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Conserved domains on  [gi|145359958|ref|NP_178970|]
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chromatin remodeling 5 [Arabidopsis thaliana]

Protein Classification

DUF4208 domain-containing protein; chromo domain-containing DEAD/DEAH box helicase( domain architecture ID 13036324)

DUF4208 domain-containing protein similar to C-terminal domain of Homo sapiens chromodomain-helicase-dna-binding Protein 1 (CHD1), an ATP-dependent chromatin remodelling protein that has an ability to assemble and organize nucleosomes both in vitro and in vivo; chromo (chromatin organization modifier) domain-containing DEAD/DEAH box containing ATP-dependent helicase catalyzes the unwinding of DNA or RNA; similar to chromodomain helicase DNA-binding (CHD) family of ATP-dependent chromatin remodelers

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03142 super family cl33647
Probable chromatin-remodeling complex ATPase chain; Provisional
612-1152 9.28e-168

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: 537.08  E-value: 9.28e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  612 KLDEQPEwLIGGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAK 691
Cdd:PLN03142  158 RLLVQPS-CIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  692 EFRKWLPGMNIIVYVGTRASREvcqqyefYNEKKVGRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQ 771
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERA-------HQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSL 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  772 LYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSFNESELAN-LHLELRPHILRRVIKD 850
Cdd:PLN03142  310 LSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQqLHKVLRPFLLRRLKSD 389
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  851 VEKSLPPKIERILRVEMSPLQKQYYKWILERNFHDLNKGvrGNQVSLLNIVVELKKCCNHPFLFESADHG--YGGDindn 928
Cdd:PLN03142  390 VEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEPGppYTTG---- 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  929 sklDKIILSSGKLVILDKLLVRLRETKHRVLIFSQMVRMLDILAEYLSLRGFQFQRLDGSTKAELRQQAMDHFNAPASDD 1008
Cdd:PLN03142  464 ---EHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958 1009 FCFLLSTRAGGLGINLATADTVVIFDSDWNPQNDLQAMSRAHRIGQQEVVNIYRFVTSKSVEEEILERAKRKMVLDHLVI 1088
Cdd:PLN03142  541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145359958 1089 QklnaEGRLEKREtkkgsNFDKNELSAILRFGAEELFKEDKN---DEeskkrllsmDIDEILERAEQ 1152
Cdd:PLN03142  621 Q----QGRLAEQK-----TVNKDELLQMVRYGAEMVFSSKDStitDE---------DIDRIIAKGEE 669
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
418-498 2.70e-24

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


:

Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 97.82  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  418 DADVIEKVLWHQLKGMGEDVQTNnkstvpvlvsqLFDTEPDWNEMEFLIKWKGQSHLHCQWKTLSDLQNLSGFKKVLNYT 497
Cdd:cd18660     1 DEDKIEKILDHRPKGPVEEASLD-----------LTDPDEPWDEREFLVKWKGKSYLHCTWVTEETLEQLRGKKKLKNYI 69

                  .
gi 145359958  498 K 498
Cdd:cd18660    70 K 70
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
531-587 1.94e-16

repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


:

Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 74.92  E-value: 1.94e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145359958  531 QNSQVERIIADRISKDGlgdvVPEYLVKWQGLSYAEATWEKDVDIAF-AQVAIDEYKA 587
Cdd:cd18659     1 EYTIVERIIAHREDDEG----VTEYLVKWKGLPYDECTWESEEDISDiFQEAIDEYKK 54
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1534-1626 5.28e-13

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


:

Pssm-ID: 464035  Cd Length: 93  Bit Score: 66.12  E-value: 5.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  1534 EQKWMEWCEDVLADEIKTLgrlQRLQTTSADLPKEKVLFKIRRYLEILGRRIDAIVLEHEEDlyKQDRMTMRLWNYVSTF 1613
Cdd:pfam13907    4 ESMDEEECKELMRPVKKSL---KRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEETKKE--KKEKLRKHLWSFVSKF 78
                           90
                   ....*....|....*
gi 145359958  1614 SN--LSGDRLNQIYS 1626
Cdd:pfam13907   79 WPnkVSGKKLKEMYK 93
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
106-420 1.83e-07

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 56.46  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  106 QPMGQREGSDPAKDSQSGYKEAYHSEDNHSNDRSEKLDSENENDNENEEEDNEMNKHQSGQADVPAD-EMLSDEYYEQDE 184
Cdd:NF033609  555 EPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDsDSASDSDSASDS 634
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  185 DNQSDHVHYKGYSNPTNSRSLPKAGSAVHSNSRTSraihknihySDSNHDHNGDADMDYEEEEDEDDPEDADFEPYDAAD 264
Cdd:NF033609  635 DSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD---------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 705
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  265 DGGASKKHGQGWDVSDEDPESDEEIDLSDYEDDYGTKKPKVRQQSKGFRKSSAGLERKSFHVSSRQKRKTSYQDDDSEED 344
Cdd:NF033609  706 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 785
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958  345 SENDNDEGFRSLARRGTTLRQNNGRSTNTIGQSSEVRSSTRSVRKVSYVESEDSEDIDDGKNRKNQKDDIEEEDAD 420
Cdd:NF033609  786 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSN 861
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
612-1152 9.28e-168

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 537.08  E-value: 9.28e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  612 KLDEQPEwLIGGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAK 691
Cdd:PLN03142  158 RLLVQPS-CIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  692 EFRKWLPGMNIIVYVGTRASREvcqqyefYNEKKVGRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQ 771
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERA-------HQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSL 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  772 LYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSFNESELAN-LHLELRPHILRRVIKD 850
Cdd:PLN03142  310 LSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQqLHKVLRPFLLRRLKSD 389
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  851 VEKSLPPKIERILRVEMSPLQKQYYKWILERNFHDLNKGvrGNQVSLLNIVVELKKCCNHPFLFESADHG--YGGDindn 928
Cdd:PLN03142  390 VEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEPGppYTTG---- 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  929 sklDKIILSSGKLVILDKLLVRLRETKHRVLIFSQMVRMLDILAEYLSLRGFQFQRLDGSTKAELRQQAMDHFNAPASDD 1008
Cdd:PLN03142  464 ---EHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958 1009 FCFLLSTRAGGLGINLATADTVVIFDSDWNPQNDLQAMSRAHRIGQQEVVNIYRFVTSKSVEEEILERAKRKMVLDHLVI 1088
Cdd:PLN03142  541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145359958 1089 QklnaEGRLEKREtkkgsNFDKNELSAILRFGAEELFKEDKN---DEeskkrllsmDIDEILERAEQ 1152
Cdd:PLN03142  621 Q----QGRLAEQK-----TVNKDELLQMVRYGAEMVFSSKDStitDE---------DIDRIIAKGEE 669
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
624-846 2.05e-130

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: 405.20  E-value: 2.05e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  624 TLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNII 703
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  704 VYVGTRASREVCQQYEFYNEKKvgRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKN 783
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYFSQT--KKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNN 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145359958  784 KLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVEnykNLSSFNESELANLHLELRPHILRR 846
Cdd:cd17993   159 RLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEE---EHDEEQEKGIADLHKELEPFILRR 218
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
412-1083 2.36e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 412.31  E-value: 2.36e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  412 DDIEEEDADVIEKVLWHQLKGMGEDVQTNNKSTVPVLVSQLFDTEPDWNEMEFLIKWKGQSHLHCQWKTLSDLQNLSGFK 491
Cdd:COG0553    33 LVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  492 KVLNYTKKVTEEIRYRTALSREEIEVNDVSKEMDLDIIKQNSQVERIIADRISKDGLGDVVPEYLVKWQGLSYAEATWEk 571
Cdd:COG0553   113 LLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLE- 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  572 dvDIAFAQVAIDEYKAREVSIAVQGKMVEQQRTKGKASLRKLDEQPEWLiGGTLRDYQLEGLNFLVNSWLNDTNVILADE 651
Cdd:COG0553   192 --LALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADD 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  652 MGLGKTVQSVSMLGFLQNTQQIpGPFLVVVPLSTLANWAKEFRKWLPGMNIIVYVGTRasrevcqqyefyNEKKVGRPIK 731
Cdd:COG0553   269 MGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR------------ERAKGANPFE 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  732 -FNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGK 810
Cdd:COG0553   336 dADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGL 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  811 FKNKDEFVENY-KNLSSFNESELANLHLELRPHILRRVIKDVEKSLPPKIERILRVEMSPLQKQYYKWILERNFHDLNKG 889
Cdd:COG0553   416 LGSLKAFRERFaRPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGA 495
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  890 V-RGNQVSLLNIVVELKKCCNHPFLFESADHGYGGDindnskldkiilsSGKLVILDKLLVRLRETKHRVLIFSQMVRML 968
Cdd:COG0553   496 EgIRRRGLILAALTRLRQICSHPALLLEEGAELSGR-------------SAKLEALLELLEELLAEGEKVLVFSQFTDTL 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  969 DILAEYLSLRGFQFQRLDGSTKAELRQQAMDHFNAPASDDFcFLLSTRAGGLGINLATADTVVIFDSDWNPQNDLQAMSR 1048
Cdd:COG0553   563 DLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPV-FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDR 641
                         650       660       670
                  ....*....|....*....|....*....|....*
gi 145359958 1049 AHRIGQQEVVNIYRFVTSKSVEEEILERAKRKMVL 1083
Cdd:COG0553   642 AHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
628-914 2.11e-91

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: 298.44  E-value: 2.11e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   628 YQLEGLNFLVNSWLNDT-NVILADEMGLGKTVQSVSMLGFLQNTQQIPG-PFLVVVPLSTLANWAKEFRKWL--PGMNII 703
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   704 VYVGTRASREVCQQyefynekKVGRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKN 783
Cdd:pfam00176   81 VLHGNKRPQERWKN-------DPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   784 KLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSFNESE--LANLHLELRPHILRRVIKDVEKSLPPKIER 861
Cdd:pfam00176  154 RWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKkgVSRLHKLLKPFLLRRTKKDVEKSLPPKVEY 233
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958   862 ILRVEMSPLQKQYYK-WILERNFHDLNKGVRGNQV--SLLNIVVELKKCCNHPFLF 914
Cdd:pfam00176  234 ILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIkaSLLNILMRLRKICNHPGLI 289
DEXDc smart00487
DEAD-like helicases superfamily;
624-815 6.27e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 115.67  E-value: 6.27e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958    624 TLRDYQLEGLNFLVNSWLNdtnVILADEMGLGKTVQSVSMLgFLQNTQQIPGPFLVVVPLSTLA-NWAKEFRKWLPGMNI 702
Cdd:smart00487    8 PLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPA-LEALKRGKGGRVLVLVPTRELAeQWAEELKKLGPSLGL 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958    703 IVYVGTRASREVCQQYEFYNEKkvgrpikFNALLTTYEVVLKD--KAVLSKIKWIYLMVDEAHRLKNS--EAQLYTALLE 778
Cdd:smart00487   84 KVVGLYGGDSKREQLRKLESGK-------TDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKL 156
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 145359958    779 FSTKNK-LLITGTP---LQNSVEELWALLHFLDPGKFKNKD 815
Cdd:smart00487  157 LPKNVQlLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
418-498 2.70e-24

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


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 97.82  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  418 DADVIEKVLWHQLKGMGEDVQTNnkstvpvlvsqLFDTEPDWNEMEFLIKWKGQSHLHCQWKTLSDLQNLSGFKKVLNYT 497
Cdd:cd18660     1 DEDKIEKILDHRPKGPVEEASLD-----------LTDPDEPWDEREFLVKWKGKSYLHCTWVTEETLEQLRGKKKLKNYI 69

                  .
gi 145359958  498 K 498
Cdd:cd18660    70 K 70
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
531-587 1.94e-16

repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 74.92  E-value: 1.94e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145359958  531 QNSQVERIIADRISKDGlgdvVPEYLVKWQGLSYAEATWEKDVDIAF-AQVAIDEYKA 587
Cdd:cd18659     1 EYTIVERIIAHREDDEG----VTEYLVKWKGLPYDECTWESEEDISDiFQEAIDEYKK 54
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1534-1626 5.28e-13

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


Pssm-ID: 464035  Cd Length: 93  Bit Score: 66.12  E-value: 5.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  1534 EQKWMEWCEDVLADEIKTLgrlQRLQTTSADLPKEKVLFKIRRYLEILGRRIDAIVLEHEEDlyKQDRMTMRLWNYVSTF 1613
Cdd:pfam13907    4 ESMDEEECKELMRPVKKSL---KRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEETKKE--KKEKLRKHLWSFVSKF 78
                           90
                   ....*....|....*
gi 145359958  1614 SN--LSGDRLNQIYS 1626
Cdd:pfam13907   79 WPnkVSGKKLKEMYK 93
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
534-588 1.06e-12

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 64.14  E-value: 1.06e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 145359958   534 QVERIIADRISKDGLGdvvpEYLVKWQGLSYAEATWEKDVDIAFAQVAIDEYKAR 588
Cdd:pfam00385    2 EVERILDHRKDKGGKE----EYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
CHROMO smart00298
Chromatin organization modifier domain;
534-589 7.59e-11

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 58.76  E-value: 7.59e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958    534 QVERIIADRISKDGlgdvVPEYLVKWQGLSYAEATWEKDVDIAFAQVAIDEYKARE 589
Cdd:smart00298    3 EVEKILDHRWKKKG----ELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKKE 54
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
106-420 1.83e-07

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 56.46  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  106 QPMGQREGSDPAKDSQSGYKEAYHSEDNHSNDRSEKLDSENENDNENEEEDNEMNKHQSGQADVPAD-EMLSDEYYEQDE 184
Cdd:NF033609  555 EPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDsDSASDSDSASDS 634
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  185 DNQSDHVHYKGYSNPTNSRSLPKAGSAVHSNSRTSraihknihySDSNHDHNGDADMDYEEEEDEDDPEDADFEPYDAAD 264
Cdd:NF033609  635 DSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD---------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 705
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  265 DGGASKKHGQGWDVSDEDPESDEEIDLSDYEDDYGTKKPKVRQQSKGFRKSSAGLERKSFHVSSRQKRKTSYQDDDSEED 344
Cdd:NF033609  706 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 785
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958  345 SENDNDEGFRSLARRGTTLRQNNGRSTNTIGQSSEVRSSTRSVRKVSYVESEDSEDIDDGKNRKNQKDDIEEEDAD 420
Cdd:NF033609  786 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSN 861
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
39-406 1.89e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 49.52  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   39 DGTYSERGFDMNMdVQYQSDpEPGcSIRQPNEtavDNVADP-VDSHYQSSTKRLGVTGRWGSTfwkdcqpmgQREGSDPA 117
Cdd:NF033609  531 NGSGSGDGIDKPV-VPEQPD-EPG-EIEPIPE---DSDSDPgSDSGSDSSNSDSGSDSGSDST---------SDSGSDSA 595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  118 KDSQSGYKEAYHSEDNHSNDRSEKLDSENENDNENEEEDNEMNKHQSGQADVPADEMLSDEYYEQDEDNQSDHVHYKGYS 197
Cdd:NF033609  596 SDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 675
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  198 NPTNSRSLPKAGSAVHSNSRTSraihknihySDSNHDHNGDADMDYEEEEDEDDPEDADFEPYDAADDGGASKKHGQGWD 277
Cdd:NF033609  676 SDSDSDSDSDSDSDSDSDSDSD---------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 746
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  278 VSDEDPESDEEIDlSDYEDDYGTKkpkvrQQSKGFRKSSAGLERKSFHVSSRQKRKTSYQDDDSEEDSENDNDEGFRSLA 357
Cdd:NF033609  747 DSDSDSDSDSDSD-SDSDSDSDSD-----SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 820
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 145359958  358 RRGTTLRQNNGRSTNTIGQSSEVRSSTRSVRKVSYVESEDSEDIDDGKN 406
Cdd:NF033609  821 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSN 869
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
114-400 8.91e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 47.60  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  114 SDPAKDSQSGYKEAYHSEDNHSNDRSEKLDSENENDNENEEEDNEMNKHQS-GQADVPAD-EMLSDEYYEQDEDNQSDHV 191
Cdd:NF033609  616 SDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDsDSDSDSDSDSDSDSDSDSD 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  192 HYKGYSNPTNSRSLPKAGSAVHSNSRTSRAIHKNihySDSNHDHNGDADMDYEEEEDEDDPEDADFEPYDAADDGGASKK 271
Cdd:NF033609  696 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 772
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  272 HGQGWDVSDEDPESDEEIDlSDYEDDYGTKKPKvRQQSKGFRKSSAGLERKSFHVSSRQKRKTSYQDDDSEEDSENDNDE 351
Cdd:NF033609  773 DSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 850
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 145359958  352 GFRSLARRGTTLRQNNGRSTNTIGQSSEVRSSTRSVRKvsyvESEDSED 400
Cdd:NF033609  851 DSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKN----EAKDSKE 895
CHROMO smart00298
Chromatin organization modifier domain;
460-499 2.03e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.96  E-value: 2.03e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 145359958    460 NEMEFLIKWKGQSHLHCQWKTLSDLQNlsGFKKVLNYTKK 499
Cdd:smart00298   16 GELEYLVKWKGYSYSEDTWEPEENLLN--CSKKLDNYKKK 53
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
612-1152 9.28e-168

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 537.08  E-value: 9.28e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  612 KLDEQPEwLIGGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAK 691
Cdd:PLN03142  158 RLLVQPS-CIKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEYRGITGPHMVVAPKSTLGNWMN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  692 EFRKWLPGMNIIVYVGTRASREvcqqyefYNEKKVGRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQ 771
Cdd:PLN03142  237 EIRRFCPVLRAVKFHGNPEERA-------HQREELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYIIIDEAHRIKNENSL 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  772 LYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSFNESELAN-LHLELRPHILRRVIKD 850
Cdd:PLN03142  310 LSKTMRLFSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWFQISGENDQQEVVQqLHKVLRPFLLRRLKSD 389
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  851 VEKSLPPKIERILRVEMSPLQKQYYKWILERNFHDLNKGvrGNQVSLLNIVVELKKCCNHPFLFESADHG--YGGDindn 928
Cdd:PLN03142  390 VEKGLPPKKETILKVGMSQMQKQYYKALLQKDLDVVNAG--GERKRLLNIAMQLRKCCNHPYLFQGAEPGppYTTG---- 463
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  929 sklDKIILSSGKLVILDKLLVRLRETKHRVLIFSQMVRMLDILAEYLSLRGFQFQRLDGSTKAELRQQAMDHFNAPASDD 1008
Cdd:PLN03142  464 ---EHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMYRGYQYCRIDGNTGGEDRDASIDAFNKPGSEK 540
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958 1009 FCFLLSTRAGGLGINLATADTVVIFDSDWNPQNDLQAMSRAHRIGQQEVVNIYRFVTSKSVEEEILERAKRKMVLDHLVI 1088
Cdd:PLN03142  541 FVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKEVQVFRFCTEYTIEEKVIERAYKKLALDALVI 620
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145359958 1089 QklnaEGRLEKREtkkgsNFDKNELSAILRFGAEELFKEDKN---DEeskkrllsmDIDEILERAEQ 1152
Cdd:PLN03142  621 Q----QGRLAEQK-----TVNKDELLQMVRYGAEMVFSSKDStitDE---------DIDRIIAKGEE 669
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
624-846 2.05e-130

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: 405.20  E-value: 2.05e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  624 TLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNII 703
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  704 VYVGTRASREVCQQYEFYNEKKvgRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKN 783
Cdd:cd17993    81 VYLGDIKSRDTIREYEFYFSQT--KKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKEFKTNN 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145359958  784 KLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVEnykNLSSFNESELANLHLELRPHILRR 846
Cdd:cd17993   159 RLLITGTPLQNSLKELWALLHFLMPGKFDIWEEFEE---EHDEEQEKGIADLHKELEPFILRR 218
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
412-1083 2.36e-126

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 412.31  E-value: 2.36e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  412 DDIEEEDADVIEKVLWHQLKGMGEDVQTNNKSTVPVLVSQLFDTEPDWNEMEFLIKWKGQSHLHCQWKTLSDLQNLSGFK 491
Cdd:COG0553    33 LVLARELLLLLLAADALLLLALLLLLELLLLLAALLLLALLLLALSALALLLLRLLLALLLLALLLLLAGLLALALLLLA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  492 KVLNYTKKVTEEIRYRTALSREEIEVNDVSKEMDLDIIKQNSQVERIIADRISKDGLGDVVPEYLVKWQGLSYAEATWEk 571
Cdd:COG0553   113 LLGLLLSLALLLLLLLLLLLLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLE- 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  572 dvDIAFAQVAIDEYKAREVSIAVQGKMVEQQRTKGKASLRKLDEQPEWLiGGTLRDYQLEGLNFLVNSWLNDTNVILADE 651
Cdd:COG0553   192 --LALLAAEAELLLLLELLLELELLAEAAVDAFRLRRLREALESLPAGL-KATLRPYQLEGAAWLLFLRRLGLGGLLADD 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  652 MGLGKTVQSVSMLGFLQNTQQIpGPFLVVVPLSTLANWAKEFRKWLPGMNIIVYVGTRasrevcqqyefyNEKKVGRPIK 731
Cdd:COG0553   269 MGLGKTIQALALLLELKERGLA-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTR------------ERAKGANPFE 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  732 -FNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGK 810
Cdd:COG0553   336 dADLVITSYGLLRRDIELLAAVDWDLVILDEAQHIKNPATKRAKAVRALKARHRLALTGTPVENRLEELWSLLDFLNPGL 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  811 FKNKDEFVENY-KNLSSFNESELANLHLELRPHILRRVIKDVEKSLPPKIERILRVEMSPLQKQYYKWILERNFHDLNKG 889
Cdd:COG0553   416 LGSLKAFRERFaRPIEKGDEEALERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAVLEYLRRELEGA 495
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  890 V-RGNQVSLLNIVVELKKCCNHPFLFESADHGYGGDindnskldkiilsSGKLVILDKLLVRLRETKHRVLIFSQMVRML 968
Cdd:COG0553   496 EgIRRRGLILAALTRLRQICSHPALLLEEGAELSGR-------------SAKLEALLELLEELLAEGEKVLVFSQFTDTL 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  969 DILAEYLSLRGFQFQRLDGSTKAELRQQAMDHFNAPASDDFcFLLSTRAGGLGINLATADTVVIFDSDWNPQNDLQAMSR 1048
Cdd:COG0553   563 DLLEERLEERGIEYAYLHGGTSAEERDELVDRFQEGPEAPV-FLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDR 641
                         650       660       670
                  ....*....|....*....|....*....|....*
gi 145359958 1049 AHRIGQQEVVNIYRFVTSKSVEEEILERAKRKMVL 1083
Cdd:COG0553   642 AHRIGQTRDVQVYKLVAEGTIEEKILELLEEKRAL 676
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
625-846 1.37e-91

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: 296.08  E-value: 1.37e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPgMNIIV 704
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTD-MNVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREVCQQYEFYNEKKVGRPI----KFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFS 780
Cdd:cd17995    80 YHGSGESRQIIQQYEMYFKDAQGRKKkgvyKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLKKLT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958  781 TKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSfnESELANLHLELRPHILRR 846
Cdd:cd17995   160 LEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFGDLKT--AEQVEKLQALLKPYMLRR 223
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
628-914 2.11e-91

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: 298.44  E-value: 2.11e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   628 YQLEGLNFLVNSWLNDT-NVILADEMGLGKTVQSVSMLGFLQNTQQIPG-PFLVVVPLSTLANWAKEFRKWL--PGMNII 703
Cdd:pfam00176    1 YQIEGVNWMLSLENNLGrGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   704 VYVGTRASREVCQQyefynekKVGRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKN 783
Cdd:pfam00176   81 VLHGNKRPQERWKN-------DPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALKSLKTRN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   784 KLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSFNESE--LANLHLELRPHILRRVIKDVEKSLPPKIER 861
Cdd:pfam00176  154 RWILTGTPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGKkgVSRLHKLLKPFLLRRTKKDVEKSLPPKVEY 233
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958   862 ILRVEMSPLQKQYYK-WILERNFHDLNKGVRGNQV--SLLNIVVELKKCCNHPFLF 914
Cdd:pfam00176  234 ILFCRLSKLQRKLYQtFLLKKDLNAIKTGEGGREIkaSLLNILMRLRKICNHPGLI 289
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
613-846 4.80e-85

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: 278.04  E-value: 4.80e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  613 LDEQPEWlIGGT---LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANW 689
Cdd:cd18054     7 LKKQPSY-IGGEnleLRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSW 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  690 AKEFRKWLPGMNIIVYVGTRASREVCQQYEFYNEKKvgRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSE 769
Cdd:cd18054    86 QREFEIWAPEINVVVYIGDLMSRNTIREYEWIHSQT--KRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDD 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145359958  770 AQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYknlSSFNESELANLHLELRPHILRR 846
Cdd:cd18054   164 SLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEEDH---GKGRENGYQSLHKVLEPFLLRR 237
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
622-847 7.21e-79

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: 259.95  E-value: 7.21e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  622 GGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMN 701
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  702 IIVYVGTRASREvcqqyEFYNEKKVgrPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFST 781
Cdd:cd17997    81 VVVLIGDKEERA-----DIIRDVLL--PGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFNS 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145359958  782 KNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVE--NYKNLSSFNESELANLHLELRPHILRRV 847
Cdd:cd17997   154 RNRLLLTGTPLQNNLHELWALLNFLLPDVFTSSEDFDEwfNVNNCDDDNQEVVQRLHKVLRPFLLRRI 221
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
622-847 1.29e-76

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: 253.83  E-value: 1.29e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  622 GGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMN 701
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  702 IIVYVGTRASREVCQQYEfynekkvgRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLyTALLE--F 779
Cdd:cd17996    81 KIVYKGTPDVRKKLQSQI--------RAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKL-TQTLNtyY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  780 STKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENY---------KNLSSFNESE----LANLHLELRPHILRR 846
Cdd:cd17996   152 HARYRLLLTGTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFntpfantgeQVKIELNEEEtlliIRRLHKVLRPFLLRR 231

                  .
gi 145359958  847 V 847
Cdd:cd17996   232 L 232
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
625-808 2.56e-76

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: 250.95  E-value: 2.56e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREVCQQYEfynekkvgRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKNK 784
Cdd:cd17919    81 YHGSQRERAQIRAKE--------KLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALRAKRR 152
                         170       180
                  ....*....|....*....|....
gi 145359958  785 LLITGTPLQNSVEELWALLHFLDP 808
Cdd:cd17919   153 LLLTGTPLQNNLEELWALLDFLDP 176
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
622-847 6.21e-70

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: 234.59  E-value: 6.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  622 GGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNtQQIPGPFLVVVPLSTLANWAKEFRKWLPGMN 701
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRE-RGVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  702 IIVYVGTRASREVCQQyEFYNEKKVGRpiKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFST 781
Cdd:cd18009    80 VLLYHGTKEERERLRK-KIMKREGTLQ--DFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELKTFNS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  782 KNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFvENY-----KNLSSFNESELA---------NLHLELRPHILRRV 847
Cdd:cd18009   157 DNRLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSF-ESWfdfssLSDNAADISNLSeereqnivhMLHAILKPFLLRRL 235
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
613-846 6.17e-69

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: 231.86  E-value: 6.17e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  613 LDEQPEWlIGGT----LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLAN 688
Cdd:cd18053     6 LKKQPSY-IGGHegleLRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  689 WAKEFRKWLPGMNIIVYVGTRASREVCQQYEFYNEKKvgRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNS 768
Cdd:cd18053    85 WQREIQTWAPQMNAVVYLGDINSRNMIRTHEWMHPQT--KRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKND 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145359958  769 EAQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYknlSSFNESELANLHLELRPHILRR 846
Cdd:cd18053   163 DSLLYKTLIDFKSNHRLLITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEEEH---GKGREYGYASLHKELEPFLLRR 237
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
625-846 5.15e-68

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: 228.78  E-value: 5.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREvcqqyefynEKKVG--RPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTK 782
Cdd:cd18003    81 YYGSAKERK---------LKRQGwmKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLNFNTQ 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145359958  783 NKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKN-LSSFNESE-------LANLHLELRPHILRR 846
Cdd:cd18003   152 RRLLLTGTPLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNpLTAMSEGSqeeneelVRRLHKVLRPFLLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
612-858 3.00e-66

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: 224.54  E-value: 3.00e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  612 KLDEQPEWLIGGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAK 691
Cdd:cd18064     3 RFEDSPSYVKWGKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  692 EFRKWLPGMNIIVYVGTRASREVCQqyefyneKKVGRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQ 771
Cdd:cd18064    83 EFKRWVPTLRAVCLIGDKDQRAAFV-------RDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  772 LYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSFNESELAN-LHLELRPHILRRVIKD 850
Cdd:cd18064   156 LSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQKLVErLHMVLRPFLLRRIKAD 235

                  ....*...
gi 145359958  851 VEKSLPPK 858
Cdd:cd18064   236 VEKSLPPK 243
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
625-846 7.49e-66

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: 222.62  E-value: 7.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQqIPGPFLVVVPLSTLANWAKEFRKWLPgMNIIV 704
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVG-IHGPFLVIAPLSTITNWEREFNTWTE-MNTIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREVCQQYEFYNEKKVGRPI----KFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFS 780
Cdd:cd18060    79 YHGSLASRQMIQQYEMYCKDSRGRLIpgayKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958  781 TKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSfnESELANLHLELRPHILRR 846
Cdd:cd18060   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKT--EEQVQKLQAILKPMMLRR 222
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
625-846 7.84e-66

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: 222.31  E-value: 7.84e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASR-EVCQQYEFYNekkvgrpiKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKN 783
Cdd:cd18006    81 YMGDKEKRlDLQQDIKSTN--------RFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSVDF 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958  784 KLLITGTPLQNSVEELWALLHFLDPGKFKNK--DEFVENYKNLSsfNESELAN-LHLELRPHILRR 846
Cdd:cd18006   153 RLLLTGTPIQNSLQELYALLSFIEPNVFPKDklDDFIKAYSETD--DESETVEeLHLLLQPFLLRR 216
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
625-846 2.50e-65

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: 221.07  E-value: 2.50e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLG--FLQNtqqIPGPFLVVVPLSTLANWAKEFRKWLPgMNI 702
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSeiFLMG---IRGPFLIIAPLSTITNWEREFRTWTE-MNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  703 IVYVGTRASREVCQQYEFYNEKKVGRPI----KFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLE 778
Cdd:cd18058    77 IVYHGSQISRQMIQQYEMYYRDEQGNPLsgifKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145359958  779 FSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSfnESELANLHLELRPHILRR 846
Cdd:cd18058   157 MALEHKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFGDLKT--EEQVKKLQSILKPMMLRR 222
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
625-846 6.04e-65

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: 220.07  E-value: 6.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREVCQQyeFYNEKKV-GRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKN 783
Cdd:cd18002    81 YWGNPKDRKVLRK--FWDRKNLyTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTLLSFHCRN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145359958  784 KLLITGTPLQNSVEELWALLHFLDPGKFKNKDEF-------VENY-KNLSSFNESELANLHLELRPHILRR 846
Cdd:cd18002   159 RLLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFnewfskdIESHaENKTGLNEHQLKRLHMILKPFMLRR 229
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
612-847 1.10e-62

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: 213.73  E-value: 1.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  612 KLDEQPEWLIGGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAK 691
Cdd:cd18065     3 RFEESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  692 EFRKWLPGMNIIVYVGTRASREVCQQYEFYnekkvgrPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQ 771
Cdd:cd18065    83 EFKRWVPSLRAVCLIGDKDARAAFIRDVMM-------PGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSK 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145359958  772 LYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSFNESELAN-LHLELRPHILRRV 847
Cdd:cd18065   156 LSEIVREFKTTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQKLVErLHAVLKPFLLRRI 232
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
625-846 1.39e-62

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: 211.91  E-value: 1.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTrasrevcqqyefynekkvgrpikfNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKNK 784
Cdd:cd17994    81 YVGD------------------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIGYK 136
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145359958  785 LLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSsfNESELANLHLELRPHILRR 846
Cdd:cd17994   137 LLLTGTPLQNNLEELFHLLNFLTPERFNNLQGFLEEFADIS--KEDQIKKLHDLLGPHMLRR 196
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
625-846 3.24e-61

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: 209.12  E-value: 3.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLgFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPgMNIIV 704
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWTE-LNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREVCQQYEFYNEKKVGRPIK----FNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFS 780
Cdd:cd18059    79 YHGSQASRRTIQLYEMYFKDPQGRVIKgsykFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958  781 TKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSfnESELANLHLELRPHILRR 846
Cdd:cd18059   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFGDLKT--EEQVQKLQAILKPMMLRR 222
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
625-846 1.65e-60

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: 207.17  E-value: 1.65e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQqIPGPFLVVVPLSTLANWAKEFRKWlPGMNIIV 704
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFLYEILLTG-IRGPFLIIAPLSTIANWEREFRTW-TDLNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREVCQQYEFYNEKKVGRPIK----FNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFS 780
Cdd:cd18061    79 YHGSLISRQMIQQYEMYFRDSQGRIIRgayrFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958  781 TKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSSfnESELANLHLELRPHILRR 846
Cdd:cd18061   159 LEHKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFGDLKT--EEQVQKLQAILKPMMLRR 222
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
929-1064 8.23e-60

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: 201.55  E-value: 8.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  929 SKLDKIIlsSGKLVILDKLLVRLRETKHRVLIFSQMVRMLDILAEYLSLRGFQFQRLDGSTKAELRQQAMDHFNAPaSDD 1008
Cdd:cd18793     3 PKIEEVV--SGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNED-PDI 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958 1009 FCFLLSTRAGGLGINLATADTVVIFDSDWNPQNDLQAMSRAHRIGQQEVVNIYRFV 1064
Cdd:cd18793    80 RVFLLSTKAGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
625-846 1.85e-59

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: 204.47  E-value: 1.85e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREVCQQYEFYNEKKVGR------------PIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQL 772
Cdd:cd18055    81 YTGDKDSRAIIRENEFSFDDNAVKggkkafkmkreaQVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145359958  773 YTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSsfNESELANLHLELRPHILRR 846
Cdd:cd18055   161 FRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADIS--KEDQIKKLHDLLGPHMLRR 232
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
625-846 6.81e-59

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: 202.99  E-value: 6.81e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREVCQQYEFYNE-------KKVGR-----PIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQL 772
Cdd:cd18056    81 YVGDKDSRAIIRENEFSFEdnairggKKASRmkkeaSVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145359958  773 YTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSsfNESELANLHLELRPHILRR 846
Cdd:cd18056   161 FRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIA--KEDQIKKLHDMLGPHMLRR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
625-846 1.26e-58

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: 202.22  E-value: 1.26e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREVCQQYEFYNE-------KKVGR-----PIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQL 772
Cdd:cd18057    81 YTGDKESRSVIRENEFSFEdnairsgKKVFRmkkeaQIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145359958  773 YTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSsfNESELANLHLELRPHILRR 846
Cdd:cd18057   161 FRVLNSYKIDYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADIS--KEDQIKKLHDLLGPHMLRR 232
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
608-847 5.66e-58

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: 201.04  E-value: 5.66e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  608 ASLRKLDEQPEWLIGGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLA 687
Cdd:cd18062     7 AVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  688 NWAKEFRKWLPGMNIIVYVGTRASREVcqqyeFYNEKKVGrpiKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKN 767
Cdd:cd18062    87 NWVYEFDKWAPSVVKVSYKGSPAARRA-----FVPQLRSG---KFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  768 SEAQLYTAL-LEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFvENYKNLS--------SFNESE----LAN 834
Cdd:cd18062   159 HHCKLTQVLnTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTF-EQWFNAPfamtgekvDLNEEEtiliIRR 237
                         250
                  ....*....|...
gi 145359958  835 LHLELRPHILRRV 847
Cdd:cd18062   238 LHKVLRPFLLRRL 250
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
604-847 1.41e-57

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: 199.90  E-value: 1.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  604 TKGKASLRKLDEQPEWLIGGTLRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPL 683
Cdd:cd18063     3 TVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIVPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  684 STLANWAKEFRKWLPGMNIIVYVGTRA-SREVCQQYefynekkvgRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEA 762
Cdd:cd18063    83 STLSNWTYEFDKWAPSVVKISYKGTPAmRRSLVPQL---------RSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  763 HRLKNSEAQLYTAL-LEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFvENYKNLS--------SFNESE-- 831
Cdd:cd18063   154 HRMKNHHCKLTQVLnTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTF-EQWFNAPfamtgervDLNEEEti 232
                         250
                  ....*....|....*...
gi 145359958  832 --LANLHLELRPHILRRV 847
Cdd:cd18063   233 liIRRLHKVLRPFLLRRL 250
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
623-846 1.26e-55

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: 192.78  E-value: 1.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  623 GTLRDYQLEGLNFLvnSWLNDTNV--ILADEMGLGKTVQsvsMLGFLQNTQQ--IPGPFLVVVPLSTLANWAKEFRKWLP 698
Cdd:cd18012     3 ATLRPYQKEGFNWL--SFLRHYGLggILADDMGLGKTLQ---TLALLLSRKEegRKGPSLVVAPTSLIYNWEEEAAKFAP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  699 GMNIIVYVGTRASREVCQQYEFYNekkvgrpikfnALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLE 778
Cdd:cd18012    78 ELKVLVIHGTKRKREKLRALEDYD-----------LVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAVKA 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  779 FSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNL--SSFNESELANLHLELRPHILRR 846
Cdd:cd18012   147 LKADHRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKPieKDGDEEALEELKKLISPFILRR 216
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
625-811 1.65e-48

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: 171.41  E-value: 1.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNtQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKE-IGIPGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREvcqqYEFYNEKKvgRPIKFNALLTTYEVVL---KDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFST 781
Cdd:cd17998    80 YYGSQEERK----HLRYDILK--GLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMTINA 153
                         170       180       190
                  ....*....|....*....|....*....|
gi 145359958  782 KNKLLITGTPLQNSVEELWALLHFLDPGKF 811
Cdd:cd17998   154 NFRLLLTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
625-846 8.72e-46

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: 165.24  E-value: 8.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFLQNTQQIpGPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDSGLI-KSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGT-RASREvcqqyefYNEKKVGRpiKFNALLTTYEVVLKDKAVLS-----KIKWIYLMVDEAHRLKNSEAQLYTALLE 778
Cdd:cd18001    80 FHGTsKKERE-------RNLERIQR--GGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSLRE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  779 FSTKNKLLITGTPLQNSVEELWALLHFLDPGK-FKNKDEFVENYKNL--------SSFNE----SELA-NLHLELRPHIL 844
Cdd:cd18001   151 IPAKNRIILTGTPIQNNLKELWALFDFACNGSlLGTRKTFKMEFENPitrgrdkdATQGEkalgSEVAeNLRQIIKPYFL 230

                  ..
gi 145359958  845 RR 846
Cdd:cd18001   231 RR 232
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
625-817 3.26e-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: 158.22  E-value: 3.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTN-----VILADEMGLGKTVQSVSMLGFLqnTQQIP--GP----FLVVVPLSTLANWAKEF 693
Cdd:cd18004     1 LRPHQREGVQFLYDCLTGRRGyggggAILADEMGLGKTLQAIALVWTL--LKQGPygKPtakkALIVCPSSLVGNWKAEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  694 RKWLPGMNIIVYV---GTRASREVCQQYEFYNEKKVgrpikfnaLLTTYEVVLKDKAVLSKIKWIYLMV-DEAHRLKNSE 769
Cdd:cd18004    79 DKWLGLRRIKVVTadgNAKDVKASLDFFSSASTYPV--------LIISYETLRRHAEKLSKKISIDLLIcDEGHRLKNSE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 145359958  770 AQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEF 817
Cdd:cd18004   151 SKTTKALNSLPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASF 198
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
625-808 1.81e-41

DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, also known Cockayne syndrome group B (CSB), Rad26 in Saccharomyces cerevisiae, and Rhp26 in Schizosaccharomyces pombe) is a DNA-binding protein that is important in transcription-coupled excision repair. ERCC6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 151.32  E-value: 1.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLvnSWLNDTNV--ILADEMGLGKTVQSVSMLGFLQNTQQIPGPFLVVVPLSTLANWAKEFRKWLPGMNI 702
Cdd:cd18000     1 LFKYQQTGVQWL--WELHCQRVggILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  703 IV------YVGTRASREVCQQYEFYNEKKVGRPikfNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTAL 776
Cdd:cd18000    79 VVlhssgsGTGSEEKLGSIERKSQLIRKVVGDG---GILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAC 155
                         170       180       190
                  ....*....|....*....|....*....|..
gi 145359958  777 LEFSTKNKLLITGTPLQNSVEELWALLHFLDP 808
Cdd:cd18000   156 KQLRTPHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
625-846 2.96e-41

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: 152.12  E-value: 2.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLvnSWLNDTNV--ILADEMGLGKTVQSVSML-----GFLQNTQQIPGPFLVVVPlSTLA-NWAKEFRKW 696
Cdd:cd17999     1 LRPYQQEGINWL--AFLNKYNLhgILCDDMGLGKTLQTLCILasdhhKRANSFNSENLPSLVVCP-PTLVgHWVAEIKKY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  697 LP--GMNIIVYVGTRASREvcqqyefyneKKVGRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYT 774
Cdd:cd17999    78 FPnaFLKPLAYVGPPQERR----------RLREQGEKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  775 ALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNL--------SSFNESE-----LANLHLELRP 841
Cdd:cd17999   148 AVKQLKANHRLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPilasrdskASAKEQEagalaLEALHKQVLP 227

                  ....*
gi 145359958  842 HILRR 846
Cdd:cd17999   228 FLLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
625-821 1.05e-40

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: 150.99  E-value: 1.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVILADEMGLGKTVQSVSMLGFL---------------QNTQQIP-----GPFLVVVPLS 684
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVlgktgtrrdrennrpRFKKKPPassakKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  685 TLANWAKEFRKWlpG-MNIIVYVGTRASREVCQQYefynekKVGRpikFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAH 763
Cdd:cd18005    81 VLYNWKDELDTW--GhFEVGVYHGSRKDDELEGRL------KAGR---LEVVVTTYDTLRRCIDSLNSINWSAVIADEAH 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145359958  764 RLKNSEAQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENY 821
Cdd:cd18005   150 RIKNPKSKLTQAMKELKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHF 207
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
625-822 1.88e-38

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: 144.36  E-value: 1.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLvnsWLN----------DTNVILADEMGLGKTVQSVSML-GFLQNTQQIPGPfLVVVPLSTLANWAKEF 693
Cdd:cd18007     1 LKPHQVEGVRFL---WSNlvgtdvgsdeGGGCILAHTMGLGKTLQVITFLhTYLAAAPRRSRP-LVLCPASTLYNWEDEF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  694 RKWLPGMNIIVYVGTRASREvcqqyefynEKKVGRPIKFNA-------LLTTYEV---VLKDKAVLSKIKWIY------- 756
Cdd:cd18007    77 KKWLPPDLRPLLVLVSLSAS---------KRADARLRKINKwhkeggvLLIGYELfrnLASNATTDPRLKQEFiaalldp 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  757 ----LMVDEAHRLKNSEAQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYK 822
Cdd:cd18007   148 gpdlLVLDEGHRLKNEKSQLSKALSKVKTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFV 217
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
625-846 1.24e-35

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: 136.26  E-value: 1.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVnswlndtnV---ILADEMGLGKTVQSVS-MLGFLQNTQQIPGPF----------------LVVVPLS 684
Cdd:cd18008     1 LLPYQKQGLAWML--------PrggILADEMGLGKTIQALAlILATRPQDPKIPEELeenssdpkklylskttLIVVPLS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  685 TLANWAKEFRK--WLPGMNIIVYVGTRasrevcqqyefyNEKKVGRPIKFNALLTTYEVVLKD----------------K 746
Cdd:cd18008    73 LLSQWKDEIEKhtKPGSLKVYVYHGSK------------RIKSIEELSDYDIVITTYGTLASEfpknkkgggrdskekeA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  747 AVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKNLSS 826
Cdd:cd18008   141 SPLHRIRWYRVILDEAHNIKNRSTKTSRAVCALKAERRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFS 220
                         250       260
                  ....*....|....*....|.
gi 145359958  827 FNESE-LANLHLELRPHILRR 846
Cdd:cd18008   221 KNDRKaLERLQALLKPILLRR 241
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
625-823 6.92e-33

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: 128.36  E-value: 6.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVN--SWLNDTNV---ILADEMGLGKTVQSVSMLGFLQNTQQIPGPFL----VVVPLSTLANWAKEFRK 695
Cdd:cd18067     1 LRPHQREGVKFLYRcvTGRRIRGShgcIMADEMGLGKTLQCITLMWTLLRQSPQCKPEIdkaiVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  696 WLPGMNIIVYVGTRASREVCQQYE-FYNE--KKVGRPIkfnaLLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQL 772
Cdd:cd18067    81 WLGGRLQPLAIDGGSKKEIDRKLVqWASQqgRRVSTPV----LIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQT 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145359958  773 YTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKN 823
Cdd:cd18067   157 YQALDSLNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFEL 207
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
625-846 3.47e-32

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: 125.40  E-value: 3.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNswlNDTNVILADEMGLGKTVQSVSMLGFLQNTqqipGPFLVVVPLSTLANWAKEFRKWLPGM---N 701
Cdd:cd18010     1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLppdD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  702 IIVYVGTRasrevcqqyefynEKKVGRPIKFNalLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFST 781
Cdd:cd18010    74 IQVIVKSK-------------DGLRDGDAKVV--IVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAALPLLK 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145359958  782 KNK--LLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENY---KNLSSFNE----SELANLHLELRPHI-LRR 846
Cdd:cd18010   139 RAKrvILLSGTPALSRPIELFTQLDALDPKLFGRFHDFGRRYcaaKQGGFGWDysgsSNLEELHLLLLATImIRR 213
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
625-809 3.28e-31

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: 123.42  E-value: 3.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNV-----ILADEMGLGKTVQSVSMLGflqnTQQIPGPF---------LVVVPLSTLANWA 690
Cdd:cd18066     1 LRPHQREGIEFLYECVMGMRVNerfgaILADEMGLGKTLQCISLIW----TLLRQGPYggkpvikraLIVTPGSLVKNWK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  691 KEFRKWLPGMNIIVYVgTRASREVcqqYEFYNEkkvgrpIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRLKNSEA 770
Cdd:cd18066    77 KEFQKWLGSERIKVFT-VDQDHKV---EEFIAS------PLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSI 146
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 145359958  771 QLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPG 809
Cdd:cd18066   147 KTTTALTSLSCERRIILTGTPIQNDLQEFFALIDFVNPG 185
DEXDc smart00487
DEAD-like helicases superfamily;
624-815 6.27e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 115.67  E-value: 6.27e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958    624 TLRDYQLEGLNFLVNSWLNdtnVILADEMGLGKTVQSVSMLgFLQNTQQIPGPFLVVVPLSTLA-NWAKEFRKWLPGMNI 702
Cdd:smart00487    8 PLRPYQKEAIEALLSGLRD---VILAAPTGSGKTLAALLPA-LEALKRGKGGRVLVLVPTRELAeQWAEELKKLGPSLGL 83
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958    703 IVYVGTRASREVCQQYEFYNEKkvgrpikFNALLTTYEVVLKD--KAVLSKIKWIYLMVDEAHRLKNS--EAQLYTALLE 778
Cdd:smart00487   84 KVVGLYGGDSKREQLRKLESGK-------TDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDGgfGDQLEKLLKL 156
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 145359958    779 FSTKNK-LLITGTP---LQNSVEELWALLHFLDPGKFKNKD 815
Cdd:smart00487  157 LPKNVQlLLLSATPpeeIENLLELFLNDPVFIDVGFTPLEP 197
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
939-1053 9.33e-29

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: 111.92  E-value: 9.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   939 GKLVILDKLLvrLRETKHRVLIFSQMVRMLDilAEYLSLR-GFQFQRLDGSTKAELRQQAMDHFNapaSDDFCFLLSTRA 1017
Cdd:pfam00271    1 EKLEALLELL--KKERGGKVLIFSQTKKTLE--AELLLEKeGIKVARLHGDLSQEEREEILEDFR---KGKIDVLVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 145359958  1018 GGLGINLATADTVVIFDSDWNPQNDLQAMSRAHRIG 1053
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
647-846 3.94e-27

DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as HIP116 or SMARCA3) has both helicase and E3 ubiquitin ligase activities and ATP-dependent nucleosome-remodeling activity. HLTF1 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350829 [Multi-domain]  Cd Length: 239  Bit Score: 111.79  E-value: 3.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  647 ILADEMGLGKTVQSVSMLGFlqntqqipGPFLVVVPLSTLANWAKEFRKWL-PG-MNIIVYVGTRASREVcqqyefyneK 724
Cdd:cd18071    52 ILADDMGLGKTLTTISLILA--------NFTLIVCPLSVLSNWETQFEEHVkPGqLKVYTYHGGERNRDP---------K 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  725 KVGrpiKFNALLTTYEVVL-----KDKAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKNKLLITGTPLQNSVEEL 799
Cdd:cd18071   115 LLS---KYDIVLTTYNTLAsdfgaKGDSPLHTINWLRVVLDEGHQIRNPNAQQTKAVLNLSSERRWVLTGTPIQNSPKDL 191
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 145359958  800 WALLHFLDPGKFKNKDEFVENY-KNLSSFNESELANLHLELRPHILRR 846
Cdd:cd18071   192 GSLLSFLHLKPFSNPEYWRRLIqRPLTMGDPTGLKRLQVLMKQITLRR 239
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
418-498 2.70e-24

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


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 97.82  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  418 DADVIEKVLWHQLKGMGEDVQTNnkstvpvlvsqLFDTEPDWNEMEFLIKWKGQSHLHCQWKTLSDLQNLSGFKKVLNYT 497
Cdd:cd18660     1 DEDKIEKILDHRPKGPVEEASLD-----------LTDPDEPWDEREFLVKWKGKSYLHCTWVTEETLEQLRGKKKLKNYI 69

                  .
gi 145359958  498 K 498
Cdd:cd18660    70 K 70
HELICc smart00490
helicase superfamily c-terminal domain;
969-1053 1.16e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 96.13  E-value: 1.16e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958    969 DILAEYLSLRGFQFQRLDGSTKAELRQQAMDHFNapaSDDFCFLLSTRAGGLGINLATADTVVIFDSDWNPQNDLQAMSR 1048
Cdd:smart00490    1 EELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGR 77

                    ....*
gi 145359958   1049 AHRIG 1053
Cdd:smart00490   78 AGRAG 82
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
625-823 1.38e-20

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


Pssm-ID: 350827 [Multi-domain]  Cd Length: 227  Bit Score: 92.57  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTN---------VILADEMGLGKTVQSVSMLG-FLQNTQQipGPFLVVVPLSTLANWAKEFR 694
Cdd:cd18069     1 LKPHQIGGIRFLYDNIIESLErykgssgfgCILAHSMGLGKTLQVISFLDvLLRHTGA--KTVLAIVPVNTLQNWLSEFN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  695 KWLPGMNIIVYVGTRA---------SREVCQQYEFYNE--KKVGrpikfnALLTTYEVV-LKDKAVLskikwiyLMVDEA 762
Cdd:cd18069    79 KWLPPPEALPNVRPRPfkvfilndeHKTTAARAKVIEDwvKDGG------VLLMGYEMFrLRPGPDV-------VICDEG 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145359958  763 HRLKNSEAQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKN 823
Cdd:cd18069   146 HRIKNCHASTSQALKNIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFER 206
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
647-823 1.91e-20

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


Pssm-ID: 350826 [Multi-domain]  Cd Length: 246  Bit Score: 92.64  E-value: 1.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  647 ILADEMGLGKTVQSVSMLGFLQNTQQIPG--PFLVVVPLSTLANWAKEFRKWLPGMN----IIVYVGTRASREVCQQYEF 720
Cdd:cd18068    32 ILAHCMGLGKTLQVVTFLHTVLLCEKLENfsRVLVVCPLNTVLNWLNEFEKWQEGLKdeekIEVNELATYKRPQERSYKL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  721 YNEKKVGrpikfNALLTTYEV-----VLKDKAVLSKIKWIY-----------LMVDEAHRLKNSEAQLYTALLEFSTKNK 784
Cdd:cd18068   112 QRWQEEG-----GVMIIGYDMyrilaQERNVKSREKLKEIFnkalvdpgpdfVVCDEGHILKNEASAVSKAMNSIRTKRR 186
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 145359958  785 LLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVENYKN 823
Cdd:cd18068   187 IVLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVN 225
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
625-820 2.43e-19

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: 88.11  E-value: 2.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNdtNVILADEMGLGKTVqsvsMLGFLQNTQQIPG---PFLVVVPLSTLANWAKEFRKwLPGMN 701
Cdd:cd18011     1 PLPHQIDAVLRALRKPPV--RLLLADEVGLGKTI----EAGLIIKELLLRGdakRVLILCPASLVEQWQDELQD-KFGLP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  702 IIVYVGTRASREVCQQYEFYNEKKVgrpikfnaLLTTYEVvLKDK----AVLSKIKWIYLMVDEAHRLKNSEAQLYTALL 777
Cdd:cd18011    74 FLILDRETAAQLRRLIGNPFEEFPI--------VIVSLDL-LKRSeerrGLLLSEEWDLVVVDEAHKLRNSGGGKETKRY 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 145359958  778 EF------STKNKLLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVEN 820
Cdd:cd18011   145 KLgrllakRARHVLLLTATPHNGKEEDFRALLSLLDPGRFAVLGRFLRL 193
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
647-846 6.50e-17

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: 82.14  E-value: 6.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  647 ILADEMGLGKTVQSVSMLGFLQNTQQ---------------------IP-GPFLVVVPLSTLANWAKEFRKWLPGMNIIV 704
Cdd:cd18072    24 ILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkdstlVPsAGTLVVCPASLVHQWKNEVESRVASNKLRV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  705 YVGTRASREvcqqyefynekKVGRPIK-FNALLTTYEVVLKD---------KAVLSKIKWIYLMVDEAHRLKNSEAQLYT 774
Cdd:cd18072   104 CLYHGPNRE-----------RIGEVLRdYDIVITTYSLVAKEiptykeesrSSPLFRIAWARIILDEAHNIKNPKVQASI 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145359958  775 ALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFknkDEFVENYKNLSsfNESELAN--LHLELRPHILRR 846
Cdd:cd18072   173 AVCKLRAHARWALTGTPIQNNLLDMYSLLKFLRCSPF---DDLKVWKKQVD--NKSRKGGerLNILTKSLLLRR 241
CD2_tandem cd18659
repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier ...
531-587 1.94e-16

repeat 2 of paired tandem chromodomains; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 to CHD9, and yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349306 [Multi-domain]  Cd Length: 54  Bit Score: 74.92  E-value: 1.94e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145359958  531 QNSQVERIIADRISKDGlgdvVPEYLVKWQGLSYAEATWEKDVDIAF-AQVAIDEYKA 587
Cdd:cd18659     1 EYTIVERIIAHREDDEG----VTEYLVKWKGLPYDECTWESEEDISDiFQEAIDEYKK 54
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
623-1170 1.22e-15

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 82.38  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  623 GTLRDYQLEGLNFLVNSWLNDTN---VILAdeMGLGKTVqsvSMLGFLQNTQQiPGPFLVVVPLSTLAN-WAKEFRKWLP 698
Cdd:COG1061    79 FELRPYQQEALEALLAALERGGGrglVVAP--TGTGKTV---LALALAAELLR-GKRVLVLVPRRELLEqWAEELRRFLG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  699 gmnIIVYVGtrasrevcqqyefyNEKKVGRPIkfnaLLTTYEVVLKdKAVLSKIK--WIYLMVDEAHRLknsEAQLYTAL 776
Cdd:COG1061   153 ---DPLAGG--------------GKKDSDAPI----TVATYQSLAR-RAHLDELGdrFGLVIIDEAHHA---GAPSYRRI 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  777 LE-FSTKNKLLITGTPLqnsveelwallhFLDpgkfkNKDEFVENYKNL-SSFNESELANLHLeLRPHILRRVikdveks 854
Cdd:COG1061   208 LEaFPAAYRLGLTATPF------------RSD-----GREILLFLFDGIvYEYSLKEAIEDGY-LAPPEYYGI------- 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  855 lppkierilRVEMSPLQKQYYKwilernfhdlnkgvrgnqvsllnivvelkkccnhpflfesadhgyggdinDNSKLDKI 934
Cdd:COG1061   263 ---------RVDLTDERAEYDA--------------------------------------------------LSERLREA 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  935 ILSSG--KLVILDKLLVRLREtKHRVLIFSQMVRMLDILAEYLSLRGFQFQRLDGSTKAELRQQAMDHFnapASDDFCFL 1012
Cdd:COG1061   284 LAADAerKDKILRELLREHPD-DRKTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAF---RDGELRIL 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958 1013 LSTRAGGLGINLATADTVVIFDSDWNPQNDLQAMSRAHRIGQQ-EVVNIYRFVTSKSVEEEILERAKRKMVLDHLVIQKL 1091
Cdd:COG1061   360 VTVDVLNEGVDVPRLDVAILLRPTGSPREFIQRLGRGLRPAPGkEDALVYDFVGNDVPVLEELAKDLRDLAGYRVEFLDE 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958 1092 NAEGRLEKRETKKGSNFDKNEL-SAILRFGAEELFKEDKNDEESKKRLLSMDIDEILERAEQVEEKHTDETEHELLGAFK 1170
Cdd:COG1061   440 EESEELALLIAVKPALEVKGELeEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLA 519
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
625-810 4.28e-15

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


Pssm-ID: 350771 [Multi-domain]  Cd Length: 218  Bit Score: 76.23  E-value: 4.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNswlNDTNVILADeMGLGKTVQSVSMLGFLQnTQQIPGPFLVVVPLSTLAN-WAKEFRKW--LPGMN 701
Cdd:cd18013     1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQ-LDDFTRRVLVIAPLRVARStWPDEVEKWnhLRNLT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  702 IIVYVGTrasrevcqqyefynEKKVGRPIKFNALLTTYEVVLKDKAV-LSKIKWIYLMV--DEAHRLKNSEAQLYTAL-- 776
Cdd:cd18013    76 VSVAVGT--------------ERQRSKAANTPADLYVINRENLKWLVnKSGDPWPFDMVviDELSSFKSPRSKRFKALrk 141
                         170       180       190
                  ....*....|....*....|....*....|....
gi 145359958  777 LEFSTKNKLLITGTPLQNSVEELWALLHFLDPGK 810
Cdd:cd18013   142 VRPVIKRLIGLTGTPSPNGLMDLWAQIALLDQGE 175
DUF4208 pfam13907
Domain of unknown function (DUF4208); This domain is found at the C-terminus of ...
1534-1626 5.28e-13

Domain of unknown function (DUF4208); This domain is found at the C-terminus of chromodomain-helicase-DNA-binding proteins. The exact function of the domain is undetermined.


Pssm-ID: 464035  Cd Length: 93  Bit Score: 66.12  E-value: 5.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  1534 EQKWMEWCEDVLADEIKTLgrlQRLQTTSADLPKEKVLFKIRRYLEILGRRIDAIVLEHEEDlyKQDRMTMRLWNYVSTF 1613
Cdd:pfam13907    4 ESMDEEECKELMRPVKKSL---KRLKKGTKGLSRKERAKILKKELLKIGDFIDSLLEETKKE--KKEKLRKHLWSFVSKF 78
                           90
                   ....*....|....*
gi 145359958  1614 SN--LSGDRLNQIYS 1626
Cdd:pfam13907   79 WPnkVSGKKLKEMYK 93
Chromo pfam00385
Chromo (CHRromatin organization MOdifier) domain;
534-588 1.06e-12

Chromo (CHRromatin organization MOdifier) domain;


Pssm-ID: 459793 [Multi-domain]  Cd Length: 52  Bit Score: 64.14  E-value: 1.06e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 145359958   534 QVERIIADRISKDGLGdvvpEYLVKWQGLSYAEATWEKDVDIAFAQVAIDEYKAR 588
Cdd:pfam00385    2 EVERILDHRKDKGGKE----EYLVKWKGYPYDENTWEPEENLSKCPELIEEFKDR 52
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
625-815 3.90e-12

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: 68.52  E-value: 3.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSwlndtNVILADEMGLGKTVQSVSMLgFL-------QNTQQIP-------------------GPFL 678
Cdd:cd18070     1 LLPYQRRAVNWMLVP-----GGILADEMGLGKTVEVLALI-LLhprpdndLDAADDDsdemvccpdclvaetpvssKATL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  679 VVVPLSTLANWAKEFRKWLPG-MNIIVYVGTRASREVCQQYEFY-NEKKVgrpikfnaLLTTYEVVLKD----------- 745
Cdd:cd18070    75 IVCPSAILAQWLDEINRHVPSsLKVLTYQGVKKDGALASPAPEIlAEYDI--------VVTTYDVLRTElhyaeanrsnr 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  746 -----------KAVLSKIKWIYLMVDEAHRLKNSEAQLYTALLEFSTKNKLLITGTPLQNSVEELWALLHFLDPGKFKNK 814
Cdd:cd18070   147 rrrrqkryeapPSPLVLVEWWRVCLDEAQMVESSTSKAAEMARRLPRVNRWCVSGTPIQRGLDDLFGLLSFLGVEPFCDS 226

                  .
gi 145359958  815 D 815
Cdd:cd18070   227 D 227
CD1_tandem_CHD1-2_like cd18666
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
418-498 5.61e-12

repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 1 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349313  Cd Length: 85  Bit Score: 63.08  E-value: 5.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  418 DADVIEKVLWHQlkgMGEDVQTNNKSTVPVLVSQL-----FDTEPDWNEMEFLIKWKGQSHLHCQW---KTLSDlQNLSG 489
Cdd:cd18666     1 EFETIERVLDHR---IGRKGATGASTTIYAVEADGdpnagFDPEDEETEIQYLIKWKGWSHIHNTWeseESLKD-QNVKG 76

                  ....*....
gi 145359958  490 FKKVLNYTK 498
Cdd:cd18666    77 MKKLENYKK 85
CD2_tandem_CHD1-2_like cd18661
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and ...
531-588 8.74e-12

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 1 and 2, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD1 and CHD2. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349308  Cd Length: 58  Bit Score: 61.55  E-value: 8.74e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145359958  531 QNSQVERIIADRISKDGLGDVvPEYLVKWQGLSYAEATWEKDVDIA-FAQVAIDEYKAR 588
Cdd:cd18661     1 QYQIVERIIAHSPQKSAASGY-PDYLCKWQGLPYSECTWEDGALISkKFQACIDEYHSR 58
CD1_tandem_CHD1_yeast_like cd18665
repeat 1 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
459-498 2.97e-11

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


Pssm-ID: 349312  Cd Length: 65  Bit Score: 60.48  E-value: 2.97e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 145359958  459 WNEMEFLIKWKGQSHLHCQWKTLSDLQNLSGFKKVLNYTK 498
Cdd:cd18665    26 KENYEFLIKWTDESHLHNTWETYESLKQVRGLKKVDNYIK 65
CHROMO smart00298
Chromatin organization modifier domain;
534-589 7.59e-11

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 58.76  E-value: 7.59e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958    534 QVERIIADRISKDGlgdvVPEYLVKWQGLSYAEATWEKDVDIAFAQVAIDEYKARE 589
Cdd:smart00298    3 EVEKILDHRWKKKG----ELEYLVKWKGYSYSEDTWEPEENLLNCSKKLDNYKKKE 54
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
645-777 7.75e-11

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: 62.04  E-value: 7.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  645 NVILADEMGLGKTVqsVSMLGFLQNTQQIPGPFLVVVPLSTLAN-WAKEFRKWL-PGMNIIVYVGTRASREvcqqyefyN 722
Cdd:cd00046     3 NVLITAPTGSGKTL--AALLAALLLLLKKGKKVLVLVPTKALALqTAERLRELFgPGIRVAVLVGGSSAEE--------R 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145359958  723 EKKVGRPIKFnaLLTTYEVVLKDK--AVLSKIK-WIYLMVDEAHRLKNSEAQLYTALL 777
Cdd:cd00046    73 EKNKLGDADI--IIATPDMLLNLLlrEDRLFLKdLKLIIVDEAHALLIDSRGALILDL 128
ResIII pfam04851
Type III restriction enzyme, res subunit;
624-791 1.48e-09

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 58.45  E-value: 1.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   624 TLRDYQLEGLNFLVNSWLN-DTNVILADEMGLGKTVQSVSMLGFLQNTQQIPgPFLVVVP-LSTLANWAKEFRKWLPGM- 700
Cdd:pfam04851    3 ELRPYQIEAIENLLESIKNgQKRGLIVMATGSGKTLTAAKLIARLFKKGPIK-KVLFLVPrKDLLEQALEEFKKFLPNYv 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   701 -NIIVYVGtrasrevcqqyEFYNEKKVGRPIKFNALLTTYEVVLKDKAVLSKIKWIYLMVDEAHRlknSEAQLYTALLEF 779
Cdd:pfam04851   82 eIGEIISG-----------DKKDESVDDNKIVVTTIQSLYKALELASLELLPDFFDVIIIDEAHR---SGASSYRNILEY 147
                          170
                   ....*....|...
gi 145359958   780 STKNKLL-ITGTP 791
Cdd:pfam04851  148 FKPAFLLgLTATP 160
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
867-1087 2.13e-09

Class II histone deacetylase complex subunits 2 and 3; This family of class II histone deacetylase complex subunits HDA2 and HDA3 is found in fungi, The member from S. pombe is referred to as Ccq1 in Swiss:Q10432. These proteins associate with HDA1 to generate the activity of the HDA1 histone deacetylase complex. HDA1 interacts with itself and with the HDA2-HDA3 subcomplex to form a probable tetramer and these interactions are necessary for catalytic activity. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDA2 and HDA3 have a conserved coiled-coil domain towards their C-terminus.


Pssm-ID: 402894  Cd Length: 281  Bit Score: 60.42  E-value: 2.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   867 MSPLQKQYYKWILERNFHDLNKGVRGNQVSLLNIVVELKKCC--------NHPFLFesADHgYggdINDNSKL----DKI 934
Cdd:pfam11496   12 MTSYQKELTEQIVSLHYSDILKYCETSDSKEDISLIKSMTLClenlslvaTHPYLL--VDH-Y---MPKSLLLkdepEKL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   935 ILSSGKLVILDKLLVRLRETKHR----VLIFSQMVRMLDILAEYLSLRGFQFQRLDG-STKAELRQQAMDHFNAPASDDF 1009
Cdd:pfam11496   86 AYTSGKFLVLNDLVNLLIERDRKepinVAIVARSGKTLDLVEALLLGKGLSYKRYSGeMLYGENKKVSDSGNKKIHSTTC 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  1010 CFLLSTR-----AGGLGINlaTADTVVIFDSDWNPQNDLQAMSRAHRIGQQEVVNIYRFVTSKSVEEEILERAKRKMVLD 1084
Cdd:pfam11496  166 HLLSSTGqltndDSLLENY--KFDLIIAFDSSVDTSSPSVEHLRTQNRRKGNLAPIIRLVVINSIEHVELCFPKPPDSPD 243

                   ...
gi 145359958  1085 HLV 1087
Cdd:pfam11496  244 YLY 246
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
625-791 5.97e-09

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: 56.55  E-value: 5.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  625 LRDYQLEGLNFLVNSWLNDTNVIladEM--GLGKTVQSVSMLGFLQNtqqipGPFLVVVPLSTLAN-WAKEFRKWLPgmn 701
Cdd:cd17926     1 LRPYQEEALEAWLAHKNNRRGIL---VLptGSGKTLTALALIAYLKE-----LRTLIVVPTDALLDqWKERFEDFLG--- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  702 iivyvgtraSREVCQQYEFYNEKKVGRPIKFnallTTYEVVLKDKAVLSKIK--WIYLMVDEAHRL--KNSEAqlytALL 777
Cdd:cd17926    70 ---------DSSIGLIGGGKKKDFDDANVVV----ATYQSLSNLAEEEKDLFdqFGLLIVDEAHHLpaKTFSE----ILK 132
                         170
                  ....*....|....
gi 145359958  778 EFSTKNKLLITGTP 791
Cdd:cd17926   133 ELNAKYRLGLTATP 146
CD_CSD cd00024
CHROMO (CHRromatin Organization Modifier) domains and chromo shadow domains; Members of this ...
535-587 2.20e-08

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


Pssm-ID: 349274 [Multi-domain]  Cd Length: 50  Bit Score: 51.71  E-value: 2.20e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145359958  535 VERIIADRISKDGLgdvvpEYLVKWQGLSYAEATWEKDVDIAFAQVAIDEYKA 587
Cdd:cd00024     3 VEKILDHRVRKGKL-----EYLVKWKGYPPEENTWEPEENLTNAPELIKEYEK 50
CD2_tandem_CHD5-9_like cd18663
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
534-589 1.59e-07

repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as mammalian helicase DNA-binding proteins CHD5, CHD6, CHD7, CHD8, and CHD9. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. CHD6, CHD7, and CHD8 enzymes have been demonstrated to have different substrate specificities and remodeling activities. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349310 [Multi-domain]  Cd Length: 59  Bit Score: 49.59  E-value: 1.59e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145359958  534 QVERIIADRISKDGL-GDVVPEYLVKWQGLSYAEATWE--KDVDiafaQVAIDEYKARE 589
Cdd:cd18663     5 EVDRILDVSVSTDPNtGEPVTHYLVKWCSLPYEDSTWEleEDVD----PAKIEEFEKLR 59
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
106-420 1.83e-07

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 56.46  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  106 QPMGQREGSDPAKDSQSGYKEAYHSEDNHSNDRSEKLDSENENDNENEEEDNEMNKHQSGQADVPAD-EMLSDEYYEQDE 184
Cdd:NF033609  555 EPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDsDSASDSDSASDS 634
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  185 DNQSDHVHYKGYSNPTNSRSLPKAGSAVHSNSRTSraihknihySDSNHDHNGDADMDYEEEEDEDDPEDADFEPYDAAD 264
Cdd:NF033609  635 DSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD---------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 705
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  265 DGGASKKHGQGWDVSDEDPESDEEIDLSDYEDDYGTKKPKVRQQSKGFRKSSAGLERKSFHVSSRQKRKTSYQDDDSEED 344
Cdd:NF033609  706 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 785
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145359958  345 SENDNDEGFRSLARRGTTLRQNNGRSTNTIGQSSEVRSSTRSVRKVSYVESEDSEDIDDGKNRKNQKDDIEEEDAD 420
Cdd:NF033609  786 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSN 861
CD2_tandem_ScCHD1_like cd18664
repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein ...
535-588 4.32e-07

repeat 2 of the paired tandem chromodomains of yeast chromodomain helicase DNA-binding protein 1, and similar proteins; Repeat 2 of tandem CHRomatin Organization Modifier (chromo) domains, found in CHD (chromodomain helicase DNA-binding) proteins such as yeast protein CHD1. The CHD proteins belong to the SNF2 superfamily of ATP-dependent chromatin remodelers and contain two signature motifs: a pair of chromodomains located in the N-terminal region, and the SNF2-like ATPase domain located in the central region of the protein. CHD chromatin remodelers are important regulators of transcription and play critical roles during developmental processes. The N-terminal chromodomains of CHD1 have been shown to guard against sliding hexasomes. Mutations in the chromodomains of mouse CHD1 result in nuclear redistribution, suggesting that the chromodomain is essential for proper association with chromatin; also, deletion of the chromodomains in the Drosophila melanogaster CHD3-4 homolog impaired nucleosome binding, mobilization, and ATPase functions. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349311  Cd Length: 59  Bit Score: 48.42  E-value: 4.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145359958  535 VERIIADRISKDGLGDVVPEYLVKWQGLSYAEATWEKDVDIA-FAQVAIDEYKAR 588
Cdd:cd18664     5 VERIIASQRASLEDGTSQLQYLVKWRRLNYDECTWEDATLIAkLAPEQVDHFQNR 59
CD2_tandem_CHD3-4_like cd18662
repeat 2 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
534-586 1.18e-06

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


Pssm-ID: 349309 [Multi-domain]  Cd Length: 55  Bit Score: 46.87  E-value: 1.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145359958  534 QVERIIADRISKDGlgdvVPEYLVKWQGLSYAEATWEK-DVDIAFAQVAIDEYK 586
Cdd:cd18662     5 QIHRIINHRVDKDG----NTWYLVKWRDLPYDQSTWESeDDDIPDYEKHIQEYW 54
CD1_tandem_CHD5-9_like cd18668
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 5-9, ...
416-484 2.55e-06

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


Pssm-ID: 349315 [Multi-domain]  Cd Length: 68  Bit Score: 46.56  E-value: 2.55e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145359958  416 EEDADVIEKVLwhqlkGMGEDVQTNNKSTVPVLVSqlfdtepdwnemEFLIKWKGQSHLHCQWKTLSDL 484
Cdd:cd18668     1 EEDTMIIEKIL-----ASRKKKKEKEEGAEEIEVE------------EYLVKYKNFSYLHCEWKTEEEL 52
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
956-1064 1.60e-05

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


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 44.62  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  956 HRVLIFSQMVRMLDILAEYLSlrgfqfqrldgstkaelrqqamdhfnapasddfcFLLSTRAGGLGINLATADTVVIFDS 1035
Cdd:cd18785     4 VKIIVFTNSIEHAEEIASSLE----------------------------------ILVATNVLGEGIDVPSLDTVIFFDP 49
                          90       100
                  ....*....|....*....|....*....
gi 145359958 1036 DWNPQNDLQAMSRAHRIGQQEVVnIYRFV 1064
Cdd:cd18785    50 PSSAASYIQRVGRAGRGGKDEGE-VILFV 77
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
39-406 1.89e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 49.52  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   39 DGTYSERGFDMNMdVQYQSDpEPGcSIRQPNEtavDNVADP-VDSHYQSSTKRLGVTGRWGSTfwkdcqpmgQREGSDPA 117
Cdd:NF033609  531 NGSGSGDGIDKPV-VPEQPD-EPG-EIEPIPE---DSDSDPgSDSGSDSSNSDSGSDSGSDST---------SDSGSDSA 595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  118 KDSQSGYKEAYHSEDNHSNDRSEKLDSENENDNENEEEDNEMNKHQSGQADVPADEMLSDEYYEQDEDNQSDHVHYKGYS 197
Cdd:NF033609  596 SDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 675
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  198 NPTNSRSLPKAGSAVHSNSRTSraihknihySDSNHDHNGDADMDYEEEEDEDDPEDADFEPYDAADDGGASKKHGQGWD 277
Cdd:NF033609  676 SDSDSDSDSDSDSDSDSDSDSD---------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 746
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  278 VSDEDPESDEEIDlSDYEDDYGTKkpkvrQQSKGFRKSSAGLERKSFHVSSRQKRKTSYQDDDSEEDSENDNDEGFRSLA 357
Cdd:NF033609  747 DSDSDSDSDSDSD-SDSDSDSDSD-----SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 820
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 145359958  358 RRGTTLRQNNGRSTNTIGQSSEVRSSTRSVRKVSYVESEDSEDIDDGKN 406
Cdd:NF033609  821 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSN 869
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
114-400 8.91e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 47.60  E-value: 8.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  114 SDPAKDSQSGYKEAYHSEDNHSNDRSEKLDSENENDNENEEEDNEMNKHQS-GQADVPAD-EMLSDEYYEQDEDNQSDHV 191
Cdd:NF033609  616 SDSASDSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDsDSDSDSDSDSDSDSDSDSD 695
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  192 HYKGYSNPTNSRSLPKAGSAVHSNSRTSRAIHKNihySDSNHDHNGDADMDYEEEEDEDDPEDADFEPYDAADDGGASKK 271
Cdd:NF033609  696 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 772
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958  272 HGQGWDVSDEDPESDEEIDlSDYEDDYGTKKPKvRQQSKGFRKSSAGLERKSFHVSSRQKRKTSYQDDDSEEDSENDNDE 351
Cdd:NF033609  773 DSDSDSDSDSDSDSDSDSD-SDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 850
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 145359958  352 GFRSLARRGTTLRQNNGRSTNTIGQSSEVRSSTRSVRKvsyvESEDSED 400
Cdd:NF033609  851 DSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKN----EAKDSKE 895
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
637-799 1.27e-04

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


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 44.16  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   637 VNSWLNDTNVILADEMGLGKTVqsVSMLGFLQ--NTQQIPGPFLVVVPLSTLAN-WAKEFRKWLPGMNIIVYVG-TRASR 712
Cdd:pfam00270    8 IPAILEGRDVLVQAPTGSGKTL--AFLLPALEalDKLDNGPQALVLAPTRELAEqIYEELKKLGKGLGLKVASLlGGDSR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359958   713 EvcQQYEFYNEKKVgrpikfnaLLTTYEVV---LKDKAVLSKIKwiYLMVDEAHRL--KNSEAQLYTALLEFSTKNK-LL 786
Cdd:pfam00270   86 K--EQLEKLKGPDI--------LVGTPGRLldlLQERKLLKNLK--LLVLDEAHRLldMGFGPDLEEILRRLPKKRQiLL 153
                          170
                   ....*....|...
gi 145359958   787 ITGTPLQNsVEEL 799
Cdd:pfam00270  154 LSATLPRN-LEDL 165
CD1_tandem_CHD3-4_like cd18667
repeat 1 of the paired tandem chromodomains of chromodomain helicase DNA-binding protein 3 and ...
461-485 2.30e-04

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


Pssm-ID: 349314 [Multi-domain]  Cd Length: 79  Bit Score: 41.17  E-value: 2.30e-04
                          10        20
                  ....*....|....*....|....*
gi 145359958  461 EMEFLIKWKGQSHLHCQWktLSDLQ 485
Cdd:cd18667    43 EREFFVKWHGMSYWHCEW--VSELQ 65
CD1_tandem cd18660
repeat 1 of paired tandem chromodomains; Repeat 1 of tandem CHRomatin Organization Modifier ...
535-570 8.71e-04

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


Pssm-ID: 349307 [Multi-domain]  Cd Length: 70  Bit Score: 39.27  E-value: 8.71e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 145359958  535 VERIIADRISKDGLGDVVP-----------EYLVKWQGLSYAEATWE 570
Cdd:cd18660     5 IEKILDHRPKGPVEEASLDltdpdepwderEFLVKWKGKSYLHCTWV 51
CD_Chp1_like cd18636
chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin ...
534-586 9.01e-04

chromodomain of chromodomain-containing protein 1, and similar proteins; CHRomatin Organization Modifier (chromo) domain of chromodomain-containing protein 1 (CHp1), and similar proteins. Chp1 is needed for RNA interference-dependent heterochromatin formation in fission yeast. Chp1 is a member of the RNA-induced transcriptional silencing (RITS) complex which maintains the heterochromatin regions. The chromodomain of the Chp1 component binds the histone H3 lysine 9 methylated tail (H3K9me) and the core of the nucleosome. A chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and which appears to play a role in the functional organization of the eukaryotic nucleus. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349286  Cd Length: 52  Bit Score: 38.97  E-value: 9.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145359958  534 QVERIIADRISKDGLGdvvpEYLVKWQGLSYAEATWEKDVDIAFAQVAIDEYK 586
Cdd:cd18636     3 EVEDILADRVNKNGIN----EYYIKWAGYDWYDNTWEPEQNLFGAEKVLKKWK 51
chromodomain cd18968
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
534-570 1.33e-03

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349324  Cd Length: 57  Bit Score: 38.48  E-value: 1.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 145359958  534 QVERIIADRISKDGLG-DVVPEYLVKWQGLSYAEATWE 570
Cdd:cd18968     3 EVEVILAARVVKDAESrKKGWKYLVKWAGYPDEENTWE 40
chromodomain cd18965
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
553-575 1.52e-03

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349321  Cd Length: 53  Bit Score: 38.23  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|...
gi 145359958  553 PEYLVKWQGLSYAEATWEKDVDI 575
Cdd:cd18965    16 LEYLVKWHGLPESENTWEREKDI 38
CD_polycomb cd18644
chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG ...
535-589 1.68e-03

chromodomain of polycomb; CHRomatin Organization Modifier (chromo) domain of the PcG (polycomb-group) chromodomain protein Polycomb (Pc) from Drosophila melanogaster, anthropod, worm, and sea cucumber, and similar proteins. Pc is a component of the Polycomb-group (PcG) multiprotein PRC1 complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. The core subunits of PRC1 are polycomb (Pc), polyhomeotic (Ph), posterior sex combs (Psc), and sex comb extra (Sce, also known as dRing). Polycomb (Pc) plays a role in modulating life span in flies, it negatively regulates longevity.


Pssm-ID: 349291  Cd Length: 54  Bit Score: 38.21  E-value: 1.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145359958  535 VERIIADRISKDglgdvVPEYLVKWQGLSYAEATWEKDVDIAFAQVaIDEYKARE 589
Cdd:cd18644     6 AEKILKKRVRKG-----KVEYLVKWKGWSNKHNTWEPEENILDRRL-IEIFERTN 54
CHROMO smart00298
Chromatin organization modifier domain;
460-499 2.03e-03

Chromatin organization modifier domain;


Pssm-ID: 214605 [Multi-domain]  Cd Length: 55  Bit Score: 37.96  E-value: 2.03e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 145359958    460 NEMEFLIKWKGQSHLHCQWKTLSDLQNlsGFKKVLNYTKK 499
Cdd:smart00298   16 GELEYLVKWKGYSYSEDTWEPEENLLN--CSKKLDNYKKK 53
chromodomain cd18966
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
534-570 2.11e-03

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349322  Cd Length: 49  Bit Score: 37.65  E-value: 2.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 145359958  534 QVERIIADRISKDGLgdvvpEYLVKWQGLSYAEATWE 570
Cdd:cd18966     2 EVERILAERRDDGGK-----RYLVKWEGYPLEEATWE 33
PRK04914 PRK04914
RNA polymerase-associated protein RapA;
754-822 2.62e-03

RNA polymerase-associated protein RapA;


Pssm-ID: 235319 [Multi-domain]  Cd Length: 956  Bit Score: 42.52  E-value: 2.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145359958  754 WIYLMVDEAHRLKNSEAQL---YTALLEFSTKNK--LLITGTPLQNSVEELWALLHFLDPGKFKNKDEFVE---NYK 822
Cdd:PRK04914  273 WDLLVVDEAHHLVWSEEAPsreYQVVEQLAEVIPgvLLLTATPEQLGQESHFARLRLLDPDRFHDYEAFVEeqqQYR 349
chromodomain cd18964
CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain ...
535-570 2.87e-03

CHROMO (CHRromatin Organization Modifier) domain; uncharacterized subgroup; The chromodomain is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins. The chromodomain is implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain. Chromodomains belong to the chromo-like superfamily of SH3-fold-beta-barrel domains which includes chromo shadow domains and chromo barrel domains. Chromodomains differ from these in that they lack the first strand of the SH3-fold-beta-barrel. This first strand is altered by insertion in the chromo shadow domains, and chromo barrel domains are typical SH3-fold-beta-barrel domains with sequence similarity to the canonical chromo domain.


Pssm-ID: 349320  Cd Length: 54  Bit Score: 37.31  E-value: 2.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 145359958  535 VERIIADR-ISKDGLGDVVpeYLVKWQGLSYAEATWE 570
Cdd:cd18964     3 VERIIGRRpSARDGPGKFL--WLVKWDGYPIEDATWE 37
CD_POL_like cd18979
chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins ...
536-570 5.42e-03

chromodomain of a Zea maize putative metaviridae (gypsy-type) retrotransposon polyproteins (Z195D10.9), and similar proteins; This subgroup includes the CHROMO (CHRromatin Organization Modifier) domain found in Zea maize Z195D10.9 protein, and other putative TY3/gypsy retrotransposon polyproteins. The pol gene in TY3/gypsy elements generally encodes domains in the following order: an aspartyl protease, a reverse transcriptase, RNase H, and an integrase, here the chromodomain is found at the C-terminus of the integrase domain. The chromodomain, is a conserved region of about 50 amino acids, found in a variety of chromosomal proteins, and implicated in the binding, of the proteins in which it is found, to methylated histone tails and maybe RNA. A chromodomain may occur as a single instance, in a tandem arrangement, or followed by a related chromo shadow domain.


Pssm-ID: 349335  Cd Length: 48  Bit Score: 36.70  E-value: 5.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 145359958  536 ERIIADRISKDGlgdvVPEYLVKWQGLSYAEATWE 570
Cdd:cd18979     4 EKVLDIRQRDKG----NKEFLVQWQGLSVEEATWE 34
 
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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