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Conserved domains on  [gi|442632632|ref|NP_001261906|]
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brahma, isoform E [Drosophila melanogaster]

Protein Classification

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
739-1368 1.59e-165

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: 529.76  E-value: 1.59e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  739 EDDEYRTEEQTYYSIAHTIheKVVEQASImVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDR 818
Cdd:PLN03142  139 EDEEYLKEEEDGLGGSGGT--RLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEY 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  819 KKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVSYKGSPQGRRLLQ-NQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYM 897
Cdd:PLN03142  216 RGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQReELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYI 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  898 IIDEGHRMKNHHCKLTQVLNThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfATTGEkvelNE 977
Cdd:PLN03142  296 IIDEAHRIKNENSLLSKTMRL-FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----ND 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  978 EETIliIRRLHKVLRPFLLRRLKKEVEHQLPDKVEYIIKCDMSALQRVLYKHMQSKGV-LLTDGSEKGKhgkggakaLMN 1056
Cdd:PLN03142  367 QQEV--VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLN 436
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1057 TIVQLRKLCNHPFMFQHIEEkycdhtgGHGVVSGPDLYRVSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGW 1136
Cdd:PLN03142  437 IAMQLRKCCNHPYLFQGAEP-------GPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMY 509
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1137 RQFGYLRLDGTTKAEDRGELLRKFNAKGSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNE 1216
Cdd:PLN03142  510 RGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKE 589
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1217 VRVLRLMTVNSVEERILAAARYKLNMDEKVIQAG-MFDQKSTGSErqQFLQTILHQDDNEEEEENEVPDDEMINMMIARS 1295
Cdd:PLN03142  590 VQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGrLAEQKTVNKD--ELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKG 667
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632632 1296 EEEIeifKRMDAERKKEDEEIHpgRERLIDESELPDWLTKDDDEVERFhyqyDEDTILGRG-----SRQRKEvDYTDS 1368
Cdd:PLN03142  668 EEAT---AELDAKMKKFTEDAI--KFKMDDTAELYDFDDEDDKDENKL----DFKKIVSDNwidppKRERKR-NYSES 735
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1425-1530 2.46e-55

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


:

Pssm-ID: 99947  Cd Length: 107  Bit Score: 187.63  E-value: 2.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1425 RSKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQ 1503
Cdd:cd05516     1 ELTKKMNKIVDVVIKYKDsDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                          90       100
                  ....*....|....*....|....*..
gi 442632632 1504 IYNEEASLIYLDSIALQKVFVGARQRI 1530
Cdd:cd05516    81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
HSA smart00573
domain in helicases and associated with SANT domains;
501-573 1.73e-23

domain in helicases and associated with SANT domains;


:

Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 95.54  E-value: 1.73e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632632    501 QKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERMRRLMA 573
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
650-691 1.23e-16

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


:

Pssm-ID: 462196  Cd Length: 44  Bit Score: 74.85  E-value: 1.23e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 442632632   650 ADMRVHVVEQCTGKKLTGDDAPMLKHLHRWLNMHPGWDWIDD 691
Cdd:pfam07533    3 GDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
PTZ00121 super family cl31754
MAEBL; Provisional
477-651 6.87e-06

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 6.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  477 IKLYKRTKRQGLREARATE----KLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANA 552
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  553 EREQKKEQEriEKERMRRLMAEDEEGyRKLIDQKK----DKRLAFLLSQTDEYISNLTQMVK------QHKDDQMKKKEE 622
Cdd:PTZ00121 1678 EEAKKAEED--EKKAAEALKKEAEEA-KKAEELKKkeaeEKKKAEELKKAEEENKIKAEEAKkeaeedKKKAEEAKKDEE 1754
                         170       180
                  ....*....|....*....|....*....
gi 442632632  623 EGKRLIQFKKELLMSGEYIGIDEGSIVAD 651
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
173-202 4.39e-05

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


:

Pssm-ID: 462622  Cd Length: 35  Bit Score: 41.94  E-value: 4.39e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 442632632   173 HLNGNQVNLLRTQITAYRLLARNKPISMQM 202
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPEL 30
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
247-401 7.17e-04

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


:

Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 42.33  E-value: 7.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   247 QPPPSAGTPPQCSTPPASNPYGPPVPGQKMQVAPPPPHMQQgqplppqppqvggpppiqqqqppqqqqqqsqppppephq 326
Cdd:pfam15240   55 PPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPR--------------------------------------- 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442632632   327 hqlPNGGKPLSMGPSGG-QPLIPSSPMQPQVrgtlPGMPPGSQVPQPGGGPQRQVPPAGMPMPKPNRITTVAKPVG 401
Cdd:pfam15240   96 ---PPPGKPQGPPPQGGnQQQGPPPPGKPQG----PPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRPPQPGNPQG 164
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
739-1368 1.59e-165

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 529.76  E-value: 1.59e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  739 EDDEYRTEEQTYYSIAHTIheKVVEQASImVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDR 818
Cdd:PLN03142  139 EDEEYLKEEEDGLGGSGGT--RLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEY 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  819 KKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVSYKGSPQGRRLLQ-NQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYM 897
Cdd:PLN03142  216 RGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQReELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYI 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  898 IIDEGHRMKNHHCKLTQVLNThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfATTGEkvelNE 977
Cdd:PLN03142  296 IIDEAHRIKNENSLLSKTMRL-FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----ND 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  978 EETIliIRRLHKVLRPFLLRRLKKEVEHQLPDKVEYIIKCDMSALQRVLYKHMQSKGV-LLTDGSEKGKhgkggakaLMN 1056
Cdd:PLN03142  367 QQEV--VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLN 436
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1057 TIVQLRKLCNHPFMFQHIEEkycdhtgGHGVVSGPDLYRVSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGW 1136
Cdd:PLN03142  437 IAMQLRKCCNHPYLFQGAEP-------GPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMY 509
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1137 RQFGYLRLDGTTKAEDRGELLRKFNAKGSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNE 1216
Cdd:PLN03142  510 RGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKE 589
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1217 VRVLRLMTVNSVEERILAAARYKLNMDEKVIQAG-MFDQKSTGSErqQFLQTILHQDDNEEEEENEVPDDEMINMMIARS 1295
Cdd:PLN03142  590 VQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGrLAEQKTVNKD--ELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKG 667
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632632 1296 EEEIeifKRMDAERKKEDEEIHpgRERLIDESELPDWLTKDDDEVERFhyqyDEDTILGRG-----SRQRKEvDYTDS 1368
Cdd:PLN03142  668 EEAT---AELDAKMKKFTEDAI--KFKMDDTAELYDFDDEDDKDENKL----DFKKIVSDNwidppKRERKR-NYSES 735
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
770-1000 2.63e-165

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: 499.20  E-value: 2.63e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  770 NGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVG 849
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  850 VVSYKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYIAPYRLLLT 929
Cdd:cd17996    81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632632  930 GTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKV--ELNEEETILIIRRLHKVLRPFLLRRLK 1000
Cdd:cd17996   161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
661-1248 5.67e-125

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 407.69  E-value: 5.67e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  661 TGKKLTGDDAPMLKHLHRWLNMHPGWDWIDDEEDSCGSNDDHKPKVEEQPTATEDATDKAQATGNDEDAKDLITKAKVED 740
Cdd:COG0553   132 LLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLEL 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  741 DEYRTEEQTYYSIAHtiHEKVVEQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKK 820
Cdd:COG0553   212 ELLAEAAVDAFRLRR--LREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  821 VmGPYLIIVPLSTLPNWVLEFEKWAPAVGVVSYKGSPQgRRLLQNQMRatKFNVLLTTYEYVIKDKAVLAKIQWKYMIID 900
Cdd:COG0553   290 A-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE-RAKGANPFE--DADLVITSYGLLRRDIELLAAVDWDLVILD 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  901 EGHRMKNHHCKLTQV---LNthyiAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPfattgekVELNE 977
Cdd:COG0553   366 EAQHIKNPATKRAKAvraLK----ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP-------IEKGD 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  978 EETiliIRRLHKVLRPFLLRRLKKEVEHQLPDKVEYIIKCDMSALQRVLYKHMqskgVLLTDGSEKGKHGKGGAKALMNT 1057
Cdd:COG0553   435 EEA---LERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV----LEYLRRELEGAEGIRRRGLILAA 507
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1058 IVQLRKLCNHPFMFQHIEEKYCDHtgghgvvsgpdlyrvSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGWR 1137
Cdd:COG0553   508 LTRLRQICSHPALLLEEGAELSGR---------------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEER 572
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1138 QFGYLRLDGTTKAEDRGELLRKFNAkGSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNEV 1217
Cdd:COG0553   573 GIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDV 651
                         570       580       590
                  ....*....|....*....|....*....|.
gi 442632632 1218 RVLRLMTVNSVEERILAAARYKLNMDEKVIQ 1248
Cdd:COG0553   652 QVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
776-1071 1.66e-117

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: 372.02  E-value: 1.66e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   776 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTISLVTYLMDRKKVMG-PYLIIVPLSTLPNWVLEFEKWA--PAVGVV 851
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   852 SYKGSPQGR-RLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHYIAPYRLLLTG 930
Cdd:pfam00176   81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   931 TPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKvelneeetiLIIRRLHKVLRPFLLRRLKKEVEHQLPDK 1010
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632632  1011 VEYIIKCDMSALQRVLYKH-MQSKGVLLTDGSEkgkHGKGGAKALMNTIVQLRKLCNHPFMF 1071
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1425-1530 2.46e-55

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


Pssm-ID: 99947  Cd Length: 107  Bit Score: 187.63  E-value: 2.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1425 RSKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQ 1503
Cdd:cd05516     1 ELTKKMNKIVDVVIKYKDsDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                          90       100
                  ....*....|....*....|....*..
gi 442632632 1504 IYNEEASLIYLDSIALQKVFVGARQRI 1530
Cdd:cd05516    81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
BROMO smart00297
bromo domain;
1423-1523 4.04e-30

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 115.45  E-value: 4.04e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   1423 DKRSKKQMHKIMSAVIKHNQDGRtLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNA 1502
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHP-LSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNA 79
                            90       100
                    ....*....|....*....|.
gi 442632632   1503 QIYNEEASLIYLDSIALQKVF 1523
Cdd:smart00297   80 RTYNGPDSEVYKDAKKLEKFF 100
DEXDc smart00487
DEAD-like helicases superfamily;
772-961 7.29e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 115.28  E-value: 7.29e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632    772 TLKEYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TISLVTYLMDRKKvmGPYLIIVPLSTL-PNWVLEFEKWAPAVG 849
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGKG--GRVLVLVPTRELaEQWAEELKKLGPSLG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632    850 VVS---YKGSPQGRRLlqNQMRATKFNVLLTTYEYVIKD--KAVLAKIQWKYMIIDEGHRMKN--HHCKLTQVLNTHYIA 922
Cdd:smart00487   83 LKVvglYGGDSKREQL--RKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKN 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 442632632    923 PYRLLLTGTPLQNKLPELWALLN--FLLPSIFKSCSTFEQW 961
Cdd:smart00487  161 VQLLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
HSA smart00573
domain in helicases and associated with SANT domains;
501-573 1.73e-23

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 95.54  E-value: 1.73e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632632    501 QKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERMRRLMA 573
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
502-568 1.17e-18

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


Pssm-ID: 462194 [Multi-domain]  Cd Length: 67  Bit Score: 81.46  E-value: 1.17e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632632   502 KLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERM 568
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1405-1524 1.33e-17

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 86.78  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1405 EESDDDslILKRRRRQNLDKRSKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDC 1483
Cdd:COG5076   124 AHLKTS--VKKRKTPKIEDELLYADNKAIAKFKKQLFLrDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNG 201
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 442632632 1484 KYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVFV 1524
Cdd:COG5076   202 RYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFL 242
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
650-691 1.23e-16

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


Pssm-ID: 462196  Cd Length: 44  Bit Score: 74.85  E-value: 1.23e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 442632632   650 ADMRVHVVEQCTGKKLTGDDAPMLKHLHRWLNMHPGWDWIDD 691
Cdd:pfam07533    3 GDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1432-1516 1.34e-16

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


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 76.20  E-value: 1.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  1432 KIMSAVIKHNqdgrtLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASL 1511
Cdd:pfam00439    3 EILDKLMEHP-----IAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSV 77

                   ....*
gi 442632632  1512 IYLDS 1516
Cdd:pfam00439   78 IYKAA 82
BRK smart00592
domain in transcription and CHROMO domain helicases;
649-693 2.78e-16

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 73.92  E-value: 2.78e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 442632632    649 VADMRVHVVEQCTGKKLTGDDAPMLKHLHRWLNMHPGWDWIDDEE 693
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
PTZ00121 PTZ00121
MAEBL; Provisional
477-651 6.87e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 6.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  477 IKLYKRTKRQGLREARATE----KLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANA 552
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  553 EREQKKEQEriEKERMRRLMAEDEEGyRKLIDQKK----DKRLAFLLSQTDEYISNLTQMVK------QHKDDQMKKKEE 622
Cdd:PTZ00121 1678 EEAKKAEED--EKKAAEALKKEAEEA-KKAEELKKkeaeEKKKAEELKKAEEENKIKAEEAKkeaeedKKKAEEAKKDEE 1754
                         170       180
                  ....*....|....*....|....*....
gi 442632632  623 EGKRLIQFKKELLMSGEYIGIDEGSIVAD 651
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
405-643 7.94e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  405 ITLLQERENRIAARISLRMQELQRLpATMSEDLRLQAAIELRALRVLNFQRQLrmefvqctrRDTTLETALNIKLYKRTK 484
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEE---------LEEELEELEEELEEAEEE 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  485 RQGLREARATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFhRNNKAQLARMNKAVMNHHANAEREQKKEQERIE 564
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALA 431
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442632632  565 KERMRRLMAEDEEGYRKLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKELLMSGEYIGI 643
Cdd:COG1196   432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
407-645 3.48e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.81  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   407 LLQERENRIAARISLRMQELQRLPatmsEDLRLQAAIELRALRVLNFQRQLRMEFVQ----CTRRDTTLETALNIKLYKR 482
Cdd:pfam02463  178 LIEETENLAELIIDLEELKLQELK----LKEQAKKALEYYQLKEKLELEEEYLLYLDylklNEERIDLLQELLRDEQEEI 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   483 TKRQGLREARAtEKLEKQQKLEAERKRRQKHLEFLAAVLQhgkDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQER 562
Cdd:pfam02463  254 ESSKQEIEKEE-EKLAQVLKENKEEEKEKKLQEEELKLLA---KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   563 IEKERmrrlmaEDEEGYRKLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKELLMSGEYIG 642
Cdd:pfam02463  330 LKKEK------EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403

                   ...
gi 442632632   643 IDE 645
Cdd:pfam02463  404 EKE 406
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
173-202 4.39e-05

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


Pssm-ID: 462622  Cd Length: 35  Bit Score: 41.94  E-value: 4.39e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 442632632   173 HLNGNQVNLLRTQITAYRLLARNKPISMQM 202
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPEL 30
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
172-202 6.20e-05

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


Pssm-ID: 214931  Cd Length: 36  Bit Score: 41.36  E-value: 6.20e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 442632632    172 QHLNGNQVNLLRTQITAYR-LLARNKPISMQM 202
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKyLLARNQPVPPEL 32
PRK11637 PRK11637
AmiB activator; Provisional
451-569 2.53e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 45.45  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  451 LNFQRQLRMEFVQCTRRDTTLETALniKLYKRTKRQGLrearATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGK-DLRE 529
Cdd:PRK11637  164 LNQARQETIAELKQTREELAAQKAE--LEEKQSQQKTL----LYEQQAQQQKLEQARNERKKTLTGLESSLQKDQqQLSE 237
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 442632632  530 FhRNNKAQLarmnkavMNHHANAEREQKK--EQERIEKERMR 569
Cdd:PRK11637  238 L-RANESRL-------RDSIARAEREAKAraEREAREAARVR 271
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
247-401 7.17e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 42.33  E-value: 7.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   247 QPPPSAGTPPQCSTPPASNPYGPPVPGQKMQVAPPPPHMQQgqplppqppqvggpppiqqqqppqqqqqqsqppppephq 326
Cdd:pfam15240   55 PPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPR--------------------------------------- 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442632632   327 hqlPNGGKPLSMGPSGG-QPLIPSSPMQPQVrgtlPGMPPGSQVPQPGGGPQRQVPPAGMPMPKPNRITTVAKPVG 401
Cdd:pfam15240   96 ---PPPGKPQGPPPQGGnQQQGPPPPGKPQG----PPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRPPQPGNPQG 164
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
367-611 1.59e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.53  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   367 SQVPQPGGGP---QRQVPPAGMPMPKPNRITTVAKPVGLDPITLLQERENRIAARISLRMQELQRLPATMSEDLRLQAAI 443
Cdd:TIGR02794   26 SVKPEPGGGAeiiQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   444 --ELRALRVLNFQRQLrmefvqctrrdttLETALNIKLYKRTKRQGLREARATEKLEKQQKLEAERKR----RQKHLEFL 517
Cdd:TIGR02794  106 qaEQAAKQAEEKQKQA-------------EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAaaeaKKKAEEAK 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   518 AAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERMRRLMAEDEEGYRKL--------IDQKKDK 589
Cdd:TIGR02794  173 KKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIfglasgsnAEKQGGA 252
                          250       260
                   ....*....|....*....|..
gi 442632632   590 RLAFLLSQTDEYISNLTQMVKQ 611
Cdd:TIGR02794  253 RGAAAGSEVDKYAAIIQQAIQQ 274
PHA03378 PHA03378
EBNA-3B; Provisional
255-388 2.95e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.36  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  255 PPQCSTPPASNPYGPPVPGQKMQVAPPPphmqqgqplpPQPPQVGGPPPIQQQQPPQQQQQQSQPPPPEPhqhqlPNGGK 334
Cdd:PHA03378  696 PPPRAPTPMRPPAAPPGRAQRPAAATGR----------ARPPAAAPGRARPPAAAPGRARPPAAAPGRAR-----PPAAA 760
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442632632  335 PLSMGPSGGQPLIPsSPMQPqvrgtlPGMPPGSQvPQPGGGPQRQVPPAGMPMP 388
Cdd:PHA03378  761 PGRARPPAAAPGAP-TPQPP------PQAPPAPQ-QRPRGAPTPQPPPQAGPTS 806
 
Name Accession Description Interval E-value
PLN03142 PLN03142
Probable chromatin-remodeling complex ATPase chain; Provisional
739-1368 1.59e-165

Probable chromatin-remodeling complex ATPase chain; Provisional


Pssm-ID: 215601 [Multi-domain]  Cd Length: 1033  Bit Score: 529.76  E-value: 1.59e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  739 EDDEYRTEEQTYYSIAHTIheKVVEQASImVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDR 818
Cdd:PLN03142  139 EDEEYLKEEEDGLGGSGGT--RLLVQPSC-IKGKMRDYQLAGLNWLIRLYENGINGILADEMGLGKTLQTISLLGYLHEY 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  819 KKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVSYKGSPQGRRLLQ-NQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYM 897
Cdd:PLN03142  216 RGITGPHMVVAPKSTLGNWMNEIRRFCPVLRAVKFHGNPEERAHQReELLVAGKFDVCVTSFEMAIKEKTALKRFSWRYI 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  898 IIDEGHRMKNHHCKLTQVLNThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfATTGEkvelNE 977
Cdd:PLN03142  296 IIDEAHRIKNENSLLSKTMRL-FSTNYRLLITGTPLQNNLHELWALLNFLLPEIFSSAETFDEWF----QISGE----ND 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  978 EETIliIRRLHKVLRPFLLRRLKKEVEHQLPDKVEYIIKCDMSALQRVLYKHMQSKGV-LLTDGSEKGKhgkggakaLMN 1056
Cdd:PLN03142  367 QQEV--VQQLHKVLRPFLLRRLKSDVEKGLPPKKETILKVGMSQMQKQYYKALLQKDLdVVNAGGERKR--------LLN 436
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1057 TIVQLRKLCNHPFMFQHIEEkycdhtgGHGVVSGPDLYRVSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGW 1136
Cdd:PLN03142  437 IAMQLRKCCNHPYLFQGAEP-------GPPYTTGEHLVENSGKMVLLDKLLPKLKERDSRVLIFSQMTRLLDILEDYLMY 509
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1137 RQFGYLRLDGTTKAEDRGELLRKFNAKGSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNE 1216
Cdd:PLN03142  510 RGYQYCRIDGNTGGEDRDASIDAFNKPGSEKFVFLLSTRAGGLGINLATADIVILYDSDWNPQVDLQAQDRAHRIGQKKE 589
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1217 VRVLRLMTVNSVEERILAAARYKLNMDEKVIQAG-MFDQKSTGSErqQFLQTILHQDDNEEEEENEVPDDEMINMMIARS 1295
Cdd:PLN03142  590 VQVFRFCTEYTIEEKVIERAYKKLALDALVIQQGrLAEQKTVNKD--ELLQMVRYGAEMVFSSKDSTITDEDIDRIIAKG 667
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632632 1296 EEEIeifKRMDAERKKEDEEIHpgRERLIDESELPDWLTKDDDEVERFhyqyDEDTILGRG-----SRQRKEvDYTDS 1368
Cdd:PLN03142  668 EEAT---AELDAKMKKFTEDAI--KFKMDDTAELYDFDDEDDKDENKL----DFKKIVSDNwidppKRERKR-NYSES 735
DEXHc_SMARCA2_SMARCA4 cd17996
DEXH-box helicase domain of SMARCA2 and SMARCA4; SWI/SNF related, matrix associated, actin ...
770-1000 2.63e-165

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: 499.20  E-value: 2.63e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  770 NGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVG 849
Cdd:cd17996     1 GGTLKEYQLKGLQWMVSLYNNNLNGILADEMGLGKTIQTISLITYLMEKKKNNGPYLVIVPLSTLSNWVSEFEKWAPSVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  850 VVSYKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYIAPYRLLLT 929
Cdd:cd17996    81 KIVYKGTPDVRKKLQSQIRAGKFNVLLTTYEYIIKDKPLLSKIKWKYMIIDEGHRMKNAQSKLTQTLNTYYHARYRLLLT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632632  930 GTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKV--ELNEEETILIIRRLHKVLRPFLLRRLK 1000
Cdd:cd17996   161 GTPLQNNLPELWALLNFLLPKIFKSCKTFEQWFNTPFANTGEQVkiELNEEETLLIIRRLHKVLRPFLLRRLK 233
DEXHc_SMARCA4 cd18062
DEXH-box helicase domain of SMARCA4; SWI/SNF related, matrix associated, actin dependent ...
750-1000 2.29e-142

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: 438.32  E-value: 2.29e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  750 YYSIAHTIHEKVVEQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIV 829
Cdd:cd18062     1 YYAVAHAVTEKVEKQSSLLVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  830 PLSTLPNWVLEFEKWAPAVGVVSYKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHH 909
Cdd:cd18062    81 PLSTLSNWVYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKQILAKIRWKYMIVDEGHRMKNHH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  910 CKLTQVLNTHYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKVELNEEETILIIRRLHK 989
Cdd:cd18062   161 CKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHK 240
                         250
                  ....*....|.
gi 442632632  990 VLRPFLLRRLK 1000
Cdd:cd18062   241 VLRPFLLRRLK 251
DEXHc_SMARCA2 cd18063
DEXH-box helicase domain of SMARCA2; SWI/SNF related, matrix associated, actin dependent ...
750-1000 2.58e-139

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: 430.25  E-value: 2.58e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  750 YYSIAHTIHEKVVEQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIV 829
Cdd:cd18063     1 YYTVAHAITERVEKQSSLLINGTLKHYQLQGLEWMVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRLNGPYLIIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  830 PLSTLPNWVLEFEKWAPAVGVVSYKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHH 909
Cdd:cd18063    81 PLSTLSNWTYEFDKWAPSVVKISYKGTPAMRRSLVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  910 CKLTQVLNTHYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKVELNEEETILIIRRLHK 989
Cdd:cd18063   161 CKLTQVLNTHYVAPRRILLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGERVDLNEEETILIIRRLHK 240
                         250
                  ....*....|.
gi 442632632  990 VLRPFLLRRLK 1000
Cdd:cd18063   241 VLRPFLLRRLK 251
HepA COG0553
Superfamily II DNA or RNA helicase, SNF2 family [Transcription, Replication, recombination, ...
661-1248 5.67e-125

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


Pssm-ID: 440319 [Multi-domain]  Cd Length: 682  Bit Score: 407.69  E-value: 5.67e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  661 TGKKLTGDDAPMLKHLHRWLNMHPGWDWIDDEEDSCGSNDDHKPKVEEQPTATEDATDKAQATGNDEDAKDLITKAKVED 740
Cdd:COG0553   132 LLLLALLLVLLAALLLLLLLLLLLALLLGRLLLLALLLLALEALLLLGLLLALALLALLELALLAAEAELLLLLELLLEL 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  741 DEYRTEEQTYYSIAHtiHEKVVEQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKK 820
Cdd:COG0553   212 ELLAEAAVDAFRLRR--LREALESLPAGLKATLRPYQLEGAAWLLFLRRLGLGGLLADDMGLGKTIQALALLLELKERGL 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  821 VmGPYLIIVPLSTLPNWVLEFEKWAPAVGVVSYKGSPQgRRLLQNQMRatKFNVLLTTYEYVIKDKAVLAKIQWKYMIID 900
Cdd:COG0553   290 A-RPVLIVAPTSLVGNWQRELAKFAPGLRVLVLDGTRE-RAKGANPFE--DADLVITSYGLLRRDIELLAAVDWDLVILD 365
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  901 EGHRMKNHHCKLTQV---LNthyiAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPfattgekVELNE 977
Cdd:COG0553   366 EAQHIKNPATKRAKAvraLK----ARHRLALTGTPVENRLEELWSLLDFLNPGLLGSLKAFRERFARP-------IEKGD 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  978 EETiliIRRLHKVLRPFLLRRLKKEVEHQLPDKVEYIIKCDMSALQRVLYKHMqskgVLLTDGSEKGKHGKGGAKALMNT 1057
Cdd:COG0553   435 EEA---LERLRRLLRPFLLRRTKEDVLKDLPEKTEETLYVELTPEQRALYEAV----LEYLRRELEGAEGIRRRGLILAA 507
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1058 IVQLRKLCNHPFMFQHIEEKYCDHtgghgvvsgpdlyrvSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGWR 1137
Cdd:COG0553   508 LTRLRQICSHPALLLEEGAELSGR---------------SAKLEALLELLEELLAEGEKVLVFSQFTDTLDLLEERLEER 572
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1138 QFGYLRLDGTTKAEDRGELLRKFNAkGSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNEV 1217
Cdd:COG0553   573 GIEYAYLHGGTSAEERDELVDRFQE-GPEAPVFLISLKAGGEGLNLTAADHVIHYDLWWNPAVEEQAIDRAHRIGQTRDV 651
                         570       580       590
                  ....*....|....*....|....*....|.
gi 442632632 1218 RVLRLMTVNSVEERILAAARYKLNMDEKVIQ 1248
Cdd:COG0553   652 QVYKLVAEGTIEEKILELLEEKRALAESVLG 682
SNF2-rel_dom pfam00176
SNF2-related domain; This domain is found in proteins involved in a variety of processes ...
776-1071 1.66e-117

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: 372.02  E-value: 1.66e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   776 YQIKGLEWLVSLYNN-NLNGILADEMGLGKTIQTISLVTYLMDRKKVMG-PYLIIVPLSTLPNWVLEFEKWA--PAVGVV 851
Cdd:pfam00176    1 YQIEGVNWMLSLENNlGRGGILADEMGLGKTLQTISLLLYLKHVDKNWGgPTLIVVPLSLLHNWMNEFERWVspPALRVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   852 SYKGSPQGR-RLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHYIAPYRLLLTG 930
Cdd:pfam00176   81 VLHGNKRPQeRWKNDPNFLADFDVVITTYETLRKHKELLKKVHWHRIVLDEGHRLKNSKSKLSKALK-SLKTRNRWILTG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   931 TPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKvelneeetiLIIRRLHKVLRPFLLRRLKKEVEHQLPDK 1010
Cdd:pfam00176  160 TPLQNNLEELWALLNFLRPGPFGSLSTFRNWFDRPIERGGGK---------KGVSRLHKLLKPFLLRRTKKDVEKSLPPK 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632632  1011 VEYIIKCDMSALQRVLYKH-MQSKGVLLTDGSEkgkHGKGGAKALMNTIVQLRKLCNHPFMF 1071
Cdd:pfam00176  231 VEYILFCRLSKLQRKLYQTfLLKKDLNAIKTGE---GGREIKASLLNILMRLRKICNHPGLI 289
DEXHc_HELLS_SMARCA6 cd18009
DEXH-box helicase domain of HELLS; HELLS (helicase, lymphoid specific, also known as Lsh or ...
770-1000 1.05e-93

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: 302.77  E-value: 1.05e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  770 NGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRkKVMGPYLIIVPLSTLPNWVLEFEKWAPAVG 849
Cdd:cd18009     1 GGVMRPYQLEGMEWLRMLWENGINGILADEMGLGKTIQTIALLAHLRER-GVWGPFLVIAPLSTLPNWVNEFARFTPSVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  850 VVSYKGSPQGRR-----LLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHYIAPY 924
Cdd:cd18009    80 VLLYHGTKEERErlrkkIMKREGTLQDFPVVVTSYEIAMRDRKALQHYAWKYLIVDEGHRLKNLNCRLIQELK-TFNSDN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632632  925 RLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFN--APFATTGEKVELNEEETILIIRRLHKVLRPFLLRRLK 1000
Cdd:cd18009   159 RLLLTGTPLQNNLSELWSLLNFLLPDVFDDLSSFESWFDfsSLSDNAADISNLSEEREQNIVHMLHAILKPFLLRRLK 236
DEXHc_SMARCA1_SMARCA5 cd17997
DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin ...
770-1000 1.31e-93

DEAH-box helicase domain of SMARCA1 and SMARCA5; SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 1 and 5 (SMARCA1 and SMARCA5) are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350755 [Multi-domain]  Cd Length: 222  Bit Score: 301.93  E-value: 1.31e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  770 NGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVG 849
Cdd:cd17997     1 GGTMRDYQIRGLNWLISLFENGINGILADEMGLGKTLQTISLLGYLKHYKNINGPHLIIVPKSTLDNWMREFKRWCPSLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  850 VVSYKGSPQGR-RLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYiAPYRLLL 928
Cdd:cd17997    81 VVVLIGDKEERaDIIRDVLLPGKFDVCITSYEMVIKEKTVLKKFNWRYIIIDEAHRIKNEKSKLSQIVRLFN-SRNRLLL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632632  929 TGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNApfattgeKVELNEEETilIIRRLHKVLRPFLLRRLK 1000
Cdd:cd17997   160 TGTPLQNNLHELWALLNFLLPDVFTSSEDFDEWFNV-------NNCDDDNQE--VVQRLHKVLRPFLLRRIK 222
DEXQc_SRCAP cd18003
DEXH/Q-box helicase domain of SRCAP; Snf2-related CBP activator (SRCAP, also known as SWR1 or ...
773-998 4.99e-85

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: 277.31  E-value: 4.99e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd18003     1 LREYQHIGLDWLATLYEKNLNGILADEMGLGKTIQTIALLAHLACEKGNWGPHLIVVPTSVMLNWEMEFKRWCPGFKILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLL-QNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNThYIAPYRLLLTGT 931
Cdd:cd18003    81 YYGSAKERKLKrQGWMKPNSFHVCITSYQLVVQDHQVFKRKKWKYLILDEAHNIKNFKSQRWQTLLN-FNTQRRLLLTGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632632  932 PLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFAttgEKVELNEEETILIIRRLHKVLRPFLLRR 998
Cdd:cd18003   160 PLQNSLMELWSLMHFLMPHIFQSHQEFKEWFSNPLT---AMSEGSQEENEELVRRLHKVLRPFLLRR 223
DEXHc_CHD1_2 cd17993
DEXH-box helicase domain of the chromodomain helicase DNA binding proteins 1 and 2, and ...
772-998 1.80e-81

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: 266.91  E-value: 1.80e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  772 TLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVV 851
Cdd:cd17993     1 ELRDYQLTGLNWLAHSWCKGNNGILADEMGLGKTVQTISFLSYLFHSQQQYGPFLVVVPLSTMPAWQREFAKWAPDMNVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  852 SYKGSPQGRRLLQ------NQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNThYIAPYR 925
Cdd:cd17993    81 VYLGDIKSRDTIReyefyfSQTKKLKFNVLLTTYEIILKDKAFLGSIKWQYLAVDEAHRLKNDESLLYEALKE-FKTNNR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632632  926 LLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEqwfnapfattgekVELNEEETILiIRRLHKVLRPFLLRR 998
Cdd:cd17993   160 LLITGTPLQNSLKELWALLHFLMPGKFDIWEEFE-------------EEHDEEQEKG-IADLHKELEPFILRR 218
DEXHc_Snf cd17919
DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins; Sucrose Non-Fermenting ...
773-952 5.00e-79

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: 258.65  E-value: 5.00e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd17919     1 LRPYQLEGLNFLLELYENGPGGILADEMGLGKTLQAIAFLAYLLKEGKERGPVLVVCPLSVLENWEREFEKWTPDLRVVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYiAPYRLLLTGTP 932
Cdd:cd17919    81 YHGSQRERAQIRAKEKLDKFDVVLTTYETLRRDKASLRKFRWDLVVVDEAHRLKNPKSQLSKALKALR-AKRRLLLTGTP 159
                         170       180
                  ....*....|....*....|
gi 442632632  933 LQNKLPELWALLNFLLPSIF 952
Cdd:cd17919   160 LQNNLEELWALLDFLDPPFL 179
DEXHc_CHD6_7_8_9 cd17995
DEXH-box helicase domain of the chromodomain helicase DNA binding protein 6, 7, 8 and 9; ...
773-998 2.63e-76

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: 252.55  E-value: 2.63e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAvGVVS 852
Cdd:cd17995     1 LRDYQLEGVNWLLFNWYNRRNCILADEMGLGKTIQSIAFLEHLYQVEGIRGPFLVIAPLSTIPNWQREFETWTDM-NVVV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQN-QM-----------RATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHY 920
Cdd:cd17995    80 YHGSGESRQIIQQyEMyfkdaqgrkkkGVYKFDVLITTYEMVIADAEELRKIPWRVVVVDEAHRLKNRNSKLLQGLK-KL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632632  921 IAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNapfattgekvELNEEETiliIRRLHKVLRPFLLRR 998
Cdd:cd17995   159 TLEHKLLLTGTPLQNNTEELWSLLNFLEPEKFPSSEEFLEEFG----------DLKTAEQ---VEKLQALLKPYMLRR 223
DEXHc_SMARCA5 cd18064
DEAH-box helicase domain of SMARCA5; SWI/SNF related, matrix associated, actin dependent ...
771-1010 5.63e-70

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: 235.33  E-value: 5.63e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  771 GTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGV 850
Cdd:cd18064    14 GKLRDYQVRGLNWLISLYENGINGILADEMGLGKTLQTISLLGYMKHYRNIPGPHMVLVPKSTLHNWMAEFKRWVPTLRA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  851 VSYKGSPQGR-RLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHYIAPYRLLLT 929
Cdd:cd18064    94 VCLIGDKDQRaAFVRDVLLPGEWDVCVTSYEMLIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR-EFKTTNRLLLT 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  930 GTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKvelneeetilIIRRLHKVLRPFLLRRLKKEVEHQLPD 1009
Cdd:cd18064   173 GTPLQNNLHELWALLNFLLPDVFNSAEDFDSWFDTNNCLGDQK----------LVERLHMVLRPFLLRRIKADVEKSLPP 242

                  .
gi 442632632 1010 K 1010
Cdd:cd18064   243 K 243
DEXHc_SMARCA1 cd18065
DEAH-box helicase domain of SMARCA1; SWI/SNF related, matrix associated, actin dependent ...
763-1000 7.83e-70

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: 234.53  E-value: 7.83e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  763 EQASIMVNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFE 842
Cdd:cd18065     6 ESPSYVKGGTLRDYQVRGLNWMISLYENGVNGILADEMGLGKTLQTIALLGYLKHYRNIPGPHMVLVPKSTLHNWMNEFK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  843 KWAPAVGVVSYKGSPQGR-RLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHYI 921
Cdd:cd18065    86 RWVPSLRAVCLIGDKDARaAFIRDVMMPGEWDVCVTSYEMVIKEKSVFKKFNWRYLVIDEAHRIKNEKSKLSEIVR-EFK 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442632632  922 APYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKvelneeetilIIRRLHKVLRPFLLRRLK 1000
Cdd:cd18065   165 TTNRLLLTGTPLQNNLHELWALLNFLLPDVFNSADDFDSWFDTKNCLGDQK----------LVERLHAVLKPFLLRRIK 233
DEXQc_INO80 cd18002
DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 ...
773-998 4.34e-66

DEAQ-box helicase domain of INO80; INO80 is the catalytic ATPase subunit of the INO80 chromatin remodeling complex. INO80 removes histone H3-containing nucleosomes from associated chromatin, promotes CENP-ACnp1 chromatin assembly at the centromere in a redundant manner with another chromatin-remodeling factor Chd1Hrp1. INO80 mutants have severe defects in oxygen consumption and promiscuous cell division that is no longer coupled with metabolic status. INO80 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350760 [Multi-domain]  Cd Length: 229  Bit Score: 223.54  E-value: 4.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd18002     1 LKEYQLKGLNWLANLYEQGINGILADEMGLGKTVQSIAVLAHLAEEHNIWGPFLVIAPASTLHNWQQEISRFVPQFKVLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQN-------QMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLnTHYIAPYR 925
Cdd:cd18002    81 YWGNPKDRKVLRKfwdrknlYTRDAPFHVVITSYQLVVQDEKYFQRVKWQYMVLDEAQAIKSSSSSRWKTL-LSFHCRNR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442632632  926 LLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGE-KVELNEEEtiliIRRLHKVLRPFLLRR 998
Cdd:cd18002   160 LLLTGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAEnKTGLNEHQ----LKRLHMILKPFMLRR 229
DEXHc_CHD2 cd18054
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 2; ...
773-998 1.18e-64

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: 219.49  E-value: 1.18e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd18054    21 LRDYQLEGLNWLAHSWCKNNSVILADEMGLGKTIQTISFLSYLFHQHQLYGPFLLVVPLSTLTSWQREFEIWAPEINVVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQN------QMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLnTHYIAPYRL 926
Cdd:cd18054   101 YIGDLMSRNTIREyewihsQTKRLKFNALITTYEILLKDKTVLGSINWAFLGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632632  927 LLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQwfnapfaTTGEKVELNEEEtiliirrLHKVLRPFLLRR 998
Cdd:cd18054   180 LITGTPLQNSLKELWSLLHFIMPEKFEFWEDFEE-------DHGKGRENGYQS-------LHKVLEPFLLRR 237
DEXHc_CHD1L cd18006
DEAH/Q-box helicase domain of CHD1L; Chromodomain helicase DNA binding protein 1 like (CHD1L, ...
773-998 5.08e-64

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: 216.92  E-value: 5.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd18006     1 LRPYQLEGVNWLLQCRAEQHGCILGDEMGLGKTCQTISLLWYLAGRLKLLGPFLVLCPLSVLDNWKEELNRFAPDLSVIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQNQMRAT-KFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYIaPYRLLLTGT 931
Cdd:cd18006    81 YMGDKEKRLDLQQDIKSTnRFHVLLTTYEICLKDASFLKSFPWASLVVDEAHRLKNQNSLLHKTLSEFSV-DFRLLLTGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632632  932 PLQNKLPELWALLNFLLPSIFkSCSTFEQWFNApFATTGEKVELNEEetiliirrLHKVLRPFLLRR 998
Cdd:cd18006   160 PIQNSLQELYALLSFIEPNVF-PKDKLDDFIKA-YSETDDESETVEE--------LHLLLQPFLLRR 216
DEXQc_arch_SWI2_SNF2 cd18012
DEAQ-box helicase domain of archaeal and bacterial SNF2-related proteins; Proteins belonging ...
769-1000 1.15e-60

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: 207.42  E-value: 1.15e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  769 VNGTLKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIslvTYLMDRK--KVMGPYLIIVPLSTLPNWVLEFEKWAP 846
Cdd:cd18012     1 LKATLRPYQKEGFNWLSFLRHYGLGGILADDMGLGKTLQTL---ALLLSRKeeGRKGPSLVVAPTSLIYNWEEEAAKFAP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  847 AVGVVSYKGSPQGRRLLQnqmRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQV---LNthyiAP 923
Cdd:cd18012    78 ELKVLVIHGTKRKREKLR---ALEDYDLVITSYGLLRRDIELLKEVKFHYLVLDEAQNIKNPQTKTAKAvkaLK----AD 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632632  924 YRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPfattgekVELNEEETILiiRRLHKVLRPFLLRRLK 1000
Cdd:cd18012   151 HRLALTGTPIENHLGELWSIFDFLNPGLLGSYKRFKKRFAKP-------IEKDGDEEAL--EELKKLISPFILRRLK 218
DEXHc_CHD3_4_5 cd17994
DEAH-box helicase domain of the chromodomain helicase DNA binding proteins 3, 4 and 5; ...
773-998 1.89e-59

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: 203.05  E-value: 1.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd17994     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSpqgrrllqnqmratkfNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHYIApYRLLLTGTP 932
Cdd:cd17994    81 YVGD----------------HVLLTSYELISIDQAILGSIDWAVLVVDEAHRLKNNQSKFFRILNSYKIG-YKLLLTGTP 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442632632  933 LQNKLPELWALLNFLLPSIFKSCSTFeqwfnapfatTGEKVELNEEETiliIRRLHKVLRPFLLRR 998
Cdd:cd17994   144 LQNNLEELFHLLNFLTPERFNNLQGF----------LEEFADISKEDQ---IKKLHDLLGPHMLRR 196
SF2_C_SNF cd18793
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ...
1096-1223 6.60e-56

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: 190.38  E-value: 6.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1096 VSGKFELLDRILPKLKATNHRVLLFCQMTQCMTIIEDYLGWRQFGYLRLDGTTKAEDRGELLRKFNAkGSDVFVFLLSTR 1175
Cdd:cd18793     9 VSGKLEALLELLEELREPGEKVLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNE-DPDIRVFLLSTK 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 442632632 1176 AGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRNEVRVLRLM 1223
Cdd:cd18793    88 AGGVGLNLTAANRVILYDPWWNPAVEEQAIDRAHRIGQKKPVVVYRLI 135
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
1425-1530 2.46e-55

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


Pssm-ID: 99947  Cd Length: 107  Bit Score: 187.63  E-value: 2.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1425 RSKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQ 1503
Cdd:cd05516     1 ELTKKMNKIVDVVIKYKDsDGRQLAEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQ 80
                          90       100
                  ....*....|....*....|....*..
gi 442632632 1504 IYNEEASLIYLDSIALQKVFVGARQRI 1530
Cdd:cd05516    81 TFNLEGSLIYEDSIVLQSVFKSARQKI 107
DEXHc_SMARCAD1 cd17998
DEXH-box helicase domain of SMARCAD1; SWI/SNF-related matrix-associated actin-dependent ...
773-952 4.18e-54

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: 187.21  E-value: 4.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKvMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd17998     1 LKDYQLIGLNWLNLLYQKKLSGILADEMGLGKTIQVIAFLAYLKEIGI-PGPHLVVVPSSTLDNWLREFKRWCPSLKVEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQNQM--RATKFNVLLTTYEYVI---KDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNThYIAPYRLL 927
Cdd:cd17998    80 YYGSQEERKHLRYDIlkGLEDFDVIVTTYNLATsnpDDRSFFKRLKLNYVVYDEGHMLKNMTSERYRHLMT-INANFRLL 158
                         170       180
                  ....*....|....*....|....*
gi 442632632  928 LTGTPLQNKLPELWALLNFLLPSIF 952
Cdd:cd17998   159 LTGTPLQNNLLELMSLLNFIMPKPF 183
DEXHc_CHD1 cd18053
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; ...
773-998 1.37e-51

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 1; Chromodomain-helicase-DNA-binding protein 1 (CHD1) is an ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. It regulates polymerase II transcription and is also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. It is not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. CHD1 is also associated with histone deacetylase (HDAC) activity. It is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350811 [Multi-domain]  Cd Length: 237  Bit Score: 182.17  E-value: 1.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd18053    21 LRDYQLNGLNWLAHSWCKGNSCILADEMGLGKTIQTISFLNYLFHEHQLYGPFLLVVPLSTLTSWQREIQTWAPQMNAVV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQN------QMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLnTHYIAPYRL 926
Cdd:cd18053   101 YLGDINSRNMIRThewmhpQTKRLKFNILLTTYEILLKDKSFLGGLNWAFIGVDEAHRLKNDDSLLYKTL-IDFKSNHRL 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632632  927 LLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQwfnapfaTTGEKVELNEEEtiliirrLHKVLRPFLLRR 998
Cdd:cd18053   180 LITGTPLQNSLKELWSLLHFIMPEKFSSWEDFEE-------EHGKGREYGYAS-------LHKELEPFLLRR 237
DEXHc_ERCC6L cd18001
DEXH-box helicase domain of ERCC6L; ERCC excision repair 6 like, spindle assembly checkpoint ...
773-998 2.14e-50

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: 178.33  E-value: 2.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRkKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd18001     1 LYPHQREGVAWLWSLHDGGKGGILADDMGLGKTVQICAFLSGMFDS-GLIKSVLVVMPTSLIPHWVKEFAKWTPGLRVKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKG-SPQGRRllQNQMR-ATKFNVLLTTYEYVIKDKAVLA-----KIQWKYMIIDEGHRMKNHHCKLTQVLntHYI-APY 924
Cdd:cd18001    80 FHGtSKKERE--RNLERiQRGGGVLLTTYGMVLSNTEQLSaddhdEFKWDYVILDEGHKIKNSKTKSAKSL--REIpAKN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  925 RLLLTGTPLQNKLPELWALLNFLLP-SIFKSCSTFEQWFNAPF-------ATTGEKVELNEeetilIIRRLHKVLRPFLL 996
Cdd:cd18001   156 RIILTGTPIQNNLKELWALFDFACNgSLLGTRKTFKMEFENPItrgrdkdATQGEKALGSE-----VAENLRQIIKPYFL 230

                  ..
gi 442632632  997 RR 998
Cdd:cd18001   231 RR 232
DEXHc_CHD5 cd18057
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 5; ...
773-998 2.46e-50

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: 178.33  E-value: 2.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd18057     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTIVFLYSLYKEGHSKGPYLVSAPLSTIINWEREFEMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQ--------NQMRA------------TKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKL 912
Cdd:cd18057    81 YTGDKESRSVIRenefsfedNAIRSgkkvfrmkkeaqIKFHVLLTSYELITIDQAILGSIEWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  913 TQVLNTHYIaPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfattgekVELNEEETiliIRRLHKVLR 992
Cdd:cd18057   161 FRVLNSYKI-DYKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226

                  ....*.
gi 442632632  993 PFLLRR 998
Cdd:cd18057   227 PHMLRR 232
DEXHc_Mot1 cd17999
DEXH-box helicase domain of Mot1; Modifier of transcription 1 (Mot1, also known as TAF172 in ...
773-998 2.59e-50

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: 178.31  E-value: 2.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVtYLMDRKKVMG------PYLIIVPLSTLPNWVLEFEKWAP 846
Cdd:cd17999     1 LRPYQQEGINWLAFLNKYNLHGILCDDMGLGKTLQTLCIL-ASDHHKRANSfnsenlPSLVVCPPTLVGHWVAEIKKYFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  847 AVG--VVSYKGSPQGRRLLQNQMraTKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLnTHYIAPY 924
Cdd:cd17999    80 NAFlkPLAYVGPPQERRRLREQG--EKHNVIVASYDVLRNDIEVLTKIEWNYCVLDEGHIIKNSKTKLSKAV-KQLKANH 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442632632  925 RLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATT--GEKVELNEEETILIIRRLHKVLRPFLLRR 998
Cdd:cd17999   157 RLILSGTPIQNNVLELWSLFDFLMPGYLGTEKQFQRRFLKPILASrdSKASAKEQEAGALALEALHKQVLPFLLRR 232
DEXHc_ERCC6 cd18000
DEXH-box helicase domain of ERCC6; ERCC excision repair 6, chromatin remodeling factor (ERCC6, ...
773-949 1.20e-49

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


Pssm-ID: 350758 [Multi-domain]  Cd Length: 193  Bit Score: 174.82  E-value: 1.20e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVV- 851
Cdd:cd18000     1 LFKYQQTGVQWLWELHCQRVGGILGDEMGLGKTIQIIAFLAALHHSKLGLGPSLIVCPATVLKQWVKEFHRWWPPFRVVv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  852 -----SYKGSPQG-----RRLLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQV---LNT 918
Cdd:cd18000    81 lhssgSGTGSEEKlgsieRKSQLIRKVVGDGGILITTYEGFRKHKDLLLNHNWQYVILDEGHKIRNPDAEITLAckqLRT 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 442632632  919 hyiaPYRLLLTGTPLQNKLPELWALLNFLLP 949
Cdd:cd18000   161 ----PHRLILSGTPIQNNLKELWSLFDFVFP 187
DEXHc_CHD6 cd18058
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; ...
773-998 2.79e-49

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 6; Chromodomain-helicase-DNA-binding protein 6 (CHD6) is a DNA-dependent ATPase that plays a role in chromatin remodeling. It regulates transcription by disrupting nucleosomes in a largely non-sliding manner which strongly increases the accessibility of chromatin. It activates transcription of specific genes in response to oxidative stress through interaction with NFE2L2.2 and acts as a transcriptional repressor of different viruses including influenza virus or papillomavirus. During influenza virus infection, the viral polymerase complex localizes CHD6 to inactive chromatin where it gets degraded in a proteasome independent-manner. CHD6 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350816 [Multi-domain]  Cd Length: 222  Bit Score: 174.85  E-value: 2.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRkKVMGPYLIIVPLSTLPNWVLEFEKWApAVGVVS 852
Cdd:cd18058     1 LREYQLEGMNWLLFNWYNRKNCILADEMGLGKTIQSITFLSEIFLM-GIRGPFLIIAPLSTITNWEREFRTWT-EMNAIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQ-----------NQMRAT-KFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHY 920
Cdd:cd18058    79 YHGSQISRQMIQqyemyyrdeqgNPLSGIfKFQVVITTFEMILADCPELKKINWSCVIIDEAHRLKNRNCKLLEGLKLMA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632632  921 IApYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNapfattgekvELNEEETiliIRRLHKVLRPFLLRR 998
Cdd:cd18058   159 LE-HKVLLTGTPLQNSVEELFSLLNFLEPSQFPSETTFLEEFG----------DLKTEEQ---VKKLQSILKPMMLRR 222
DEXHc_CHD3 cd18055
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 3; ...
773-998 6.10e-49

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: 174.43  E-value: 6.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd18055     1 LHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPDFYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQN-----------------QMRA---TKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKL 912
Cdd:cd18055    81 YTGDKDSRAIIREnefsfddnavkggkkafKMKReaqVKFHVLLTSYELVTIDQAALGSIRWACLVVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  913 TQVLNTHYIaPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfattgekVELNEEETiliIRRLHKVLR 992
Cdd:cd18055   161 FRVLNGYKI-DHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEF----------ADISKEDQ---IKKLHDLLG 226

                  ....*.
gi 442632632  993 PFLLRR 998
Cdd:cd18055   227 PHMLRR 232
DEXHc_CHD7 cd18059
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 7; ...
773-998 5.77e-48

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: 170.98  E-value: 5.77e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVtYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWApAVGVVS 852
Cdd:cd18059     1 LREYQLEGVNWLLFNWYNTRNCILADEMGLGKTIQSITFL-YEIYLKGIHGPFLVIAPLSTIPNWEREFRTWT-ELNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQ--------NQMR----ATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHY 920
Cdd:cd18059    79 YHGSQASRRTIQlyemyfkdPQGRvikgSYKFHAIITTFEMILTDCPELRNIPWRCVVIDEAHRLKNRNCKLLEGLKMMD 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632632  921 IApYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNapfattgekvELNEEETiliIRRLHKVLRPFLLRR 998
Cdd:cd18059   159 LE-HKVLLTGTPLQNTVEELFSLLHFLEPSRFPSETTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD8 cd18060
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; ...
773-998 1.59e-47

DEAH-box helicase domain of the chromodomain helicase DNA binding protein 8; Chromodomain-helicase-DNA-binding protein 8 (CHD8) is a DNA helicase that acts as a chromatin remodeling factor and regulates transcription. It also acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. It suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity and of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. It also acts as a negative regulator of Wnt signaling pathway and CTNNB1-targeted gene expression. CHD8 is also involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. It also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. CHD8 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350818 [Multi-domain]  Cd Length: 222  Bit Score: 169.85  E-value: 1.59e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDrKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVs 852
Cdd:cd18060     1 LREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYN-VGIHGPFLVIAPLSTITNWEREFNTWTEMNTIV- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQN-QMR-----------ATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNtHY 920
Cdd:cd18060    79 YHGSLASRQMIQQyEMYckdsrgrlipgAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLK-HM 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632632  921 IAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNapfattgekvELNEEETiliIRRLHKVLRPFLLRR 998
Cdd:cd18060   158 DLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_CHD4 cd18056
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 4; ...
773-998 4.69e-46

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: 166.01  E-value: 4.69e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVGVVS 852
Cdd:cd18056     1 LHPYQLEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQ--------NQMR------------ATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKL 912
Cdd:cd18056    81 YVGDKDSRAIIRenefsfedNAIRggkkasrmkkeaSVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  913 TQVLNThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFnapfattgekVELNEEETiliIRRLHKVLR 992
Cdd:cd18056   161 FRVLNG-YSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEF----------ADIAKEDQ---IKKLHDMLG 226

                  ....*.
gi 442632632  993 PFLLRR 998
Cdd:cd18056   227 PHMLRR 232
DEXHc_ERCC6L2 cd18005
DEXH-box helicase domain of ERCC6L2; ERCC excision repair 6 like 2 (ERCC6L2, also known as ...
773-998 3.78e-45

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: 163.70  E-value: 3.78e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVTYLM-------DRKKVM-------------GPYLIIVPLS 832
Cdd:cd18005     1 LRDYQREGVEFMYDLYKNGRGGILGDDMGLGKTVQVIAFLAAVLgktgtrrDRENNRprfkkkppassakKPVLIVAPLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  833 TLPNWVLEFEKWAP-AVGVVSYKGSPQGrrlLQNQMRATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCK 911
Cdd:cd18005    81 VLYNWKDELDTWGHfEVGVYHGSRKDDE---LEGRLKAGRLEVVVTTYDTLRRCIDSLNSINWSAVIADEAHRIKNPKSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  912 LTQVLNThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPF------ATTGEKVELNEEetilIIR 985
Cdd:cd18005   158 LTQAMKE-LKCKVRIGLTGTLLQNNMKELWCLLDWAVPGALGSRSQFKKHFSEPIkrgqrhTATARELRLGRK----RKQ 232
                         250
                  ....*....|...
gi 442632632  986 RLHKVLRPFLLRR 998
Cdd:cd18005   233 ELAVKLSKFFLRR 245
DEXHc_CHD9 cd18061
DEAH-box helicase domain of the chromodomain helicase DNA binding protein 9; ...
773-998 1.32e-44

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: 161.33  E-value: 1.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTISLVtYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWApAVGVVS 852
Cdd:cd18061     1 LREYQLEGLNWLLFNWYNRRNCILADEMGLGKTIQSITFL-YEILLTGIRGPFLIIAPLSTIANWEREFRTWT-DLNVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  853 YKGSPQGRRLLQ--------NQMR----ATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHY 920
Cdd:cd18061    79 YHGSLISRQMIQqyemyfrdSQGRiirgAYRFQAIITTFEMILGGCPELNAIDWRCVIIDEAHRLKNKNCKLLEGLKLMN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632632  921 IApYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNapfattgekvELNEEETiliIRRLHKVLRPFLLRR 998
Cdd:cd18061   159 LE-HKVLLTGTPLQNTVEELFSLLHFLEPLRFPSESTFMQEFG----------DLKTEEQ---VQKLQAILKPMMLRR 222
DEXHc_RAD54 cd18004
DEXH-box helicase domain of RAD54; RAD54 proteins play a role in recombination. They are ...
773-998 3.83e-39

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: 146.28  E-value: 3.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVS--LYNNNLNG---ILADEMGLGKTIQTISLVTYLMDRKKVMGP----YLIIVPLSTLPNWVLEFEK 843
Cdd:cd18004     1 LRPHQREGVQFLYDclTGRRGYGGggaILADEMGLGKTLQAIALVWTLLKQGPYGKPtakkALIVCPSSLVGNWKAEFDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  844 W----APAVGVVSYKGSPQGRRLLQNQMRATkFNVLLTTYEYVIKDKAVLAK-IQWKYMIIDEGHRMKNHHCKLTQVLNT 918
Cdd:cd18004    81 WlglrRIKVVTADGNAKDVKASLDFFSSAST-YPVLIISYETLRRHAEKLSKkISIDLLICDEGHRLKNSESKTTKALNS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  919 hYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKvELNEEETILIIRRLH---KVLRPFL 995
Cdd:cd18004   160 -LPCRRRLLLTGTPIQNDLDEFFALVDFVNPGILGSLASFRKVFEEPILRSRDP-DASEEDKELGAERSQelsELTSRFI 237

                  ...
gi 442632632  996 LRR 998
Cdd:cd18004   238 LRR 240
DEXDc_SHPRH-like cd18008
DEXH-box helicase domain of SHPRH-like proteins; The SHPRH-like subgroup belongs to the ...
773-998 8.51e-39

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: 145.51  E-value: 8.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLynnnlNGILADEMGLGKTIQTISLV------------TYLMDRKKVMGPY-----LIIVPLSTLP 835
Cdd:cd18008     1 LLPYQKQGLAWMLPR-----GGILADEMGLGKTIQALALIlatrpqdpkipeELEENSSDPKKLYlskttLIVVPLSLLS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  836 NWVLEFEK-WAPAVG-VVSYKGSPQGRRLLQnqmrATKFNVLLTTY-----EY-----------VIKDKAVLAKIQWKYM 897
Cdd:cd18008    76 QWKDEIEKhTKPGSLkVYVYHGSKRIKSIEE----LSDYDIVITTYgtlasEFpknkkgggrdsKEKEASPLHRIRWYRV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  898 IIDEGHRMKNHHCKLTQV---LNTHyiapYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKve 974
Cdd:cd18008   152 ILDEAHNIKNRSTKTSRAvcaLKAE----RRWCLTGTPIQNSLDDLYSLLRFLRVEPFGDYPWFNSDISKPFSKNDRK-- 225
                         250       260
                  ....*....|....*....|....
gi 442632632  975 lneeetilIIRRLHKVLRPFLLRR 998
Cdd:cd18008   226 --------ALERLQALLKPILLRR 241
DEXHc_ATRX-like cd18007
DEXH-box helicase domain of ATRX-like proteins; This family includes ATRX-like members such as ...
773-965 2.03e-35

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: 135.50  E-value: 2.03e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLE--W--LVSLYNNNLNG---ILADEMGLGKTIQTISLVTYLMDRKKVMGPYLIIVPLSTLPNWVLEFEKWA 845
Cdd:cd18007     1 LKPHQVEGVRflWsnLVGTDVGSDEGggcILAHTMGLGKTLQVITFLHTYLAAAPRRSRPLVLCPASTLYNWEDEFKKWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  846 PAVGVVSY--KGSPQGRRLLQnqmRATKFN-------VLLTTYEY---VIKDKAVLAKIQWKYM-----------IIDEG 902
Cdd:cd18007    81 PPDLRPLLvlVSLSASKRADA---RLRKINkwhkeggVLLIGYELfrnLASNATTDPRLKQEFIaalldpgpdllVLDEG 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632632  903 HRMKNHHCKLTQVLNTHyIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAP 965
Cdd:cd18007   158 HRLKNEKSQLSKALSKV-KTKRRILLTGTPLQNNLKEYWTMVDFARPKYLGTLKEFKKKFVKP 219
BROMO smart00297
bromo domain;
1423-1523 4.04e-30

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 115.45  E-value: 4.04e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   1423 DKRSKKQMHKIMSAVIKHNQDGRtLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNA 1502
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHP-LSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNA 79
                            90       100
                    ....*....|....*....|.
gi 442632632   1503 QIYNEEASLIYLDSIALQKVF 1523
Cdd:smart00297   80 RTYNGPDSEVYKDAKKLEKFF 100
DEXHc_RAD54B cd18066
DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as ...
773-998 4.61e-29

DEXH-box helicase domain of RAD54B; DNA repair and recombination protein RAD54B, also known as RDH54, binds to double-stranded DNA, displays ATPase activity in the presence of DNA, and may have a role in meiotic and mitotic recombination. RAD54B is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350824 [Multi-domain]  Cd Length: 235  Bit Score: 117.25  E-value: 4.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSL-----YNNNLNGILADEMGLGKTIQTISLVTYLMDR-----KKVMGPYLIIVPLSTLPNWVLEFE 842
Cdd:cd18066     1 LRPHQREGIEFLYECvmgmrVNERFGAILADEMGLGKTLQCISLIWTLLRQgpyggKPVIKRALIVTPGSLVKNWKKEFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  843 KW--APAVGVVSYKGSPQGRRLLQnqmrATKFNVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLnTHY 920
Cdd:cd18066    81 KWlgSERIKVFTVDQDHKVEEFIA----SPLYSVLIISYEMLLRSLDQISKLNFDLVICDEGHRLKNTSIKTTTAL-TSL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  921 IAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFATTGEKVELNEEETILIIR--RLHKVLRPFLLRR 998
Cdd:cd18066   156 SCERRIILTGTPIQNDLQEFFALIDFVNPGILGSLSTYRKVYEEPIVRSREPTATPEEKKLGEARaaELTRLTGLFILRR 235
DEXHc_HLTF1_SMARC3 cd18071
DEXH-box helicase domain of HLTF1; Helicase like transcription factor (HLTF1, also known as ...
773-998 6.31e-29

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: 116.80  E-value: 6.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNL-----------------------------NGILADEMGLGKTIQTISLVtylmdrkkVMG 823
Cdd:cd18071     1 LLPHQKQALAWMVSRENSQDlppfweeavglflntitnfsqkkrpelvrGGILADDMGLGKTLTTISLI--------LAN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  824 PYLIIVPLSTLPNWVLEFEKWAP--AVGVVSYKGSPQGR--RLLqnqmraTKFNVLLTTY-----EYVIKDKAVLAKIQW 894
Cdd:cd18071    73 FTLIVCPLSVLSNWETQFEEHVKpgQLKVYTYHGGERNRdpKLL------SKYDIVLTTYntlasDFGAKGDSPLHTINW 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  895 KYMIIDEGHRMKNHHCKLTQ-VLNTHyiAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFaTTGEKV 973
Cdd:cd18071   147 LRVVLDEGHQIRNPNAQQTKaVLNLS--SERRWVLTGTPIQNSPKDLGSLLSFLHLKPFSNPEYWRRLIQRPL-TMGDPT 223
                         250       260
                  ....*....|....*....|....*
gi 442632632  974 ELneeetiliiRRLHKVLRPFLLRR 998
Cdd:cd18071   224 GL---------KRLQVLMKQITLRR 239
DEXDc smart00487
DEAD-like helicases superfamily;
772-961 7.29e-29

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 115.28  E-value: 7.29e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632    772 TLKEYQIKGLEWLvslYNNNLNGILADEMGLGKTIQ-TISLVTYLMDRKKvmGPYLIIVPLSTL-PNWVLEFEKWAPAVG 849
Cdd:smart00487    8 PLRPYQKEAIEAL---LSGLRDVILAAPTGSGKTLAaLLPALEALKRGKG--GRVLVLVPTRELaEQWAEELKKLGPSLG 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632    850 VVS---YKGSPQGRRLlqNQMRATKFNVLLTTYEYVIKD--KAVLAKIQWKYMIIDEGHRMKN--HHCKLTQVLNTHYIA 922
Cdd:smart00487   83 LKVvglYGGDSKREQL--RKLESGKTDILVTTPGRLLDLleNDKLSLSNVDLVILDEAHRLLDggFGDQLEKLLKLLPKN 160
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 442632632    923 PYRLLLTGTPLQNKLPELWALLN--FLLPSIFKSCSTFEQW 961
Cdd:smart00487  161 VQLLLLSATPPEEIENLLELFLNdpVFIDVGFTPLEPIEQF 201
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1098-1212 8.61e-28

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


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 108.84  E-value: 8.61e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  1098 GKFELLDRILPKLKatNHRVLLFCQMTQcmTIIEDYLGWRQ-FGYLRLDGTTKAEDRGELLRKFNAKGSDVfvfLLSTRA 1176
Cdd:pfam00271    1 EKLEALLELLKKER--GGKVLIFSQTKK--TLEAELLLEKEgIKVARLHGDLSQEEREEILEDFRKGKIDV---LVATDV 73
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 442632632  1177 GGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIG 1212
Cdd:pfam00271   74 AERGLDLPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
1427-1524 1.04e-26

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


Pssm-ID: 99950  Cd Length: 103  Bit Score: 105.50  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1427 KKQMHKIMSAVIKH-NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIY 1505
Cdd:cd05519     2 KAAMLEIYDAVLNCeDETGRKLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANARTY 81
                          90
                  ....*....|....*....
gi 442632632 1506 NEEASLIYLDSIALQKVFV 1524
Cdd:cd05519    82 NQEGSIVYEDAVEMEKAFK 100
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
1427-1523 4.12e-26

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


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 103.99  E-value: 4.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1427 KKQMHKIMSAVIKHNQDgrtLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYN 1506
Cdd:cd04369     2 KKKLRSLLDALKKLKRD---LSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYN 78
                          90
                  ....*....|....*..
gi 442632632 1507 EEASLIYLDSIALQKVF 1523
Cdd:cd04369    79 GPGSPIYKDAKKLEKLF 95
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
1440-1529 9.55e-26

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


Pssm-ID: 99946  Cd Length: 105  Bit Score: 103.15  E-value: 9.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1440 HNQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIAL 1519
Cdd:cd05515    16 TDGRGRRLSLIFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNEPDSQIYKDALTL 95
                          90
                  ....*....|
gi 442632632 1520 QKVFVGARQR 1529
Cdd:cd05515    96 QKVLLETKRE 105
DEXHc_RAD54A cd18067
DEXH-box helicase domain of RAD54A; DNA repair and recombination protein RAD54A, also known as ...
773-998 1.46e-25

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: 107.17  E-value: 1.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWL----VSLYNNNLNG-ILADEMGLGKTIQTISLVTYLM----DRKKVMGPYLIIVPLSTLPNWVLEFEK 843
Cdd:cd18067     1 LRPHQREGVKFLyrcvTGRRIRGSHGcIMADEMGLGKTLQCITLMWTLLrqspQCKPEIDKAIVVSPSSLVKNWANELGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  844 W-APAVGVVSYKG--SPQGRRLLQNQMRATKFN----VLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVL 916
Cdd:cd18067    81 WlGGRLQPLAIDGgsKKEIDRKLVQWASQQGRRvstpVLIISYETFRLHVEVLQKGEVGLVICDEGHRLKNSDNQTYQAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  917 NThYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPF------ATTGEKVELNEEETiliiRRLHKV 990
Cdd:cd18067   161 DS-LNTQRRVLLSGTPIQNDLSEYFSLVNFVNPGILGTAAEFKKNFELPIlkgrdaDASEKERQLGEEKL----QELISI 235

                  ....*...
gi 442632632  991 LRPFLLRR 998
Cdd:cd18067   236 VNRCIIRR 243
DEXHc_HARP_SMARCAL1 cd18010
DEXH-box helicase domain of SMARCAL1; SMARCAL1 (SWI/SNF related, matrix associated, actin ...
773-952 5.08e-24

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: 101.90  E-value: 5.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSlynNNLNGILADEMGLGKTIQTISLVTYLMDRkkvmGPYLIIVPLSTLPNWVLEFEKWAPAV---G 849
Cdd:cd18010     1 LLPFQREGVCFALR---RGGRVLIADEMGLGKTVQAIAIAAYYREE----WPLLIVCPSSLRLTWADEIERWLPSLppdD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  850 VVSYKGSPQGRRLLQNQmratkfnVLLTTYEYVIKDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQV---LNTHyiAPYRL 926
Cdd:cd18010    74 IQVIVKSKDGLRDGDAK-------VVIVSYDLLRRLEKQLLARKFKVVICDESHYLKNSKAKRTKAalpLLKR--AKRVI 144
                         170       180
                  ....*....|....*....|....*.
gi 442632632  927 LLTGTPLQNKLPELWALLNFLLPSIF 952
Cdd:cd18010   145 LLSGTPALSRPIELFTQLDALDPKLF 170
HSA smart00573
domain in helicases and associated with SANT domains;
501-573 1.73e-23

domain in helicases and associated with SANT domains;


Pssm-ID: 214727 [Multi-domain]  Cd Length: 73  Bit Score: 95.54  E-value: 1.73e-23
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632632    501 QKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERMRRLMA 573
Cdd:smart00573    1 QKLEEERRRKQHWDHLLEEMIWHAKDFKEEHKWKIAAAKKMAKAVMDYHQNKEKEEERREEKNEKRRLRKLAA 73
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
1426-1527 2.65e-23

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


Pssm-ID: 99948  Cd Length: 103  Bit Score: 95.97  E-value: 2.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1426 SKKQMHKIMSAVIKH-NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQI 1504
Cdd:cd05517     1 LKQILEQLLEAVMTAtDPSGRLISELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKT 80
                          90       100
                  ....*....|....*....|...
gi 442632632 1505 YNEEASLIYLDSIALQKVFVGAR 1527
Cdd:cd05517    81 FNEPGSQVYKDANAIKKIFTAKK 103
DEXHc_ARIP4 cd18069
DEXH-box helicase domain of ARIP4; Androgen receptor-interacting protein 4 (ARIP4, also called ...
773-965 5.69e-23

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: 99.12  E-value: 5.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLvslYNN------------NLNGILADEMGLGKTIQTISLVTYLMdRKKVMGPYLIIVPLSTLPNWVLE 840
Cdd:cd18069     1 LKPHQIGGIRFL---YDNiieslerykgssGFGCILAHSMGLGKTLQVISFLDVLL-RHTGAKTVLAIVPVNTLQNWLSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  841 FEKWAPavgvvSYKGSPQGRR------LLQNQMRATKFN------------VLLTTYE-YVIKDKAVLakiqwkyMIIDE 901
Cdd:cd18069    77 FNKWLP-----PPEALPNVRPrpfkvfILNDEHKTTAARakviedwvkdggVLLMGYEmFRLRPGPDV-------VICDE 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442632632  902 GHRMKNHHCKLTQVLNtHYIAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAP 965
Cdd:cd18069   145 GHRIKNCHASTSQALK-NIRSRRRIVLTGYPLQNNLIEYWCMVDFVRPDFLGTRQEFSNMFERP 207
HELICc smart00490
helicase superfamily c-terminal domain;
1129-1212 8.97e-23

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 93.82  E-value: 8.97e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   1129 IIEDYLGWRQFGYLRLDGTTKAEDRGELLRKFNakgSDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRA 1208
Cdd:smart00490    2 ELAELLKELGIKVARLHGGLSQEEREEILDKFN---NGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRA 78

                    ....
gi 442632632   1209 HRIG 1212
Cdd:smart00490   79 GRAG 82
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
1441-1522 1.53e-21

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


Pssm-ID: 99951  Cd Length: 103  Bit Score: 90.86  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1441 NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQ 1520
Cdd:cd05520    17 NNQGQLLAEPFLKLPSKRKYPDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNVPNSRIYKDAEKLQ 96

                  ..
gi 442632632 1521 KV 1522
Cdd:cd05520    97 KL 98
DEXHc_TTF2 cd18072
DEAH-box helicase domain of TTF2; Transcription termination factor 2 (TTF2 also called ...
773-998 2.01e-20

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: 92.16  E-value: 2.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSLYNNNLNG-ILADEMGLGKTIQTISLVTYLMDRKK----------------------VMGPYLIIV 829
Cdd:cd18072     1 LLLHQKQALAWLLWRERQKPRGgILADDMGLGKTLTMIALILAQKNTQNrkeeekekalteweskkdstlvPSAGTLVVC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  830 PLSTLPNWVLEFEKW--APAVGVVSYKGSpqgrrllqNQMRATK----FNVLLTTYEYVIKD---------KAVLAKIQW 894
Cdd:cd18072    81 PASLVHQWKNEVESRvaSNKLRVCLYHGP--------NRERIGEvlrdYDIVITTYSLVAKEiptykeesrSSPLFRIAW 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  895 KYMIIDEGHRMKNHH-------CKLTqvlnthyiAPYRLLLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFA 967
Cdd:cd18072   153 ARIILDEAHNIKNPKvqasiavCKLR--------AHARWALTGTPIQNNLLDMYSLLKFLRCSPFDDLKVWKKQVDNKSR 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 442632632  968 TTGEkvelneeetiliirRLHKVLRPFLLRR 998
Cdd:cd18072   225 KGGE--------------RLNILTKSLLLRR 241
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
1426-1522 7.14e-20

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


Pssm-ID: 99949 [Multi-domain]  Cd Length: 103  Bit Score: 86.35  E-value: 7.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1426 SKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQI 1504
Cdd:cd05518     1 RKKRMLALFLYVLEYREgSGRRLCDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARH 80
                          90
                  ....*....|....*...
gi 442632632 1505 YNEEASLIYLDSIALQKV 1522
Cdd:cd05518    81 YNEEGSQVYEDANILEKV 98
DEXDc_RapA cd18011
DEXH-box helicase domain of RapA; In bacteria, RapA is an RNA polymerase (RNAP)-associated ...
795-952 1.39e-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: 88.89  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  795 ILADEMGLGKTIQTISLVTYLMDRKKVmGPYLIIVPLSTLPNWVLE-FEKWAPAVGVVSYKGSPQGRRLLQNQMRAtkFN 873
Cdd:cd18011    21 LLADEVGLGKTIEAGLIIKELLLRGDA-KRVLILCPASLVEQWQDElQDKFGLPFLILDRETAAQLRRLIGNPFEE--FP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  874 VLLTTYEYV---IKDKAVLAKIQWKYMIIDEGHRMKNHHC-------KLTQVLNTHyiAPYRLLLTGTPLQNKLPELWAL 943
Cdd:cd18011    98 IVIVSLDLLkrsEERRGLLLSEEWDLVVVDEAHKLRNSGGgketkryKLGRLLAKR--ARHVLLLTATPHNGKEEDFRAL 175

                  ....*....
gi 442632632  944 LNFLLPSIF 952
Cdd:cd18011   176 LSLLDPGRF 184
SnAC pfam14619
Snf2-ATP coupling, chromatin remodelling complex; This domain appears to play a crucial role ...
1308-1375 3.39e-19

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


Pssm-ID: 464219 [Multi-domain]  Cd Length: 69  Bit Score: 83.08  E-value: 3.39e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442632632  1308 ERKKEDEEIHPGR-ERLIDESELPDWLTKDDDEVERFHYQYDEDTILGRGSRQRKEVDYTDSLTEKEWL 1375
Cdd:pfam14619    1 ERRREEAEQLPPLpSRLMEESELPEWYLKDDDEEKKEDKEELDEQVYGRGKRKRKEVSYSDGLTEEQWL 69
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
1431-1530 5.08e-19

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


Pssm-ID: 99954 [Multi-domain]  Cd Length: 113  Bit Score: 84.31  E-value: 5.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1431 HKIMSAVIKH-NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEA 1509
Cdd:cd05524     8 QELYDTIRNYkSEDGRILCESFIRVPKRRNEPEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPD 87
                          90       100
                  ....*....|....*....|.
gi 442632632 1510 SLIYLDSIALQKVFVGARQRI 1530
Cdd:cd05524    88 SPEHKDACKLWELFLSARNEV 108
DEXHc_ATRX cd18068
DEXH-box helicase domain of ATRX; Transcriptional regulator ATRX (also called alpha ...
794-986 5.52e-19

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: 88.41  E-value: 5.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  794 GILADEMGLGKTIQTISLV-TYLM-DRKKVMGPYLIIVPLSTLPNWVLEFEKWAPAVG---------VVSYKgSPQGRRL 862
Cdd:cd18068    31 CILAHCMGLGKTLQVVTFLhTVLLcEKLENFSRVLVVCPLNTVLNWLNEFEKWQEGLKdeekievneLATYK-RPQERSY 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  863 LQNQMRATKfNVLLTTYEYV--------IKDKAVLAKIQWKYM--------IIDEGHRMKNHHCKLTQVLNThYIAPYRL 926
Cdd:cd18068   110 KLQRWQEEG-GVMIIGYDMYrilaqernVKSREKLKEIFNKALvdpgpdfvVCDEGHILKNEASAVSKAMNS-IRTKRRI 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  927 LLTGTPLQNKLPELWALLNFLLPSIFKSCSTFEQWFNAPFaTTGEKVELNEEETILIIRR 986
Cdd:cd18068   188 VLTGTPLQNNLIEYHCMVNFVKPNLLGTIKEFRNRFVNPI-QNGQCADSTLVDVRVMKKR 246
HSA pfam07529
HSA domain; This domain is predicted to bind DNA and is often found associated with helicases. ...
502-568 1.17e-18

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


Pssm-ID: 462194 [Multi-domain]  Cd Length: 67  Bit Score: 81.46  E-value: 1.17e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632632   502 KLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERM 568
Cdd:pfam07529    1 RDEPERREKTHHDYLLEEILWHSKDFKQERRWKRARAKKLARAVAQYHKNIEKEEQKRIEREEKQRL 67
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
1405-1524 1.33e-17

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 86.78  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1405 EESDDDslILKRRRRQNLDKRSKKQMHKIMSAVIKHNQ-DGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDC 1483
Cdd:COG5076   124 AHLKTS--VKKRKTPKIEDELLYADNKAIAKFKKQLFLrDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNG 201
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 442632632 1484 KYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVFV 1524
Cdd:COG5076   202 RYKSFEEFVSDLNLMFDNCKLYNGPDSSVYVDAKELEKYFL 242
BRK pfam07533
BRK domain; The function of this domain is unknown. It is often found associated with ...
650-691 1.23e-16

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


Pssm-ID: 462196  Cd Length: 44  Bit Score: 74.85  E-value: 1.23e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 442632632   650 ADMRVHVVEQCTGKKLTGDDAPMLKHLHRWLNMHPGWDWIDD 691
Cdd:pfam07533    3 GDERVPVVNRKTGKKLTGDKAPKLKDLEEWLEENPGYEVDPR 44
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
1432-1516 1.34e-16

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


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 76.20  E-value: 1.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  1432 KIMSAVIKHNqdgrtLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASL 1511
Cdd:pfam00439    3 EILDKLMEHP-----IAAPFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPGSV 77

                   ....*
gi 442632632  1512 IYLDS 1516
Cdd:pfam00439   78 IYKAA 82
BRK smart00592
domain in transcription and CHROMO domain helicases;
649-693 2.78e-16

domain in transcription and CHROMO domain helicases;


Pssm-ID: 197800  Cd Length: 45  Bit Score: 73.92  E-value: 2.78e-16
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 442632632    649 VADMRVHVVEQCTGKKLTGDDAPMLKHLHRWLNMHPGWDWIDDEE 693
Cdd:smart00592    1 DGEERVPVINRETGKKLTGDDAPKAKDLERWLEENPEYEVAPRSA 45
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
1433-1528 9.36e-15

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


Pssm-ID: 99955 [Multi-domain]  Cd Length: 106  Bit Score: 71.65  E-value: 9.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1433 IMSAVIKH-NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASL 1511
Cdd:cd05525    10 ICDAIITYkDSNGQSLAIPFINLPSKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSP 89
                          90
                  ....*....|....*..
gi 442632632 1512 IYLDSIALQKVFVGARQ 1528
Cdd:cd05525    90 IGRDVCRLRKAYYQAKH 106
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
1429-1524 2.63e-14

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


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 70.28  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1429 QMHKIMSAVIKHNQdgrtlSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEE 1508
Cdd:cd05509     5 QLKKVLDSLKNHKS-----AWPFLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGP 79
                          90
                  ....*....|....*.
gi 442632632 1509 ASLIYLDSIALQKVFV 1524
Cdd:cd05509    80 DTEYYKCANKLEKFFW 95
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1434-1523 2.63e-13

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


Pssm-ID: 99953 [Multi-domain]  Cd Length: 104  Bit Score: 67.65  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1434 MSAVIKH-----NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEE 1508
Cdd:cd05522     6 IKNILKGlrkerDENGRLLTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNEN 85
                          90
                  ....*....|....*
gi 442632632 1509 ASLIYLDSIALQKVF 1523
Cdd:cd05522    86 DSQEYKDAVLLEKEA 100
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
1416-1524 4.62e-13

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


Pssm-ID: 99936  Cd Length: 115  Bit Score: 67.04  E-value: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1416 RRRRQNLD-KRSKKQMHKIMSAVIKHNQdgrtlSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKD 1494
Cdd:cd05504     2 RRSEGRHHgPLNLSALEQLLVEIVKHKD-----SWPFLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSD 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 442632632 1495 FMQLCQNAQIYNEEASLIYLDSIALQKVFV 1524
Cdd:cd05504    77 IQLVFSNCFLYNPEHTSVYKAGTRLQRFFI 106
DEXQc_bact_SNF2 cd18013
DEXQ-box helicase domain of bacterial SNF2 family proteins; Proteins belonging to the SNF2 ...
773-963 4.10e-12

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: 67.37  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVSlynNNLNGILADeMGLGKTIQTISLVTYLMDRKKVmGPYLIIVPLSTLPN-WVLEFEKWAPAVG-- 849
Cdd:cd18013     1 PHPYQKVAINFIIE---HPYCGLFLD-MGLGKTVTTLTALSDLQLDDFT-RRVLVIAPLRVARStWPDEVEKWNHLRNlt 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  850 VVSYKGSPQGRRLLQNqmraTKFNVLLTTYEYVIK-DKAVLAKIQWKYMIIDEGHRMKNHHCKLTQVLNTHyiAPY--RL 926
Cdd:cd18013    76 VSVAVGTERQRSKAAN----TPADLYVINRENLKWlVNKSGDPWPFDMVVIDELSSFKSPRSKRFKALRKV--RPVikRL 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 442632632  927 L-LTGTPLQNKLPELWALLNFL--LPSIFKSCSTF-EQWFN 963
Cdd:cd18013   150 IgLTGTPSPNGLMDLWAQIALLdqGERLGRSITAYrERWFD 190
DEXQc_SHPRH cd18070
DEXQ-box helicase domain of SHPRH; E3 ubiquitin-protein ligase SHPRH is a ubiquitously ...
773-962 1.66e-11

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: 66.60  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLEWLVslynnNLNGILADEMGLGKTIQTISLV------------TYLMDRKKVM-------------GPYLI 827
Cdd:cd18070     1 LLPYQRRAVNWML-----VPGGILADEMGLGKTVEVLALIllhprpdndldaADDDSDEMVCcpdclvaetpvssKATLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  828 IVPLSTLPNWVLEFEKWAP-AVGVVSYKG--------SPQGRRLLQNQMRATKFNVL---------------LTTYEYVI 883
Cdd:cd18070    76 VCPSAILAQWLDEINRHVPsSLKVLTYQGvkkdgalaSPAPEILAEYDIVVTTYDVLrtelhyaeanrsnrrRRRQKRYE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  884 KDKAVLAKIQWKYMIIDEGHRMKNHHCKLTQ-VLNTHYIApyRLLLTGTPLQNKLPELWALLNFLLPSIFksCSTFEQWF 962
Cdd:cd18070   156 APPSPLVLVEWWRVCLDEAQMVESSTSKAAEmARRLPRVN--RWCVSGTPIQRGLDDLFGLLSFLGVEPF--CDSDWWAR 231
Bromo_Rsc1_2_I cd05521
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
1441-1521 3.50e-11

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


Pssm-ID: 99952  Cd Length: 106  Bit Score: 61.57  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1441 NQDGRTLSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEdcKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQ 1520
Cdd:cd05521    18 EENGIEIHPIFNVLPLRKDYPDYYKIIKNPLSLNTVKKRLP--HYTNAQEFVNDLAQIPWNARLYNTKGSVIYKYALILE 95

                  .
gi 442632632 1521 K 1521
Cdd:cd05521    96 K 96
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
1461-1513 3.50e-10

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


Pssm-ID: 99945  Cd Length: 98  Bit Score: 58.58  E-value: 3.50e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442632632 1461 PDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIY 1513
Cdd:cd05513    32 PGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYNKPDTIYY 84
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
1460-1531 8.15e-10

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


Pssm-ID: 99929  Cd Length: 107  Bit Score: 57.82  E-value: 8.15e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632632 1460 LPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVFvgaRQRIT 1531
Cdd:cd05497    37 LPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNKPGDDVVLMAQTLEKLF---LQKLA 105
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
1460-1523 2.91e-09

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


Pssm-ID: 99930  Cd Length: 102  Bit Score: 55.75  E-value: 2.91e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442632632 1460 LPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVF 1523
Cdd:cd05498    35 LHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHPVHAMARKLQDVF 98
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
1448-1524 2.00e-08

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


Pssm-ID: 99927  Cd Length: 108  Bit Score: 53.60  E-value: 2.00e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442632632 1448 SEPFMKL--PSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVFV 1524
Cdd:cd05495    22 SLPFRQPvdPKLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYNRKTSRVYKYCTKLAEVFE 100
SSL2 COG1061
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
725-932 2.18e-08

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


Pssm-ID: 440681 [Multi-domain]  Cd Length: 566  Bit Score: 58.88  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  725 NDEDAKDLITKAKVEDDEYRTEEQTYYSIAHTIHEKVVEQASIMVNGTLKEYQIKGLE-WLVSLYNNNLNGILADEMGLG 803
Cdd:COG1061    33 NLVEARRLAIKEGTREDGRRLPEEDTERELAEAEALEAGDEASGTSFELRPYQQEALEaLLAALERGGGRGLVVAPTGTG 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  804 KTIQTISLVTYLMDRKKVmgpyLIIVPLSTLPN-WVLEFEKWAPAVGVVSYKgspqgrrllqnqmRATKFNVLLTTYEYV 882
Cdd:COG1061   113 KTVLALALAAELLRGKRV----LVLVPRRELLEqWAEELRRFLGDPLAGGGK-------------KDSDAPITVATYQSL 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442632632  883 IKdKAVLAKIQ--WKYMIIDEGHrmknhHC---KLTQVLNtHYIAPYRLLLTGTP 932
Cdd:COG1061   176 AR-RAHLDELGdrFGLVIIDEAH-----HAgapSYRRILE-AFPAAYRLGLTATP 223
ResIII pfam04851
Type III restriction enzyme, res subunit;
772-932 3.40e-08

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 54.60  E-value: 3.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   772 TLKEYQIKGLE-WLVSLYNNNLNGILADEMGLGKTIQTISLVTYLM---DRKKVmgpyLIIVP-LSTLPNWVLEFEKWAP 846
Cdd:pfam04851    3 ELRPYQIEAIEnLLESIKNGQKRGLIVMATGSGKTLTAAKLIARLFkkgPIKKV----LFLVPrKDLLEQALEEFKKFLP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   847 AVGVVSYKGSPQGRRLLQNQMRatkfnVLLTTYE--YVIKDKAVLAKI--QWKYMIIDEGHRM--KNHhcklTQVLNtHY 920
Cdd:pfam04851   79 NYVEIGEIISGDKKDESVDDNK-----IVVTTIQslYKALELASLELLpdFFDVIIIDEAHRSgaSSY----RNILE-YF 148
                          170
                   ....*....|..
gi 442632632   921 IAPYRLLLTGTP 932
Cdd:pfam04851  149 KPAFLLGLTATP 160
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
1461-1520 5.08e-08

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


Pssm-ID: 99944  Cd Length: 98  Bit Score: 52.40  E-value: 5.08e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1461 PDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQ 1520
Cdd:cd05512    32 PDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKDTIFYRAAVRLR 91
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
1461-1506 6.20e-08

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


Pssm-ID: 99957  Cd Length: 112  Bit Score: 52.36  E-value: 6.20e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 442632632 1461 PDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYN 1506
Cdd:cd05528    34 PDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYN 79
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
1448-1510 9.60e-08

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


Pssm-ID: 99942 [Multi-domain]  Cd Length: 112  Bit Score: 52.06  E-value: 9.60e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632632 1448 SEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEAS 1510
Cdd:cd05510    26 STPFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYNSDPS 88
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
1448-1510 3.58e-07

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


Pssm-ID: 99943 [Multi-domain]  Cd Length: 112  Bit Score: 50.34  E-value: 3.58e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442632632 1448 SEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEAS 1510
Cdd:cd05511    18 SWPFHTPVNKKKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDS 80
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
1447-1523 3.76e-07

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


Pssm-ID: 99931  Cd Length: 102  Bit Score: 49.98  E-value: 3.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442632632 1447 LSEPFMKL--PSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVF 1523
Cdd:cd05499    20 YNWPFLDPvdPVALNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTDVYMMGHQLEEVF 98
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
773-932 5.45e-07

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: 50.77  E-value: 5.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  773 LKEYQIKGLE-WLvsLYNNNLNGILADEMGLGKTIQTISLVTYLMdRKKVmgpyLIIVPLSTLPN-WVLEFEKWAP--AV 848
Cdd:cd17926     1 LRPYQEEALEaWL--AHKNNRRGILVLPTGSGKTLTALALIAYLK-ELRT----LIVVPTDALLDqWKERFEDFLGdsSI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  849 GVVSYKgspqgrrllqNQMRATKFNVLLTTYEYVIKDKAVLAKI--QWKYMIIDEGHrmknHHC--KLTQVLnTHYIAPY 924
Cdd:cd17926    74 GLIGGG----------KKKDFDDANVVVATYQSLSNLAEEEKDLfdQFGLLIVDEAH----HLPakTFSEIL-KELNAKY 138

                  ....*...
gi 442632632  925 RLLLTGTP 932
Cdd:cd17926   139 RLGLTATP 146
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
1450-1523 2.53e-06

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


Pssm-ID: 99935  Cd Length: 97  Bit Score: 47.37  E-value: 2.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442632632 1450 PFMkLPSRQRL-PDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVF 1523
Cdd:cd05503    20 PFL-EPVNTKLvPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSEVGRAGHNMRKFF 93
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
1426-1523 3.01e-06

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


Pssm-ID: 99932  Cd Length: 103  Bit Score: 47.31  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1426 SKKQmHKIMSAVIKHNQDGRTlSEPFMKL--PSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQ 1503
Cdd:cd05500     2 TKHQ-HKFLLSSIRSLKRLKD-ARPFLVPvdPVKLNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCL 79
                          90       100
                  ....*....|....*....|
gi 442632632 1504 IYNEEASLIYLDSIALQKVF 1523
Cdd:cd05500    80 TFNGPEHPVSQMGKRLQAAF 99
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
1447-1523 3.05e-06

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


Pssm-ID: 99934 [Multi-domain]  Cd Length: 109  Bit Score: 47.67  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1447 LSEPFMKlPSRQRLPDYYEIIKRPVD---IKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEASLIYLDSIALQKVF 1523
Cdd:cd05502    21 LSLPFHE-PVSPSVPNYYKIIKTPMDlslIRKKLQPKSPQHYSSPEEFVADVRLMFKNCYKFNEEDSEVAQAGKELELFF 99
PTZ00121 PTZ00121
MAEBL; Provisional
477-651 6.87e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 6.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  477 IKLYKRTKRQGLREARATE----KLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANA 552
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  553 EREQKKEQEriEKERMRRLMAEDEEGyRKLIDQKK----DKRLAFLLSQTDEYISNLTQMVK------QHKDDQMKKKEE 622
Cdd:PTZ00121 1678 EEAKKAEED--EKKAAEALKKEAEEA-KKAEELKKkeaeEKKKAEELKKAEEENKIKAEEAKkeaeedKKKAEEAKKDEE 1754
                         170       180
                  ....*....|....*....|....*....
gi 442632632  623 EGKRLIQFKKELLMSGEYIGIDEGSIVAD 651
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
405-643 7.94e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  405 ITLLQERENRIAARISLRMQELQRLpATMSEDLRLQAAIELRALRVLNFQRQLrmefvqctrRDTTLETALNIKLYKRTK 484
Cdd:COG1196   283 LEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEE---------LEEELEELEEELEEAEEE 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  485 RQGLREARATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFhRNNKAQLARMNKAVMNHHANAEREQKKEQERIE 564
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALA 431
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442632632  565 KERMRRLMAEDEEGYRKLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKELLMSGEYIGI 643
Cdd:COG1196   432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1448-1523 2.38e-05

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


Pssm-ID: 99928  Cd Length: 119  Bit Score: 45.14  E-value: 2.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632632 1448 SEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYN-EEASLIYLDSIALQKVF 1523
Cdd:cd05496    23 SEPFRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTpNKRSRIYSMTLRLSALF 99
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
407-645 3.48e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.81  E-value: 3.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   407 LLQERENRIAARISLRMQELQRLPatmsEDLRLQAAIELRALRVLNFQRQLRMEFVQ----CTRRDTTLETALNIKLYKR 482
Cdd:pfam02463  178 LIEETENLAELIIDLEELKLQELK----LKEQAKKALEYYQLKEKLELEEEYLLYLDylklNEERIDLLQELLRDEQEEI 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   483 TKRQGLREARAtEKLEKQQKLEAERKRRQKHLEFLAAVLQhgkDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQER 562
Cdd:pfam02463  254 ESSKQEIEKEE-EKLAQVLKENKEEEKEKKLQEEELKLLA---KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   563 IEKERmrrlmaEDEEGYRKLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKELLMSGEYIG 642
Cdd:pfam02463  330 LKKEK------EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403

                   ...
gi 442632632   643 IDE 645
Cdd:pfam02463  404 EKE 406
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
409-591 3.89e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.61  E-value: 3.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   409 QERENRIAARISLRMQELQRLPATMSEDLRLQAAIE-LRALRVlnfqrqlrMEFVQCTRRDTTLETALNiklyKRTKRQG 487
Cdd:pfam13868  169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDeLRAKLY--------QEEQERKERQKEREEAEK----KARQRQE 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   488 LREARATEKLEKQQKLEAERKRRQkhlEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHAN--AEREQKKEQERIEK 565
Cdd:pfam13868  237 LQQAREEQIELKERRLAEEAEREE---EEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKqiEEREEQRAAEREEE 313
                          170       180
                   ....*....|....*....|....*.
gi 442632632   566 ERMRRLMAEDEEGYRKLIDQKKDKRL 591
Cdd:pfam13868  314 LEEGERLREEEAERRERIEEERQKKL 339
QLQ pfam08880
QLQ; The QLQ domain is named after the conserved Gln, Leu, Gln motif. The QLQ domain is found ...
173-202 4.39e-05

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


Pssm-ID: 462622  Cd Length: 35  Bit Score: 41.94  E-value: 4.39e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 442632632   173 HLNGNQVNLLRTQITAYRLLARNKPISMQM 202
Cdd:pfam08880    1 PFTPAQLQELRAQILAYKYLSRNQPVPPEL 30
QLQ smart00951
QLQ is named after the conserved Gln, Leu, Gln motif; QLQ is found at the N-terminus of SWI2 ...
172-202 6.20e-05

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


Pssm-ID: 214931  Cd Length: 36  Bit Score: 41.36  E-value: 6.20e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 442632632    172 QHLNGNQVNLLRTQITAYR-LLARNKPISMQM 202
Cdd:smart00951    1 SPFTPAQLELLRAQILAYKyLLARNQPVPPEL 32
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1165-1215 6.81e-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: 42.69  E-value: 6.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442632632 1165 SDVFVFLLSTRAGGLGLNLQTADTVVIFDSDWNPHQDLQAQDRAHRIGQRN 1215
Cdd:cd18785    20 ASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKDE 70
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
1424-1506 8.29e-05

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


Pssm-ID: 99939  Cd Length: 104  Bit Score: 43.12  E-value: 8.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1424 KRSKKQMHKIMSAVIKHNQdgrtlSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQ 1503
Cdd:cd05507     2 RAWKKAILLVYRTLASHRY-----ASVFLKPVTEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAI 76

                  ...
gi 442632632 1504 IYN 1506
Cdd:cd05507    77 MYN 79
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
1427-1512 9.85e-05

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


Pssm-ID: 99937  Cd Length: 97  Bit Score: 42.91  E-value: 9.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1427 KKQMHKIMSAVIKHNQdgrtlSEPFMKLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYN 1506
Cdd:cd05505     2 LQKCEEILSKILKYRF-----SWPFREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYY 76

                  ....*.
gi 442632632 1507 EEASLI 1512
Cdd:cd05505    77 ENGSYV 82
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
1428-1523 1.19e-04

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


Pssm-ID: 99938  Cd Length: 99  Bit Score: 42.70  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1428 KQMHKIMSAVIKHnQDGRTLSEPFMklPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNE 1507
Cdd:cd05506     3 KQCGTLLRKLMKH-KWGWVFNAPVD--VVALGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNP 79
                          90
                  ....*....|....*.
gi 442632632 1508 EASLIYLDSIALQKVF 1523
Cdd:cd05506    80 PGNDVHTMAKELLKIF 95
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
485-636 1.31e-04

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.48  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   485 RQGLREARAtekleKQQKLEAERKRRQKhleflaavlqhgkdlREFHRNNKAQLARMNKavMNHHANAEREQKKEQERIE 564
Cdd:pfam15709  335 RDRLRAERA-----EMRRLEVERKRREQ---------------EEQRRLQQEQLERAEK--MREELELEQQRRFEEIRLR 392
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442632632   565 KERMR--RLMAEDEEGYRKLIDQKKDKRLAfllSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRliqfKKELLM 636
Cdd:pfam15709  393 KQRLEeeRQRQEEEERKQRLQLQAAQERAR---QQQEEFRRKLQELQRKKQQEEAERAEAEKQR----QKELEM 459
Bromo_polybromo_VI cd05526
Bromodomain, polybromo repeat VI. Polybromo is a nuclear protein of unknown function, which ...
1427-1531 1.56e-04

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


Pssm-ID: 99956  Cd Length: 110  Bit Score: 42.74  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1427 KKQMHKIMSAVIKH-NQDGRTLSEPFMKLPSRQRLPDYYEiiKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIY 1505
Cdd:cd05526     5 QELLATLFVSVMNHqDEEGRCYSDSLAELPELAVDGVGPK--KIPLTLDIIKRNVDKGRYRRLDKFQEDMFEVLERARRL 82
                          90       100
                  ....*....|....*....|....*.
gi 442632632 1506 NEEASLIYLDSIALQKVFVGARQRIT 1531
Cdd:cd05526    83 SRTDSEIYEDAVELQQFFIKIRDELC 108
PRK11637 PRK11637
AmiB activator; Provisional
451-569 2.53e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 45.45  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  451 LNFQRQLRMEFVQCTRRDTTLETALniKLYKRTKRQGLrearATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGK-DLRE 529
Cdd:PRK11637  164 LNQARQETIAELKQTREELAAQKAE--LEEKQSQQKTL----LYEQQAQQQKLEQARNERKKTLTGLESSLQKDQqQLSE 237
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 442632632  530 FhRNNKAQLarmnkavMNHHANAEREQKK--EQERIEKERMR 569
Cdd:PRK11637  238 L-RANESRL-------RDSIARAEREAKAraEREAREAARVR 271
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
1432-1512 2.94e-04

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


Pssm-ID: 99958  Cd Length: 128  Bit Score: 42.32  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632 1432 KIMSAVIKHNQDG-RTLSEPFM-KLPSRQRLPDYYEIIKRPVDIKKILQRIEDCKYADLNELEKDFMQLCQNAQIYNEEA 1509
Cdd:cd05529    28 RLISGLDKLLLSLqLEIAEYFEyPVDLRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAETFNEPN 107

                  ...
gi 442632632 1510 SLI 1512
Cdd:cd05529   108 SEI 110
PTZ00121 PTZ00121
MAEBL; Provisional
484-633 3.41e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  484 KRQGLREARATEKLEKQQKLEAERKRRQKHLEFL----AAVLQHGKDLREFHRNNKAQLARMN-----KAVMNHHANAER 554
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaeEARIEEVMKLYEEEKKMKAEEAKKAeeakiKAEELKKAEEEK 1632
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  555 ---EQKKEQERIEKERMRRLMAEDEEGYRKLIDQKK----DKRLAFLLSQTDEYisnltqmvKQHKDDQMKKKEEEGKRL 627
Cdd:PTZ00121 1633 kkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeeDKKKAEEAKKAEED--------EKKAAEALKKEAEEAKKA 1704

                  ....*.
gi 442632632  628 IQFKKE 633
Cdd:PTZ00121 1705 EELKKK 1710
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
247-401 7.17e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 42.33  E-value: 7.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   247 QPPPSAGTPPQCSTPPASNPYGPPVPGQKMQVAPPPPHMQQgqplppqppqvggpppiqqqqppqqqqqqsqppppephq 326
Cdd:pfam15240   55 PPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPR--------------------------------------- 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442632632   327 hqlPNGGKPLSMGPSGG-QPLIPSSPMQPQVrgtlPGMPPGSQVPQPGGGPQRQVPPAGMPMPKPNRITTVAKPVG 401
Cdd:pfam15240   96 ---PPPGKPQGPPPQGGnQQQGPPPPGKPQG----PPPQGGGPPPQGGNQQGPPPPPPGNPQGPPQRPPQPGNPQG 164
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
251-398 7.39e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   251 SAGTPPQC-STPPASNPYGPPVPGQKMQVAPPPPHMQQGQPLPPQPPQVGGPPPIQQQQPPQQQQQQSQPPPPEPHQHQL 329
Cdd:pfam03154  196 TAGPTPSApSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQM 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   330 PNGGKPLSMGPS----------------GGQPLIPSSPmQPQVRG---TLPGMPPGSQVPQPGGGPQRQ-VPPAGMPMP- 388
Cdd:pfam03154  276 PPMPHSLQTGPShmqhpvppqpfpltpqSSQSQVPPGP-SPAAPGqsqQRIHTPPSQSQLQSQQPPREQpLPPAPLSMPh 354
                          170
                   ....*....|.
gi 442632632   389 -KPNRITTVAK 398
Cdd:pfam03154  355 iKPPPTTPIPQ 365
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
249-390 1.01e-03

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


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 42.67  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   249 PPSAGTPP-----QCSTPPASNPYGPP-VPGQKMQVAPPPPHMQQGQPLPpqppqvggpppiqqqqppqqqqqqsqpppp 322
Cdd:pfam15822   75 GPSPGPPApfppsGPSCPPPGGPYPAPtVPGPGPIGPYPTPNMPFPELPR------------------------------ 124
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   323 ephqhqlPNGG--KPLSMGPSGGQPLIPSSPMQPqvrgTLPGMPPGSQVPQPGGGPQRQVPPAGMPMPKP 390
Cdd:pfam15822  125 -------PYGAptDPAAAAPSGPWGSMSSGPWAP----GMGGQYPAPNMPYPSPGPYPAVPPPQSPGAAP 183
PTZ00121 PTZ00121
MAEBL; Provisional
478-764 1.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  478 KLYKRTKRQGLREARATEKLEKQQKLEAERKRRQKHleflAAVLQHGKDLREFHRnnKAQLARMNKAVMNHHANAEREQK 557
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK----NMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKK 1614
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  558 KEQERIEKERMRRlmaedEEGYRKLIDQKKDKRlafllsqtDEYISNLTQMVKQH-----KDDQMKKKEEEGKRliqfKK 632
Cdd:PTZ00121 1615 AEEAKIKAEELKK-----AEEEKKKVEQLKKKE--------AEEKKKAEELKKAEeenkiKAAEEAKKAEEDKK----KA 1677
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  633 ELLMSGEyigidegsivaDMRVHVVEQCTGKKLTGDDAPMLKHLHRwlnmhpgwDWIDDEEDSCGSNDDHKPKVEEQPTA 712
Cdd:PTZ00121 1678 EEAKKAE-----------EDEKKAAEALKKEAEEAKKAEELKKKEA--------EEKKKAEELKKAEEENKIKAEEAKKE 1738
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442632632  713 TEDATDKAQATGNDEDAKDLITKAKVEddEYRTEEQTYYSIAHTIHEKVVEQ 764
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEEKKKIAHLKKE--EEKKAEEIRKEKEAVIEEELDEE 1788
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
406-577 1.49e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 43.02  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   406 TLLQERENRIAARislrmqelQRLPATMSEDLRLQAAielRALRVLNFQRQLRMEFVQctrRDTTLETALNIKLYKRTKR 485
Cdd:pfam15709  323 ALLEKREQEKASR--------DRLRAERAEMRRLEVE---RKRREQEEQRRLQQEQLE---RAEKMREELELEQQRRFEE 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   486 QGLREARATEklEKQQKLEAERKRrqkHLEFLAAVLQHGKDLREFHRNNKaQLARMNKAVMNHHANAEREQKKEQERIEK 565
Cdd:pfam15709  389 IRLRKQRLEE--ERQRQEEEERKQ---RLQLQAAQERARQQQEEFRRKLQ-ELQRKKQQEEAERAEAEKQRQKELEMQLA 462
                          170
                   ....*....|..
gi 442632632   566 ERMRRLMAEDEE 577
Cdd:pfam15709  463 EEQKRLMEMAEE 474
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
367-611 1.59e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.53  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   367 SQVPQPGGGP---QRQVPPAGMPMPKPNRITTVAKPVGLDPITLLQERENRIAARISLRMQELQRLPATMSEDLRLQAAI 443
Cdd:TIGR02794   26 SVKPEPGGGAeiiQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   444 --ELRALRVLNFQRQLrmefvqctrrdttLETALNIKLYKRTKRQGLREARATEKLEKQQKLEAERKR----RQKHLEFL 517
Cdd:TIGR02794  106 qaEQAAKQAEEKQKQA-------------EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAaaeaKKKAEEAK 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   518 AAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERIEKERMRRLMAEDEEGYRKL--------IDQKKDK 589
Cdd:TIGR02794  173 KKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIfglasgsnAEKQGGA 252
                          250       260
                   ....*....|....*....|..
gi 442632632   590 RLAFLLSQTDEYISNLTQMVKQ 611
Cdd:TIGR02794  253 RGAAAGSEVDKYAAIIQQAIQQ 274
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
407-577 1.94e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  407 LLQERENRIA-----ARISLRMQELQrlpatmsEDLRlQAAIELRALRVLNFQRQLRMEFVQCTRRDTTLETALNIKLYK 481
Cdd:COG1196   194 ILGELERQLEplerqAEKAERYRELK-------EELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  482 RTKRQGLREARATEKLEKQQKLEAERKRRQKHLEfLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQE 561
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAELAR-LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
                         170
                  ....*....|....*.
gi 442632632  562 RIEKERMRRLMAEDEE 577
Cdd:COG1196   345 ELEEAEEELEEAEAEL 360
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
410-586 2.89e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 41.95  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   410 ERENRIAARISLRMQELQRlpatMSEdLRLQAAIELRALRVLNFQRQLRME------FVQCTR--------RDTTLETAL 475
Cdd:pfam15558    4 ERDRKIAALMLARHKEEQR----MRE-LQQQAALAWEELRRRDQKRQETLErerrllLQQSQEqwqaekeqRKARLGREE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   476 NIKLYKRTKRQGLREARATEKLEKQQKL----------EAE-RKRRQKHLefLAAVLQHGKDLREfhRNNKAQLARMNKA 544
Cdd:pfam15558   79 RRRADRREKQVIEKESRWREQAEDQENQrqeklerarqEAEqRKQCQEQR--LKEKEEELQALRE--QNSLQLQERLEEA 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 442632632   545 VMNHHANAEREQKKEQ-----ERIEKERMRRLMA----EDEEGYRKLIDQK 586
Cdd:pfam15558  155 CHKRQLKEREEQKKVQennlsELLNHQARKVLVDcqakAEELLRRLSLEQS 205
PHA03378 PHA03378
EBNA-3B; Provisional
255-388 2.95e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.36  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  255 PPQCSTPPASNPYGPPVPGQKMQVAPPPphmqqgqplpPQPPQVGGPPPIQQQQPPQQQQQQSQPPPPEPhqhqlPNGGK 334
Cdd:PHA03378  696 PPPRAPTPMRPPAAPPGRAQRPAAATGR----------ARPPAAAPGRARPPAAAPGRARPPAAAPGRAR-----PPAAA 760
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442632632  335 PLSMGPSGGQPLIPsSPMQPqvrgtlPGMPPGSQvPQPGGGPQRQVPPAGMPMP 388
Cdd:PHA03378  761 PGRARPPAAAPGAP-TPQPP------PQAPPAPQ-QRPRGAPTPQPPPQAGPTS 806
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
478-634 3.12e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  478 KLYKRTKRQGLREARATEKLEKQ-QKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQ 556
Cdd:COG4717    57 ELFKPQGRKPELNLKELKELEEElKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442632632  557 KKEQERIEKERMRRLMAEDEEgYRKLIDQKKDKRLAflLSQTDEYISNLTQMVKQHKDDQMKKKEEEGKRLIQFKKEL 634
Cdd:COG4717   137 LEAELAELPERLEELEERLEE-LRELEEELEELEAE--LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
486-629 3.52e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 3.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   486 QGLREARATEKLEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQK-------- 557
Cdd:pfam13868  161 LKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARqrqelqqa 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   558 ---------------KEQERIEKERMRRLMAEDEEGYRKLIDQKKDKRLafllsqtdEYISNLTQMV---KQHKDDQMKK 619
Cdd:pfam13868  241 reeqielkerrlaeeAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL--------EHRRELEKQIeerEEQRAAEREE 312
                          170
                   ....*....|
gi 442632632   620 KEEEGKRLIQ 629
Cdd:pfam13868  313 ELEEGERLRE 322
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
793-931 3.68e-03

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: 39.69  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  793 NGILADEMGLGKTIQ-TISLVTYLMD-RKKVmgpyLIIVPLSTLPN----WVLEFEKWAPAVGVVSYKGSPQGRRLLQNQ 866
Cdd:cd00046     3 NVLITAPTGSGKTLAaLLAALLLLLKkGKKV----LVLVPTKALALqtaeRLRELFGPGIRVAVLVGGSSAEEREKNKLG 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632632  867 mratKFNVLLTTYEYVIKDKAVLAKI---QWKYMIIDEGHRM----KNHHCKLTQVLNTHYIAPYRLLLTGT 931
Cdd:cd00046    79 ----DADIIIATPDMLLNLLLREDRLflkDLKLIIVDEAHALlidsRGALILDLAVRKAGLKNAQVILLSAT 146
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
408-629 3.78e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   408 LQERENRIAARISLRMQELQRLPATMSEDLRLQAAIELRALRVlnfQRQLRMEFVQCTRRDTTLETALNIKLYKRTKRQG 487
Cdd:TIGR00618  192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA---LQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   488 LREARATEK-LEKQQKLEAERKRRQKHLEFLAAVLQHGKDLREFHRNNKAQLARMNKAVMNHHANAEREQKKEQERI--- 563
Cdd:TIGR00618  269 IEELRAQEAvLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllq 348
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   564 ----EKERMRRlMAEDEEGYRKLIDQKKDKRLAFLLSQTDeyISNLTQMVKQHKDDQMKKKEEEGKRLIQ 629
Cdd:TIGR00618  349 tlhsQEIHIRD-AHEVATSIREISCQQHTLTQHIHTLQQQ--KTTLTQKLQSLCKELDILQREQATIDTR 415
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
410-634 4.70e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.65  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   410 ERENRIAARISLRMQELQRLPATMSEDLRLQAAIELRALRVLNFQRQLRMEFVQctrrdtTLETALNIKLYKRTKRQGLR 489
Cdd:pfam17380  313 ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIR------QEEIAMEISRMRELERLQME 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   490 EARATEKLekQQKLEAERKrrQKHLEflaavlqhgkdlREFHRNNKAQLARMNKAvmnhhanaereqKKEQERIEKERMR 569
Cdd:pfam17380  387 RQQKNERV--RQELEAARK--VKILE------------EERQRKIQQQKVEMEQI------------RAEQEEARQREVR 438
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442632632   570 RLMAEDEEGYR--KLIDQKKDKRLAFLLSQTDEYISNLTQMVKQHKDdqmKKKEEEGKRLIqFKKEL 634
Cdd:pfam17380  439 RLEEERAREMErvRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD---RKRAEEQRRKI-LEKEL 501
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
251-390 5.04e-03

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 39.47  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632   251 SAGTPPqcsTPP----ASNPYGPPVPGQKmQVAPPPPhmqqgqplppqppqvggpppiqqqqppqqqqqqSQPPPPEPHQ 326
Cdd:pfam06346   42 SAAIPP---PPPlpggTSIPPPPPLPGAA-SIPPPPP---------------------------------LPGSTGIPPP 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442632632   327 HQLPNG-GKPLSMGPSGGQPLIPSSPmqPQVRGTlPGMPPGSQVPqpgGGPQRQVPPAGMPMPKP 390
Cdd:pfam06346   85 PPLPGGaGIPPPPPPLPGGAGVPPPP--PPLPGG-PGIPPPPPFP---GGPGIPPPPPGMGMPPP 143
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
409-607 8.73e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  409 QERENRIAARISLRMQELQRLPAtmsedlRLQAAIELRALRVLNFQRQLRmEFVQCTRRDTTLETALNIKLYKRTKRQGL 488
Cdd:COG4717   304 AEELQALPALEELEEEELEELLA------ALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAALL 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  489 REARAT---------EKLEKQQKLEAERKRRQKHLEFLAAVLQH------GKDLREFHRNNKAQLARMNKAVMNHHA--- 550
Cdd:COG4717   377 AEAGVEdeeelraalEQAEEYQELKEELEELEEQLEELLGELEEllealdEEELEEELEELEEELEELEEELEELREela 456
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442632632  551 -------NAEREQKKEQERIEKERMRRLMAEDEEGYRKL----------IDQKKDKRLAFLLSQTDEYISNLTQ 607
Cdd:COG4717   457 eleaeleQLEEDGELAELLQELEELKAELRELAEEWAALklalelleeaREEYREERLPPVLERASEYFSRLTD 530
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
416-626 9.01e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 9.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  416 AARISLRMQELQRLPATMSEDLRLQAAIELRALRVLNFQRQLRMEFVQCTRRDTTLETALNiklykrTKRQGLREARAte 495
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA------ALEAELAELEK-- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  496 kleKQQKLEAERKRRQKHLEFLAAVLQ----HGKDLREFHRNNKAQLARMN---KAVMNHHANAEREQKKEQERI----- 563
Cdd:COG4942    91 ---EIAELRAELEAQKEELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLqylKYLAPARREQAEELRADLAELaalra 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632632  564 ----EKERMRRLMAEDEEGYRKLIDQKKDKR--LAFLLSQTDEYISNLTQMVKQHK--DDQMKKKEEEGKR 626
Cdd:COG4942   168 eleaERAELEALLAELEEERAALEALKAERQklLARLEKELAELAAELAELQQEAEelEALIARLEAEAAA 238
HDA2-3 pfam11496
Class II histone deacetylase complex subunits 2 and 3; This family of class II histone ...
1097-1229 9.41e-03

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: 40.00  E-value: 9.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632632  1097 SGKFELLDRILP-----KLKATNHrVLLFCQMTQCMTIIEDYLGWRQFGYLRLDGTT-KAEDRGELLRKFNAKGSDVFVF 1170
Cdd:pfam11496   89 SGKFLVLNDLVNllierDRKEPIN-VAIVARSGKTLDLVEALLLGKGLSYKRYSGEMlYGENKKVSDSGNKKIHSTTCHL 167
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632632  1171 LLSTRAGGLGLNLQT---ADTVVIFDSDWNPHQDLQAQDRAHRIGQRNEVRVLRLMTVNSVE 1229
Cdd:pfam11496  168 LSSTGQLTNDDSLLEnykFDLIIAFDSSVDTSSPSVEHLRTQNRRKGNLAPIIRLVVINSIE 229
 
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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