit Score: 50.00  E-value: 3.72e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 192807314 1459 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1527
Cdd:cd05500    31 PVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFNGPEHPVSQMGKRLQAAF 99
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
695-913 5.04e-07

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 54.26  E-value: 5.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  695 SDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNG--------VLKQYQIKGLE-WL 765
Cdd:COG1061    14 LRSSLLLLDLERLELSLLRNLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGdeasgtsfELRPYQQEALEaLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  766 VSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRIngpfLIIVPLSTLSN-WAYEFDKWAPSVVKVSYKgspaarraf 844
Cdd:COG1061    94 AALERGGGRGLVVAPTGTGKTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGDPLAGGGK--------- 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 192807314  845 vpqlRSGKFNVLLTTYEYIIKDKHiLAKI--RWKYMIVDEGHrmknhHC---KLTQVLNtHYVAPRRLLLTGTP 913
Cdd:COG1061   161 ----KDSDAPITVATYQSLARRAH-LDELgdRFGLVIIDEAH-----HAgapSYRRILE-AFPAAYRLGLTATP 223
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1463-1535 7.04e-07

Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99929  Cd Length: 107  Bit Score: 49.34  E-value: 7.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 192807314 1463 ELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGsliyeDSIVL--QSVFTSVRQKIE 1535
Cdd:cd05497    36 NLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPG-----DDVVLmaQTLEKLFLQKLA 105
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1459-1527 1.88e-06

Bromodomain, uncharacterized subfamily specific to plants. Might function as a global transcription factor. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99938  Cd Length: 99  Bit Score: 47.71  E-value: 1.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 192807314 1459 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVF 1527
Cdd:cd05506    27 VVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNPPGNDVHTMAKELLKIF 95
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1430-1516 2.34e-06

Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99937  Cd Length: 97  Bit Score: 47.53  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1430 KKMKKIVDAVIKYKDSSSGRQLsevfiqlPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTF 1509
Cdd:cd05505     3 QKCEEILSKILKYRFSWPFREP-------VTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKY 75

                  ....*..
gi 192807314 1510 NLEGSLI 1516
Cdd:cd05505    76 YENGSYV 82
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
364-570 5.14e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  364 VEILQEREY-------RLQARIAHRIQELENLPGSLAgdlRTKATIELKALRLLNFQRQLRQEvvvcmrrDTALETALNA 436
Cdd:COG1196   283 LEEAQAEEYellaelaRLEQDIARLEERRRELEERLE---ELEEELAELEEELEELEEELEEL-------EEELEEAEEE 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  437 KAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQK 516
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 192807314  517 KENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAyLLQQTDEYVANLTELVRQ 570
Cdd:COG1196   433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEE 485
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1452-1510 6.76e-06

Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with the thyroid hormone receptor in a ligand-dependent fashion and enhances thyroid hormone-dependent activation from thyroid response elements. Brd8 is thought to be a nuclear receptor coactivator. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99939  Cd Length: 104  Bit Score: 46.20  E-value: 6.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1452 SEVFIQ-LPSRKElPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1510
Cdd:cd05507    21 ASVFLKpVTEDIA-PGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYN 79
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1147-1195 1.21e-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: 45.00  E-value: 1.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 192807314 1147 SEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQ 1195
Cdd:cd18785    20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGK 68
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1452-1510 1.28e-05

Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, and SLIK. SAGA is involved in the RNA polymerase II-dependent transcriptional regulation of about 10% of all yeast genes. The SPT7 bromodomain has been shown to weakly interact with acetylated histone H3, but not H4. The human representative of this subfamily is cat eye syndrome critical region protein 2 (CECR2). Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99942 [Multi-domain]  Cd Length: 112  Bit Score: 45.90  E-value: 1.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 192807314 1452 SEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFN 1510
Cdd:cd05510    26 STPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYN 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
365-551 2.17e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  365 EILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKR 444
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  445 QSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVAtyhANTEREQKKENERIEK 524
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---EAAEEEAELEEEEEAL 461
                         170       180
                  ....*....|....*....|....*..
gi 192807314  525 ERMRRLMAEDEEGYRKLIDQKKDKRLA 551
Cdd:COG1196   462 LELLAELLEEAALLEAALAELLEELAE 488
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
44-223 5.02e-05

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 46.52  E-value: 5.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    44 GPSPGPPSAGHPIPT-QGP---GGYPQDNMHQMHKPmesmHEKGMSDDPRYNQMKGM--GMRSGGHA-GMGPPpspmdqh 116
Cdd:pfam15822   88 GPSCPPPGGPYPAPTvPGPgpiGPYPTPNMPFPELP----RPYGAPTDPAAAAPSGPwgSMSSGPWApGMGGQ------- 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   117 sqgYPSPlggsehaSSPVPASGPSSGPQMSSGPGGAPldgadPQALGQQNRG----PTPFnqnqlhqlraqimaykmlar 192
Cdd:pfam15822  157 ---YPAP-------NMPYPSPGPYPAVPPPQSPGAAP-----PVPWGTVPPGpwgpPAPY-------------------- 201
                          170       180       190
                   ....*....|....*....|....*....|.
gi 192807314   193 gqPLPdhlqmavQGKRPMPGMQqqmPTLPPP 223
Cdd:pfam15822  202 --PDP-------TGSYPMPGLY---PTPNNP 220
Bromo_polybromo_VI cd05526
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which ...
1446-1536 5.27e-05

Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99956  Cd Length: 110  Bit Score: 43.89  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314 1446 SSGRQLSEVFIQLPSRKELPEyyELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQS 1525
Cdd:cd05526    21 EEGRCYSDSLAELPELAVDGV--GPKKIPLTLDIIKRNVDKGRYRRLDKFQEDMFEVLERARRLSRTDSEIYEDAVELQQ 98
                          90
                  ....*....|.
gi 192807314 1526 VFTSVRQKIEK 1536
Cdd:cd05526    99 FFIKIRDELCK 109
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1459-1529 6.52e-05

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99927  Cd Length: 108  Bit Score: 43.59  E-value: 6.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 192807314 1459 PSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTS 1529
Cdd:cd05495    31 PKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRVYKYCTKLAEVFEQ 101
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
782-881 7.97e-05

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 45.40  E-value: 7.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  782 GLGKTiqTIALITYLMEHKRiNGPFLIIVPLSTLSNWAYE----FDKWAPSVVK--VSYKGSPA-ARRAFVPQLRSGKFN 854
Cdd:cd17924    42 GVGKT--TFGLATSLYLASK-GKRSYLIFPTKSLVKQAYErlskYAEKAGVEVKilVYHSRLKKkEKEELLEKIEKGDFD 118
                          90       100
                  ....*....|....*....|....*..
gi 192807314  855 VLLTTYEYIIKDKHILAKIRWKYMIVD 881
Cdd:cd17924   119 ILVTTNQFLSKNFDLLSNKKFDFVFVD 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
367-538 8.53e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 8.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  367 LQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQS 446
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  447 LREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKER 526
Cdd:COG1196   415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
                         170
                  ....*....|..
gi 192807314  527 MRRLMAEDEEGY 538
Cdd:COG1196   495 LLLEAEADYEGF 506
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
43-218 1.72e-04

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 46.15  E-value: 1.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    43 MGPSPGPPSAGHPIPTQGPGGYPQDNM-HQMHKPMESMHEKGMSDdpRYNQMKGMGMRSGGHAGMGPPPSPMDQHSQGyp 121
Cdd:pfam09606  174 MGPNGGPGQGQAGGMNGGQQGPMGGQMpPQMGVPGMPGPADAGAQ--MGQQAQANGGMNPQQMGGAPNQVAMQQQQPQ-- 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   122 splggsEHASSPVPASGPSSGPQMSSGpggapldgaDPQALGQQnrgpTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLq 201
Cdd:pfam09606  250 ------QQGQQSQLGMGINQMQQMPQG---------VGGGAGQG----GPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQ- 309
                          170
                   ....*....|....*..
gi 192807314   202 mavQGKRPMPGMQQQMP 218
Cdd:pfam09606  310 ---QTRQQQQQQGGNHP 323
PTZ00121 PTZ00121
MAEBL; Provisional
437-548 7.95e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  437 KAYKRSKRQSLREARITEKLEKQQKIEQERKRrqkhQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHAntEREQK 516
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKK 1614
                          90       100       110
                  ....*....|....*....|....*....|..
gi 192807314  517 KENERIEKERMRRlmaedEEGYRKLIDQKKDK 548
Cdd:PTZ00121 1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKK 1641
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
45-227 1.57e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   45 PSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYNqMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPL 124
Cdd:PRK07764  619 AAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG-GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAA 697
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  125 GGSEHA-SSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQnqlhqlraqimaykmLARGQPLPDHLQMA 203
Cdd:PRK07764  698 PAQPAPaPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP---------------PDPAGAPAQPPPPP 762
                         170       180
                  ....*....|....*....|....
gi 192807314  204 VQGKRPMPGMQQQMPTLPPPSVSA 227
Cdd:PRK07764  763 APAPAAAPAAAPPPSPPSEEEEMA 786
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
97-222 1.82e-03

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.79  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314    97 GMRSGGHAGMGPPPSPMDQHSQGYPsPLGGSEHASSPVPASGPSSGPQMSSGPggapldgadPQALGQQNRGPTPFNQNQ 176
Cdd:pfam15240   53 GFPPQPPASDDPPGPPPPGGPQQPP-PQGGKQKPQGPPPQGGPRPPPGKPQGP---------PPQGGNQQQGPPPPGKPQ 122
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 192807314   177 lhqlraqimaykmlarGQPLPDhlqmavQGKRPMPGMQQQMPTLPP 222
Cdd:pfam15240  123 ----------------GPPPQG------GGPPPQGGNQQGPPPPPP 146
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
400-564 1.86e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.83  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  400 ATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKaykrskRQSLREARiTEKLEKQQKIEQERKRRQKHQEYLNSI 479
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAA------KTELEDLE-KEIKRLELEIEEVEARIKKYEEQLGNV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314  480 lqhaKDFKEYHrSVTGKIQKLTKAVATY-----HANTEREQKKENERIEKERMRRLMAE--DEEGYRKLIDQKKDKRLAY 552
Cdd:COG1579    86 ----RNNKEYE-ALQKEIESLKRRISDLedeilELMERIEELEEELAELEAELAELEAEleEKKAELDEELAELEAELEE 160
                         170
                  ....*....|..
gi 192807314  553 LLQQTDEYVANL 564
Cdd:COG1579   161 LEAEREELAAKI 172
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
782-913 2.22e-03

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 40.69  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   782 GLGKTIqtIALITYL--MEHKRINGPFLIIVPLSTLSNWAYE-FDKWA-PSVVKVSYKGSPAARRAFVPQLRSGkfNVLL 857
Cdd:pfam00270   24 GSGKTL--AFLLPALeaLDKLDNGPQALVLAPTRELAEQIYEeLKKLGkGLGLKVASLLGGDSRKEQLEKLKGP--DILV 99
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 192807314   858 TTYE---YIIKDKHILAKIrwKYMIVDEGHRM--KNHHCKLTQVLNTHYVAPRRLLLTGTP 913
Cdd:pfam00270  100 GTPGrllDLLQERKLLKNL--KLLVLDEAHRLldMGFGPDLEEILRRLPKKRQILLLSATL 158
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
357-547 7.03e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 7.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   357 KPRGLDPVEILQEREY-------RLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTA 429
Cdd:TIGR02169  669 SRSEPAELQRLRERLEglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   430 LETALNAK-----------AYKRSKRQSLREA-----------RITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFK 487
Cdd:TIGR02169  749 LEQEIENVkselkeleariEELEEDLHKLEEAlndlearlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 192807314   488 EYHRSvtgKIQKLTKAVATYHAN-TEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKD 547
Cdd:TIGR02169  829 EYLEK---EIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
413-559 8.89e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 8.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 192807314   413 QRQLRQEVvvcMRRDTALETALNAKAYKRSKRQSLREARITEklEKQQKIEQERKRRQKHQEYLNSILQHAKdfkEYHRS 492
Cdd:pfam15709  360 QRRLQQEQ---LERAEKMREELELEQQRRFEEIRLRKQRLEE--ERQRQEEEERKQRLQLQAAQERARQQQE---EFRRK 431
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 192807314   493 VTgKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEgyrklidqkkdKRLAYLLQQTDE 559
Cdd:pfam15709  432 LQ-ELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE-----------ERLEYQRQKQEA 486
 
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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